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CAZyme Information: jhhlp_001546-t41_1-p1

You are here: Home > Sequence: jhhlp_001546-t41_1-p1

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 Lomentospora prolificans
Lineage Ascomycota; Sordariomycetes; ; Microascaceae; Lomentospora; Lomentospora prolificans
CAZyme ID jhhlp_001546-t41_1-p1
CAZy Family AA7
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1235 NLAX01000004|CGC3 137512.95 5.9192
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_LprolificansJHH5317 8768 N/A 208 8560
Gene Location Start: 2207903; End:2213251  Strand: +

Full Sequence      Download help

MASVVENSSN  TLSNGSTAQG  VPKDGTGVVK  LDPWLSPFEP  VLQRRFAKAH  EWISLLNETE60
GGLDKFSKGS  ERFGLNVDKD  NNVIYREWAP  NATEAFLIGE  FNNWERGAHP  MKKNEFGVFE120
ITVPAKDGQV  AIPHNSKIKI  SLTLPNGERA  DRLPAWIKYV  TQEISVSPAY  DARFWNPPVS180
ERYQFKHSRP  KKPQSLRIYE  AHVGISSPEL  RVTTYQEFTK  NMLPRIKALG  YNAIQLMAIM240
EHAYYASFGY  QVNNFFAASS  RYGPPEDLKE  LVDTAHSLGL  VVLLDVVHSH  ASKNVLDGLN300
EFDGSDHQYF  HEGGKGRHEL  WDSRLFNYGN  HEVLRFLLSN  LRFWMDEYQF  DGFRFDGVTS360
MLYAHHGIGT  GFSGGYHEYF  GAEVDEEGVV  YLMLANEMLH  RLYPEVITVA  EDVSGMPALC420
LPLSLGGVGF  DYRLAMAIPD  MWIKILKETK  DEDWDIGSIC  WTLTNRRHGE  KTIAYCESHD480
QALVGDKTIM  MHLCDAELYT  NMSNLTPLTP  VIDRGMALHK  MIRLLTHGLG  GEGYLNFEGN540
EFGHPEWLDF  PREGNQNSFW  YARRQLNLTE  DNLLRYQYLN  EFDRLMNLCE  EKLGWLHAPQ600
AYISLKHEGD  KVIVFERGDG  VFIFNFHPTE  SFTDYRIGIN  VPGTYKCVLN  TDSKEVGGHD660
RIDINTRYHT  TAMEWNGRKN  WTHIYIPCRT  AMNLLNPPSP  PSTSNLHLSA  SIHNRSLSSV720
KMFKSGLSSF  ARAARPALTP  RSALRPSSLR  YPVTNRWAST  ASVGNGKIHQ  VIGAVVDVKF780
DTAKLPPILN  ALETDNNGNK  LVLEVAQHLG  ENVVRCIAMD  GTEGLVRGAK  ALDTGAPITI840
PVGPATLGRI  MNVTGDPIDE  RGPIKSEKTR  PIHAEAPEFV  DQSTTAEILV  TGIKVVDLLA900
PYARGGKIGL  FGGAGVGKTV  FIQELINNIA  KAHGGYSVFT  GVGERTREGN  DLYHEMQETS960
VIQLDGESKV  ALVFGQMNEP  PGARARVALT  GLTVAEYFRD  EEGQDVLLFI  DNIFRFTQAG1020
SEVSALLGRI  PSAVGYQPTL  AVDMGGMQER  ITTTRKGSIT  SVQAVYVPAD  DLTDPAPATT1080
FAHLDATTVL  SRGISELGIY  PAVDPLDSKS  RMLDPRIVGE  EHYEIATRVQ  QILQEYKSLQ1140
DIIAILGMDE  LSEADKLTVE  RARKIQRFLS  QPFTVAEVFT  GIQGRLVDLK  DTITSFKAIL1200
NGEGDSLPEN  AFYMVGDFAS  VKEKAEKILA  ELEKN1235

Enzyme Prediction      help

EC 2.4.1.18:166 2.4.1.18:50

CAZyme Signature Domains help

Created with Snap611231852473083704324945556176797418028649269881049111111731293GH13
Family Start End Evalue family coverage
GH13 247 540 2.1e-152 0.9965870307167235

CDD Domains      download full data without filtering help

Created with Snap61123185247308370432494555617679741802864926988104911111173180584AmyAc_bac_euk_BE7581231atpB7661228atpD1691PLN024477651227PRK12597
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
200460 AmyAc_bac_euk_BE 0.0 180 584 2 406
Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes. Branching enzymes (BEs) catalyze the formation of alpha-1,6 branch points in either glycogen or starch by cleavage of the alpha-1,4 glucosidic linkage yielding a non-reducing end oligosaccharide chain, and subsequent attachment to the alpha-1,6 position. By increasing the number of non-reducing ends, glycogen is more reactive to synthesis and digestion as well as being more soluble. This group includes bacterial and eukaryotic proteins. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
214349 atpB 0.0 758 1231 8 489
ATP synthase CF1 beta subunit
211621 atpD 0.0 766 1228 3 461
ATP synthase, F1 beta subunit. The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. Proton translocating ATP synthase, F1 beta subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), A subunit. [Energy metabolism, ATP-proton motive force interconversion]
215246 PLN02447 0.0 1 691 35 725
1,4-alpha-glucan-branching enzyme
183615 PRK12597 0.0 765 1227 3 460
F0F1 ATP synthase subunit beta; Provisional

