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CAZyme Information: MGYG000003687_01449

You are here: Home > Sequence: MGYG000003687_01449

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Paenibacillus polymyxa
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus polymyxa
CAZyme ID MGYG000003687_01449
CAZy Family GT2
CAZyme Description D-alanine--poly(phosphoribitol) ligase subunit 1
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
5233 MGYG000003687_4|CGC6 594460.77 4.926
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003687 5656034 Isolate China Asia
Gene Location Start: 262845;  End: 278546  Strand: -

Full Sequence      Download help

MRNALIQNIY  PLTPMQEGLL  YHSILDEHSE  AYFDQTVITI  NERLNAETLK  ESFQTLIDRY60
DVLRTVFVYK  ETDQPLQVVL  ANKEATIDYR  DITELNEAEQ  RLYVDNFTIN  DRKMRFDLEK120
DLLIRISVLA  LSDTSCKMVL  SFHHIIMDGW  CIGTIAKDLF  QIYRAYSIKQ  KPELDAVFPY180
SRYISWLGQQ  NKKTALAYWE  QQLSGVEEQS  GLPLSSKSTE  DGSYKLNNHI  FTLDEQLTRS240
LEMIAQQNQV  TLSSVFHGIW  GLLLQRYNDT  KDVVFGSVVS  GRPAELEGSE  KMVGLFINTI300
PVRICHKEAQ  TFSQIIKQFQ  QNMMESGKYH  FLSLADIQML  TPLGKSLIHH  IIAFENYPIT360
EELAGGEGEQ  LVSIVETEGF  EQTNYDFNIG  VIPGKELKVK  FGYNSIAYQA  SDIQRIELHL420
KQIAEQVVSN  PHMDVDDIDL  LSGEEKHRIL  RDFNDTNALY  PQSQTIQQLF  EEQAALTPNR480
LAAAFADGRL  TYLELNERAN  RLARVLRMKG  VQTGQIVGIA  AYRSPEMLVG  IMAILKAGGA540
YLPINPEDPL  ERIQYIAGNS  GASILLVQQE  IQSTLKDLSQ  NISVLAIGAD  WATEKTNLEP600
YSGPEDVAYV  IYTSGSTGKP  KGVMIRHTSI  VNRLHWMQKK  YPIGVDDTIL  QKTPYTFDVS660
VWELFWWAIA  GASVYFLPPD  GEKDPKLLVN  TVAEQKITTL  HFVPSMLSVF  LEYVEQHQAE720
GKLSSIKRVF  ASGEALTVKQ  ARRFNTLLRK  PNGTTLHNLY  GPTEATVDAT  WFDCPDGDDL780
QSIPIGKPID  NNRLYILDQE  GRLLPVGIPG  ELYIAGTGVA  QGYINQPDLT  DERFTDSPFV840
IGERMYKTGD  LAKWLPDGNV  EYLGRTDHQV  KIRGYRIETG  EIEKVLLSHH  DIREAVVLSR900
KDQEDETYLC  AYIVSDRELL  TQEIRSYLKA  SLPLYMVPAH  LIQIAAIPLT  NNGKVNRGAL960
PEPHHVIREQ  GFVAPRTDTE  TRLVRLWEDI  LHVSPIGVHS  HFFELGGHSL  KATILIGKII1020
REFQVELPMR  EIFEYPTVES  MSKLIERTIG  RGAGTFTEIA  LLSGQAYYPV  SSSQRRQMIL1080
HQLEGAELVY  NMPSVMLVQG  HLDQERLKMA  FTTLIHRHEA  LRTSFSWING  EPVQSVHDEV1140
EFELKIHSLT  SKEDLEEQQI  ETVLSEFVQP  FDLSRAPLLR  GELIPLTENQ  NMLLVDLHHI1200
ISDGVSMSII  MDEFVKAYDG  QALPPLSVQY  KDYANWHNEQ  INHGFIKEQE  SYWLDLFKHE1260
PPVLELPTDF  PRPSIQSYEG  NTVSRILGDD  ITEPLHKLAA  ETQSTLFMIL  LAVYNVVLSK1320
HARQDDIVIG  TPVAGRRHPD  TEKIVGMFVN  TLALRTSPSA  EKSLSAFLDE  VKETVLSAFE1380
