Species | Paenibacillus_B thiaminolyticus | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_B; Paenibacillus_B thiaminolyticus | |||||||||||
CAZyme ID | MGYG000002490_03177 | |||||||||||
CAZy Family | GT2 | |||||||||||
CAZyme Description | D-alanine--poly(phosphoribitol) ligase subunit 1 | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 117873; End: 127097 Strand: + |
MQEPQKLDKS NVEDILALTP MQSGMLLQYL KDPDTTQYVE LIELGISGDI DTSLFEQSWS | 60 |
CVVQANEALR TLFRWEEVNQ PVQIVLKQHR PVIRYENYSE LDEEARARQI AARIAADRQE | 120 |
KFKLDQVPFR LTLCKQTGRN HTLLISFHHI LLDGWSTGIL LKEWLGAYRM LAQGMKPELR | 180 |
RKPPFKQFVA LLQQQDKKKQ ASYWSRYLHE LEAKPIPVSR GGASPEKASI AVHTEKRSGT | 240 |
YVADLHRFAR TAQVTQAALF YTAWGILLQH YTNSDDVLFG VTVSGRNTSI SGMEDMAGLF | 300 |
INTLPLRLKA GPEHGLPDLL ADVNRSIQAH EEHAGTSLTD IKGYGGMRTE GVPFDSLLVV | 360 |
ENYPLDKAVT SAEGPLAIAS HHIEEETEFD LTVRITAAEE LEMTFAYNEQ AHRSDTVAKL | 420 |
ACHYLYIIEQ IIQTSTQVTA YHETRLQDIG ILTAEEREQI RHFNLTTASY PREKTIHELF | 480 |
EEQVRLAPEG TAVTDEQRSC TYRELNEQAN RIARALRADG VERGQVVGLM ANRSIDMIAG | 540 |
IFGILKAGGV YLPLDSAHPA ERIAYMLQDG KVGTVLASAG LEPLVPEQTK VWVLNEALLG | 600 |
CGEATDMPSV NGPEHPAYVM YTSGSTGTPK GVAVGHRNVV RLVRNTNYVQ VEAGDCMLQA | 660 |
GAIGFDALTF EVFGALLNGG SLHIADKHTL LDSSRLDAFL RSRNISVALL TPALFNQLAQ | 720 |
QRPQMFAGLR HLIVGGDVLS PKHIEAVRQA CPGLAMWNAY GPTENTVIST CFRIDREYAE | 780 |
HIPIGPPISN STAYIVDRHD NLLPIGVPGE LLVGGDGVAL GYLNQPELTS EKFVPDPYCP | 840 |
GGVMYRTGDM ACWQEDGSLE YMGRIDQQVK IRGHRIEIGE IETMLLRHPS VQEAAVTALQ | 900 |
RGGHTELCAY VVASGQAPVS ELRDYLAATL PDYMIPSHVV PLEHIPLTPN GKLDRKALPA | 960 |
PAERVRSARD AALPRTELER LIAEAWQAVL ELESVSIHDK YFEVGGNSIN LIQLQSKLQR | 1020 |
QLKREVPIVT LFQYPTVHEL AAHLAGEADG TRGRASEQAA ASREDEPHSQ AAAGSARPGN | 1080 |
EGSRDIAVIG MAGRFPGARS IAEFWSNLQQ GQESISFFTD DELAEYGFDR DLLQRPEFVK | 1140 |
AKGVLDEMDH FDPAFFGYTP DQAAIMDPQV RLLHECAWHA LEDAGCDPER YGGSIGLFAG | 1200 |
VTNNFHWLSQ LSERLHGNLS DMFEVDSLND TYTVSTRISH KLNLRGPAIS LQTACSTSLV | 1260 |
AVHVACQSIL SGDCDLALAG GASIVLPHKS GYLYQEGMVK SPDGHCRSFD AQAKGTIGGD | 1320 |
GVGFVALKPL EAAKKDGDRI YAVIKGSAIN NDGSRKVGYT APSVEGQMDV IKRALAAAQV | 1380 |
PSDSITYVEA HGSGTPLGDP IEIEALTKAF QTDRTGFCRI GSVKTNIGHL DAAAGVAGLM | 1440 |
KTALALHHKR IPQSLHFETP NPNIDFANSP FVVNTALAEW RNDAGPLRAG VSSFGIGGTN | 1500 |
AHVILEEAPT REAGGDGRSS QLLALSARTP AALDAMTANL GAYLDERREL CLADVAYTLQ | 1560 |
SGRRHFKYRR ILSCDTIGEA IEALTPVEGR NSFDERKVVT FAADDGGSPV VFMFSGQGSQ | 1620 |
YVNMGADLYR DEPVFRAEMD RCFRLYRDIA GRDMKEILYP SGDAEAAALQ LNQTKHIQPV | 1680 |
MFMFEYALAR LVMAWGVKPE AMIGYSFGEF TAACLADVMS LEDAMRLIIL RGELMQQVPA | 1740 |
