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CAZyme Information: OTA35730.1

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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 Hortaea werneckii
Lineage Ascomycota; Dothideomycetes; ; Teratosphaeriaceae; Hortaea; Hortaea werneckii
CAZyme ID OTA35730.1
CAZy Family GH72
CAZyme Description Non-reducing end alpha-L-arabinofuranosidase [Source:UniProtKB/TrEMBL;Acc:A0A1Z5TIA3]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1648 183201.07 6.0155
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_HwerneckiiEXF-2000 15649 1157616 29 15620
Gene Location Start: 146792; End:153759  Strand: -

Full Sequence      Download help

MHLKPVALAA  ALAPFAAALD  VQVASSGGNK  TSYHQYGFLH  EDINNSGDGG  IYAELIVNRA60
FQSSEMYPVS  LNGYHSLHGA  RLSIQNLSQP  LSAALDSSMR  VAAGNGSSRA  GFENEGYWGM120
NVECQKYTGS  FWVRGAYDGS  FTASLQSNLT  DDVFGSVEVP  SQAVADDWVE  HTFTLTPDRD180
APNSNNTFAI  TFNPAGTENG  YLDFNLISLF  PPTYKDRPNG  LRVDLAQVLE  AYHPTVFRFP240
GGNMLEGNTN  ETYWDWKKTL  GPLRERPGFP  GVWGYMQTNG  LGLMEYLEMA  EDINNMTIGK300
QRRLSRRQLS  NVDHSLVVGV  WAGLSLNGDI  TPRNDLQPFI  DDALNEIEFI  RGPVDSPWGS360
RRAELGHPEP  FNLQYVEVGN  EDWLAGAPEG  WNSYKEYRFP  MFMQAINDAY  PDIQVIASGA420
TSDNYTFPAP  AIGDYHPYRE  PDALVEEFNR  FDNDLGHIVG  EVSATFPNNG  SKFDGPLFEF480
PAWIGAVGSA  ISMIGYERNA  DRIPGTFYAP  ILRNMNRWQW  AVTMIQHAAD  PALTTRSVSW540
YIWEALAASP  ISHTLPANEQ  FGPVFYVAGR  DENRHDALVW  KGACYNISSN  DIYNSTYRAN600
STRVPVSVHF  DGVEAGTEAT  LTMVTNPGGD  PYAMVDPLEG  NEVVSTTETP  ITANADGVFE660
FYMTELSLAV  LDTGVNKRVA  GAPYSPISKS  KHDWKPRMAG  KPPGYRPSRY  GEGAREFWQS720
TLRGVKRSDS  TVIDPIKHFL  STELRAFKES  RNALQATQKS  FDHVIARYLS  QSKTKEASSL780
REDAFQVHEA  RRAYIKASMD  FCTGAPQVRA  SLDKLIVRIF  SDQWKDMRAS  REANNGIFAK840
LSSEMERVRG  WSSEMDNSER  AFKRELLTAR  RQIEDSVSSR  IRPSRELEDY  SASTVPYLGS900
GAGGATGITS  KSANERLEQQ  GWLFMKTTTG  KPARTVWSRR  WVFVKSGIFG  WLIQGAKSGG960
VEESEKIGVL  LCSIRPAFQE  DRRFCFEIKT  KDTSIILQAE  TQDELTEWIS  ALEVAKKKAL1020
EDPTSTETSP  LSSGVDPAFA  VSSPVAPEFA  AKLGDSQPDE  ARESEASVDQ  RRITIKVFLE1080
PLRLLQRRLS  YLVRNANSED  PDSLEEVLKV  LIKLEADVPQ  RSSSVESWED  ITYEGGSPTT1140
AGDQQKSPRR  YGKNVKASLR  IDGNLYGDPA  RTGREVQKFK  LPAQPVVYAP  QGMQASVTRD1200
FNVSAKALFH  VMFGDKSAVF  QLLYANRWAD  KISQSPWSKP  AEAKGPWTRK  FTSQDQDSPM1260
SDTQTVDVSN  DHLCYVVTNN  KNPWRLPYAT  RFGLVTKIVI  THTSKSKCKL  AIFQQVNWLQ1320
APQWSYIKHL  IEKQALNSLE  ADALDLTNVA  MDQVAKLGNH  SKTNRAIEIF  GGIGQQLQVP1380
QIDVSAVPNV  ARSIAANGAR  PQETTGLPRL  VLDDVFAKTL  QLVSMVIDIL  IAVGKGAVGV1440
CTAHTFLVAL  LATSMIYNSW  YGYRDSLLWY  QERSAGKFMS  RVGVTPDPVM  GRSIYLRDLE1500
ELVMPADVNE  TLDAMAPSSS  MAEAKTCRTT  FSDMIAADDA  SIATPQKHAA  RLHNTRDAIA1560
RYRHDLLIAL  RVVNRVENDV  LKAEWEDWVR  SEERKCAKVE  RMLQRGESGK  KSSKSKLDVD1620
AQLGEEFAEY  CRSCRTEVAG  LLNETRIM1648

