ID A0A3Q2ZP07_KRYMA Unreviewed; 2010 AA.
AC A0A3Q2ZP07;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Kinesin family member 26A {ECO:0000313|Ensembl:ENSKMAP00000005523.1};
GN Name=KIF26A {ECO:0000313|Ensembl:ENSKMAP00000005523.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000005523.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000005523.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR RefSeq; XP_017271503.1; XM_017416014.1.
DR STRING; 37003.ENSKMAP00000005523; -.
DR Ensembl; ENSKMAT00000005620.1; ENSKMAP00000005523.1; ENSKMAG00000004200.1.
DR GeneID; 108235779; -.
DR KEGG; kmr:108235779; -.
DR CTD; 58004; -.
DR GeneTree; ENSGT00940000159075; -.
DR OMA; RIMMVTC; -.
DR OrthoDB; 5356153at2759; -.
DR Proteomes; UP000264800; Unplaced.
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; cd00106; KISc; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21608:SF6; KINESIN-LIKE PROTEIN KIF26A; 1.
DR PANTHER; PTHR21608; UNCHARACTERIZED; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
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:UP000264800}.
FT DOMAIN 380..733
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 23..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1241..1260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1267..1400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1434..1465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1561..1678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1698..1764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1783..1827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1910..1937
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 192..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1267..1312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1326..1382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1434..1449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1561..1673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1705..1734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1743..1761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1783..1815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 478..485
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 2010 AA; 215645 MW; 74884053197FB833 CRC64;
MSSGNLVSDG GDLHSRLFTV EGCPGGEAAV TPRKRLQSAE EARCSSRPAP EGAGSVSISE
SEEKGGGSCQ QCQKKVSELK KQALALADQN SLKDPGYATF LFEHLHTPGN PEIDCCQVCS
TPLHQLRREA LQMLHSPVLT FSSDMAAMPR ASLLPQPSRF TVSSSSVHAK QLLKSQPAPR
SVLPLGERHK VPGWSQNSSA SSGSKTSVQV TVAGGQLTGS LSTVTIQAQQ YLDGMWSISR
VNNFLPQPKP ARGLMGDADS DVTALEASVT TMTSTTTSSS SSTLAPCRLE CSSQAGLPAP
ITTASTSPAS SSAASFFIRA AQKLNLSSKR KKHQPSPLHP QEPSIYPTNF SGILQVSPPP
APPCLLRAVS KVKENPGMGK VKVMMRICPS LEAVDSSEFQ SFLKVDSRKK QLTLYDSASS
PHSSSGHRRS ATVAVPKIFA FDAVFTQDAS QAEVCSGTVA EVIQSVVNGA DGCIFCFGQV
KLGKTYTMIG KDSSTQSLGI VPCAISWLFK LINERKEKTG TRFSVRVSAV EIFGKDEELK
DLLSEVSTGS LQEGQSPGIH LREDPICGTQ LQNQSELRAP TAEKAAFFLD AALAARSTSR
PNVDEDERRN SHMLFTLHIY QYRMEKSGKG GMSGGRSRLH LIDLGSCEKV LSKSRDGGGS
LCLSLNALGN VIMALANGAK HVPYKDSKLT MLLRESLGNI NCRTTMIAHI SDSPANYADS
LTTIQLASRI HRMRKKKSKY ASSSSGGESS CEEGRVRRPP HLRPFHPRTV ALDPDLPALL
SDPEYSSSSE QSCDTVIYVG PGGTAISDRE LSDNEGPPAF VPIIPSLNKK KSVKEGPLDR
DQFFKCNTFA ELQERLECID GSEEPTAFVG EGKRNQASPK TDKSKENQGS NSPKTVANIS
NNQEGISTKQ FPKPVPMQPS CSPNVKSKLD IAKTQCIPEE RAPSENIHNI CRTSADGEKS
LITESQVNSN SLATSTVLNS EPVVREKVYA NKKALPKPAP PPLQQKENAE NEERSSTRMP
PVGMSHQAVK RKDPCTSPFF RAPMEVCQVR STMRERCMDR DILRATVTLQ QPVELNGEDE
LVFTVVEELS IGSIVDKGRP SSIISFNSDC SLQALASGSR PVSIISSIND EFDAYTSAVG
GSEVNVAVVT PLQEGAMEGI DSRGSSISSW LSEVSVCTLE SEGAHSTDVF LPQVKHLGSE
ATFYFDSLDM FHCASSTRDP KNSLNDSGFS FSEQDSDSAA SSKLSLTKCP PSPESTKGSL
RFTSKLTKAH SLSSSSPPQG SSIVHSSLPR KIKPTSSISH SSSSSSSSGR DPPRQEAKQE
DPWQRSNNHS EPQISDSSST SRFLRNPPSG IISSRTPNNS SSVPRPPKVP GSTSSQRVVD
GCEKSATKNP PSKMPQLRRG ATTLGTVPVI HFSTDHKGTQ DIIASATSLK FSSLGKNNKA
NSQKPSNLPK PGCVSPPPPP VRKSSLDHKT KILLPQSALK SAYGEAGKTS GTRVAVSEDE
LEVHQKLDST NLKTSSLNTA KVTSSLKAKG SRGEAGLHYG SQMSLEKCES LSLSGSRAAL
SRENSGASLG SKSNKSIPRF GIPNSSSSPI ATFQSTQSQG NISKSSQVKA SVNPRALGTV
NGSKARSLSA NNSKGLSSST KSLATPVTRN TNTNLPPSGR TAAPRTTAPV SNKPGRGTIM
GTKQAIRAAN SRVTELATGN ISGKHGRGSG DSDSGNDSGV NVNDDKSPTA MLPSPYSKIT
APRRPQRYSS GHGSDNSSVL SGELPPAMGR TALFYHSGGS SGYESMIRDS EATGSASSAH
DSMSESGMSS SGRARSSKYP KKRANGFQRR RLIPAPLPDT SSLGKKVGTA GQWVDLPPMS
GPLKESFEIK VYEIDDVERL QRRRQEETTE QPFQDVDKGL LYFNSKLKIL ERRQQQVREL
RVKHQVLLEE LEDTKVRLMM EPSKWAGEFE VDPNLDKESP EYLEALAQAT EELEFCVNLC
KSHVMMVTCF DISTPPTCVT QEGLLREVEV
//
