CAZyme Information: HMPREF1544_07231-t46_1-p1

Basic Information

• Species: Mucor circinelloides
• Lineage: Mucoromycota; Mucoromycetes; ; Mucoraceae; Mucor; Mucor circinelloides
• CAZyme ID: HMPREF1544_07231-t46_1-p1
• CAZy Family: GT1
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
625		71146.57	7.2124

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Mcircinelloides1006PhL	12410	1220926	183	12227

• Gene Location: location=KE123999:69530-71941(+)

Full Sequence      

MLKDVVSYVKGLKKRHLMGVGLFFILFFVLFQINYLKNTEPAIVTEDLVSSQKRYLVIIG
TEARFATRRSVIRSAYFNIDDNLIPASDFDQVEYAFLVHGGPPTSNSPERRAFETEKMEY
NDIYTLPNDQTFTSGTAFHWINATTWSKPFDYVIIQDIHSFVHLDRLIHDLDSATTTMDQ
MGNNGKGMVVSWGKFQHLLNNPTAADVSTASHVAVWENSIESVDTNNLIITNVYQDQDFL
DLSALYQLQPILPKSKAKSIAVVTSSYIYDYCMEPSGTRASLNKRSYADKHGYAFVARSR
EFAQQAMRPDQRRTVWGKIDVIQKVLPKYDWVFWLDMDAVVMNSKQTIEGLLQRLEINDS
THFIIVRPGTDKMINAGVFLIRNSPWSFQFLQEIQNQSEWYRQGPSYEQGAMWDVMRREE
FIQHTKFLDRENHLFNTFPKFYQQDDFIVHFAPDKCPNSATLKGLAAADSIQKGHAVTMD
SQSYGANILYRSEPYDPYIPNNQRGTDGAGGAGNQKTARVQQQVDEVVGIMQENIDKVMQ
RGERLDDLRGKTEDLQATAGHFRRGANQVRKRMWWKDLKWKIIIAVTILVILGIIIGSIV
GTQTKNNSSSNQPAATQPAATSPSS

Enzyme Prediction     

No EC number prediction in HMPREF1544_07231-t46_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT34	279	452	1.3e-20	0.8495934959349594

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395764	Synaptobrevin	1.12e-29	513	586	1	74	Synaptobrevin.
277222	R-SNARE_VAMP4	1.37e-25	514	579	1	66	SNARE motif of VAMP4. The VAMP-4 (vesicle-associated membrane protein 4) protein belongs to the R-SNARE subgroup of SNAREs and interacts with syntaxin 16 (Qa), Vti1a (Qb) and syntaxin 6 (Qc). This complex plays a role in maintenance of Golgi ribbon structure and normal retrograde trafficking from the early endosome to the trans-Golgi network (TGN). SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins contain coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles.
277221	R-SNARE_VAMP8	1.73e-23	514	579	1	66	SNARE motif of VAMP8. The lysosomal VAMP8 (vesicle-associated membrane protein 8, also called endobrevin) protein belongs to the R-SNARE subgroup of SNAREs and interacts with STX17 (Qa) and SNAP29 (Qb/Qc). The complex plays a role in autophagosome-lysosome fusion via regulating the transport from early endosomes to multivesicular bodies. Autophagosome transports cytoplasmic materials including cytoplasmic proteins, glycogen, lipids, organelles, and invading bacteria to the lysosome for degradation. SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins contain coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles.
277196	R-SNARE	2.96e-23	516	574	2	60	SNARE motif, subgroup R-SNARE. SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). In contrast to Qa-, Qb- and Qc-SNAREs that are localized to target organelle membranes, R-SNAREs are localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Examples for members of the Qa SNAREs are syntaxin 18, syntaxin 5, syntaxin 16, and syntaxin 1.
277227	R-SNARE_Snc1	7.57e-23	516	574	2	60	SNARE motif of Snc1. Saccharomyces cerevisiae SNARE protein Snc1p forms a complex with synaptobrevin homolog Sso1p (Qa) and the SNAP-25 homolog Sec9p (Qb/c) which is involved in exocytosis. Snc1 is a member of the R-SNARE subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDS09137.1|GT34	2.02e-115	38	478	107	652
CDS05704.1|GT34	7.07e-108	66	478	155	690
CAG4711197.1|GT34	1.17e-15	251	395	2	146
ACO66271.1|GT34	2.24e-15	202	486	132	419
CAG1843115.1|GT34	4.35e-15	277	452	105	300

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2NPS_A	2.46e-15	508	581	1	74	Crystal Structure of the Early Endosomal SNARE Complex [Mus musculus]
7BV6_A	1.65e-13	513	579	2	68	Crystal structure of the autophagic STX17/SNAP29/VAMP8 SNARE complex [Homo sapiens],7BV6_E Crystal structure of the autophagic STX17/SNAP29/VAMP8 SNARE complex [Homo sapiens],7BV6_I Crystal structure of the autophagic STX17/SNAP29/VAMP8 SNARE complex [Homo sapiens],7BV6_M Crystal structure of the autophagic STX17/SNAP29/VAMP8 SNARE complex [Homo sapiens],7BV6_Q Crystal structure of the autophagic STX17/SNAP29/VAMP8 SNARE complex [Homo sapiens],7BV6_U Crystal structure of the autophagic STX17/SNAP29/VAMP8 SNARE complex [Homo sapiens]
3B5N_A	8.97e-13	516	574	3	61	Structure of the yeast plasma membrane SNARE complex [Saccharomyces cerevisiae],3B5N_E Structure of the yeast plasma membrane SNARE complex [Saccharomyces cerevisiae],3B5N_I Structure of the yeast plasma membrane SNARE complex [Saccharomyces cerevisiae]
4WY4_A	2.21e-11	516	578	2	64	Crystal structure of autophagic SNARE complex [Homo sapiens]
1SFC_A	5.17e-11	514	579	29	94	Neuronal Synaptic Fusion Complex [Rattus norvegicus],1SFC_E Neuronal Synaptic Fusion Complex [Rattus norvegicus],1SFC_I Neuronal Synaptic Fusion Complex [Rattus norvegicus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q92356|SYB1_SCHPO	9.99e-28	492	591	2	106	Synaptobrevin homolog 1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=syb1 PE=3 SV=1
sp|P33328|SNC2_YEAST	1.06e-21	492	588	4	99	Synaptobrevin homolog 2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=SNC2 PE=1 SV=2
sp|P31109|SNC1_YEAST	4.38e-17	492	585	4	97	Synaptobrevin homolog 1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=SNC1 PE=1 SV=1
sp|O75379|VAMP4_HUMAN	8.66e-15	511	590	47	126	Vesicle-associated membrane protein 4 OS=Homo sapiens OX=9606 GN=VAMP4 PE=1 SV=2
sp|Q9WUF4|VAMP8_RAT	1.01e-14	507	583	2	78	Vesicle-associated membrane protein 8 OS=Rattus norvegicus OX=10116 GN=Vamp8 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000027	0.000002

TMHMM  Annotations     

Start	End
17	36
582	601