Enzyme Prediction      help

EC 3.2.1.55:10

CAZyme Signature Domains help

Created with Snap821642473294124945766597418249069881071115312361318140014831565117426GH51
Family Start End Evalue family coverage
GH51 206 542 2.5e-57 0.49047619047619045

CDD Domains      download full data without filtering help

Created with Snap821642473294124945766597418249069881071115312361318140014831565708855BAR_SIP3_fungi9181020PH_SIP311971336DUF47829191021PH_ACAP208429AbfA
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
153293 BAR_SIP3_fungi 2.39e-56 708 855 66 214
The Bin/Amphiphysin/Rvs (BAR) domain of fungal Snf1p-interacting protein 3. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. This group is composed of mostly uncharacterized fungal proteins with similarity to Saccharomyces cerevisiae Snf1p-interacting protein 3 (SIP3). These proteins contain an N-terminal BAR domain followed by a Pleckstrin Homology (PH) domain. SIP3 interacts with SNF1 protein kinase and activates transcription when anchored to DNA. It may function in the SNF1 pathway. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
270098 PH_SIP3 8.69e-55 918 1020 1 104
Snf1p-interacting protein 3 Pleckstrin homology (PH) domain. SIP3 interacts with SNF1 protein kinase and activates transcription when anchored to DNA. It may function in the SNF1 pathway. SIP3 contain an N-terminal Bin/Amphiphysin/Rvs (BAR) domain followed by a PH domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
406424 DUF4782 1.12e-26 1197 1336 3 145
Domain of unknown function (DUF4782). This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 150 amino acids in length. The family is found in association with pfam02893.
270070 PH_ACAP 4.81e-23 919 1021 1 98
ArfGAP with coiled-coil, ankyrin repeat and PH domains Pleckstrin homology (PH) domain. ACAP (also called centaurin beta) functions both as a Rab35 effector and as an Arf6-GTPase-activating protein (GAP) by which it controls actin remodeling and membrane trafficking. ACAP contain an NH2-terminal bin/amphiphysin/Rvs (BAR) domain, a phospholipid-binding domain, a PH domain, a GAP domain, and four ankyrin repeats. The AZAPs constitute a family of Arf GAPs that are characterized by an NH2-terminal pleckstrin homology (PH) domain and a central Arf GAP domain followed by two or more ankyrin repeats. On the basis of sequence and domain organization, the AZAP family is further subdivided into four subfamilies: 1) the ACAPs contain an NH2-terminal bin/amphiphysin/Rvs (BAR) domain (a phospholipid-binding domain that is thought to sense membrane curvature), a single PH domain followed by the GAP domain, and four ankyrin repeats; 2) the ASAPs also contain an NH2-terminal BAR domain, the tandem PH domain/GAP domain, three ankyrin repeats, two proline-rich regions, and a COOH-terminal Src homology 3 domain; 3) the AGAPs contain an NH2-terminal GTPase-like domain (GLD), a split PH domain, and the GAP domain followed by four ankyrin repeats; and 4) the ARAPs contain both an Arf GAP domain and a Rho GAP domain, as well as an NH2-terminal sterile-a motif (SAM), a proline-rich region, a GTPase-binding domain, and five PH domains. PMID 18003747 and 19055940 Centaurin can bind to phosphatidlyinositol (3,4,5)P3. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
226064 AbfA 2.60e-20 208 429 37 223
Alpha-L-arabinofuranosidase [Carbohydrate transport and metabolism].

