ID A0A139IE14_9PEZI Unreviewed; 1074 AA.
AC A0A139IE14;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN ORFNames=AC579_4044 {ECO:0000313|EMBL:KXT12960.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT12960.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXT12960.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT12960.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) 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}.
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:KXT12960.1}.
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DR EMBL; LFZO01000134; KXT12960.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139IE14; -.
DR STRING; 113226.A0A139IE14; -.
DR Proteomes; UP000073492; 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 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 InterPro; IPR031852; Vik1/Cik1_MT-bd.
DR PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR PANTHER; PTHR47972:SF28; PROTEIN CLARET SEGREGATIONAL; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16796; Microtub_bd; 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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Coiled coil {ECO:0000256|SAM:Coils};
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:UP000073492}.
FT DOMAIN 683..1066
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 600..666
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 24..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 776..783
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1074 AA; 118020 MW; 144CF654A6039383 CRC64;
MERPQSQLEN VRPSGLKPPS RLPALSGNNA SRTLQETTSS DLNARTASGN GNGNGPAAAP
TNAYSYGHAI VPSKHKVYGL PEPPTKRKTL AERAAEPLRS HIPSKSSISS GFGSRPKTNL
DYYRNPANTA ISSSTNAARP NSRQANGVPR YPAPRAVKSS LNLHAQAQYD DQESDGETSV
VGRRDGTPVL SFNHHAASNG NSLHIRKTRT HSNLRQQNSL QSQSASARSQ HLSTAIASDC
RDSSASSAQS SRQSSNSSSS SSTSTSTAPT QQDTMQPGGP VGARKPSREV SLSAAFAGLS
LTPRLNSVSR HRPSLESIME EKSPSKIPKF ACAPQASLRH TQSAQVLRTP SPLKQKQSIA
GLRTPVSNTR HREVMPVFLT KEALTPVAAF DTNVRLDSME KMFNSLKSDM AKANDSKEAI
ETSLELYKTQ AAELQAEKRD LASQCKSLSS DLERARTELH TTSTDLRQVR RDHERELHDL
ERKHDKELAD LRFKQEREES RVEREREKEA DRLRKEMEEA KSAWEKEKDR EISDMATQHW
DELDQIKTAQ EKELSDLRAK VHELEEAGES RATESAFEVQ LLRDTVASTQ SQLDASNATI
ASLMSRITTF EARISTLEQE KNSLISKAHF LEGNQEAQSQ EFTVMQQKME EAIAVKEATV
ETLRKEEALR RKLNAMILEL RGNIRVFVRT RPLLKGEDDP AKVEYLDQDS LEGCKEMVVH
APTTQTATGK QRNEKHQYDF DRVFTPGTPN PTVFEECRDL IQSVVDGYNV SILSYGQTGS
GKTYGMTGPE GIIPSSIRML LSEMGRLKEK GWEYAVEANF VEVYNETLND LLGDAKTWDD
TDDLGASVRG KKKEKHEIHH DAATGKTTVT NLTTIGLWPP PNDDGNWPPP APVDTDGEDG
ELAVSYTEKA VTNLLDTAAK NRRVAATKAN ERSSRSHSIF MLTLKGSCPA SGEHSEGVLN
LVDLAGSERL KQSGAEGSRM KETQAINKSL SSLGDVIAAL ANKSGNSEAH VPYRNSKLTY
LLQSSLGGTT AGKSSRTLML LHLSPLQAHW QESRSSLLFG SKVHGTHIGT AKKR
//
