CAZyme Information: evm.model.AC2VRR_s00012g53-p1

Basic Information

• Species: Albugo candida
• Lineage: Oomycota; NA; ; Albuginaceae; Albugo; Albugo candida
• CAZyme ID: evm.model.AC2VRR_s00012g53-p1
• CAZy Family: AA2
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
536		58508.13	9.6324

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Acandida2VRR	15896	911350	72	15824

• Gene Location: location=Acan2VRR_SC012:111769-113566(-)

Full Sequence      

MASTAAGRSSVSAARTSEVERIIATADVAADYPGKAVKYRGRRSTWPGALGLLLFFAGSI
AGLTYFGIQKRNQVRYGTASDAAILDMYGSGTRIPDGRMPQPDPDVVVLNPAEYQDLTCE
QPNYITKKNRIVAQFKSGREVIMNIKGVNWLGMQDNKYVPKGLWDGKKDGNTLTRYAIFL
SENGFNAVRLALSVDAALRNVVPDETLINTKSNRALKTSRYIPLLSSIIQGLGVYHIAVV
LNFQVLSALVKESGLWEGSSIKLADTQKAISNLANELCNSKHYNIIGIDLKDNVAMATWG
DKSESDWAQAATTLGNHVIRECPRWLVFVQGIEGPSRRNSFVAEDGSEKIVRLKYFTGSD
LSGVATAPIVLKKKGKLVYSPKYFTSSYQLLDFFFSGGTPKGGLLMDYVESTNATLKKNV
DLSMEYMFGSALASDSAVVLSSFGGLVGSLDRTELKTSTRIIEILISKMQNRTGGLAGGF
WWQLNPDAVYPYRAPDLANGTKAGLLLESWKVANMPVLRELEKMAAVPNVNFVPCV

Enzyme Prediction     

No EC number prediction in evm.model.AC2VRR_s00012g53-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	140	488	4.3e-137	0.997093023255814

CDD Domains     

evm.model.AC2VRR_s00012g53-p1 has no CDD domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCA23923.1|GH5_20	0.0	1	536	1	536
UIZ25210.1|GH5_20	1.31e-183	7	535	11	540
CCA19804.1|GH5_20	1.17e-94	34	535	25	520
CCD28218.1|GH5_20	7.22e-93	258	535	3	278
ABC87090.1|GH5_20	9.03e-93	6	535	103	627

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VVG_A	1.17e-16	137	510	22	361	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	1.56e-16	137	510	22	361	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	1.97e-16	137	510	55	394	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]
3QHO_A	1.97e-16	137	510	55	394	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]
3QHM_A	3.49e-16	137	510	55	394	Crystal analysis of the complex structure, E342A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHM_B Crystal analysis of the complex structure, E342A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHM_C Crystal analysis of the complex structure, E342A-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|P23548|GUN_PAEPO	4.94e-18	124	516	39	373	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
sp|P19487|GUNA_XANCP	1.47e-14	142	521	41	368	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|P50400|GUND_CELFI	3.39e-08	137	511	57	399	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
0.999893	0.000128

TMHMM  Annotations     

Start	End
46	68