CAZyme Hits      help

Created with Snap8216424732941249457665974182490698810711153123613181400148315651677UQC86406.1|GH514675QDO67168.1|GH511684UPK90404.1|GH513676UJO24967.1|GH514681QRD05473.1|GH51
Hit ID E-Value Query Start Query End Hit Start Hit End
UQC86406.1|GH51 4.42e-313 1 677 2 650
QDO67168.1|GH51 1.89e-309 4 675 5 647
UPK90404.1|GH51 1.59e-301 1 684 2 662
UJO24967.1|GH51 5.82e-299 3 676 4 673
QRD05473.1|GH51 8.37e-297 4 681 5 663

PDB Hits      download full data without filtering help

Created with Snap821642473294124945766597418249069881071115312361318140014831565365586ZPS_AAA2204194ATW_A2204193S2C_A2204193UG3_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
6ZPS_AAA 4.26e-94 36 558 18 531
Chain AAA, MgGH51 [Meripilus giganteus],6ZPV_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPW_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPX_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPY_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPZ_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZQ0_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZQ1_AAA Chain AAA, MgGH51 [Meripilus giganteus]
4ATW_A 5.73e-09 220 419 48 211
The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_B The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_C The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_D The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_E The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8],4ATW_F The crystal structure of Arabinofuranosidase [Thermotoga maritima MSB8]
3S2C_A 5.76e-09 220 419 48 211
Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_B Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_C Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_D Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_E Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_F Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_G Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_H Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_I Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_J Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_K Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3S2C_L Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1]
3UG3_A 6.00e-09 220 419 68 231
Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_B Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_C Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_D Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_E Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG3_F Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form [Thermotoga maritima],3UG4_A Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_B Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_C Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_D Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_E Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG4_F Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima arabinose complex [Thermotoga maritima],3UG5_A Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_B Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_C Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_D Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_E Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima],3UG5_F Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima xylose complex [Thermotoga maritima]

Swiss-Prot Hits      download full data without filtering help

Created with Snap82164247329412494576659741824906988107111531236131814001483156512673sp|U6A629|ABFA_PENCN19671sp|Q0CTV2|ABFA_ASPTN6671sp|A2Q7E0|ABFA_ASPNC6671sp|P42254|ABFA_ASPNG19671sp|Q8NK90|ABFA_ASPKW
Hit ID E-Value Query Start Query End Hit Start Hit End Description
sp|U6A629|ABFA_PENCN 1.26e-174 12 673 11 630
Alpha-L-arabinofuranosidase A OS=Penicillium canescens OX=5083 GN=abfA PE=1 SV=1
sp|Q0CTV2|ABFA_ASPTN 1.28e-106 19 671 26 625
Probable alpha-L-arabinofuranosidase A OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=abfA PE=3 SV=1
sp|A2Q7E0|ABFA_ASPNC 1.22e-100 6 671 13 625
Probable alpha-L-arabinofuranosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=abfA PE=3 SV=1
sp|P42254|ABFA_ASPNG 2.27e-100 6 671 13 625
Alpha-L-arabinofuranosidase A OS=Aspergillus niger OX=5061 GN=abfA PE=1 SV=1
sp|Q8NK90|ABFA_ASPKW 7.87e-100 19 671 26 625
Alpha-L-arabinofuranosidase A OS=Aspergillus kawachii (strain NBRC 4308) OX=1033177 GN=abfA PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000250 0.999711 CS pos: 18-19. Pr: 0.9654

TMHMM  Annotations      help

There is no transmembrane helices in OTA35730.1.