ID A0A498M4W0_LABRO Unreviewed; 1134 AA.
AC A0A498M4W0;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Kinesin KIF1C {ECO:0000313|EMBL:RXN15908.1};
GN ORFNames=ROHU_008566 {ECO:0000313|EMBL:RXN15908.1};
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:RXN15908.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN15908.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN15908.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN15908.1};
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 TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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:RXN15908.1}.
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DR EMBL; QBIY01012820; RXN15908.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498M4W0; -.
DR STRING; 84645.A0A498M4W0; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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; cd01365; KISc_KIF1A_KIF1B; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 6.10.250.2520; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR032405; Kinesin_assoc.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR47117:SF6; KINESIN-LIKE PROTEIN KIF1C ISOFORM X1; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, 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}; Reference proteome {ECO:0000313|Proteomes:UP000290572}.
FT DOMAIN 5..349
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 394..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 436..463
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 622..656
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 796..830
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 846..893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..1048
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1134 AA; 128026 MW; 30EB9FF55EB52DB7 CRC64;
MASSSVKVAV RVRPFNSREI NRGAKCVIQM QDKSTCIANP KQHKEAPKNF TFDYSYWSHS
SEEDPSFASQ RKVYQDIGEE MLLHAFEGYN VCIFAYGQTG AGKSYTMMGK QDPGQQGIIP
QMCEDLFRQT ADNTAPDLSF SVEVSYMEIY CERVRDLLNP KSRGSLRVRE HPIMGPYVED
LSKMAVTNYS DIADLMDTGN KARTVAATNM NETSSRSHAV FTILFTQRRH DNMTSLDTEK
VSKISLVDLA GSERADSSGA KGMRLKEVAN INKSLTTLGK VISALADMHS TKKRRSDFIP
YRDSVLTWLL RENLGGNSRT AMIAALSPAD INYEETLSTL RYADRAKQIK CNAVINEDPN
ARLVRELKEE VNRLKELLLS QGLSNLITAS GSESGRPALG GASGELHQPS LSYEPSTSDA
PMEGVAPTSP TAHISKEEAA ERLKETEKII AELNETWEEK LRKTESIRQE REALLAEMGV
SVKEDGGTTP HLVNLNEDPL MSECLIYYIK DGVTRVGQED VDIRLTGQFI KELHCVFCSE
VNENNEVVVT LEPLVGAETY VNGKRITDGV VLKQGNRIVM GKNHVFRFNH PEQARLERER
SATQEQQGEP VDWSYAQEEL LEKQGIDIKQ EMEKRLQDLE NQYRKEKEEA DQILEQQRLM
QSIVKKCGLP SSGKRREPLR VYQIPQRRRI PTTQESKHRL SLEELRTQAV KEICYEVALG
DFRHTRQEIE ALAIVRMKEL CRTYRQKDPQ ERESWKSVAK DVCETVGIGE EEGDREERTA
TTAGGGGGGE GGKTDMGELK AHIDKLTDIL QEVKLQNNMK DEEIRSLRDR MVKMEKIFPV
EVEGDETDLG LDGARGDDSP VQVNRRDEDS GYRRGRHRWQ YPEKYHDPKR RKGANNQPNN
ALYPPAPSGH SQNNPFSSAS SRFNSQTPRN PNGPFLPGTG RFLPPQERRL QFPFKNNPQH
RSFIWGPSSG GESGNDPSAQ SGTDSVHTFQ SSPSPNKGQW PNSHHQQRRN HGNRGYGNWG
NRQRSRNRGR NPFDGYLTNE QAGNVERKDS VQGQHKQGRA RYTWYSPDFA SDQSTGDGFQ
HNYNQSRQGV YKHPNSHYQH PQKQDNPPEM SQHASEGNTN PQSIPDCSST PMET
//
