ID A0A0V0TG64_9BILA Unreviewed; 1713 AA.
AC A0A0V0TG64;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Kinesin-like protein unc-104 {ECO:0000256|ARBA:ARBA00020751};
GN Name=unc-104 {ECO:0000313|EMBL:KRX37539.1};
GN ORFNames=T05_9226 {ECO:0000313|EMBL:KRX37539.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX37539.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX37539.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX37539.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX37539.1}.
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DR EMBL; JYDJ01000305; KRX37539.1; -; Genomic_DNA.
DR Proteomes; UP000055048; Unassembled WGS sequence.
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; cd22705; FHA_KIF1; 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:SF5; -; 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; 2.
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; 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:UP000055048}.
FT DOMAIN 8..359
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1602..1700
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1454..1479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 616..665
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 99..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1713 AA; 195288 MW; 1DF9227CC309D692 CRC64;
MITSSMTSVK VAVRVRPFNS REINQKCKCA ISMENQLTVI HGRKDRQERT HSFTYDYSYW
SVDPNHPSYA SQKDVYNDLG LEMLDHAFQG YNVCIFAYGQ TGAGKSFTMM GKPTEEEQGI
IPQFCKDLFS RISASVQSNE NLQFSVEVSY MEIYCERVRD LLNPKNTTNL RVREHPLMGP
YVEDLTKLAV TTYEDIANLI DEGNKSRTVA ATNMNETSSR SHAVFTLVVT QRRHDSETDL
NTEKVSRICL VDLAGSERAD STGAEGIRLK EGANINKSLT TLGKVISALA EMSSQSGSIA
KKKRKADFIP YRDSVLTWIL RENLGGNSKT AMIAAISPAD INYEETLSTL RYADRAKKIV
CRAVVNEDPN AKIIRELKSE VFRLKELLTK QGINPDSDLA MERKIVARQN SVYSAMEEDT
IDRLKASEKL IAELNETWEE KLRRTEAIRA SREAELKEMG LATREDGQTL GVFQPKTVPH
LVNLNEDPLI SECLLYYLKE GTTKVGRADA PVRQDIQLSG QWIQTEHCEF ENKCGVVALV
PQDTAMCFVN GKTVNEPTVL HSGNRVILGK YHVFRFNNPQ ELMQSRYNST IQTSEEPIDW
SYAQHELLEK QGIDLKVEME KKIMELEEQY RKEKEEFTIA FEKQKREYET RIETLQKQVD
LAQSMISSTS SICTWDSERV IGIQSFDENS WSEHEEALAR WAFMKWKYFQ FTSLRDDLWG
NAIFLKEANA ISVELKKQVH PFDTMVQFQF VLLTDTMYSP LPPDLLPPGE DLSCRPYPKT
VVAVEVQDLK NGAIHFWSLE KLRQRLTHMR AIYNVELYVS PLITPDSTHA EQNLFQCWSA
CSNQSHFNFC HLAPNRQRLE LMRELYISEY SDCGPNCTEA IMDSISGADP FYDRFPWFRL
VGRAFVYLTN LMYNVALVHK VAIVNEKGDV QGYLRVGIQV VDKEEEKPDI NNRVRQCARL
TFREEKFFKR KFQKDISNHS INALTLEDRV VEGNSSEQLN LNTEGHVKSS NTLESSAIIG
KSFGKTSSAP LEFPAHMKED QEFIFRVTVL QALKVPPEFI DLFCQFNFLH RHDEAFSTEP
IKNNGKEALS FYYVQNLSVT VSKAFLHYVN HYPIIFEVFG HFQPQAGTDS LIPMKNAPGN
VFSQENSSFS CRKNPVFQPD LMISTPVKSH RTGALPLSSC NPVRSKYDLL VYFEICELAQ
NGEYSPACVD HTQNAPTQGV FLLHQGIQRR VRITICHEKS NDLNWIDCQE LVIGRIRSTP
ESNLEDIDVL SLGLFPGRVY YQFEAAWDSS LHNSPLLNRV TPFGEQVFMT VSLYMEIENC
TQLAVISKDL VVVLYSRDSK LSAASRSIRS LLAGSFHYPE RNKVSGVYEL LLKEAVDSGS
PGSLRRRRRV LDTSSTYVRG EENLGNWRPR GDSLIFDHQW ELEKLTRLQN VERMRLFLRL
RQRLKSVNLL GKSSSDEEAT NGIKTPVSPT EPKWPIPNQV TLNDKEAGIV KKILKFVRLH
IPTNKEPPTG NKSGAATDTA YETDTSTFGN STSASSVSFS SGKYTFSHND LVSKVKSRSS
SDLKHLLSPE EIDKLKKSLS FNKLSTVGFY IAEVFEKRVG VVVSKKGYMN FLEEKARGWR
KRWVVVRRPY ILLFNDEKDP VIRGLINLAY ARVEYSEDQQ AMLKVPNTFS VCTNHRGFLM
QTLTSEEMQD WLYAINPLLA GQMKSKHGKQ SDS
//
