ID A1C771_ASPCL Unreviewed; 1633 AA.
AC A1C771;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Kinesin-like protein unc-104 {ECO:0000256|ARBA:ARBA00020751};
GN ORFNames=ACLA_072750 {ECO:0000313|EMBL:EAW14242.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW14242.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW14242.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027045; EAW14242.1; -; Genomic_DNA.
DR RefSeq; XP_001275668.1; XM_001275667.1.
DR STRING; 344612.A1C771; -.
DR EnsemblFungi; EAW14242; EAW14242; ACLA_072750.
DR GeneID; 4708099; -.
DR KEGG; act:ACLA_072750; -.
DR VEuPathDB; FungiDB:ACLA_072750; -.
DR eggNOG; KOG0245; Eukaryota.
DR HOGENOM; CLU_001485_20_2_1; -.
DR OMA; RIDKPKR; -.
DR OrthoDB; 126886at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; 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; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
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:UP000006701};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 8..362
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1514..1621
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 40..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1415..1435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1474..1494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1417..1431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1478..1493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 111..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1633 AA; 182898 MW; 966E04558C3F6724 CRC64;
MAPGGGGNIK VVVRVRPFNS REIDRGAKCI VQMKGNQTVL VPPPGADEKS RKAGGKGAAE
GPKAFAFDRS YWSFDKNAPN YAGQDNLFAD LGVPLLDNAF QGYNNCIFAY GQTGSGKSYS
MMGYGKEYGV IPRICQEMFQ RIAKIQEDKN LNCTVEVSYL EIYNERVRDL LNPSNKGNLK
VREHPSTGPY VEDLAKLAVR SFSEIDNLMD EGNKARTVAA TNMNETSSRS HAVFTLTLTQ
KRHDAETSMD TEKVSRISLV DLAGSERANS TGATGARLKE GAEINRSLST LGRVIAALAD
VASGKKKNAS MVPYRDSILT WLLKDSLGGN SMTAMIAAIS PADINFDETL STLRYADSAK
RIKNHAVVNE DPNARMIREL KEELAQLRAK LGGGTTAGAG GAAMPAEESY PPDTPLEKQM
VSIQKADGTV TKVSKAEIVE QLNQSEKLYK DLNQTWEEKL EKTEQIHRER EAALEELGIS
IEKGFVGLST PKKMPHLVNL SDDPLLAECL VYNIKPGTTT VGNMEQGSHV EIRLNGSKIL
PNHCTFENMD NVVTIVPSEG AVVMVNGLRI VEPKRLKSGF RIILGDFHIF RFNHPQEARA
ERVEQSLLRH SVTTSQLGSP APVRTHDRTM SKTGSELDGD SSRADSPTSA QRARESDWFY
ARREAVSAVL GPDHISHMPD DELDALFEDV QKVRATRRGL VENEEDSDSL SSYPVRDKYM
SNGTIDNFSL DTAITMPGTP GQQDYGEGQD GNDFTLQAAR QEMQRQLDMQ KEEFKEKLRD
DEASEQGGED LRSEKARMEE ALRTAKEEYE EQLRKQKEAF ENHMKEMGQP VPRIYENGFA
KLDEREIGIA NSVFQHWSQQ NYVRMAEKIL QHASLVKEAQ VMSQIMDKNV SFQFAIIDHG
NNMASSYDLV LNGISGDEDI VLEEAKKPCI AVRVIDFKQC VIHLWSIEKL QRRLQAMRQL
HQYIDRPDYI QHFRLENPFS EPCSPQYSLV GDADIPLTAV FETRVQDFSV EVVSPYTQNV
IGIVRLSLEP SSAQAPSSTL KFNVVMRDMI GFAEWEGTEV HAQLFVPGIS EEGGATTTQM
ISGFDESPIR FESVHSMSLP LSSPRTAALK ICVYARVTHM HLDKLLSWDE MRDSAELPPQ
RRKTPRIAES EFFSEERHDV FARMQVLELA ESGEYLPVEV VQSNSLDAGT YQLHQGLQRR
IFVNLTYSST ESLPWDDLTN MRVGSVRLLD PWGKIPDQDL QTPDVHLKFV HEPMTKDNAD
GTSHVTLIAQ WDSSLHGSLL LDRVTAEKYR VQVTVRWDLV SSRLQDPVPF EVDLTLQIQG
RTYVRPQSMF KQLFNSTRIV HSTVRMFSLA VRPVSAKRAA DLWRMNTQND YVKGEELLTR
WSPRKVSLVR DYIAARKRRR RLAELNAAKG ALSANSLVPS PARSGRSTPL RSQELNERRT
KILRKYLDLW ATKTDPIDAI LVRSNTEPPA NGAAFATRAK QASPSSDDGS SVSDQELLRP
RFVATIQTLP KNQTSLKSGY LLTPDDTNSH WVRRFVELRR PYLHIYSVPE GDEINAINLR
SSRVDHEPDF ARLLAGADNG MSTKGRPHVF AIYGTQNTFL FAARTEAQKV EWILKIDESY
FSNSASRASL NGN
//
