ID A0A401L8F4_ASPAW Unreviewed; 1641 AA.
AC A0A401L8F4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Kinesin-like protein KIF1C {ECO:0000313|EMBL:GCB27782.1};
GN ORFNames=AAWM_10667 {ECO:0000313|EMBL:GCB27782.1};
OS Aspergillus awamori (Black koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=105351 {ECO:0000313|EMBL:GCB27782.1, ECO:0000313|Proteomes:UP000286921};
RN [1] {ECO:0000313|EMBL:GCB27782.1, ECO:0000313|Proteomes:UP000286921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 58123 {ECO:0000313|EMBL:GCB27782.1,
RC ECO:0000313|Proteomes:UP000286921};
RA Kusuya Y., Shimizu M., Takahashi H., Yaguchi T.;
RT "Aspergillus awamori IFM 58123T.";
RL Submitted (SEP-2016) 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:GCB27782.1}.
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DR EMBL; BDHI01000029; GCB27782.1; -; Genomic_DNA.
DR STRING; 105351.A0A401L8F4; -.
DR Proteomes; UP000286921; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; 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; 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; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR PANTHER; PTHR47117:SF1; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF12473; DUF3694; 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; 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}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
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:UP000286921};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 6..361
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1516..1628
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 36..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1419..1440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1471..1497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..781
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1480..1495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 110..117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1641 AA; 182823 MW; 76D8A313BAAFCA3A CRC64;
MAGGGNIKVV VRVRPFNSRE IDRGAKCIVQ MKDNQTVLST PPGADDKARK AGGGKGADGG
PKSFAFDRSY WSFDKNAPNY ASQDNLFLDL GVPLLDNAFQ GYNNCIFAYG QTGSGKSYSM
MGYGKEYGVI PRICQDMFER IHSIQQDKNL GCTVEVSYLE IYNERVRDLL NPSNKGNLKV
REHPSTGPYV EDLAKLVVRS FEEIENLMDE GNKARTVAAT NMNETSSRSH AVFTLTLTQK
RHDAETSMDT EKVSRISLVD LAGSERANST GATGARLKEG AEINRSLSTL GRVIAALADV
AAGKKKNASM VPYRDSILTW LLKDSLGGNS MTAMIAAISP ADINFEETLS TLRYADSAKR
IKNHAVVNED PNARMIRELK EELAQLRSKL GGGAAGPGAG SAAGAIPAEE YYPPDTPLEK
QLVSIQQPDG SITKVSKAEI VEQLNQSEKL YKDLNQTWEE KLAKTEEIHK ERESALEELG
ISIEKGFIGL STPKKMPHLV NLSDDPLLAE CLVYNIKPGT TIVGNMDQGS HVEIRLNGSK
ILDDHCRFEN VDNVVTIIPT EGAAVMVNGL RIDKPKRLKS GFRIILGDFH IFRFNHPQEA
RAERVEQSLL RHSVTTSQLG SPAPNKTHDR TLSKTGSEVD GDSSRADSPM PSQRGRESDW
FYARREAVSA VLGPDQISHM PDDELDALFE DVQKVRATRR GLMENEEDSD SLSSFPVRDK
YMSNGTIDNF SLDTAITMPG TPHPNDENDG QNGGEATLQS VRQDMQRQLD RQKEEYQDKL
RNAEASSTQG VDDLRSEKAR MEEALRTAKE EFEEQLKKQK EAFESHMKDL GQPVPKIYEN
GFAKLDDREL EVAKTVYRHW SQQNYVRMAE KVLQHASLLK EAQVMSHIMD KNVVFQFAII
DHGHNMASSY DLVLNGISGD EDVVLDEAKK PCVAVRVIDF KQCVIHLWSI EKLQRRVQAM
RQLHQYIDRP DYIQHFKLEN PFSEPCSPQY SLVGDADIPL TAVFETRVQD VSVEVTSPYT
QNVIGIIRLS LEPSSAQAPS STLKFNVVMR DMVGFAEWEG SDVHAQLFVP GISDEGGATT
TQMITGFDES PVRFESVHSM SLPLSSPRTA ALKICVYAKV TQMHLDKLLS WDDMRDSAEP
APKKRKTPRI AETEFYSEER HDVFARAQVL ELAESGEYLP VEVVQSNSLD AGTYQLHQGL
QRRVLVNLTY SSTESLPWDN ITNIRVGSVR LLDPWGKIPD QDLQTPDVAL KFVQEPNVKE
NADGTSNITI IGQWDSSLHG SLLLDRVTAD KYRVQVTLRW DLLSSRLQDP VPFEIDLTLQ
IQGRTYVRPQ SMFKQFFNST RIVHSTVRMF SLVVRPVSAK RAADLWRMNT QNDYVKGEEL
LITWAPRKVS LVRDYIAARK RRRRVAELNA AKGALSANSL VASPPRSGRS TPLRSQERAD
RRAKLLQKYV DLWGKKTDPI EAILVRSNTE PPAGGAAFAS RAKQSSSSDD GSSVQDEASL
KPRFVASVQA LPKNDSSLKS GYLLTPDDTN SHWVRRFVEL RRPYLHIYSV PDGDEINAIN
LRNSRVDHAP DFARLLDGPG AAGSDRGSSP RGRPNVFAVY GAQNTFLFAA RTEAQKVEWI
LKIDESYFSS PGARAMANHN A
//
