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Database: UniProt
Entry: A0A167MGT5_PHYB8
LinkDB: A0A167MGT5_PHYB8
Original site: A0A167MGT5_PHYB8 
ID   A0A167MGT5_PHYB8        Unreviewed;      1400 AA.
AC   A0A167MGT5;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Kinesin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=PHYBLDRAFT_95995 {ECO:0000313|EMBL:OAD72799.1};
OS   Phycomyces blakesleeanus (strain ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC
OS   33097 / NRRL 1555).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Phycomycetaceae; Phycomyces.
OX   NCBI_TaxID=763407 {ECO:0000313|EMBL:OAD72799.1, ECO:0000313|Proteomes:UP000077315};
RN   [1] {ECO:0000313|Proteomes:UP000077315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 1555(-) {ECO:0000313|Proteomes:UP000077315};
RG   DOE Joint Genome Institute;
RA   Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA   Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA   Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA   Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA   Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA   Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA   McCluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA   Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA   Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA   Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA   Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA   De vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA   Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA   Gabaldon T., Grigoriev I.V.;
RT   "Expansion of signal transduction pathways in fungi by whole-genome
RT   duplication.";
RL   Submitted (JUN-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}.
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DR   EMBL; KV440982; OAD72799.1; -; Genomic_DNA.
DR   RefSeq; XP_018290839.1; XM_018443941.1.
DR   STRING; 763407.A0A167MGT5; -.
DR   GeneID; 29004846; -.
DR   VEuPathDB; FungiDB:PHYBL_95995; -.
DR   InParanoid; A0A167MGT5; -.
DR   OrthoDB; 1360435at2759; -.
DR   Proteomes; UP000077315; 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   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 6.10.250.2520; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 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; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR47117:SF6; KINESIN-LIKE PROTEIN KIF1C ISOFORM X1; 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   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00240; FHA; 1.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 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};
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:UP000077315}.
FT   DOMAIN          1..347
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          486..537
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
FT   REGION          566..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          657..694
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1121..1153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          712..754
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        657..672
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        673..694
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         84..91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OAD72799.1"
FT   NON_TER         1400
FT                   /evidence="ECO:0000313|EMBL:OAD72799.1"
SQ   SEQUENCE   1400 AA;  157878 MW;  31B2EA38EAFF5BB1 CRC64;
     HSEIARGATC LIRMDGDQTI ITKPSLAGQP KEEDTKAFTF DRSYWSADKN DPNFATQKTV
     YNDLGRELLD HAFHGYNCCI FAYGQTGSGK SYSMMGYGKD KGIIPLTCSE LFDRIAESTT
     DVLSFQVEVS YIEIYNEKVR DLLNPSNKSN LKVREHPSLG PYVEDLSRLA VKSFEDISHL
     MNEGNKARTV AATNMNETSS RSHAVFTIFL TSARYDETAK LSTEKVARIR CVGKVIPILI
     SSLVDLAGSE RADSTGATGM RLKEGANINK SLTTLGKVIS SLAEHGDTKK GKKSKEAFVP
     YRDSVLTWLL KDSLGGNSKT AMIAAISPAD YEETLSTLRY ADQAKKIKNK AVVNEDPNAK
     LIRELKEELQ ALRDTLMVYA PDEVDRIIVF TDASGHTQHL TREEVVDQLQ TAEKLLNQVN
     RTWEEKLHST ETIHQDREKA LEELGVMVEK NNMGVYTPKS VPHLVNLNED PLMTECLVYQ
     LKPGKTRVGR LDSTIPAEIR LSGPNIKDNH CFFEHNDGIV TLYPDEGSMT MVNGMRISDS
     KRLHSGFRVI LGDYHVFRFN HPEEARRERD LQQRTTGSAA GLEPGSSQAL DMMCRPVSPS
     ASSMREMAQS PEVVDWGFAR REAVLNYYSA ESNLGGLTDE DLEKLFDDVF RIRQSRKKRF
     DGRSEADPDD ETLSRTSTSS SARPSHGQST VFGEDQSVSS LYLDTSTMTP NRDDLLRQVK
     EEMQQQLDLQ KQAFEEKIKL LESVRAEMER MMDQQRYAYE SKIKRIAMHL PPGTSLQSPT
     LPSVATEHET ILIYQTFLKW KSLRYVWMAE TIMSHAALLK EANVISKELN KNVIYQFFVL
     HDHASVNPVS FWESGSELQP KGGGRLSRLS SETMPCVGVL VVDRKHEVTY VWSIEETQAR
     LVRMRSLYDF TERPLENNES LTEQQDPFYE SPCPRYSLLG LAKVPIQNLA FQVPVESMVD
     VVCRHSGHVL GHLRVLITPI ARSMARRAGN SQLTLPLSRQ SSRDSHQERF LHVGQQQVFE
     VRIISLDGLS ESDATQVHAQ FRLSSFGNIE PNSPVDRIYA TDPISGFGTL PIDFHYAQTL
     STTVTADMLE VITTKTLTVE IHGHLQSHFL RNMVQQSVER EELASPVATR PRMTLEPIPP
     AHSRRPSDSP EDGQIREEVH DIVAWVKICE LEAEGEYEPV RVVYDSNNNN PKKSDGGGVF
     SLRQGLQRRI SLSLMHASGR KLRWEAIEEM SIGNVRLLNS KGQEIAPAVH SDVPVYLFAE
     QELVYHSNGT STLSAQGPWD SSLHNSLYLN RVSPDNQLVL LSLSWKVNCS SQCTVPIKFS
     MDLAVMIQER DARLTAAVFS FLRSQRILRK MSAIFVLKLH PPMSRKLKDL WRLNTTHRYV
     RGEELLGPWR PRGVSLVHEY
//
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