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Database: UniProt
Entry: A0A182VT77_9DIPT
LinkDB: A0A182VT77_9DIPT
Original site: A0A182VT77_9DIPT 
ID   A0A182VT77_9DIPT        Unreviewed;      1867 AA.
AC   A0A182VT77;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Kinesin-like protein unc-104 {ECO:0000256|ARBA:ARBA00020751};
OS   Anopheles minimus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=112268 {ECO:0000313|EnsemblMetazoa:AMIN001267-PA, ECO:0000313|Proteomes:UP000075920};
RN   [1] {ECO:0000313|Proteomes:UP000075920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MINIMUS1 {ECO:0000313|Proteomes:UP000075920};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles minimus MINIMUS1.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AMIN001267-PA}
RP   IDENTIFICATION.
RC   STRAIN=MINIMUS1 {ECO:0000313|EnsemblMetazoa:AMIN001267-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR   STRING; 112268.A0A182VT77; -.
DR   EnsemblMetazoa; AMIN001267-RA; AMIN001267-PA; AMIN001267.
DR   VEuPathDB; VectorBase:AMIN001267; -.
DR   OrthoDB; 126886at2759; -.
DR   Proteomes; UP000075920; 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; 1.
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}.
FT   DOMAIN          3..351
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          1717..1815
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          426..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          930..950
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1127..1159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1638..1664
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          359..386
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          653..702
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        930..949
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1142..1158
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         97..104
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1867 AA;  208339 MW;  4B0CBB5A99197606 CRC64;
     MSSVKVAVRV RPFNSREIAR ESKCIIEMSG NTTCITNPKV PPGSSESVKR FNYDYSYWSH
     DPRDLEFSTQ AMVYSDIGEE MLQHSFDGYN VCIFAYGQTG AGKSYTMMGK QEDSQEGVIP
     MICKDLFRRI QETESDDLKY SVEVSYMEIY CERVRDLLNP KNKGNLKVRE HPLLGPYVED
     LSKLAVTSYQ DIHDLIDEGN KARTVAATNM NETSSRSHAV FTIFFTQKRQ DRMTSLETEK
     VSKISLVDLA GSERADSTGA KGTRLKEGAN INKSLTTLGK VISALAEIAS KNKKSKKADF
     IPYRDSVLTW LLRENLGGNS KTAMIAAISP ADINYDETLS TLRYADRAKQ IVCKAVVNED
     ANAKLIRELK EEIQKLRELL KAEGIEVQEG PDGKVVCEKR DANKDECLIK SDKIESVGGV
     VITEEGEDGE KKIHSPNRNR KRTGSSTEMA VDQLQASEKL IAELNETWEE KLKRTEQIRV
     QREAVFAEMG VAVKEDGITV GVFSPKKSPH LVNLNEDPTL SECLLYYIKD GLTRLGTSEA
     NVPQDIQLSG SHILKEHCVF ENKDGVVTLV PHKDALVYVN GRKVIEPEVL QTGSRVILGR
     NHVFRFTHPE QAREKREKNK EVDVCETPGN SGEIADWNFA QCELLEKQGI DLKAEMEKRL
     LALEEQYKRE KRAADQEFEE QRKTYEARID ALQKQVEEQS MTMSMYSSYS PEDFHQEEDI
     FVNPLFESCW TAREAGLAAW AFRKWRYHQF TSLRDDLWGN AIFLKEANAI SVELKKKVQF
     QFTLLTDTLY SPLPPELTPA PAVGALTNGG QEDEFGQTPI PRTIVAVEVT DTKNGATHYW
     SLEKLRYRLE LMRQIYNTSD TSPELMSFVL ELSSGEHTPE HSGTQHPAFA HPPLSVSKQQ
     QDHHVAEQPA AARLLGGLAP NCDGGKCLSS PTNSVASNSS SSCGTASPPS PPSVIFDGDA
     ATSISSCSFG RAGTRLTLAN LMPSRQRLEL MREMYHNEAE LSPTSPDYNV ESLTGGDPFY
     DRFPWFRMVG RSFVYLSNLL YPVPLVHKVA IVNERGDVRG YLRVAVQPVM DEENADFSNG
     VKQSARILFD EEQNGQHKVP KIRTIPDKDE KYIEGGNDMG TKLEELEQED ADSGRGDSSV
     ASELHESNDQ EPGEHLQPGK EFTFRVTVLQ ATGIAAEYAD IFCQFNFLHR HEEAFSTEPV
     KNSGSGAPLG FYHVQNITVP VTKSFIEYLK TQPIVFKVFG HYQHHPLHKD AKQDCQITRP
     PPRRMLPPSI PISQPVRSPK FGPLPCPPSS TVLAKHDVLV WFEICELAPN GEYVPAVVDH
     SDDLPCRGLF LLHQGIQRRI RITIVHEPTP EVKWKDIREL VVGRIRNQPE PADDEDSDSC
     VLSLGLFPGE VLEVPGDDRS FFRFEAAWDS SLHNSALLNR VTQTGEQIYI TLSAYLELDN
     CARPAIITKD LSMIIYGRDA RTGPRSLKHL FSGQYRNPEA NRLSGVYELS LRRASEAGSP
     GVQRRQRRVL DTSSTYVRGE ENLHGWRPRG DSLIFDHQWE LEKLTRLEEV GRVRHLLLLR
     ERLGMDTTPN PTTKTEKDVC NLAQRASASP VHMVIPPSPQ TPVKDQQSPA LPERDLSVRE
     TELVWKCVKL IQGRIGGKEL GADGNGSGTQ ASDASPGDEG CADMNASYIS SNSIELCSPE
     RVDVPNGWEA PAPAPQTQEL SLRLYVPELE EIRVSPVVAR KGYLNVLEHG GSGWKKRWVT
     VRRPYVFIFR SDKDPVERAV LNLATAQVEC SEDQAAMVKV PNTFSVVTKH RGYLLQTLGD
     KEVHDWLYAI NPLLAGQIRS RLARKNISSI SSNGSGAGDQ LQATTGASAL AVAAAQGNGS
     SSSSGGK
//
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