HQEYPFEQLV  EKLALRRDVS  RSPIFDTMFV  MQNTKGQPLQ  SSGLEFKPFP  FNPGVSRFDL1440
TLSAEETGSY  LHLNLEYNSA  LFQKDTVERF  LDHMVVVLRS  FVAHSTQTIG  DTDLLTTVEK1500
EVILKKFNGT  AAPYPREKTI  HQLFEEQVER  TPEHPAALYQ  DRQLTYRELN  TQANRVAHVL1560
RKKGIGPDQM  VGIAVHRSLE  MIVGLLGILK  AGGAYLPLHP  EDPEERLGFM  LEDSGASILL1620
TQRDQLDRLR  PHEADRELIA  IEDLLMEGME  LTGEECEKNP  EPVNRSSDLV  YVIYTSGSTG1680
KPKGVMIEHA  SLINRLHWME  QRIPFGAEDV  ILQKTPYTFD  VSLWELFSWA  IQGATVCFLE1740
PGGEKDPATI  AETVEANGVT  AIHFVPSMLG  AFLEYIEHSG  AAGKMRSVRR  VFASGEALMT1800
EHVRRFNRLL  GTEGATLHNL  YGPTEATVEV  AYYDCPADQE  PESIPIGKPI  DNVKLYILDH1860
KDRLQPIGVP  GELHIGGDCV  ARGYVNRKEL  TEEKFVADPY  AAGGRMYRTG  DLARWLPDGN1920
IEYMGRIDHQ  VKIRGYRIEL  GEIEAALLAY  EGIKAATVLA  LDDRDGGKYL  CAYFESGEGL1980
NTSILRAHLK  ALIPDYMVPS  HFVRLDVMPH  LSSGKVNRKA  LPEPDHGMRA  TSYVAPRNET2040
ERKLAEIWEK  LLDISSIGIH  DNFFELGGHS  LTATRLMSRI  NKLLQVEIPL  RNIFAHPTIE2100
EMSVLICGPE  VAVGTMMDIA  PSELRDSYPV  TSVQKRQMIL  HQFEGAETAY  NMPFALLMEG2160
ELDIQRLERV  FRDLIDRHEA  LRTSFEWGTE  EPVQKIHSEV  PFQLSLQQAD  DIGIEAQDKQ2220
IQAIFKTFVR  PFNLGQAPLL  RAKLVRISDN  RHILMVDMHH  IVADGVSMSV  LANDFTTLYH2280
GNSLPPLRIQ  YKDYAVWNSE  WIKEGHLIKQ  EQYWLDLFSD  ELPVLNLPTD  FTRPQVQSFE2340
GDRYSFQADK  TLREGLQQFV  AENRTTLFMV  LLSAYNVLLH  KYSGQEDIVV  GSPIAGRNHT2400
DLENIMGMFV  NTLVLRNRPA  ADKTLKQFLL  EVQSSSLEAF  EHQDYPIEDL  VDKLELHRDL2460
SRNPLFDTMF  SLENTDSVSL  LTDGISISPY  SVEAGIAKVD  LTLTAEADQE  GLSFRIDYCN2520
KLFYKESIER  MSKHYLQILQ  TIVDSADARI  GDVNMVTVSE  EEILLTKFNT  VPASNEKENR2580
KLLHQLFEEQ  VAKTPERVAV  SFEEQQWTYS  ELNDKANQLA  RVLREKGVQA  NTLVGMMVER2640
SFEMIVGILG  ILKAGGAYVP  LAPDYPAERI  SLMLYDCKIT  LLLASHHVLT  ESTFIKEAGA2700
DAFAGEILDL  DQLDTIVKDL  DSSNLPYVNE  PDDLAYVLYT  SGSTGKPKGN  LTMHYNVERL2760
IKNSNYIDLT  EQDILLQLSN  YAFDGSVFDI  FGALVNGSKL  VLLRKENMLN  PEKLSSLIRN2820
ENVSVFFITT  ALFNTLIETN  IECFTTIRKI  LFGGERVSLP  HVSKLFEHIG  PHKMLHMYGP2880
TESTVFATCY  GVDQIHERKG  TIPIGAPITG  TTVYILDKNL  KLQPIGIPGE  LCIAGDALSQ2940
GYLNLPDFTN  EKFIDNPFNP  GEKMYKTGDI  AKWLPDGNIE  FVGRQDHLVK  IRGFRIELGE3000
IENRLLSHER  IKEAIVVAKP  DPSGQNRISA  YMVTDGELNT  SAIRRYLAKY  LPDYMLPSSL3060
ILLDSLPLNA  NGKVDQKKLP  EPHINLDLST  LYEPPTSPTE  EKLVKIWEGV  LGQEGIGISH3120
SFFDLGGDSI  KAIQVIARLS  QEGLKLDMKD  IFQHPTVQQV  APYVQRRTRI  IDQKAVTGEV3180
QLTPIQRWFF  ENVQDDRNHF  NQAVMLFTSG  VFDEEALKTA  LENIIIHHDA  LRMAYEIGQS3240
SVCQYHTETQ  LRPFHLNIYN  LQGNNDAESK  IEEEASRLQA  TMDLRAGEMI  RVGLFQTDQG3300
