CAZyme Information: ALNC14_005500:RNA-p1

Basic Information

• Species: Albugo laibachii
• Lineage: Oomycota; NA; ; Albuginaceae; Albugo; Albugo laibachii
• CAZyme ID: ALNC14_005500:RNA-p1
• CAZy Family: AA17
• CAZyme Description: cell 5A endo1 putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
588		64394.96	6.7567

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AlaibachiiNc14	14629	890382	180	14449

• Gene Location: location=FR824048:296542-298535(+)

Full Sequence      

MEGSSAQHPHDQYGELQTPMYTYSRLNPDNVDSARSSEITGGLTSDRVRIGNDVAVRGSL
GDRGIEAYVPAEPISEKARDYKGRIRTWPGLLLLFLLLGASAIAVTYYAVQTRDSRDAQA
DRAAKYAFEEAQIEGGKGARGDELIADDGVIGNPKKYPPSTCYLPNYLSKNGKLYSVAPN
GTEVEFVIKGVTWYVLQARTGMESGQYILLGLWENLLNGTSAYQIASFLSNNNFNAVRIP
LMASAILRNSRPNANLINRQENRAVSIANYMSFLKSIITVLQFRKIGVVLSMQTLTPTDA
GGLWFNSQVTEENFLLAIDKLTASLCTYQYWNVIGIDLTNEPHKATWGDESPTDFNVGAR
KIAARMLDGCPNWIGLVQGITGRQTVEVQGKAVNFTDWYGGGLQGVKSTGMHFSVANKVV
YAPHFNSPAVYPQSIFYANGTWDEATGKLVGYVELNDASLQSRTSAMMDNMFGFLSSETG
PAILMGQFSGLYGLDAHPLKTSKRVLDQIISVVSQPGWAGGFVMALNPETSFQYNPADTV
GKFAEGVLSDDWLSANKPYLAALEKMDTMENLRKLPCFPRPSKLKGSK

Enzyme Prediction     

No EC number prediction in ALNC14_005500:RNA-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	183	530	1.5e-154	0.997093023255814

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225344	BglC	3.53e-10	171	567	32	391	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
395098	Cellulase	7.06e-04	211	450	17	225	Cellulase (glycosyl hydrolase family 5).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCA14407.1|GH5_20	0.0	1	588	1	588
CCA19804.1|GH5_20	2.40e-196	81	578	30	521
ABL75349.1|GH5_20	4.22e-190	54	587	113	637
ABC87091.1|GH5_20	2.21e-185	23	587	49	608
ABK59038.1|GH5_20	2.21e-185	23	587	49	608

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VVG_A	1.22e-26	180	552	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	1.66e-26	180	552	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	3.38e-26	180	552	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]
3AXX_A	3.38e-26	180	552	55	394	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	4.55e-26	180	552	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P23548|GUN_PAEPO	2.50e-23	177	558	47	373	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
sp|P54583|GUN1_ACIC1	9.60e-15	188	552	64	377	Endoglucanase E1 OS=Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) OX=351607 GN=Acel_0614 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000054	0.000001

TMHMM  Annotations     

Start	End
88	110