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Database: UniProt
Entry: G2WQK5_VERDV
LinkDB: G2WQK5_VERDV
Original site: G2WQK5_VERDV 
ID   G2WQK5_VERDV            Unreviewed;      1329 AA.
AC   G2WQK5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Inner centromere protein {ECO:0000313|EMBL:EGY13965.1};
GN   ORFNames=VDAG_00647 {ECO:0000313|EMBL:EGY13965.1};
OS   Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS   (Verticillium wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY13965.1, ECO:0000313|Proteomes:UP000001611};
RN   [1] {ECO:0000313|Proteomes:UP000001611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VdLs.17 / ATCC MYA-4575 / FGSC 10137
RC   {ECO:0000313|Proteomes:UP000001611};
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(2011).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000256|ARBA:ARBA00004186}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the INCENP family.
CC       {ECO:0000256|ARBA:ARBA00010042}.
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DR   EMBL; DS572695; EGY13965.1; -; Genomic_DNA.
DR   RefSeq; XP_009650319.1; XM_009652024.1.
DR   STRING; 498257.G2WQK5; -.
DR   EnsemblFungi; EGY13965; EGY13965; VDAG_00647.
DR   GeneID; 20702110; -.
DR   KEGG; vda:VDAG_00647; -.
DR   eggNOG; ENOG502S0AD; Eukaryota.
DR   HOGENOM; CLU_003318_1_0_1; -.
DR   InParanoid; G2WQK5; -.
DR   OMA; PVPKWAQ; -.
DR   OrthoDB; 1368690at2759; -.
DR   Proteomes; UP000001611; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR   InterPro; IPR005635; Inner_centromere_prot_ARK-bd.
DR   PANTHER; PTHR13142; INNER CENTROMERE PROTEIN; 1.
DR   PANTHER; PTHR13142:SF1; INNER CENTROMERE PROTEIN; 1.
DR   Pfam; PF03941; INCENP_ARK-bind; 1.
PE   3: Inferred from homology;
KW   Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001611}.
FT   DOMAIN          1220..1274
FT                   /note="Inner centromere protein ARK-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03941"
FT   REGION          92..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          422..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          534..574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          602..631
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          692..1240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..130
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..225
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..283
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..309
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        348..373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..441
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..511
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        544..573
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        692..715
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        716..780
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        858..923
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        931..991
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1024..1056
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1080..1098
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1099..1114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1145..1185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1218..1235
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1329 AA;  144378 MW;  E7167F76D3F75D5D CRC64;
     MAAMRGARVP VGSATWIAGE RSSAEDIVKT ETEEFSYSVR NEFDWLNEHM ADVFNENAIN
     VAEMFKTPGK LRGKTPRTAR KVITGEPRVP LSDIFSSASK GAPTPFTQQL GRLQSPRLQA
     SSSRSPLANK TASPLRPLPS MRPQPTKNAA LPTDSGYYGS QSQDVMDVDH HVHATQSTQP
     FSPVREADTN EDVAFHVDEP STHESPTVTK TMQSPTMTFQ TAREEQTTRV LKDVTQKMAS
     PVPNPSPARS PAKQTSTYPV ISPPSRFAHS SSPKKSSPLK TSPAKNFDEP MSDAPSENHS
     PNADEARSPS EGSSPIRPVV RKRSLNFASL PAREPLTHKK SLGARQSRPS HDSRQSYLGR
     HTGGKSLSNV DILSSTDDED EYQDGMELGG IIAGTHKTTN DEVFADNHNK VYTQRLQDQI
     SLLGKSQPNA SRPSKSIPSS AVLQAAAAVA SAPEVKEKTP EKSPAKTPSR SSPKKQAAPP
     TPGAFPDDDD EEEEWIAPPA VPEKDHIESS PRPALPKSYT ADIMEGIHGM DSVSGAEFVL
     PKQRQAGSRS TSPQRGPVVP ERTTSTLGHT KSASVSVLPE LGMASGPAGV NSPLKAISVS
     NPALTSVSET GRPQTPKSPS RSFRDSPLKQ VKNKLSSIIK SSRGLLASSA AISAEGKSLL
     SPSSTRLGFH ADPSASSLAT LATTADSLYP DLSQRATNDA PVVSSSGSPT RPVAKRTRSS
     TEREKEEKRK EKETQKEARL MNEQMDKLEK AREKEREKAR VFSKEQERIA AFEKKVAAQK
     EQEVAQTPAP KQEKPTRTSP RKTKAQLEAA AKAAAEEDAD MNDAPGSMAP PSVPRSAGPG
     QASRAREVRR PLKPTKETAT KSRQAPTVIR VNTGSQHSQY HPSNSSLSSN LHDTLGTSQP
     QLKSKASSAS LQQKPSLSSL RGSTAGRPKA LELAAKRKEV EEKEAQRKRD AKAEIERKRA
     ALQEEERRQE QQKRLEAEKQ KAKEREQAAS QAEAKKNAAR QAAIERAKQT RAPPPAVRAQ
     PTGPPDYNTG SDKAAASSQP PRPVSRMNTA SQRPQEDLGR PVSAVLNQGA KAPPKRPLQQ
     ETNDGASRHP QARNGPSYQS KDSKRRRTSD DFFDELDMDS QPPNIKGPPV RPSGGLKKDM
     SNKSMFSAGY ANVPPQSASR DLFKATVTAQ HHSAVKSTQP MDMSQRRPGP QGAAGAKSAA
     KSATRSSPRF QNGESIELPE IDTDDEDEEE DDANFGAAAW VDSPELRRAL TRQETMDPSQ
     IFGPPAPLVM EEVFSKSKDR WHKFRARTSS ANWSGTDRLT EDEIRKDLVA RDRMRKDGAW
     TFEMSKDLA
//
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