QHLLIAIHHL  VIDGVSWRIL  LEDLESAYTQ  ALQGEDIALP  DKTDSFQYWS  DRLAEYSNSR3360
TLLKEKAYWQ  QIEGVQCESP  FPQKSTVTDE  GGVKKERTSI  AVRLDKQDTQ  LLLGTAHQAY3420
NTEINDLLLS  ALGLAIKQWA  GSKIFAINLE  GHGREEIMEE  IDVTRTIGWF  TSMFPIVLDM3480
RDSEDISSVI  RRTKEMIRHI  PNRGIGYGVL  KYLTDVEHTQ  DLDFNIQPQI  SFNYLGQFMD3540
GTQEGSFESS  PLSPGRSVGE  GAESHFTLDI  NSIVSQDQLL  LEFGYIRGEH  ADHAIEQLSL3600
MYIEHLKMLI  NHCTSISQKV  LTPSDYQDHT  LSIPELDQIL  KQFGGTEQVE  HIYSLTPMQQ3660
GMLFHYMMEP  ETTAYVEQVA  IEMEGELQQE  LLEQSFQELL  AKYEVLRTNF  VFTSIREPRQ3720
VVRKHQHAEF  QFYDLTGMDE  QEITAYLEDH  KKQDLLRGFD  LSNEALIRIN  VLKTTPDKFL3780
MMWTFHHMIM  DGWCVGIVYH  DFMSMYLDLK  NGRPLKSETA  PAYSTYIRWL  EKQDKGESMQ3840
YWKQALDGYA  QCAVIPKTFK  LQAKEGGYRT  SQLEFSLDQT  MTRRLTEIAS  HNRITVNTLF3900
QSIWGALLQR  YNNTNDVVFG  AVVSGRPPVI  PDIESMVGIF  INTIPVRIYG  EENESFIEMA3960
KRAQQSSIES  VKYEYTSLAD  IQSVTTLKQS  LLDHIIVFEN  YPEYGEEEAL  QKHNLKIHVR4020
DMAFYEQTNY  DFNLIVSLKD  ELNIKFLYNA  DTLSREFVER  IKNHLNGVVR  QIVDNPEMSI4080
SSIEVTSLPE  KEVILNEFNN  TTAIYPRAKT  IHQLFEEQVG  RTPEHPAALY  KGRQLTYREL4140
NAQANRLAHV  LREKGVGPDR  VVGIAVHRSL  EMIIGLLGIL  KAGGAYLPLN  PEDPEERLAF4200
MLEDSGASIL  LTQQELVEQL  RCHGTTRELI  AIEDLLVQEK  EQTEREKNPE  SINRSTDLVY4260
VIYTSGSTGK  PKGVMIEHAS  LINRLHWMQK  RIPFGAEDVI  LQKTPYTFDV  SLWELFSWAI4320
QGATVCFLEP  GGEKDPATIA  ETVESNRVTA  LHFVPSMLGA  FLEYMEHSGA  AGKMRSVRRV4380
FASGEALMTE  HVRRFNCLIG  GGGATLHNLY  GPTEATVEVA  YYDCPVEHEP  ESIPIGKPID4440
NVKLYILDKK  DRLQPIGIPG  ELHIGGDCVA  RGYVNREELT  EEKFVEDPYE  PGGRMYRTGD4500
LARWLPDGNI  EYMGRIDHQV  KIRGYRIELG  EIEAALLAHD  GVRAAAVLAR  ADDRTGMPSL4560
GAYVVAEPHV  TTAMLRQNLS  VSVPEYMIPA  YFVFLDQMPL  TSSGKINRRM  LLEIELEFGT4620
GTEYVEPSSE  LEKELVEIWM  SVLGIEHVGI  DDNFFELGGH  SLTAIQLASR  LQGIWSSELR4680
LSSIYQYPTV  RELALHVEGM  EENHSALAQQ  FDQIIALLHQ  KLNVKGWLQQ  EQFNGKSYIV4740
LHLEDGAISF  EKEIMELLDM  KCDESIQPHY  ITWHGEETLR  LEEANLEDIK  SIWTERIDND4800
LDVFSKAILS  LGVIERLPVS  PTQRYHLQHS  DISGTIIPLE  KHMNMEYVEE  AIRQIIREQD4860
LMRSTLCEEN  GELQWQVREA  PDHLPVPLVD  ISMYDEDTQQ  VILNNIVWPY  FYRQHELSNS4920
LLYRILIVKK  NLKDYMLILP  FSHSIFDFMS  SEIIKHQFNT  YYECVRAGKE  TPKGSRNRYS4980
DFTAHIMEGP  QGVDDLELAT  TYNLDKFDRA  IGRITDFVSQ  KAVLEGHTTV  IWDLKSSERA5040
VHLDNTSHWE  VAFFTFTAFC  KMYFELSQVP  IWVTQYGRSF  GEKRYYDVIG  EFVDHIPILT5100
NLDQNLVSLE  QQVRQSVQWA  AEHNISFANL  MYNPDVQNDY  PLSGGYLQQA  LDRMPIVFNF5160
LGELRSEHQL  LQTVDLGNVN  VEGRTRILCE  VWHDSESNLF  VALTLPFSED  ESIVRNHLQS5220
ALEQLERRWA  TVL5233

