CAZyme Information: EPrPVT00000013989-p1

Basic Information

• Species: Phytopythium vexans
• Lineage: Oomycota; NA; ; Pythiaceae; Phytopythium; Phytopythium vexans
• CAZyme ID: EPrPVT00000013989-p1
• CAZy Family: AA17
• CAZyme Description: Kinesin

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1952		217576.48	7.3254

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PvexansDAOMBR484	11991	1223560	34	11957

Full Sequence      

MDAMTAADDAAARASLLRPAYDDDSASSSDDEHEDTSDVVMLVSVPEMEAGGQPHARASA
EQASAPPDRPPRRRTRLLMPVMALCAVSMALTVGGYAMARYSVRRAASSLEGEFDLHKLT
SAMHPNASTIDSPFYQRSSAFDRSVDRGRGVVICLYDDILAMGLSLIRELRCHGNQELIQ
VYHCLPDEISNANRALLLRADDRLEIVDVCSDLIERKLMSRDMADKFRNWWIKPLAAFHT
DIREVMLLDVDDVLMKDPAVLRESEGYKKTGTTFFYDRVIGHCDKFFNKRDGYLQYLTKV
LKKFDYEAFNLTGVISAWPNNDMKDHPDSLCGSILQYMPVESDTPEMLYVNGKALIDPFP
QGVDYVRKARTNNMFNLVPTHMTPRQTRHEVERRQNTDKVTYHMECLTGLGSTPLPSSFA
GHLLRRRLFFLGITTGVEGALRHCETYELRRLAIDDASEDRLLMRGSHMALTGSAMLSFP
PFGGQDVAFDPAWLVRAMQVRPSVFASPAYRRSKTFDKDVGRDKGIVVCMHNGNMAMGLS
LIRELRCHGNQELIQVYHCLNEISNNNRAQLLRTDDRLEIVDVCSDFIERKIMSKDLAVN
FRNWWIKPLAVIHTDIREVMLLDADDVLMKDPAVLRESEGYKRTGTTFFYDRVASSCSKF
FNRRDIFTPYLTKLFHKFDYEAFNLTEYAPSDHLLNSFAYAGKTCHEQDSSMVLIDKSRM
GAAREIMWWFITKERFRFTYSWGDKETFWLSYELAHVDYFFSPWGVSVISSWPNSDMQSH
PDSLCGSIVQYMPVNDEMAEMLYVNGKALLHPFPQGVSRVANAKPNNMFNLVPTHMTPRQ
PRREVEQRHNTDRVTYEVECLTGLGSVPLPKSFAGHLLRRRLFFLAISTGVNGALQHCET
YEQPVAGRRLDFAGTLRGGAMHRGGHPARVSVSVSSVSPSSSASSSRRGSLGASPASSFF
SPARMQRLSLSSSSLGGHGGSGLASSSSSSSGLPPRGSNFKVVIRVRPPLPRELHGDHPF
QNVIGVDASGHVLTVSENLSALAVGSGGGGAGDDGVAGDESGSSAAGIAAYGHHVFSFDH
VYDQLCTQRAVYENTAKAVVESSLEGYNATIFAYGQTGTGKTYTMEGFNSGAPALGVDVE
ARGIIPRAIEQIFGHIQQHVSPRLRFLVRASYLQIYNESISDLLKPERANLTIREDKRRG
VFVEGLSEWVVRSPEEIYGLMERGGAMRATGSTKMNELSSRSHAVFIIIAEQSRTSYVDA
RGNDMSPEDFTALAQAFQARHGQAQAQGGSGKLPPKLESMVRQSFKVGKLNLVDLAGSER
VRLSGATGQRLEESKKINQSLSALGNVISALTDARGRQHIPYRDSKLTRILEDSLGGNCK
TTMMAMISPALEAMTESLSTLKFANRAKNIKNEAKVNEDLDQKSLLRKYERELRRLRAEL
EEKSRNVVDKRRLLELDEQRRRAEEDKMAAIRALEERSREFMREKEEKKKLEQRISMLTS
QMLMSNQRRLPLEHQDRIRKEYECRLADLEKERETIEEEKAQVDRYKQLLLKQRDIMIAL
TQRLNERDEQITALQDELDAYDRHQKELEEKLDEKTAHLIHLQRVTMEHNASSPGKIDAE
LVKALGDWGAASSGSAGLNSMAASPPVAPELLITHKQFRPHAAEQVIMNSNNTLTSGSGG
GALLSADEKIQELKALVDTQGAEQLRLAKELEDVKSEKVSVEFVLRERVEKLVQIELAAR
LKSVETGGGGGNNSDEQERARQLQRQLEVVAMENRRLRDQLASPRGGDRAGELEARCETL
VKERRAVQTIMEHKIKALVNAVSEASDATLRSAGGVERLGESAAWLTREVHALQRLVNAS
ILALRNADAGSNAVVGSSNSRPADGAARTTAVEQKLSRTSVAVPTGAPQLPTSYGKEGML
PQKTSSSAGLSVDELIQQRREQLQRERQDNMG

