CAZyme Information: ALNC14_116380:RNA-p1

Basic Information

• Species: Albugo laibachii
• Lineage: Oomycota; NA; ; Albuginaceae; Albugo; Albugo laibachii
• CAZyme ID: ALNC14_116380:RNA-p1
• CAZy Family: GT2
• CAZyme Description: cell 5A endo1 putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
529		59231.09	6.4054

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=FR824347:9241-10830(-)

Full Sequence      

MSYVRPSERFTVMSSHLPQVTDKSEKFKGRIRTYPGLILFLLIVGVAAGLIVYGGVQARR
DRDEAAKRYNDFIFYKRKIRDGGVNEEGDLVSDDGQVGNPLKYPDMGCELPNYLSKGGKI
VAVSKNGTQVTIGIKGTNWFGMETSLRIPYGLWENSENGTSAYEIAAFLSRNNFNSVRLP
LSIANILSNKAPEKNLINMATNRAINLKTYISMIQSIIKVLGYRRISVLLSLHTLTPQAS
GGAWYSEKLGISEKDYFNAVDKLTSSLCSSKYWNIVGVDLKNEPYESSWGGEAPDWHRGA
TLIGNRVVSDCKNWLAFVEGINSQHTITLQGKTDTYYDWWGGGLQKAKQLPVELKVQNKV
VYAPHYYTTAVNPAWYFYGGGTFGPSGVYTDYIELDNATLYSNVADTMYDMFGYLVDETE
NAVLLGEFGGLYEKDAHPRKTTQRTIDATIQVMMKKGYCGGYMWSLNPESAYQFNPADTG
GKFTEGLLEDDWLTPNKVFIRALEAMDGLKDLKRFPCFHEEIDSISTED

Enzyme Prediction     

No EC number prediction in ALNC14_116380:RNA-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	130	470	5.6e-146	0.9941860465116279

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225344	BglC	3.96e-15	134	513	47	397	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
395098	Cellulase	5.36e-10	141	470	5	272	Cellulase (glycosyl hydrolase family 5).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCA15003.1|GH5_20	0.0	1	529	1	529
CCA25494.1|GH5_20	0.0	1	529	1	529
ABL75350.1|GH5_20	1.52e-235	22	524	77	579
ABC87086.1|GH5_20	2.26e-232	22	524	76	578
ABL75351.1|GH5_20	2.91e-230	22	524	75	577

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VVG_A	2.39e-44	113	494	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	2.39e-44	113	494	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	1.25e-43	113	494	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	1.25e-43	113	494	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	4.55e-43	113	494	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|P23548|GUN_PAEPO	5.47e-30	113	497	39	372	Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
sp|P54583|GUN1_ACIC1	1.89e-29	130	498	60	383	Endoglucanase E1 OS=Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) OX=351607 GN=Acel_0614 PE=1 SV=1
sp|Q05332|GUNG_ACET2	4.13e-14	116	494	48	431	Endoglucanase G OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celG PE=3 SV=1
sp|P04956|GUNB_ACET2	6.47e-12	275	484	196	415	Endoglucanase B OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celB PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999815	0.000201

TMHMM  Annotations     

Start	End
36	58