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Database: UniProt
Entry: A0A0G4MG18_9PEZI
LinkDB: A0A0G4MG18_9PEZI
Original site: A0A0G4MG18_9PEZI 
ID   A0A0G4MG18_9PEZI        Unreviewed;      1762 AA.
AC   A0A0G4MG18;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
DE   Flags: Fragment;
GN   ORFNames=BN1708_016233 {ECO:0000313|EMBL:CRK33152.1};
OS   Verticillium longisporum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK33152.1, ECO:0000313|Proteomes:UP000044602};
RN   [1] {ECO:0000313|EMBL:CRK33152.1, ECO:0000313|Proteomes:UP000044602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VL1 {ECO:0000313|EMBL:CRK33152.1};
RA   Wang D.B., Wang M.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CVQH01022472; CRK33152.1; -; Genomic_DNA.
DR   STRING; 100787.A0A0G4MG18; -.
DR   OrthoDB; 5479089at2759; -.
DR   Proteomes; UP000044602; Unassembled WGS sequence.
DR   GO; GO:0000776; C:kinetochore; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IEA:InterPro.
DR   CDD; cd05154; ACAD10_11_N-like; 1.
DR   Gene3D; 1.25.40.930; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR041726; ACAD10_11_N.
DR   InterPro; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR015661; Bub1/Mad3.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR012572; Mad3/Bub1_II.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR14030:SF4; BUB1 KINASE, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR14030; MITOTIC CHECKPOINT SERINE/THREONINE-PROTEIN KINASE BUB1; 1.
DR   Pfam; PF01636; APH; 1.
DR   Pfam; PF08171; Mad3_BUB1_II; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000044602}.
FT   DOMAIN          1036..1356
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          271..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          314..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          532..798
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1457..1735
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..598
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..615
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        630..650
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        659..680
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        687..709
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        751..768
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1464..1485
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1487..1502
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1517..1537
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1538..1567
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1577..1595
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1637..1654
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1700..1714
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1762
FT                   /evidence="ECO:0000313|EMBL:CRK33152.1"
SQ   SEQUENCE   1762 AA;  195962 MW;  C45A17E6D2A406A8 CRC64;
     MPSIPRATLN NPDPQSQPDP GDRSHLPVSI VSDPPPPPAT CISIFVVDTR TEPTMAGRVR
     QPIDQKSLER YIEQNVPEIK VPVDLKQFGF GQSNPTYQLT AADGQRYVLR KKPPGKLLSK
     AAHKVEREYR IIHALETTDV PVPRAYCLCE DDTVIGTPFY IMEFLDGRIL EDAAMPGLGA
     DERRALWHAA VDTLARLHRV RPADVGLASF GRATGFYDRQ IQTLALFYEE YAAWLEGAGR
     WAQAEEVYKL GIERGARPEQ RLMRKFNEFE QRQAAQGPEA TGAPSSPALP AMRPALAAKV
     DPYAAAAAAA AAAENPQAPQ PGQGVGGQTA KPGKAKMSIF SDASAEPSAL SARPASSEGW
     DTIDSLANRK KENVMQAKPW VGETMKAGGK KSSAPKMQIF KDTSKPKVAE THTLVPSTEQ
     VVVNPVSGKR ERVFVDLEAV YPAPELPGSE LSFEEVWAMN RGWLDHSWEE DVMMDTLPED
     DVENLGHMVK EKLTVYTETV TLDENGNIQK KGKSKKMKTM EFNETQIIKA NLDSPSKPTK
     LKKRNATAEP TMTLHTKAAT DDIYEIFSQP LKPTQPLEDE EEDEDESDED DYETDGDGDY
     TSGAESTITT TRQVDTSEAG EDDDDEPSDV KSVSEWSDFS TRRHVPDLNE DDEVEESNDT
     QVSNLIDINE DENSLPSSRE PTGPREEDEQ EPDDFYEEDD DVDDDLQTPI EEDYPPRTQT
     VFVPIPPEDY EPRTRPYRDP VEAANNRLPF MTPITERTES SLGVLTARRP QMSPTKKDDN
     EESDDDDGAR ADQLFSSPLR EIYNDAQPTR VPQPILEKPK PKPLGVKTIP PKGPVITDPQ
     CNPVDDVVRK EILAKMHPPL SSYAGFFDHQ AEKHGKGSEI RKVAKLMAKA RSSGERTSNA
     FSVVEVEFPD TPTTYTIRKE LGAGAFAPVY LVENSTADQE DEDQENNGVA VMGRGAFAVR
     QRSTLEALKM EQPPTKMHPP LSSYAGFFDH QAEKHGKGSE IRKAAKLMAK ARSSGERTSN
     AFSVVEVEFP DTPTTYTIRK ELGAGAFAPV YLVENSTADQ EVEDQENNGA AVMGKGAFAV
     RQRGTLEALK MEQPPSAWEF HMIRLAHSRV GPQHRAAASL TYAHEMHLYQ DEGFLLLPLH
     PHGSLLDVVN LFRAEPSAVM DEQLGMFFTI ELMRTIEALH ARGLLHGDLK PDNCLLRLDN
     GDAANAAPLA TQYRADGTGG WAARGVVLID FGRGIDMRNF GPDTQFVADW KTGAHDCAEM
     REGRPWTWQI DYHGLAGVIY CLLFGRYIET SKPKVAETHT LVPSTEQVVV NPVSGKRERV
     FVDLEAVYPA PELPGSELSF EEVWAMNRGW LDHSWEDHVM MDPLPEDEVE NLGHMVKEKL
     TVYTETVTLD ENGNIQKKGK SKKTRTMEFN ETQIIKANLD SPSKPTKLKK RNATAEPTMT
     LHTKAATDDI YEIFNQPLKP TQPLEDEEEE EDESDEDDYE TDGDGDYTSG AESTITTTRQ
     VDTSEAGEDD DDEPSDVKSV SEWSDFSTRR HVPDINEGNQ VDESNDTQVS NLIDINEDEN
     SLPSSRDPTG SREEDEQEPS DLYEEDDDVD DDLQTPIEDY PPRTQTVFVP IPPEDYEPRT
     RPYRDPVEAA NNRLPFMTPI TERTESSLGV LTARRPQMSP TKKDDNDESD DDDGARADQL
     FSSPLREIYN DAQPARVPQP ILEKPKPKPL GVKTIPPKGP VITARNSEDE DQENNGVAVM
     GRGAFAVRQR STLEALKMEQ PP
//
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