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CAZyme Information: PV06_03534-t43_1-p1

You are here: Home > Sequence: PV06_03534-t43_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 Exophiala oligosperma
Lineage Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala oligosperma
CAZyme ID PV06_03534-t43_1-p1
CAZy Family GH106
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
713 78181.13 5.2686
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_EoligospermaCBS72588 11938 N/A 45 11893
Gene Location Start: 2096658; End:2100487  Strand: -

Full Sequence      Download help

MTVYGGHSSR  TTLVSLLLVV  MMMMATLSQK  FSRCQVDASP  SMVITTTDPG  TSSSNVAAAA60
AATQQQQQRD  GGIPLNVSDD  ASIRHAASVA  AYSLQSFYNG  NRTGGTLGKF  PYPPYYWWLS120
GAAWDGMLHY  WLFTGDESYN  NITWMALVSQ  ISPTNNYLPV  AEMFDEGNDD  IAFWAFAAMF180
AAEHSFPDPP  SPRYPSWLRI  CENVFDDFVT  RWEKSSDTCG  GGLRWQVFSS  SAGWDYKNSI240
SNGGFFQLAA  RLARYTGNGT  YLTWAEKVWD  WSERIGLVEA  TDLNVYDGAG  IDSGLNCTKL300
DHTQWSYNIA  VYLYGAAVMH  NITVPAGTGV  RQRRGVWTNR  TEGLLGVAER  MFFGADDGGS360
DGLKNASGVM  VEQACELDWS  CDVDQFSFKA  YLARWMADTT  VLVPHLKGRV  GGLLKSSAKV420
AVKACTNVDA  GDARFKCGAH  WYMGKWDGSI  GVGQSLSVLE  VVQSLLVNDT  KAPENVQFIK480
CDATSWDDQV  VLFKLAVIVS  PSKSCDVVVA  NAGITGPDEI  FTLEDPSTEP  TKPELRILNL540
NLVGAMYTFK  LGQHYLRARP  ESEDGRDRCF  IFKGSVAGLL  DQPGSFQYSA  SKFGLRGLMR600
SARWTSWQEG  IRVNYIAPWY  TKTTILKPQV  IEILASKGIE  FSETADCTTA  VLRIACDKSI660
NGHSFAILPR  SVAEHGYVDA  QLDDDQGEPW  NSLQKAALAA  SIRTMAASTQ  TAQ713

Enzyme Prediction      help

EC 3.2.1.101:2

CAZyme Signature Domains help

Created with Snap357110614217821324928532035639242746349953457060664167713348GH76
Family Start End Evalue family coverage
GH76 82 471 5.3e-83 0.9357541899441341

CDD Domains      download full data without filtering help

Created with Snap357110614217821324928532035639242746349953457060664167782459Glyco_hydro_76475675ADH_SDR_c_like466667SDR_c478628adh_short471627FabG
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
397638 Glyco_hydro_76 2.42e-134 82 459 1 348
Glycosyl hydrolase family 76. Family of alpha-1,6-mannanases.
187584 ADH_SDR_c_like 9.68e-32 475 675 50 243
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs. This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
212491 SDR_c 1.49e-19 466 667 38 233
classical (c) SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
395056 adh_short 6.92e-17 478 628 53 189
short chain dehydrogenase. This family contains a wide variety of dehydrogenases.
223959 FabG 4.49e-16 471 627 54 195
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism, General function prediction only].

CAZyme Hits      help

Created with Snap357110614217821324928532035639242746349953457060664167773474UJO17342.1|GH7673518USW51892.1|GH7672476SMQ49163.1|GH7672476SMR48979.1|GH7672476SMY22864.1|GH76
Hit ID E-Value Query Start Query End Hit Start Hit End
UJO17342.1|GH76 1.35e-118 73 474 22 402
USW51892.1|GH76 2.19e-117 73 518 20 444
SMQ49163.1|GH76 8.24e-116 72 476 18 400
SMR48979.1|GH76 8.24e-116 72 476 18 400
SMY22864.1|GH76 8.24e-116 72 476 18 400