Enzyme Prediction     

EC	-	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT71	524	786	3.2e-45	0.9659090909090909
GT71	148	293	2e-25	0.5303030303030303

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214526	KISc	3.53e-138	999	1417	1	335	Kinesin motor, catalytic domain. ATPase. Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.
395169	Kinesin	1.06e-135	1073	1410	39	326	Kinesin motor domain.
276812	KISc	1.89e-122	999	1408	1	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.
276822	KISc_KIF3	7.84e-118	999	1410	2	334	Kinesin motor domain, kinesins II or KIF3_like proteins. Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and 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 this group 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.
276823	KISc_KIF4	1.50e-110	1001	1411	4	341	Kinesin motor domain, KIF4-like subfamily. Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCA15193.1|GT71	CCA15193.1|GT71	9.71e-107	519	899	127	516
CCA22801.1|GT71	CCA22801.1|GT71	2.60e-105	490	898	36	430
BAP68847.1|GT71	BAP68847.1|GT71	9.13e-89	466	808	13	358
AIG56397.1|GT71	AIG56397.1|GT71	5.95e-69	503	882	72	452
AIG56246.1|GT71	AIG56246.1|GT71	1.10e-55	524	869	65	435

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3B6U_A	3B6U_A	1.44e-82	1076	1430	70	372	Crystal structure of the motor domain of human kinesin family member 3B in complex with ADP [Homo sapiens],3B6U_B Crystal structure of the motor domain of human kinesin family member 3B in complex with ADP [Homo sapiens]
1GOJ_A	1GOJ_A	2.17e-80	1076	1420	49	340	Structure of a fast kinesin: Implications for ATPase mechanism and interactions with microtubules [Neurospora crassa]
3B6V_A	3B6V_A	2.53e-79	1076	1429	70	395	Crystal structure of the motor domain of human kinesin family member 3C in complex with ADP [Homo sapiens],3B6V_B Crystal structure of the motor domain of human kinesin family member 3C in complex with ADP [Homo sapiens]
7A3Z_A	7A3Z_A	1.28e-75	1076	1438	49	355	Chain A, Osmotic avoidance abnormal protein 3 [Caenorhabditis elegans]
2Y5W_A	2Y5W_A	1.04e-73	1075	1432	52	355	Crystal structure of Drosophila melanogaster kinesin-1 motor domain dimer [Drosophila melanogaster],2Y5W_B Crystal structure of Drosophila melanogaster kinesin-1 motor domain dimer [Drosophila melanogaster],2Y65_A Crystal structure of Drosophila melanogaster kinesin-1 motor domain dimer-tail complex [Drosophila melanogaster],2Y65_B Crystal structure of Drosophila melanogaster kinesin-1 motor domain dimer-tail complex [Drosophila melanogaster],2Y65_C Crystal structure of Drosophila melanogaster kinesin-1 motor domain dimer-tail complex [Drosophila melanogaster],2Y65_D Crystal structure of Drosophila melanogaster kinesin-1 motor domain dimer-tail complex [Drosophila melanogaster]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|F1QN54|KIF3B_DANRE	sp|F1QN54|KIF3B_DANRE	2.41e-82	1075	1444	57	374	Kinesin-like protein KIF3B OS=Danio rerio OX=7955 GN=kif3b PE=2 SV=1
sp|O15066|KIF3B_HUMAN	sp|O15066|KIF3B_HUMAN	1.10e-81	1076	1444	57	373	Kinesin-like protein KIF3B OS=Homo sapiens OX=9606 GN=KIF3B PE=1 SV=1
sp|Q61771|KIF3B_MOUSE	sp|Q61771|KIF3B_MOUSE	1.48e-81	1076	1444	57	373	Kinesin-like protein KIF3B OS=Mus musculus OX=10090 GN=Kif3b PE=1 SV=1
sp|P46871|KRP95_STRPU	sp|P46871|KRP95_STRPU	3.28e-81	1076	1443	56	371	Kinesin-II 95 kDa subunit OS=Strongylocentrotus purpuratus OX=7668 GN=KRP95 PE=1 SV=1
sp|P46872|KRP85_STRPU	sp|P46872|KRP85_STRPU	1.42e-80	1076	1449	58	380	Kinesin-II 85 kDa subunit OS=Strongylocentrotus purpuratus OX=7668 GN=KRP85 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000065	0.000000

TMHMM  Annotations     

Start	End
77	99