ID A0A0B7NE53_9FUNG Unreviewed; 1752 AA.
AC A0A0B7NE53;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN Name=PARPA_07280.1 scaffold 26887 {ECO:0000313|EMBL:CEP13231.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP13231.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP13231.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP13231.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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; LN729408; CEP13231.1; -; Genomic_DNA.
DR STRING; 35722.A0A0B7NE53; -.
DR OrthoDB; 1342602at2759; -.
DR Proteomes; UP000054107; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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; cd01372; KISc_KIF4; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
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; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR PANTHER; PTHR47969:SF15; ZGC:66125; 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 PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Reference proteome {ECO:0000313|Proteomes:UP000054107}.
FT DOMAIN 5..375
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 242..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1313..1360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1493..1524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1543..1576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1712..1731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 815..860
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 886..998
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1094..1121
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 578..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1075
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1494..1524
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"
SQ SEQUENCE 1752 AA; 196329 MW; 7DC2C7403640475E CRC64;
MTSTAVRVAL RVRPLTQKEQ YSNCTECISF IPNQPQILIG KDHSFTYDYV FDTNSLQQSI
YETSVVPLAE KFVDGFNATI LAYGQTGSGK TFSMGTALDE HTDSEQQGVV PRFIHDLFRR
LDAKKQSQKV LEYQVYVSFL ELYNEDFVDL LNAYSQTHNR KRSNSVSHFA PPPCEVQIRE
DVHGQIYWSG VREEPCSSPD ELLRYLTKGS LCRTTGSTDM NSVSSRSHAI FSVVLKQKVP
DSNNEDAAAS AEQDQAVPTK DTGNSSSNTL VSKFHFVDLA GSERLKRTKA EGNRAREGIS
INSGLLALGN VISALGDESR KSVHIPYRDS KLTRLLQDSL GGNSQTLMMA CVSPSDSNFL
ETLSTLKYAN RARNIKNKVT INQEFAGSSV EVNQLRAQVA RLKLELNALR ATFASSGGMK
STTTSAVTAT DGNVSSSDMM INNMLYNHET VGGGSTAAAK ALKEEIDRLK ARLRSMSDDI
CRITTERDSL QMERELAQHM SSEQWPNLME QLQRRPSSAS LTDPNMPISS LPIISQYQKT
IQSLRSELTD TQERLAFSES IRAPLMHAMA VPPSANATPH ASFRTHAAQQ QQQQHSSTTS
RRRGIGKKRR NLNGSTTTSR NVTFRSTKRS KVPNMPTSVN KNTSSAAVYN KQSSISSSNN
NNSLEDDNEQ DLQEWLKATM GSIQTSESSG LRIDAKNSIS NARSQIDKAL KVLDEFKIKE
PESEQPEANQ VEYDCDLLND DELFIKLQSD DIQSLFGDLE EQEPQDDETC AKAPRYRMAS
TETMMTDDND LAELYESNPQ LHRMLNQIQS DIQVNEDLVL QLEKTEVEYS QMRKKFEKKL
FSLRDEILSL RQQQQQQKKE ALASTTTTAT TTTTTTAAAY NMNSIRHAYE AKMKNLMNQL
SELRRKYSQT SSTMQSSRNQ NENMLRALRV NVESLKVEKR RMIKRMKDEA ERVKEKLHNH
EREIQQLRRK QTKDNEIKKK LEREVKQMQL VIGKKTDESV VTAEKLKSLV KILKKAVREG
GVLDEKLLAS CGSLLDIGSA LVQSSRVGRM SRNRRNNSNH QRRRQQEHQG VPAEVRAGKK
KALLDNALYQ LIQGKQAVEE MKQLLAKRND LSQRKIEYQS ERELLVLDQD TKDLSSIDNA
FRQVIDENIE TVEAEISYIN ARIHAIHNDA AAEIMQEDEN DEEIIDIGSV VSHKKRRVTF
QEELEEEHEE DNWHDMDALE ERYSLPASAG PEQSLEMISK IFKSLADDEA KYVMETVIDD
IVLLRMEEHN NKMSIQQLEK TTQDLRRTLI VMKKAAIETT IENEKKLKRL SLQQAGGGAG
SSHASGSGSS RRTSMSRECS SSKMSCRSSP TNEDSSDADS AIDLHNEDQY QHVETMFEKI
YTDGLSGKMP TYDYGVAMAE ATAPVLMAEN ELSPYLRPRP VTALAGSKMI SADKHGVPVQ
APMKPSTSPL VSRRRDSMSS PEQFLLQFLQ TPKDVRPAPP SSPLMKPAEF ARYQQDRESS
TNSLARNNSR NFSAVPRRSS LQSDNGSYCS LYSSNHGYSQ QMIRASSGGG VGGGKLASNN
EPFHNHAPPP PQPATTILNR RRAFSFQQPP SPTPQAAPTS TVRRRSLLRE LTNNEPDQTL
VHSTNKHHFD YSNHGTALIP TFSSHNHSAA NISSNARPHS VLAFHAAAAA STPRPVSSKA
AVYPSARRES PNNSYELRKS AVANNVFDRL SSGHTHASQA KKRLGGYQRY SSSSIDDLRM
QWANELSERN ED
//
