ID A0A498MHB2_LABRO Unreviewed; 1051 AA.
AC A0A498MHB2;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Kinesin KIF25 {ECO:0000313|EMBL:RXN16765.1};
GN ORFNames=ROHU_027242 {ECO:0000313|EMBL:RXN16765.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN16765.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN16765.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN16765.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN16765.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the HEBP family.
CC {ECO:0000256|ARBA:ARBA00009817}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXN16765.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QBIY01012771; RXN16765.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498MHB2; -.
DR STRING; 84645.A0A498MHB2; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 3.20.80.10; Regulatory factor, effector binding domain; 1.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011256; Reg_factor_effector_dom_sf.
DR InterPro; IPR006917; SOUL_haem-bd.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919:SF171; ACETYL-COA ACETYLTRANSFERASE, CYTOSOLIC; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR Pfam; PF00225; Kinesin; 2.
DR Pfam; PF04832; SOUL; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF55136; Probable bacterial effector-binding domain; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Coiled coil {ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A498MHB2};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572}.
FT DOMAIN 462..834
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 708..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 432..459
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 531..538
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1051 AA; 115498 MW; 6A9B51B9E5057F6F CRC64;
MNTDAIVIVS AARTPIGSFN GALSSVPLND LGTVVIKDVL KRANLKPEDI SEVIMGHVLT
AGHGQNPARQ ASVGAGIPYS VPAWSCQMIC GSGLKAVCLG AQSIMTKEST IVVAGGMESM
SRAPHIMQMR SGVKMGDATL QDSILTDGLI DAFYSYHMGI TAENVAKQWE VSREAQDQFA
VTSQNRTEAA QKAGYFDQEI VPVTVPSRKG KRCFCPVEVK ADEFPRHGSN IDAMSKLKPY
FVKDGSGTVT AGNASGINDG AAATVLMSQS EAQRRGLKPM ARITSWAQAG LDPSVMGTGP
IPAIRKAVEK AGWKLDEVDL FEINEAFAAQ SVAVVKELGL NPDKCLGKLR RERDNDLHTQ
RQNHQQQRKV QKSTHAALYK LLSEVQMLKQ DLRDVFTIYV GFAKELEEQS KQLFECVGTA
RNAIQDSQSD DLQKLQGQVT ALECSLQEEK ERCREERELR GNIRVHCRVR PILQFDHIPG
SPTTNGSSSC EAVVQAVNDD SVFVNCAKTS SPVMNKIFEF ERYNVCIMAY GQTGSGKTHT
MIGSRSEDPT AAVQDSQQGI IPKAANELFK LISEKPADSH TVEMSVVEVY NNEVLDLLAR
DEDGVTVGVK REVITTSTGT SEVPCLTYEL VRSSAEVMQL INSVLKLRSH CPTLVHMDSS
RSHFIVTLTV TSKSPDALAL ARRLQNARQD VQRVSQKEWW SPRCRRAASS RSSSPASSPC
HSPCHSPRPS ITQPPLKTKL QLVDLAGRIS GVTGAALWES SCINRSLSAL SDVLGALAER
RPHVPYRNSK LTHLLQDAIG GDAKLLIMLC VSPTQRFLTE SLQSLGFGAR ARQVTYNLLH
IEDIPLKKMF TGFLCLVITV KMLKAIGQTF FSSGLQNPKS TTQQSKGEDY EVRTYHTTNW
VSTAVTGMEQ DSALSTGFRR LFKYIQGNNE KKSKVEMTAP VSCLIEPGAG PACESTFTVS
FYIPEEHQAD PPKPTDPDVF IENRKELTVF VRTFGGFANS ESCRAELLNL IESLKRDGMK
FKEAPFYRAG YDSPFKLTNR RNEVWLIKDE E
//
