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Database: UniProt
Entry: A0A0V1NNV0_9BILA
LinkDB: A0A0V1NNV0_9BILA
Original site: A0A0V1NNV0_9BILA 
ID   A0A0V1NNV0_9BILA        Unreviewed;      1538 AA.
AC   A0A0V1NNV0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Kinesin-like protein KIF14 {ECO:0000313|EMBL:KRZ85703.1};
GN   Name=pdhk-2 {ECO:0000313|EMBL:KRZ85703.1};
GN   ORFNames=T08_8158 {ECO:0000313|EMBL:KRZ85703.1};
OS   Trichinella sp. T8.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ85703.1, ECO:0000313|Proteomes:UP000054924};
RN   [1] {ECO:0000313|EMBL:KRZ85703.1, ECO:0000313|Proteomes:UP000054924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS272 {ECO:0000313|EMBL:KRZ85703.1};
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:KRZ85703.1}.
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DR   EMBL; JYDM01000135; KRZ85703.1; -; Genomic_DNA.
DR   Proteomes; UP000054924; Unassembled WGS sequence.
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; cd00106; KISc; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR027640; Kinesin-like_fam.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR24115; KINESIN-RELATED; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 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|ARBA:ARBA00023054};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
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:UP000054924}.
FT   DOMAIN          94..412
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          30..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          785..822
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         178..185
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1538 AA;  173097 MW;  0489405AC86B6DCF CRC64;
     MEKSRRFFPP LSTPDLPKKF FSNPFSECRE KVTTPSKNGK PYNGKTESLS SGEKALTNNA
     EITDDSCNLS IIDEVGSLQS NIGSTEDNLE NRSRICVAIR VRPVLETDPD KMPYCNRVVH
     VNQKLSSIRI MKGKVGQEFK FSHCFDSHSQ QEDIFNELSE PLITQLLRGI NCTLMAYGQT
     GSGKTYSMMG SSTKPGIIPR ICEKLKIRLC ENEPEILSKL KMSYYEIYNE KIYDLLANGD
     KSCSLKVRED PKTGAFVDGL RAVEVDKNAD ILHLIAVGNK RRMMAATRNN NHSSRSHVIL
     SLKLVQNDSS NKILYSLLNL VDLAGSESGA TSERLDETSS INKSLHCLGR VIQQLRDGSA
     HISYRDSVLT RLLKESLGGN ALTTLLATVT PLHAHIEQTL NTLRYANFAR EVVNYVQINE
     ASTVNENQLV TAMLQSKLEY EHKIKELHML LRMYKNNAVG QMNCDFESVS DTTVISEKTL
     TGDSITSLTA ESELDVEVLD SPYLLWLSCE SDLNFSAISL PLKFGSNKIG CDSAVDIVVE
     GTMLSGVECT VFRSVEDAIH VVPEIGKELY VNGKQVTTLT MLNYGDRLCL AGEHFLKLCS
     MNTVPKLNSG ELQDAKLEFL MSQNQRLILQ LANAAAHDVR EEIKETDVNN TPSNANFATQ
     TDSVENFQMV NKPLKFDFSH LLNHNLNALF DLELFVREAN YLCKCWNVPY SYTVQCDPGF
     ESEIPTLTVV MHNDIMKTDV DLSADYFSEN WLILRSLQQS KKRSKFNDQM AKMFYQAKSG
     ESVHQHQMPD PQIQSQSETA TWEQSSENGT SESASILSEP SEQNRIVASE TWDSFAERNS
     KNCTNSKTIL DWFLLSARNF HGLLVNLLKD NESEGCYLSK RKKGQLLVGF QNLHIYGQVM
     AEMPNSFPES AFLIGQLDAA MNNCFAALLT FIQVIKNDEF VTNDKVNSVI RMLLKVFETV
     GCLSFVLPTV GASHTFKGDC SNCKLSESLY GALFKGLYSG FKKMAAVVGN MLDGENSHVQ
     RGQRETLRRM CLFNSIEKLR RVLKECKRNS EYTNQAICNT AFRIIRPMMH SVSSTAGFSD
     PAFRAEAVFN LGQLALDLEK LHFRLLLILS ICCPVELFSC GAVPTLDDVT SFMLVFYAES
     VEGLFLDCIG VLIPSRNSTS HTDIAITSRY CLQHENIENT KVMTYVSFNH GYETGFINKI
     SDIYVPNKND TNRAKWQPPP NIAIIKLRMP IAFNHNVQPI CLPEVNEMIT FEHRCFYYRF
     SRIGFTVSYF MPLGLKLLPH EYCKMLIGSS RLDSLTQLCC EERNLFSTLH TEFMYNMVPD
     GSSLICRKHG IFYFFGVQDW MWFPKPRSHT RPIIIFTAIS AFTDSSYCGR SGLAGGVLAY
     TVAFFGEAEG RMFVDCIGLL VPSSNSSYSD TVVTSRYCVQ FKFYYVGGAK ITFIPISMRQ
     ITDEQCKSII GNSRKDNVSQ MCFEEQGPFA LLNAEFSAAM IPTGFPLICV KHELSYLYGI
     QDWLRFPKPG ENLKPIAIFT ATSPFSFRIN RFINETSF
//
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