GAMLSVPLPE QEVRLRLDGS LSLAVVNGPS CIVSGTEEEI AAFEHRMKAE KIMCMRLPVA | 1800 |
TAGHSSLLHA VKEPFAAAMR QVRLRPPALP YVSTTTGTWI TAEEAADPDY WIRHLTDTVR | 1860 |
FADGMALLVQ EPRRLFVEIG PGHDLTLLAR RHLGSGREQQ ALNLVRPAQR GGSDSALLVN | 1920 |
RIGRLWLHGQ SIDWQAFHGE VRAIISLPSY PFARERYWPQ ASGGALAAPG TARSKGRPAS | 1980 |
GQMGKQTDMS DWFYVPTWKK SPTAASRKGD AAASWKEDTA GNWLVFADGA GLAADLVKHL | 2040 |
SERGAQVVTV RAGERFEQEG TMQYTVHPRN ERHYAKLFSE LQADGRLPNR MLHAWGVSAP | 2100 |
SRSDQQWIRT AQDLGFYSVL YTAKALKQQQ AREEMRMWVV TDSMHAIAGE PVLYPEKATV | 2160 |
LGPCRVIPQE LPHIQCRSID IVLPEAGSWQ RDRLVGRLLD EFGAAGTELA VAYRDNARWV | 2220 |
LDYEPFTISE PEAQTQGPRQ GGVYLITGGL GYIGHTLGGY LARSVQAKLA LTSRSLFPPR | 2280 |
AEWDTWLSVH GKEDAVSVQI GKLRQLEAQG AEVLVLSADA ADQGQMETVI RQAEAAFGPL | 2340 |
NGVIHAAGMT GDAAFRMLEE TDELLCEQHF RAKMYGLLVL EQVLAGKELD FCLLASSLSP | 2400 |
MLGGLGFSAY AAANHFMDAF VHDRNRRQRI PWTSVNWDGW QLEADQTIRG QAGASISELL | 2460 |
IAPAEGVELL RRLLSVRDMS QIVISTGDLG ARIDKWVRRE GQQEEPEAFR HGEGSYYSRP | 2520 |
ALSGEYVAPA TETERKLCGM WEQFFRIDRI GVQDDFFELG GDSLKAITVV SAIHKELSVE | 2580 |
IGLPVFFNMP TIQQLSAYID GAERSAYHDI ESAEAKDYYE LSSAQKRLYL IQQMEQGHTG | 2640 |
YNEIVAGVLE GRLDRTRLEA ALRRLVERHE SLRTSFELVN GKPMQKINEA VAIELEYEDY | 2700 |
SAAVTPLDSL DGEEKMDDRI RAAVATFVRS FDLTRAPLMR AGLIKLGEER HVLMVDLHHI | 2760 |
VSDGLSQDIF VNDFLALYAG RELPELPLQY KDFSEWQNRM MDTDEMKRQG AFWLERLKDA | 2820 |
PRLSLRTDYP RPDTRSFAGS LVPFELDAER TQGLKSLCLK EDVTLFMALL AIFNLLLAKV | 2880 |
CGQDDIVVGT PVVGRKQQAL QLIVGKFVNM LPLRNRLQEE MSFRNLLQAV RSTTLDAFAH | 2940 |
QDFQFEEMVQ QAGRERELGR NPIFDVVFAL QNMQNPEMSI PGLILKPFPF IHDASHFDLS | 3000 |
LIAEEDGDRL AFKFEYSTRL FQRDTIDRFA AYLQDIVFDV LAHPDKKIQE IKIAHHLAEP | 3060 |
EAVFLAGAQG EFGL | 3074 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd12117 | A_NRPS_Srf_like | 0.0 | 478 | 958 | 1 | 483 | The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C). 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 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. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain. |
cd05930 | A_NRPS | 0.0 | 488 | 958 | 1 | 444 | The adenylation domain of nonribosomal peptide synthetases (NRPS). 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. |
PRK12316 | PRK12316 | 0.0 | 7 | 1115 | 1548 | 2668 | peptide synthase; Provisional |
PRK12467 | PRK12467 | 0.0 | 32 | 1053 | 66 | 1106 | peptide synthase; Provisional |
PRK12467 | PRK12467 | 0.0 | 32 | 1051 | 1133 | 2169 | peptide synthase; Provisional |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BAY90071.1 | 0.0 | 163 | 3061 | 269 | 2678 |
