ID A0A2D0QV82_ICTPU Unreviewed; 964 AA.
AC A0A2D0QV82;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN Name=kif23 {ECO:0000313|RefSeq:XP_017322219.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017322219.1};
RN [1] {ECO:0000313|RefSeq:XP_017322219.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017322219.1};
RG RefSeq;
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,
CC ECO:0000256|RuleBase:RU000394}.
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DR RefSeq; XP_017322219.1; XM_017466730.3.
DR AlphaFoldDB; A0A2D0QV82; -.
DR GeneID; 124627994; -.
DR CTD; 9493; -.
DR OrthoDB; 5403873at2759; -.
DR Proteomes; UP000221080; Chromosome 4.
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; cd01368; KISc_KIF23_like; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 2.60.40.4330; Kinesin-like protein Kif23, Arf6-interacting domain; 1.
DR InterPro; IPR032384; Kif23_Arf-bd.
DR InterPro; IPR038105; Kif23_Arf-bd_sf.
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:SF600; KINESIN-LIKE PROTEIN KIF23; 1.
DR PANTHER; PTHR24115; KINESIN-RELATED; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16540; MKLP1_Arf_bdg; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|RuleBase:RU000394};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}.
FT DOMAIN 25..437
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 561..637
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 196..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..700
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..933
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 112..119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 964 AA; 109604 MW; 114A4ECE6F4EBB1E CRC64;
MIRPTKGKTP RRPPPKKPTN NLKDPVGVYC RVRPLGPEDG ECCIEVISST TIQLHAPDGL
KANRNGEFKE TQYSFKKVFG IKTTQRELFE DVAKPLVDDL IHGKNGLLFT YGVTGSGKTY
TMTGSPGQGG LLPRSLDMIF NSIGPYQAKR FVFKPDDKNG MEVQNQVDAL LERQKQESQL
FVPKTPSSRQ RVDPEFADMI TPEEASKAEG VDEDSSYSVF VSYIEIYNNY IYDLLEEAPF
DPIRPKPPQS KILREDQNHN MYVAGCTELE VKSTEEAFEV FWRGQKKRRI ANTQLNRESS
RSHSVFIIKL AQAPLDADGD NVLQDKNQVN VSQLCLVDLA GSERTSRTRA EGSRLREAGN
INQSLMTLRT CIEVLRENQM CGTNKMVPYR DSKVTHLFKN YFDGEGKVRM VVCVNPKADD
YEETMLVMRF AEMTQEVEVA RPVDRPICGF AAGRRQRNQA FKEELSRRLE ERGGPIDGEP
SSALSQFLQN LPPLPPCEIS DPSDDHTLPR FIEALEKRHK IRLMMTEEYN KAANMLKSML
QELDGNLISK ENFIHDQRSK LGEKDKMIHN QKNEIDRLEK KSKMLEYKID LLQKTTNIYE
EDKRTLQNEL ESREQRLQRE LSEKKRMEAR MQGLVSDEKL RWQKECERRV NAKELEMQNK
LWVKDEKLKQ LKAIVTESKT DTRPDKPQRP SREKDRVPAK RSASPSPMPS NFSCQASDYI
LPKVVRPAPL SPSTSSVSVA SSISDWEQRT PQGNMQGSPS PPYGRSRAQG LPGSLSRQRG
RCWARECEVQ VQPAEVDQKE CVYRTGPAVR PVHRRSHSAG GERWVDHKPT TNVELDTVMQ
PSVPNSIKVT TPSEKALSKC DKYMLTHQEV ASDGEIQTKL IKGEVFKTRG GGQAVQFTDI
ETLKQENAVG PSRKRRSSEN RQDEPKDGDW TDVETRCAVA VEMRAGSNLG PGYQHHGYPK
RRKP
//