Enzyme Prediction      help

No EC number prediction in MGYG000003687_01449.

CDD Domains      download full data without filtering help

Created with Snap261523784104613081569183120932354261628783139340136633924418644484709497141134613A_NRPS_Bac468963A_NRPS_Bac15222025A_NRPS_Bac41124611A_NRPS_AB3403-like25853082A_NRPS_Bac
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd17655 A_NRPS_Bac 0.0 4113 4613 1 488
bacitracin synthetase and related proteins. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
cd17655 A_NRPS_Bac 0.0 468 963 1 489
bacitracin synthetase and related proteins. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
cd17655 A_NRPS_Bac 0.0 1522 2025 1 490
bacitracin synthetase and related proteins. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
cd17646 A_NRPS_AB3403-like 0.0 4112 4611 1 488
Peptide Synthetase. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
cd17655 A_NRPS_Bac 0.0 2585 3082 1 489
bacitracin synthetase and related proteins. This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.

CAZyme Hits      help

Created with Snap26152378410461308156918312093235426162878313934013663392441864448470949715423183QND46664.1|GT11933161BAY90071.1|GT21803161BAZ00088.1|GT21803161BAZ75991.1|GT21803161BAY30132.1|GT2
Hit ID E-Value Query Start Query End Hit Start Hit End
QND46664.1 0.0 542 3183 1 2679
BAY90071.1 8.24e-304 193 3161 312 3280
BAZ00088.1 1.39e-301 180 3161 300 3289
BAZ75991.1 1.39e-301 180 3161 300 3289
BAY30132.1 1.09e-300 180 3161 300 3291

PDB Hits      download full data without filtering help

Created with Snap261523784104613081569183120932354261628783139340136633924418644484709497146120306MFY_A46121136MFZ_A364046992VSQ_A106820216P1J_A106919356OYF_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
6MFY_A 0.0 461 2030 202 1721
Crystalstructure of a 5-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis],6MG0_A Crystal structure of a 5-domain construct of LgrA in the thiolation state [Brevibacillus parabrevis],6MG0_B Crystal structure of a 5-domain construct of LgrA in the thiolation state [Brevibacillus parabrevis]
6MFZ_A 0.0 461 2113 202 1804
Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis]
2VSQ_A 3.51e-227 3640 4699 1 1041
Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis]
6P1J_A 3.03e-225 1068 2021 6 964
Thestructure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo2 serine module [Eleftheria terrae],6P1J_B The structure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo2 serine module [Eleftheria terrae]
6OYF_A 1.90e-205 1069 1935 4 873
Thestructure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo1 serine module [Eleftheria terrae],6OZV_A The structure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo1 serine module in complex with AMP [Eleftheria terrae],6P4U_A The structure of condensation and adenylation domains of teixobactin-producing nonribosomal peptide synthetase Txo1 serine module in complex with Mg and AMP [Eleftheria terrae]

Swiss-Prot Hits      download full data without filtering help

Created with Snap261523784104613081569183120932354261628783139340136633924418644484709497110653640sp|P39846|PPSB_BACSU63639sp|Q04747|SRFAB_BACSU63639sp|P94459|PPSD_BACSU10653639sp|P39847|PPSC_BACSU10654705sp|Q70LM4|LGRD_BREPA
Hit ID E-Value Query Start Query End Hit Start Hit End Description
P39846 0.0 1065 3640 8 2554
Plipastatin synthase subunit B OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsB PE=1 SV=1
Q04747 0.0 6 3639 6 3574
Surfactin synthase subunit 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAB PE=1 SV=3
P94459 0.0 6 3639 7 3596
Plipastatin synthase subunit D OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsD PE=1 SV=2
P39847 0.0 1065 3639 8 2548
Plipastatin synthase subunit C OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsC PE=1 SV=2
Q70LM4 0.0 1065 4705 5 3623
Linear gramicidin synthase subunit D OS=Brevibacillus parabrevis OX=54914 GN=lgrD PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000049 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003687_01449.