CAZyme Information: SDRG_04821-t26_1-p1

Basic Information

• Species: Saprolegnia diclina
• Lineage: Oomycota; NA; ; Saprolegniaceae; Saprolegnia; Saprolegnia diclina
• CAZyme ID: SDRG_04821-t26_1-p1
• CAZy Family: GH16
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
489	JH767143|CGC3	52723.18	8.2677

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=JH767143:346071-347571(+)

Full Sequence      

MRPSIIFATALLGLTTAQQPTTSQTFRGTLLHSSYAPSHPTLVCRHTNYVAEGNKIFAVD
PANPSTKTELFIKGVTWSGMELPNQGVPMGLWGANLTQIDSGIKGTSLAAMMQLMTNASI
NVVRFPLTADAVVKDTPPKITYVHRENKEIALYPPGFEPRTSDFVARLIGAFQKYRIGIV
LDIHDLVDNFATDAYWYYPKPSTVEETLAYKAAVVLATNYCKATYWNVLGLDLKNAMTDV
TWAKSANDARSVSDWASAAQVIAAKVNALCPQWLVLTTGASSASGESFSVPSRANETFPF
WDGGNFQNATSRPLEGATNVVYAPHAHVHGMLPQAYLYAKAAGCGANLPSTPTKEDTTCS
VFLNGALVANTKRALSCQKSKYACASYVPMAVPELQANVAAMLQSALGGVVAEAKHPIVF
SGFSAVYEPTLQPQQSAAFDAMLQFIVQNTSGGFYANLNPDTEMYLEAPPAGKTIIGKTR
LRTKSFCTR

Enzyme Prediction     

No EC number prediction in SDRG_04821-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	68	341	5.6e-49	0.7296511627906976

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
341270	ACS	0.008	387	425	115	145	Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme). Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCA26601.1|GH5_20	1.08e-32	40	476	138	531
ABL75348.1|GH5_20	5.35e-32	44	461	145	519
CCA14407.1|GH5_20	4.59e-31	39	473	157	542
ABL75347.1|GH5_20	6.24e-31	44	461	144	518
UIZ24458.1|GH5_20	6.75e-27	44	461	141	515

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3QHN_A	1.08e-11	49	349	41	320	Crystal analysis of the complex structure, E201A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHN_B Crystal analysis of the complex structure, E201A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHN_C Crystal analysis of the complex structure, E201A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii]
3VVG_A	3.32e-11	49	349	8	287	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]
2ZUM_A	4.43e-11	49	349	41	320	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	4.43e-11	49	349	41	320	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]
3QHM_A	4.43e-11	49	349	41	320	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     

SDRG_04821-t26_1-p1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000253	0.999733	CS pos: 17-18. Pr: 0.9799

TMHMM  Annotations     

There is no transmembrane helices in SDRG_04821-t26_1-p1.