ID A0A3P8P835_ASTCA Unreviewed; 2013 AA.
AC A0A3P8P835;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Kinesin-like protein KIF13B {ECO:0000313|Ensembl:ENSACLP00000013173.1};
GN Name=KIF13B {ECO:0000313|Ensembl:ENSACLP00000013173.1};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000013173.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000013173.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000013173.1}
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}.
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DR STRING; 8154.ENSACLP00000013173; -.
DR Ensembl; ENSACLT00000013502.1; ENSACLP00000013173.1; ENSACLG00000008995.1.
DR GeneTree; ENSGT00940000155500; -.
DR OMA; MAIQTEH; -.
DR OrthoDB; 126886at2759; -.
DR Proteomes; UP000265100; Chromosome 15.
DR Bgee; ENSACLG00000008995; Expressed in anal fin and 7 other cell types or tissues.
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 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; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
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; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR47117:SF3; KINESIN FAMILY MEMBER 14-LIKE; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF01302; CAP_GLY; 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 PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM01052; CAP_GLY; 1.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF74924; Cap-Gly domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 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 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}.
FT DOMAIN 10..358
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1911..1953
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 849..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1499..1526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1574..1593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1601..1824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1953..2013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 369..415
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1615..1629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1630..1664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1676..1699
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1705..1752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1766..1800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 108..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 2013 AA; 222932 MW; 175C7E470E7CF59B CRC64;
MDDNSVSDSN VKVAVRVRPM NRREKDLKTK CVVEIDGNQT VLHPAVTSMN TADPRNQPKV
FAYDYCFWSM DDSQKDKFAG QDVVFQCLGE SLLDNAFMGY NACIFAYGQT GSGKSYTMMG
SSEQPGLIPR LCSSLFSRTE KEAREGESFT VEVSYMEIYN EKVRDLLDPK GSRQALRVRE
HKVLGPYVDG LSRLAVTSYE DIESLMSEGN KSRTVAATNM NEESSRSHAV FNIILTHTLM
DLRSGTSGEK VSKLSLVDLA GSERAAKTGA AGERLKEGSN INKSLSTLGL VISALADHGA
GKNKSKFVPY RDSVLTWLLK DSLGGNSRTA MVATISPAAD NYDETLSTLR YADRAKNIVN
HAVVNEDPNA RIIRELREEV EKLKEQLTEA ESMKAPELKE RLEESEKLIQ DMTVTWEDKL
RKTEAIAQER QRQLESLGIS LQSSGIRVVD DKCYLVNLNA DPALNELLVY YLKDHTRVGS
ADSQDIQLCG MAIQAEHCVI DVTESHGVVL TPHRNAKTYV NGTEVVNPVQ LHHGDRILWG
NNHFFRINLP RQRVQKGGEE EEDAAMTKRS SSDCLEVGEP DACSDVSSER SFGYEFAQAE
VMMKGMWNND PLQSVLQTLE KQHQEEKRCA LERQRQMYEQ ELQQLRQRVT PEKPSGVPGS
ATAAVLSAGS NKRVRRWSED REAMITRSLR RLKEQIVRAR LLAQEAGFIA EELNKRTEYL
VTLQIPAANL DANRKRDAVL SEPAIQVRRK GKGKQIWALE KMENRLVDMR ELYQEWKELD
EDNPVMRSYF KRADPFFDEQ ENHSLIGVAN VFLACLFYDV KLQYAVPIIN QKGEVAGRLH
IEVWRGTESC EEEGGGGPDK QLSSTDGDPH ERRLRCVVKI LQATGLPRHL SNFVFCQYRF
WAQEEPVFTA PEVASSSSAS ASRDPQCTVV FDSTKELSVP VSEDFVEFLA EGAVAIEVYG
HKQANHRRNL ALWDLGVIQA KTRSLRERWS EVTRQLELWV KVMELNEAGE FTAVEVVPAK
DVRTGGIFQL RQGQSRRVQV EVCPVPDSGT MPLVAASILS VSIGDVKVRQ VRLPKNDPKQ
VTDEEMDSYQ EVDLERMREQ WLVTLTQRQE YLDQQLQKIV CKADKSEDDV ERESQLLECR
LTLTEERNAV MVPSAGSGIP GAPVERVPVP GMETHTPALF LDLSADDFQS SLSAPLAGGQ
DALLSGEDED DFFDLHIVKH YDPEVKAEAS WDSTVHECPQ LSRVAPADQR VYLTVRTVVQ
LSHPAHMQLV LRKRICVSVT GRQGFAQSLL KRMSQRSSVS GCGITFEVVS NIPGDIHGPE
DREMLARLAA SAEDEQSAAS EAAIEKYLRS VLAVENILTL DRLRQEVAVR EQLAGRGRAA
RRCLSSPDIE RLSDSSLDLG SSPLKLKDFK AWDSHHDLSV APPPPSRRTL PSSLSQNLNA
ETVKAVPRLL KSLLPGGKEG RDQTAVHQQS LPRIVVQSAS VEEDMSKQRQ AVPIDETEIP
RSVPLPPPII PETEDSTTSP VSEASSGYMS TSISTVTLSE VYTLSWDLPS SYGSRDGFET
VLDEHEEENV VTQKFSPFSD TTQSDTLILD QSGPQELLSL RQKADAESME QEPSEPDVMP
SQQEPNRLLS DQLKEAEKSD PAAEAELPDQ TEQKQDRGSE QRDHSEVAQN NGTKQTEVRH
VDHSEPKTPS REDLEVAATN KVECELAFSN ETQRSAQEGA RRLESTVLQP QQRTQEQTAS
DFIQDPSPSL IQASSPDPGP PVDLAAQASS KQQSTSDVPE TNGASFLPSS SATSEVQQPA
ASVKPAKGPI SSPKSGPSVA NPFKIQKVKS SDLKSFLQIL SEEEHDTPTL VNQPSSCGTG
PNLSVPKESL EIISDTEDGD TAASAVLPEW LKEGEFVSVG ANKSGTVRYL GPTDFAEGTW
VGVELEVPAG KNDGSVAGKH YFHCNPGYGV LVRPDRVTRG DPKRHRQQQQ KRRSAHLSGS
SPNLAALTAL AKGEGGTGST GRGRGENRKS WNT
//
