ID   CTK2_XENLA              Reviewed;         643 AA.
AC   P79955;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Carboxy-terminal kinesin 2;
DE   AltName: Full=XCTK2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=9049251; DOI=10.1083/jcb.136.4.859;
RA   Walczak C.E., Verma S., Mitchison T.J.;
RT   "XCTK2: a kinesin-related protein that promotes mitotic spindle assembly in
RT   Xenopus laevis egg extracts.";
RL   J. Cell Biol. 136:859-870(1997).
CC   -!- FUNCTION: Promotes mitotic spindle assembly.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC   -!- DOMAIN: Composed of three structural domains; a small globular N-
CC       terminal, a central alpha-helical coiled coil and a large globular C-
CC       terminal which is responsible for the motor activity (it hydrolyzes ATP
CC       and binds microtubules).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. NCD subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00283}.
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DR   EMBL; U82809; AAB40402.1; -; mRNA.
DR   RefSeq; NP_001081003.1; NM_001087534.1.
DR   AlphaFoldDB; P79955; -.
DR   SMR; P79955; -.
DR   IntAct; P79955; 1.
DR   DNASU; 394322; -.
DR   GeneID; 394322; -.
DR   KEGG; xla:394322; -.
DR   CTD; 394322; -.
DR   Xenbase; XB-GENE-865859; kifc1.L.
DR   OrthoDB; 364605at2759; -.
DR   BRENDA; 5.6.1.4; 6725.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 394322; Expressed in blastula and 15 other 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-KW.
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   Gene3D; 3.40.850.10; -; 1.
DR   InterPro; IPR027640; Kinesin-like_fam.
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   PANTHER; PTHR24115; PTHR24115; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW   Motor protein; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..643
FT                   /note="Carboxy-terminal kinesin 2"
FT                   /id="PRO_0000125379"
FT   DOMAIN          294..633
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          1..116
FT                   /note="Globular"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          81..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          117..296
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        23..42
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..101
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         386..393
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   643 AA;  71949 MW;  D3D92D08B88E5057 CRC64;
     MDSTDKKVQV ASRLPVPPKR KYVSNDENQE QMQRKRLRSS LESELPAVRV AASIATSKPR
     AAPVAALPKP QVIGRQSLAV MRPKNSGPGI TSTSFSGKTK VSSSVTQPAA IGAEKKKRAA
     WDLKGQVNDM RDTVSNYKGK MQNLTGENAR LLNSKEKLQR EVEVLASENS KLSQERCTLE
     SQLREVRQQV STFEREVARL TELCQRQEKE LSSHTNTIEE LQGANAILTK QLLDKEVKLD
     CVSGENTSLK HTVNEQTDEI AALKVCLAEK DTEVHSLDTE RRRLHNLVQE LKGNIRVFCR
     VRPTLTPERE LPAGHISFPS NDGKAIVLSK MEESHIGREK KDAVKYDFNF DCVFPPPCSQ
     ESVFEEISLL VQSALDGYPV CIFAYGQTGS GKTYTMEGPE DVTDDSMGMI PRAIHQIFSS
     AEELKAKGWQ YTFTASFLEI YNETIRDLLI NRPDKKLEYE IRKVNSANML LYVTNLRYVK
     VSCVEEVHEL LKIAKANRSV AKTAINDRSS RSHSVFQLKI EGENKQRDLK TSSMISLIDL
     AGSERLDRSL STGDRLKETQ CINTSLSTLG MVITSLCNKD SHIPYRNSKL TYLLQNSLGG
     NAKVLMFVNI SPLEENFAES LNSLRFASKV NECVIGTARA NRK