CAZyme Information: AMAG_18849-t26_1-p1

Basic Information

• Species: Allomyces macrogynus
• Lineage: Blastocladiomycota; Blastocladiomycetes; ; Blastocladiaceae; Allomyces; Allomyces macrogynus
• CAZyme ID: AMAG_18849-t26_1-p1
• CAZy Family: GT58
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1377		150526.50	9.4861

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AmacrogynusATCC38327	19333	578462	535	18798

Full Sequence      

MDPRPSVPPMPATPSRRPSALMTGPRAPSPMIASSHGSSLASLPSAGSGSSAASRASSTS
SIPSSGVRQPRFDPVTPTRSPSAGVPSAVRAPAYRGLPARSNSTSNSSLPGANGFLSPRA
PSRQGSISAPSGGVIPPPPMSPLAAPILGPILALDPAPMSPGTEPHHAHHGGHHHHHGGH
HRRHSTKETVQVTVRMRPLNEIETRTGTTVAWDVDSADARVRGALDAVGPGGKRVHLANA
PLPEYQYDHAFDGSANAPLYVASVRQLVHSAMEGYNGTVFAYGQTASGKTYTMMGTDREP
GVIPLAIHDVFQYIKMSEGQREFLLRVSYLEIYNETIRDLLSPETTDLRIHEDKRRGVYV
SPLKEDTVTHPSQVMRAIHRGEANRHISETDYNEHSSRSHTLFQMVIESRDARTNGQVKI
SLLNLIDLAGSEKAVSNADRRKEGAFINKSLLTLGTVISKLTEEKATHIPYRDSKLTRIL
QSSLSGNARVSVICTISPSSANVEESTNTLKFAARVKKVVTRAHTNTVLDDKALLQQYRK
EIMELKDKLQQTNEALARERHEELMQIKAEKEKALEELHQQQLLRTALKERIDHLTRLIL
TSGSISQVQVGPGAVAGNGASATSPLTATGPPNATPSMRIEALNNELVGKDVELTRLQSV
AHDLQETMKKYAPVVTALQKGDTSRAVQLAKALPSADGTLSAASWGFLNESGSVGYWWVR
ERWAGSRDEFTAMQRKQEDMPQWPEPLRSLYRLTNQHDYYLQPIVDREHDRATSEWHTAR
CVLLGDAAHPATPELFQGANLAVEDAAMLAGLIASCPPSTPPAKIFAEFAAKRLKHVTRI
QKMSYSQTKLSQLQSKPTVMLRNAALKLIPTRLLESRLRKTAAWDPNAASRSARRDPRPR
AAAHRPWAWPRHVLFIVVDGVVKGSANSKPTHEILLQDVLFHQLDPEEPATDCLYSSASE
TGIANNAARVFSGFYRRVPYVVVVKTGLVAERTSAKPGNRGKRDSQLIVYKFFHYVNYST
YGTQLFVKIDRHFRRLGLRATDAKYMLVADADTKIAPDGLSILVDRMENDPTLLGTCGET
CVENKFDSFVAAGQTFEYWLTHAVLKAFEGFYSNVLVLSGCFTIYRLKFDDGTAAIIDAR
LKDKLQQTNEALARERHEELMQIKAEKEKALEELHQQQLLRTALKERIDHLTRLILTSGS
ISQVQVGPGAVAGNGASATSPLTATGPPNATPSMRIEALNNELVGKDVELTRLQSVAHDL
QETMKKYAPVVTALQKGDTSRAVQLAKALPSADGTLSAALSRSTSASDLGGSLDSLDVNT
EIVHLKQKNRELEIVVADTEDRYAALAQDYDRAVAEHAVAQRGLQDEVRTLKATVAD

Enzyme Prediction     

EC	2.4.1.16:11

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	911	1133	2.6e-56	0.4459203036053131

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
276825	KISc_CENP_E	1.17e-157	189	519	1	321	Kinesin motor domain, CENP-E/KIP2-like subgroup. Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
395169	Kinesin	8.91e-140	195	519	1	326	Kinesin motor domain.
214526	KISc	9.07e-134	190	526	2	335	Kinesin motor, catalytic domain. ATPase. Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.
276812	KISc	4.80e-115	190	517	2	326	Kinesin motor domain. Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
276820	KISc_KHC_KIF5	4.75e-104	190	519	4	325	Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAB4088094.1|CBM0	CAB4088094.1|CBM0	9.50e-45	187	519	461	788
CAE6002787.1|CBM57	CAE6002787.1|CBM57	4.61e-44	186	519	1046	1371
BBN07176.1|CBM0	BBN07176.1|CBM0	5.66e-44	187	519	595	923
QHO44399.1|CBM0	QHO44399.1|CBM0	1.35e-43	187	539	397	746
VDD58389.1|CBM0	VDD58389.1|CBM0	1.40e-43	190	519	385	706

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1T5C_A	1T5C_A	4.32e-75	190	531	6	340	Crystal structure of the motor domain of human kinetochore protein CENP-E [Homo sapiens],1T5C_B Crystal structure of the motor domain of human kinetochore protein CENP-E [Homo sapiens]
6M4I_A	6M4I_A	5.84e-74	190	528	13	344	Chain A, Centromere-associated protein E [Homo sapiens],6M4I_B Chain B, Centromere-associated protein E [Homo sapiens]
2VVG_A	2VVG_A	7.82e-70	186	526	2	342	Chain A, KINESIN-2 [Giardia intestinalis],2VVG_B Chain B, KINESIN-2 [Giardia intestinalis]
4HNA_K	4HNA_K	6.59e-69	187	541	6	347	Kinesin motor domain in the ADP-MG-ALFX state in complex with tubulin and a DARPIN [Homo sapiens]
1GOJ_A	1GOJ_A	1.07e-68	185	540	3	351	Structure of a fast kinesin: Implications for ATPase mechanism and interactions with microtubules [Neurospora crassa]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q6S001|KIF11_DICDI	sp|Q6S001|KIF11_DICDI	2.92e-99	245	606	117	494	Kinesin-related protein 11 OS=Dictyostelium discoideum OX=44689 GN=kif11 PE=3 SV=1
sp|B9FFA3|KN7E_ORYSJ	sp|B9FFA3|KN7E_ORYSJ	6.29e-96	185	602	115	530	Kinesin-like protein KIN-7E, chloroplastic OS=Oryza sativa subsp. japonica OX=39947 GN=KIN7E PE=3 SV=2
sp|F4K3X8|KN7L_ARATH	sp|F4K3X8|KN7L_ARATH	1.51e-95	186	607	63	474	Kinesin-like protein KIN-7L, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=KIN7L PE=3 SV=2
sp|Q9SJU0|KN7M_ARATH	sp|Q9SJU0|KN7M_ARATH	1.74e-95	185	602	100	509	Kinesin-like protein KIN-7M, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=KIN7M PE=2 SV=2
sp|Q8W5R5|KN7D_ARATH	sp|Q8W5R5|KN7D_ARATH	2.26e-95	185	602	94	503	Kinesin-like protein KIN-7D, mitochondrial OS=Arabidopsis thaliana OX=3702 GN=KIN7D PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000043	0.000000

TMHMM  Annotations     

There is no transmembrane helices in AMAG_18849-t26_1-p1.