CAZyme Information: MGYG000002334_00431

Basic Information

• Species: Bifidobacterium thermophilum
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium thermophilum
• CAZyme ID: MGYG000002334_00431
• CAZy Family: CBM26
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1209		130850.63	4.3039

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002334	2291643	Isolate	not provided	not provided

• Gene Location: Start: 560153; End: 563782 Strand: +

Full Sequence      

MRGSRLSCVLCALLSMFMVMPASVASAATDGSGGSGEVTIHYYDSAGWAKPFAYMYGDGV
RSASWPGERMTDDGDGWYSVTVDAPHGLRVLFSDNGKSQHPGANQPGYEVNGEAWFVGST
RHDSMPEGMKVHFYDYANWGKVRLYYYSEAARGPTWPGEAMHADGDGWYTATIFGTQPAR
VLFNDGGSRQTPASGQEGHLVTAEAWCRNGVWTDTRPDGVLVMFHKPSGWGSPRIYYYTS
DADTGPAWPGNAMKHMADGWYSYTITKYAKARVLFNDGGHQVPAKSAPGYEASGVCRWDG
GDWSCGDPAIDGDDDGVPDVLGMMLGGDSDTDGDGLPDAFETIRTGTDPSRADSDGDGVA
DGDEDPDGDGLTNLNEREIGTDPMAADTDGDGLTDGEETTRTHTDPLKSDTDGDGVDDRR
EIQWGTDPLVPQETFDVTAPAEDVGQGDVDVSVSVNLPASQAATLDVRRYDNPSYFPDDM
PGLIGDAYEFTVDGQVGSATLRFRFDESLLSDSSFDPAICWFDEKEQRLEELDTTVTGNE
ATATVSHFSKYVLVNRTTFHDSFSWEDVWGDEQFNAVQTVFVIDDSGSMWSNDRGKKRLS
VARDLVGRFPGNTRTGVVRFADGATDLTGGLTDAQTAKNALADANFHDSGGTSMYLAVRQ
ALNMFQGDDDATLRNIIVLSDGETADTRLHDSVVAEANKRKVKINAVGLGGGGPGSYFER
WMKPLASQTGGESYLAQDADALAGIYENIGKLIDIETDSDGDGIPDWYEDHLVLFNGVSL
KLDKNNPDTDGDGIPDGEEIDRLDYRYNADRTKVIVTGRLITNPTLVDSYGDGIADADEP
DPTTDPMNPDTDGDGLTDGDEVRRNFDPTSPDPDGDGRRDDRELADDTSPYVYDKAWYEQ
FACFVVGALAGDFITDDDDPVTLAGQIIGGVIPTSDVRDAIANVKHGDYAFAAISAAGIV
PAAGDAAKGAAKAGRFILRNIDDPAKAARLLAILEESCPSVVAKLGGSDGFVKAAASFSQ
TGHARLTKKEKQHLVKAVNKAGLAKHLVTSGRDLPIAATIDTGKNVWNERWLKRGDIIDE
HLNGHSTGRGLGRTFPVADRLENRVLVSTKSLDLDARSYQTPGRLRSRLNKYVKDLEGFE
DKYFNKVDGNGNKYMYWGKEKFTANKYDSKMLEVVFPDTAIGNDIAEALRAFQREHAGTG
MQIVYKIAK

Enzyme Prediction     

No EC number prediction in MGYG000002334_00431.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM26	222	285	1.6e-19	0.8933333333333333
CBM26	130	193	1.3e-18	0.8933333333333333
CBM26	39	108	1.5e-18	0.9333333333333333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam16738	CBM26	2.05e-19	222	279	1	60	Starch-binding module 26. CBM26 is a carbohydrate-binding module that binds starch.
pfam16738	CBM26	6.12e-19	131	195	1	68	Starch-binding module 26. CBM26 is a carbohydrate-binding module that binds starch.
pfam16738	CBM26	5.81e-18	40	104	1	68	Starch-binding module 26. CBM26 is a carbohydrate-binding module that binds starch.
cd13444	CDI_toxin_EC869_like	1.66e-17	1058	1207	3	139	Zn-dependent DNAse of the contact-dependent growth inhibition (CDI) system of Escherichia coli EC869, and related proteins. CDI toxins are expressed by gram-negative bacteria as part of a mechanism to inhibit the growth of neighboring bacteria. This model represents the C-terminal toxin domain of CdiA effector proteins. CdiA secretion is dependent on the outer membrane protein CdiB. Upon binding to a receptor on the surface of target bacteria, the CDI toxin is delivered. A wide variety of C-terminal toxin domains appear to exist; this particular example from Escherichia coli EC869 and other bacteria appears to function as a Zn2+-dependent DNAse degrading the genome of target cells.
cd00198	vWFA	3.21e-15	580	734	4	160	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AGH40717.1	0.0	1	1209	1	1209
CBK93270.1	3.22e-218	307	1209	338	1237
QEH68420.1	8.64e-60	37	308	886	1161
QUL54870.1	3.12e-55	307	837	376	903
CDZ23468.1	4.19e-49	330	803	369	844

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2C3G_A	7.49e-11	125	217	3	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P30269	1.40e-06	33	166	815	973	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 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
0.000230	0.999069	0.000197	0.000180	0.000161	0.000144

TMHMM  Annotations     

start	end
7	29