ID A0A3B4FNL8_9CICH Unreviewed; 1701 AA.
AC A0A3B4FNL8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Kinesin-like protein KIF13B {ECO:0000313|Ensembl:ENSPNYP00000010851.1};
GN Name=KIF13B {ECO:0000313|Ensembl:ENSPNYP00000010851.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000010851.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000010851.1}
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 Ensembl; ENSPNYT00000011114.1; ENSPNYP00000010851.1; ENSPNYG00000008080.1.
DR GeneTree; ENSGT00940000155500; -.
DR Proteomes; UP000261460; 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 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 1..302
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1615..1657
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 498..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1326..1351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1458..1479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1506..1528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1542..1563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 317..359
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 560..592
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 512..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1333..1351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 52..59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1701 AA; 190360 MW; 5EBC660D5361E5B1 CRC64;
CSTVFAYDYC FWSMDETDKE KFAGQEVVFQ CLGESLLHNA FQGYNACIFA YGQTGSGKSY
TMMGSVDQPG LIPRLCSALF ERTQKEQREE ESFTVEVSYM EIYNEKVRDL LDPKGGRQTL
RVREHKVLGP YVDGLSRLAV ASYKDIESLM SEGNKSRTVA ATNMNEESSR SHAVFNIILT
HTLKDLKSGT SGEKVSRLSL VDLAGSERAA KTGAAGERLK EGSNINKSLT TLGLVISALA
EQGTAKNKTK FVPYRDSVLT WLLKDCLGGN SRTAMVATVS PAADNYEETL STLRYADRAK
NIVNHAVVNE DPNARIIREL REEVEKLRVQ LTQAESLKAP ELKDRLEESE KLIQEMTVTW
EEKLRKTEEI AQERQKQLES LGISLQSSGI KVGDDKSFLV NLNADPALNE LLVYYLKEHT
KVGSADSQDI QLCGMGIQAE HCVIDITAEA AVILAPYRNA RTCVNGSPVT SALQLHHGDR
ILWGNNHFFR INLPKRRSRA ADDEEGEGGV MKNSGSSEQL DADGDTASEV SSEVSFSYEF
AQTEVMMKAL GSNDPMQAVL QSLERQHEEE KRSALERQRQ MYEQELQQLR KKLNPERLST
GQSGGPTIGQ QGPGQQSHYR SMERLSIGGM SHSSSAQSRL RQWSEDREAV LVRSLRRLRE
QIVRANLLVQ EACFIADELE RHTEYRVTLQ IPSDNLNANR KRDAVLSEPA IQVRRRGRGK
QIWSLEKMEN RLVDMRELYQ EWQDYHLNNP DDQAMCPYLR RADPFFDEQE NHSLIGVANV
FLSCLFYDVK LQYAVPIINQ KGEVAGRLHV EVVRVGGGLE DNMAGGDEPD NNQDIEVQDR
KLVCMIKILQ ATGLPQYLSN FVFCQYSFWD QPEPIIVAPE VDTSSSSPSN KDPHCMVVFD
SCKELAVSVT EEFIEHLTEG AVAIEVYGHR QADAGRNPAL WDLSIIQAKT RTLRDRWSEV
TRKLELWIQI LEINENGDFV PVEVVPARDV RTGGIFQLRQ GQSRRIQVDV RSVQDSGTMP
LIAEIVLAVS VGCVEIRNTT ANQEADEMDS YQERDLERLR RQWLGALTKR QEYLDQHLQS
LVSKAEKTED DMEREAQLLE WRLTLTEERN AVMVPSAGSG IPGAPAEWYQ SHKVFIFLYN
SQDQFEVPEA GGWDAILNGE DEDDFFDLQI VRHYDGEVKA EASWDSTVHE CPQLSRGGSY
PEQRVYLTIR VVVQLSHPAD MQLVLRKRIC VNVNPGRQGF AHNFLRRMST RSTVPGCGVT
FEVVSNIPGD APGSEDREML ARLAASAHNS QSGDDEAAIE KYLRSVLSLE NILTLDRLRQ
EVAVKEQLTS RGKSNRRSIS SPSVNRLSGS RQDLSTTCLL DDKGRWESQQ DIYMPSQFPR
TLPRPNQEPE QVKALVPQMP KLLKSLFPVR DEKKELRPSP QNQQVSRWSS AIPWKPCIEF
TAILRPPAKD RRAELPEVSP LPVHDPHDTT PLSPLSQSSS GYFSASVSTA TLCDVLQPSS
SSSSLLAAET TLPTNPQQQG ADRNDIVTSP SQFGAKVSVV ASPASHNSAN HNSITSDVSS
EQKLINSGGN EGFERLEIFV DDDERGGEDV LPDWLTEGAY VTVGNNKAGT VRYIGVTQFA
EGVWVGVELD TPVGKNDGSV GGQRYFYCKP GYGVLVRPNR LSSRERTNRQ TGEFTPSAHV
PILRGEAIVA RRGENRKSWS S
//