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
//