PDB Hits      download full data without filtering help

Created with Snap3571106142178213249285320356392427463499534570606641677834736RY0_A4756396ZYZ_A5066353PGX_A5016675MLN_A5066674URE_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
6RY0_A 5.57e-85 83 473 36 410
Chain A, Mannan endo-1,6-alpha-mannosidase [Thermochaetoides thermophila DSM 1495],6RY1_A Chain A, Mannan endo-1,6-alpha-mannosidase [Thermochaetoides thermophila DSM 1495],6RY2_A Chain A, Mannan endo-1,6-alpha-mannosidase [Thermochaetoides thermophila DSM 1495],6RY5_A Chain A, Mannan endo-1,6-alpha-mannosidase [Thermochaetoides thermophila DSM 1495],6RY6_A Chain A, Mannan endo-1,6-alpha-mannosidase [Thermochaetoides thermophila DSM 1495],6RY7_A Chain A, Mannan endo-1,6-alpha-mannosidase [Thermochaetoides thermophila DSM 1495]
6ZYZ_A 7.52e-11 475 639 80 231
Chain A, Borneol dehydrogenase from salvia rosmarinus [Salvia rosmarinus],6ZYZ_B Chain B, Borneol dehydrogenase from salvia rosmarinus [Salvia rosmarinus],6ZYZ_C Chain C, Borneol dehydrogenase from salvia rosmarinus [Salvia rosmarinus],6ZYZ_D Chain D, Borneol dehydrogenase from salvia rosmarinus [Salvia rosmarinus],6ZZ0_A Chain A, Borneol Dehydrogenase (salvia rosmarinus) apo structure [Salvia rosmarinus],6ZZ0_B Chain B, Borneol Dehydrogenase (salvia rosmarinus) apo structure [Salvia rosmarinus],6ZZ0_C Chain C, Borneol Dehydrogenase (salvia rosmarinus) apo structure [Salvia rosmarinus],6ZZ0_D Chain D, Borneol Dehydrogenase (salvia rosmarinus) apo structure [Salvia rosmarinus],6ZZT_A Chain A, BORNEOL DEHYDROGENASE [Salvia rosmarinus],6ZZT_B Chain B, BORNEOL DEHYDROGENASE [Salvia rosmarinus],6ZZT_C Chain C, BORNEOL DEHYDROGENASE [Salvia rosmarinus],6ZZT_D Chain D, BORNEOL DEHYDROGENASE [Salvia rosmarinus],7O6Q_A Chain A, borneol dehydrogenase [Salvia rosmarinus],7O6Q_B Chain B, borneol dehydrogenase [Salvia rosmarinus],7O6Q_C Chain C, borneol dehydrogenase [Salvia rosmarinus],7O6Q_D Chain D, borneol dehydrogenase [Salvia rosmarinus]
3PGX_A 5.67e-08 506 635 107 226
Crystal structure of a putative carveol dehydrogenase from Mycobacterium paratuberculosis bound to nicotinamide adenine dinucleotide [Mycobacterium avium subsp. paratuberculosis],3PGX_B Crystal structure of a putative carveol dehydrogenase from Mycobacterium paratuberculosis bound to nicotinamide adenine dinucleotide [Mycobacterium avium subsp. paratuberculosis],3PGX_C Crystal structure of a putative carveol dehydrogenase from Mycobacterium paratuberculosis bound to nicotinamide adenine dinucleotide [Mycobacterium avium subsp. paratuberculosis],3PGX_D Crystal structure of a putative carveol dehydrogenase from Mycobacterium paratuberculosis bound to nicotinamide adenine dinucleotide [Mycobacterium avium subsp. paratuberculosis]
5MLN_A 6.98e-08 501 667 79 235
The crystal structure of alcohol dehydrogenase 10 from Candida magnoliae [Starmerella magnoliae],5MLN_B The crystal structure of alcohol dehydrogenase 10 from Candida magnoliae [Starmerella magnoliae]
4URE_A 7.53e-08 506 667 84 241
Molecular Genetic and Crystal Structural Analysis of 1-(4- Hydroxyphenyl)-Ethanol Dehydrogenase from Aromatoleum aromaticum EbN1 [Aromatoleum aromaticum EbN1],4URE_B Molecular Genetic and Crystal Structural Analysis of 1-(4- Hydroxyphenyl)-Ethanol Dehydrogenase from Aromatoleum aromaticum EbN1 [Aromatoleum aromaticum EbN1],4URF_A Molecular Genetic and Crystal Structural Analysis of 1-(4- Hydroxyphenyl)-Ethanol Dehydrogenase from Aromatoleum aromaticum EbN1 [Aromatoleum aromaticum EbN1],4URF_B Molecular Genetic and Crystal Structural Analysis of 1-(4- Hydroxyphenyl)-Ethanol Dehydrogenase from Aromatoleum aromaticum EbN1 [Aromatoleum aromaticum EbN1]

Swiss-Prot Hits      download full data without filtering help

Created with Snap357110614217821324928532035639242746349953457060664167773473sp|P36091|DCW1_YEAST72462sp|Q6FLP9|DCW1_CANGA73467sp|O74556|YCZ2_SCHPO75473sp|Q75DG6|DCW1_ASHGO75473sp|Q5AD78|DCW1_CANAL
Hit ID E-Value Query Start Query End Hit Start Hit End Description
sp|P36091|DCW1_YEAST 1.31e-98 73 473 22 392
Mannan endo-1,6-alpha-mannosidase DCW1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=DCW1 PE=1 SV=1
sp|Q6FLP9|DCW1_CANGA 7.07e-97 72 462 18 378
Mannan endo-1,6-alpha-mannosidase DCW1 OS=Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) OX=284593 GN=DCW1 PE=3 SV=1
sp|O74556|YCZ2_SCHPO 1.27e-91 73 467 20 385
Putative mannan endo-1,6-alpha-mannosidase C970.02 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPCC970.02 PE=3 SV=1
sp|Q75DG6|DCW1_ASHGO 1.45e-88 75 473 24 394
Mannan endo-1,6-alpha-mannosidase DCW1 OS=Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) OX=284811 GN=DCW1 PE=3 SV=2
sp|Q5AD78|DCW1_CANAL 6.12e-87 75 473 21 395
Mannan endo-1,6-alpha-mannosidase DCW1 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=DCW1 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.020302 0.979660 CS pos: 28-29. Pr: 0.9409

TMHMM  Annotations      help

There is no transmembrane helices in PV06_03534-t43_1-p1.