ID A0A2K5JP61_COLAP Unreviewed; 1788 AA.
AC A0A2K5JP61;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Kinesin family member 1B {ECO:0008006|Google:ProtNLM};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000030659.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000030659.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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 STRING; 336983.ENSCANP00000030659; -.
DR Ensembl; ENSCANT00000053867.1; ENSCANP00000030659.1; ENSCANG00000036500.1.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
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 CDD; cd22727; FHA_KIF1B; 1.
DR CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR CDD; cd01233; PH_KIFIA_KIFIB; 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 Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR022140; Kinesin-like_KIF1-typ.
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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR049780; PH_KIFIA_KIFIB.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR47117:SF4; KINESIN-LIKE PROTEIN KIF1B ISOFORM X1; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF12473; DUF3694; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF12423; KIF1B; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
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:UP000233080}.
FT DOMAIN 5..355
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 543..599
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 1621..1719
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1470..1490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1538..1579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 662..718
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1470..1488
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 1788 AA; 201382 MW; 847500337E4B73CE CRC64;
MSGASVKVAV RVRPFNSRET SKESKCIIQM QGNSTSIINP KNPKEAPKSF SFDYSYWSHT
SPEDPCFASQ NRVYNDIGKE MLLHAFEGYN VCIFAYGQTG AGKSYTMMGK QEESQAGIIP
QLCEELFEKI NDNCNEEMSY SVEVSYMEIY CERVRDLLNP KNKGNLRVRE HPLLGPYVED
LSKLAVTSYT DIADLMDAGN KARTVAATNM NETSSRSHAV FTIVFTQKKH DNETNLSTEK
VSKISLVDLA GSERADSTGA KGTRLKEGAN INKSLTTLGK VISALAEVDN CTSKVCKKKK
KTDFIPYRDS VLTWLLRENL GGNSRTAMVA ALSPADINYD ETLSTLRYAD RAKQIKCNAV
INEDPNAKLV RELKEEVTRL KDLLRAQGLG DIIDNLKDFQ NNKHRYLLAS ENQRPGHFST
ASMGSLTSSP SSCSLNSQVG LTSVTSIQER IMSTPGGEEA IERLKESEKI IAELNETWEE
KLRKTEAIRM EREALLAEMG VAIREDGGTL GVFSPKKTPH LVNLNEDPLM SECLLYYIKD
GITRVGQADA ERRQDIVLSG AHIKEEHCIF RSERNNSGEV IVTLEPCERS ETYVNGKRVS
QPVQLRSGNR IIMGKNHVFR FNHPEQARAE REKTPSAETP SEPVDWTFAQ RELLEKQGID
MKQEMEKRLQ EMEILYKKEK EEADLLLEQQ RLDYESKLQA LQKQVETRSL AAETTEEEEE
EEEVPWTQHE FELAQWAFRK WKSHQFTSLR DLLWGNAVYL KEANAISVEL KKKVQFQFVL
LTDTLYSPLP PELLPTEMEK THEDRPFPRT VVAVEVQDLK NGATHYWSLE KLKQRLDLMR
EMYDRAGEMA SSAQDESETT VTGSDPFYDR FHWFKLVGSS PIFHGCVNER LADRTPSPTF
STADSDITEL ADEQQDEMED FDDEAFVDDA GSDAGTEEGS DLFSDGHDPF YDRSPWFILV
GRLSGTAKIS FDNEYFNQSD FSSVAMTRSG LSLEELRIVE GQGQSSEVIT PPEEINRMND
LDLKSSTLLD GKMVMEGFSE EIGNHLKLGS AFTFRVTVLQ ASGILPEYAD IFCQFNFLHR
HDEAFSTEPL KNNGRGSPLG FYHVQNIAVE ITESFVDYIK TKPIVFEVFG HYQQHPLHLQ
GQELNSPPQP CRRFFPPPMP LSKPVPATKL NTMSKTSLGQ SMSKYDLLVW FEISELEPTG
EYIPAVVDHT AGLPCQGTFL LHQGIQRRIT VTIIHEKGSE LHWKDVRELV VGRIRNKPEV
DEAAVDAILS LNIISAKYLK SSHNSSSIWF SFMHKILCLQ FISTYPVCFQ LDHCIQPAVI
TKDVCMVFYS RDAKISPPRS LRSLFGSGYS KSPDSNRVTG IYELSLCKMS DTGSPGMQRR
RRKILDTSVA YVRGEENLAG WRPRGDSLIL EHQWELEKLE LLHEVEKTRH FLLLRERLGD
SIPKSMSDSL SPSLSSGTLS TSTSISSQIS TTTFESAITP SESSGYDSAD IESLVDREKE
LATKCLQLLT HTFNREFSQV HGSISDCKLS DISPIGRDPS ESSFSSATLT PSSTCPSLVD
SRSNSLDQKT PEANSRASSP CAEFEQFQIV PAVETPYLAR AGKNEFLNLV PDIEEIRPGS
VVSKKGYLHF KEPLYSNWAK HFVVVRRPYV FIYNSDKDPV ERGIINLSTA QVEYSEDQQA
MVKTPNTFAV CTKHRGVLLQ ALNDKDMNDW LYAFNPLLAG TIRPGHLASE TIREDKSVSF
SCQEVFQDER GKGKPPETSV ALPVVLGLFY TILYFPCSDL SVSPSLRH
//