BAY30132.1 | 0.0 | 245 | 3061 | 361 | 2689 |
BAZ00088.1 | 0.0 | 245 | 3053 | 361 | 2682 |
BAZ75991.1 | 0.0 | 245 | 3053 | 361 | 2682 |
AFY93865.1 | 0.0 | 449 | 1958 | 305 | 1861 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2VSQ_A | 1.26e-179 | 6 | 1050 | 3 | 1046 | Structureof surfactin A synthetase C (SrfA-C), a nonribosomal peptide synthetase termination module [Bacillus subtilis] |
4MZ0_A | 9.81e-167 | 1086 | 1958 | 41 | 935 | ChainA, CurL [Moorena producens 3L],4MZ0_B Chain B, CurL [Moorena producens 3L] |
7S6C_A | 1.64e-158 | 1083 | 2440 | 31 | 1372 | ChainA, 6-deoxyerythronolide-B synthase EryA2, modules 3 and 4, Lsd14 Polyketide synthase fusion [synthetic construct],7S6C_B Chain B, 6-deoxyerythronolide-B synthase EryA2, modules 3 and 4, Lsd14 Polyketide synthase fusion [synthetic construct],7S6C_C Chain C, 6-deoxyerythronolide-B synthase EryA2, modules 3 and 4, Lsd14 Polyketide synthase fusion [synthetic construct],7S6C_D Chain D, 6-deoxyerythronolide-B synthase EryA2, modules 3 and 4, Lsd14 Polyketide synthase fusion [synthetic construct],7S6D_A Chain A, 6-deoxyerythronolide-B synthase EryA2, modules 3 and 4, Lsd14 Polyketide synthase fusion [synthetic construct],7S6D_B Chain B, 6-deoxyerythronolide-B synthase EryA2, modules 3 and 4, Lsd14 Polyketide synthase fusion [synthetic construct],7S6D_C Chain C, 6-deoxyerythronolide-B synthase EryA2, modules 3 and 4, Lsd14 Polyketide synthase fusion [synthetic construct] |
7M7J_A | 7.95e-155 | 1086 | 2599 | 35 | 1485 | ChainA, EryAI [Saccharopolyspora erythraea],7M7J_B Chain B, EryAI [Saccharopolyspora erythraea] |
7M7I_A | 7.95e-155 | 1086 | 2599 | 35 | 1485 | ChainA, EryAI [Saccharopolyspora erythraea],7M7I_B Chain B, EryAI [Saccharopolyspora erythraea] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
O30409 | 2.39e-278 | 44 | 3067 | 3159 | 5644 | Tyrocidine synthase 3 OS=Brevibacillus parabrevis OX=54914 GN=tycC PE=1 SV=1 |
P0C064 | 3.43e-271 | 13 | 3051 | 1059 | 3562 | Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2 |
P0C063 | 1.68e-268 | 13 | 3051 | 1059 | 3563 | Gramicidin S synthase 2 OS=Aneurinibacillus migulanus OX=47500 GN=grsB PE=3 SV=2 |
Q04747 | 1.00e-266 | 7 | 3051 | 1 | 2515 | Surfactin synthase subunit 2 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAB PE=1 SV=3 |
O30408 | 1.22e-260 | 9 | 3053 | 6 | 2520 | Tyrocidine synthase 2 OS=Brevibacillus parabrevis OX=54914 GN=tycB PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000047 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.