CAZyme Information: MGYG000002570_01412

Basic Information

• Species: Ruminococcus_E sp003526955
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Ruminococcus_E; Ruminococcus_E sp003526955
• CAZyme ID: MGYG000002570_01412
• CAZy Family: CBM26
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1063		119772.47	4.0474

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002570	2026568	MAG	China	Asia

• Gene Location: Start: 6601; End: 9792 Strand: -

Full Sequence      

MRNKKIIALVLILTTILSIFSLPASAAEKIEDQITVYYYNENNWKSPYIYYYCDNLAPVT
WPGKQMNDFGDGWYSYTINNLKTAKVIFSDNGANQNPAQNQEGYSVSGEKWYLNGSWYDS
EPNGITVHFNNYNDWDNVNIYYYSGNKTGTSWTGNPMIPDGDGWYTYKIYGFDEAKVLFN
NGKGIQIPGQNQEGFAVSGEMWYRNGEWTAERPDDVTVYFYKPDNWSAPNIYYYKDINDT
GKAWPGNAMSFVRDNWYSYTITKYSSAKVLFNSGSNQIPPQNQPGFDVKGIVWYKDGVMC
NAETDADNDGLPDYMEMVLGTNLNNKDTDSDGLLDGYEVLTLGTDPLKADTDGNGVKDSD
EDADGDKLTNLEEYKLDTSPINPDTDGDGLNDYEEVYTYHTDPLNADTDGDTLSDGDDVA
LGFSPLLKDTDSNGILDCDEKIKQEITQEIKNEEAPQISEVQVSFEGTGNISNTTTIENI
YGKDILSSEVVGLIGAPVEITTTSEFENATITFKYDKSRLGDTKEEDLAVMWYDEENGVY
QILDNETVLDKEKQTVSYKTTHFSKYMVVDKNIWYNTWRTNIDYRVGTTTKLYYDFAFVV
DTSGSMEGQRIEYAKQSMNNFVDCLTDNDNACLVSFESNAYLKARLGATKGTLHTAINSL
NAYGGTYVSSGLNMALNQLIASTSGNQKAIVLICDGDVDSVQSYVNIAKANNIKIFAINV
ISADNDILQSMADETGGEYYYAYTAEELLTAFSHISSESLFNFDLTDTDGDGLPDTFEKN
GMRLANGKIVYTAPNKPDTDGDGLTDGEEMGILRRSGVLIFPSLELPFKPLFNNNMYIGK
GAYSSSALYFNNKSDPSNGDSDGDNLYDNEDPYPFEFNTFKKYDRDAVIEYCDKYAKNPN
TDVYNYFQRGDCANFASQCVHAGGIEMDEDWYFKEKGFGFFGLFYVGDDFSLEWSVAYNN
YLYFKNNIGLTNGEEIVFNSKEEMQEALKSKKYNIQPGDLMYMQWDEEEPHHATVIYSVN
SNTLNYSAHTDAHRDADVNDLFWKNYPDGKLYILHIKDTVITS

Enzyme Prediction     

No EC number prediction in MGYG000002570_01412.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM26	35	104	1.7e-19	0.9333333333333333
CBM26	217	289	6e-19	0.9733333333333334
CBM26	126	196	2.2e-17	0.9466666666666667

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00198	vWFA	2.54e-22	594	741	1	161	Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.
smart00327	VWA	2.82e-22	595	753	1	175	von Willebrand factor (vWF) type A domain. VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.
pfam00092	VWA	2.43e-21	595	752	1	171	von Willebrand factor type A domain.
pfam16738	CBM26	1.01e-19	36	100	1	68	Starch-binding module 26. CBM26 is a carbohydrate-binding module that binds starch.
cd01465	vWA_subgroup	1.90e-18	596	752	3	170	VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Not much is known about the function of the VWA domain in these proteins. The members do have a conserved MIDAS motif. The biochemical function however is not known.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AGH40717.1	1.61e-121	33	810	37	800
QEH68420.1	2.69e-65	34	303	887	1160
ADZ82879.1	8.21e-58	34	303	699	1067
QUL54870.1	6.66e-42	286	779	365	837
ADZ21303.1	1.50e-41	29	308	560	832

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2C3G_A	4.25e-10	34	122	7	97	ChainA, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans C-125],2C3H_A Chain A, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_B Chain B, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_C Chain C, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_D Chain D, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_E Chain E, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_F Chain F, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_G Chain G, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans],2C3H_H Chain H, ALPHA-AMYLASE G-6 [Halalkalibacterium halodurans]
7MIX_D	1.00e-07	595	740	253	411	ChainD, Voltage-dependent calcium channel subunit alpha-2/delta-1 [Homo sapiens],7MIY_D Chain D, Voltage-dependent calcium channel subunit alpha-2/delta-1 [Homo sapiens],7UHF_D Chain D, Voltage-dependent calcium channel subunit alpha-2/delta-1 [Homo sapiens],7UHG_D Chain D, Voltage-dependent calcium channel subunit alpha-2/delta-1 [Homo sapiens],7VFS_B Chain B, Voltage-dependent calcium channel subunit alpha-2/delta-1 [Homo sapiens],7VFU_B Chain B, Voltage-dependent calcium channel subunit alpha-2/delta-1 [Homo sapiens],7VFV_B Chain B, Voltage-dependent calcium channel subunit alpha-2/delta-1 [Homo sapiens],7VFW_B Chain B, Voltage-dependent calcium channel subunit alpha-2/delta-1 [Homo sapiens]
6JP8_F	1.29e-07	595	740	227	385	ChainF, Voltage-dependent calcium channel subunit alpha-2/delta-1 [Oryctolagus cuniculus],6JPA_F Chain F, Voltage-dependent calcium channel subunit alpha-2/delta-1 [Oryctolagus cuniculus],6JPB_F Chain F, Voltage-dependent calcium channel subunit alpha-2/delta-1 [Oryctolagus cuniculus]
6JP5_F	1.30e-07	595	740	255	413	ChainF, Voltage-dependent calcium channel subunit alpha-2/delta-1 [Oryctolagus cuniculus]
3JBR_F	1.31e-07	595	740	255	413	Cryo-EMstructure of the rabbit voltage-gated calcium channel Cav1.1 complex at 4.2 angstrom [Oryctolagus cuniculus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P30269	5.21e-09	36	255	708	974	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
P00691	1.28e-08	217	287	564	641	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P54289	5.48e-07	595	740	253	411	Voltage-dependent calcium channel subunit alpha-2/delta-1 OS=Homo sapiens OX=9606 GN=CACNA2D1 PE=1 SV=3
O08532	7.19e-07	595	740	253	411	Voltage-dependent calcium channel subunit alpha-2/delta-1 OS=Mus musculus OX=10090 GN=Cacna2d1 PE=1 SV=1
P13806	7.19e-07	595	740	255	413	Voltage-dependent calcium channel subunit alpha-2/delta-1 OS=Oryctolagus cuniculus OX=9986 GN=CACNA2D1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000248	0.999109	0.000174	0.000156	0.000137	0.000128

TMHMM  Annotations     

start	end
7	26