CAZyme Information: SDRG_12428-t26_1-p1

Basic Information

• Species: Saprolegnia diclina
• Lineage: Oomycota; NA; ; Saprolegniaceae; Saprolegnia; Saprolegnia diclina
• CAZyme ID: SDRG_12428-t26_1-p1
• CAZy Family: GH72
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
555		61025.45	5.8556

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SdiclinaVS20	17448	1156394	89	17359

• Gene Location: location=JH767180:325136-327217(+)

Full Sequence      

MRRESSIRTPTEGDYAQPTYLDDKPDVTVYRESDMTARESIMDELPAIRLTHNESARSFK
GRYRVWPGVLLLLGLTAVAAVLMVYFADQQRTSMLDIRLAVQMREYKMRQIDTGLTSGSG
AGLPPLVDTDGTVNNPQVYPPQTCKLPNYVSKNNKIYAVAPNGTEVPLGIKGLNWFGMET
GQAIPFGLWTNDKNGTTAFQVAEFLVTNKINSIRLPVCIQSIVNNIQPNKNLINSAENRA
LDVSSYMALLKSIISTLAYRRISVLISLHTLTPTDSGGAWFSDAVPVEMFMTAVDLLTTN
LCNDKYWNIIGLDVKNEPHLSTWGDDGPKDFRNGATDISHRMLKGCPNWLAFVEGIVNMG
QPVSFNGVAMTYNDWWGGGLQAAGAKPVVLNTAHKVVYAPHYYTPAVYPQAYLYGGGTSG
PGGIITNYVELSDADLRLRVSGTMEVMFGHLAKTHDAAIVLGEFGGLYASDAHPQRTTKR
CTDYTIEAMLQPGYSGGYVWSLNPESAYQFNPADVAGTFTEGVVQIDWRTANLPFVQGMQ
AMDALADLRLFPCFS

Enzyme Prediction     

No EC number prediction in SDRG_12428-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	165	506	1.5e-145	0.997093023255814

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225344	BglC	9.41e-12	153	480	32	337	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
395098	Cellulase	6.85e-11	187	506	17	272	Cellulase (glycosyl hydrolase family 5).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABG80555.1|GH5_20	8.38e-195	59	555	143	634
ABG80554.1|GH5_20	8.38e-195	59	555	143	634
ABC87090.1|GH5_20	7.50e-192	57	555	136	629
ABK59037.1|GH5_20	7.50e-192	57	555	136	629
ABL75349.1|GH5_20	3.22e-191	54	555	133	629

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VVG_A	7.37e-38	149	530	8	363	The Crystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3VVG_B The Crystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3VVG_C The Crystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3W6L_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6L_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6L_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3]
3W6M_A	1.01e-37	149	530	8	363	Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6M_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6M_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3]
2ZUM_A	3.17e-37	149	530	41	396	Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],2ZUN_A Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],2ZUN_B Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],2ZUN_C Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3]
3AXX_A	3.17e-37	149	530	41	396	Functional analysis of hyperthermophilic endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],3AXX_B Functional analysis of hyperthermophilic endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],3AXX_C Functional analysis of hyperthermophilic endocellulase from the Archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3]
3QHO_A	1.12e-36	149	530	41	396	Crystal analysis of the complex structure, Y299F-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHO_B Crystal analysis of the complex structure, Y299F-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHO_C Crystal analysis of the complex structure, Y299F-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P19487|GUNA_XANCP	1.21e-29	151	532	27	358	Major extracellular endoglucanase OS=Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) OX=190485 GN=engXCA PE=1 SV=2
sp|P54583|GUN1_ACIC1	4.79e-28	162	532	56	381	Endoglucanase E1 OS=Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) OX=351607 GN=Acel_0614 PE=1 SV=1
sp|P23548|GUN_PAEPO	6.89e-26	149	534	39	373	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
sp|P10474|GUNB_CALSA	3.95e-24	167	506	644	971	Endoglucanase/exoglucanase B OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=celB PE=3 SV=1
sp|P50400|GUND_CELFI	7.07e-24	170	530	63	400	Endoglucanase D OS=Cellulomonas fimi OX=1708 GN=cenD PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999606	0.000423

TMHMM  Annotations     

Start	End
65	87