CAZyme Hits      help

Created with Snap611231852473083704324945556176797418028649269881049111111731694UPK94817.1|CBM48|GH13_81694UNI16208.1|CBM48|GH13_81694QKD59535.1|CBM48|GH13_81694QGI86417.1|CBM48|GH13_81694QGI69049.1|CBM48|GH13_8
Hit ID E-Value Query Start Query End Hit Start Hit End
UPK94817.1|CBM48|GH13_8 0.0 1 694 1 697
UNI16208.1|CBM48|GH13_8 0.0 1 694 1 697
QKD59535.1|CBM48|GH13_8 0.0 1 694 1 697
QGI86417.1|CBM48|GH13_8 0.0 1 694 1 697
QGI69049.1|CBM48|GH13_8 0.0 1 694 1 697

PDB Hits      download full data without filtering help

Created with Snap61123185247308370432494555617679741802864926988104911111173287004BZY_A356965CLT_A75812315FL7_D75912315LQX_D76612314B2Q_E
Hit ID E-Value Query Start Query End Hit Start Hit End Description
4BZY_A 2.36e-305 28 700 31 701
Crystal structure of human glycogen branching enzyme (GBE1) [Homo sapiens],4BZY_B Crystal structure of human glycogen branching enzyme (GBE1) [Homo sapiens],4BZY_C Crystal structure of human glycogen branching enzyme (GBE1) [Homo sapiens]
5CLT_A 1.43e-302 35 696 6 665
Crystal structure of human glycogen branching enzyme (GBE1) in complex with acarbose [Homo sapiens],5CLT_B Crystal structure of human glycogen branching enzyme (GBE1) in complex with acarbose [Homo sapiens],5CLT_C Crystal structure of human glycogen branching enzyme (GBE1) in complex with acarbose [Homo sapiens],5CLW_A Crystal structure of human glycogen branching enzyme (GBE1) in complex with maltoheptaose [Homo sapiens],5CLW_B Crystal structure of human glycogen branching enzyme (GBE1) in complex with maltoheptaose [Homo sapiens],5CLW_C Crystal structure of human glycogen branching enzyme (GBE1) in complex with maltoheptaose [Homo sapiens]
5FL7_D 6.45e-266 758 1231 33 507
Structure of the F1c10 complex from Yarrowia lipolytica ATP synthase [Yarrowia lipolytica],5FL7_E Structure of the F1c10 complex from Yarrowia lipolytica ATP synthase [Yarrowia lipolytica],5FL7_F Structure of the F1c10 complex from Yarrowia lipolytica ATP synthase [Yarrowia lipolytica]
5LQX_D 2.15e-265 759 1231 1 474
Chain D, ATP synthase beta subunit [Ogataea angusta],5LQX_E Chain E, ATP synthase beta subunit [Ogataea angusta],5LQX_F Chain F, ATP synthase beta subunit [Ogataea angusta],5LQY_D Chain D, ATP synthase beta subunit [Ogataea angusta],5LQY_E Chain E, ATP synthase beta subunit [Ogataea angusta],5LQY_F Chain F, ATP synthase beta subunit [Ogataea angusta],5LQZ_D Chain D, ATP synthase beta subunit [Ogataea angusta],5LQZ_E Chain E, ATP synthase beta subunit [Ogataea angusta],5LQZ_F Chain F, ATP synthase beta subunit [Ogataea angusta]
4B2Q_E 1.39e-262 766 1231 6 471
Model of the yeast F1Fo-ATP synthase dimer based on subtomogram average [Saccharomyces cerevisiae],4B2Q_F Model of the yeast F1Fo-ATP synthase dimer based on subtomogram average [Saccharomyces cerevisiae],4B2Q_e Model of the yeast F1Fo-ATP synthase dimer based on subtomogram average [Saccharomyces cerevisiae],4B2Q_f Model of the yeast F1Fo-ATP synthase dimer based on subtomogram average [Saccharomyces cerevisiae]

Swiss-Prot Hits      download full data without filtering help

Created with Snap6112318524730837043249455561767974180286492698810491111117327694sp|Q8NKE1|GLGB_RHIID17694sp|Q96VA4|GLGB_ASPOR7221233sp|P23704|ATPB_NEUCR22694sp|Q9Y8H3|GLGB_EMENI28692sp|Q6CCT1|GLGB_YARLI
Hit ID E-Value Query Start Query End Hit Start Hit End Description
sp|Q8NKE1|GLGB_RHIID 0.0 27 694 15 680
1,4-alpha-glucan-branching enzyme OS=Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194) OX=747089 GN=GLC3 PE=2 SV=2
sp|Q96VA4|GLGB_ASPOR 0.0 17 694 3 683
1,4-alpha-glucan-branching enzyme OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=gbeA PE=2 SV=1
sp|P23704|ATPB_NEUCR 0.0 722 1233 1 516
ATP synthase subunit beta, mitochondrial OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=atp-2 PE=2 SV=1
sp|Q9Y8H3|GLGB_EMENI 0.0 22 694 6 678
1,4-alpha-glucan-branching enzyme OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=be1 PE=2 SV=3
sp|Q6CCT1|GLGB_YARLI 0.0 28 692 5 680
1,4-alpha-glucan-branching enzyme OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=GLC3 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000059 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in jhhlp_001546-t41_1-p1.