ID K2SZW0_MACPH Unreviewed; 1142 AA.
AC K2SZW0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Zinc finger LIM-type protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=MPH_00454 {ECO:0000313|EMBL:EKG22200.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG22200.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG22200.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG22200.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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:EKG22200.1}.
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DR EMBL; AHHD01000027; EKG22200.1; -; Genomic_DNA.
DR AlphaFoldDB; K2SZW0; -.
DR STRING; 1126212.K2SZW0; -.
DR VEuPathDB; FungiDB:MPH_00454; -.
DR eggNOG; KOG1703; Eukaryota.
DR eggNOG; KOG2710; Eukaryota.
DR HOGENOM; CLU_001321_1_0_1; -.
DR InParanoid; K2SZW0; -.
DR OrthoDB; 1329523at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd09391; LIM1_Lrg1p_like; 1.
DR CDD; cd09392; LIM2_Lrg1p_like; 1.
DR CDD; cd04397; RhoGAP_fLRG1; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 4.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR042869; ARHGAP11A/B.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR15670; RHO GTPASE ACTIVATING PROTEIN 11A; 1.
DR PANTHER; PTHR15670:SF4; RHO GTPASE-ACTIVATING PROTEIN 11A; 1.
DR Pfam; PF00412; LIM; 3.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00132; LIM; 3.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 3.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 3.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW LIM domain {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 66..126
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 129..189
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 438..500
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 804..1007
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1049..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1067
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1142 AA; 126292 MW; 70915B9F87976047 CRC64;
MAAPSEGPPS RDGLGPPDDA ALAPGDAGHN IQDERERARR QENGGDSSRP SRERSRNGSR
RPSGSRICGK CGGHLTGQFV RALGDTFHLE CFTCHDCDKI VASKFFPVPE QGPNQYPLCE
TDYFRRLDLL CFSCGGALRG SYITALDRKY HIEHFTCSVC PTVFGAQDSY YEHDGSVYCH
FHYSTKFAQR CNGCQTAILK QFVEIFRNGQ NQHWHPECYM IHKFWNVRLH TTGQPVVEKA
LAGEEDTDEL RKDVRLEEER IEERVNWIWK TLSAFEERSA TCISDMLLHV SNGAYFDGVL
AARRFIVHID LLFEGADELD KLLADQTQKG LSYSREAKLL CKKVVAFFQL LAQSQDTGVR
RLGVTQELLS LVTGLAHYLK LLIRICLQGA LKFERETGSA QGLSGFMDQI NSLESKLEQD
SNTDTGNDSV ALVQRTADTC PICDKPVEDK CTTASSRVFH LPCMKCQSCD KELRDLHDAR
WSASTEKLLC TGCAASVSDA GAGFVQVTRL RQYVHLLRVA HARLLATLRT SGALPHTSDD
PNLMDYDSNS GHRVSPAGSE PPAEPPLLRS DTRSKSYTGH NNEKASPSSY EQTLGDIRRL
RSTRLDKHLS NTMKRARTSR IMDGPEGMTI RPGSAGEARG HGPNNMTIEQ GRDYNETGPL
TFGTNGGIAL DDIPRLVAAE QARDQRPNAA KYARDHLVGQ EPRPKLVNGH RRDVSGGQEL
EKAAAGEGHY GKKYFSELTA LEYFIVRHVA VLSMEPLLEG HFNQEELLEL IENQKRPTFW
NKFGKAFKGK EQPKGGKRKG VFGKSLEFVV EKDGAESTDC VGPGTLKVPA LVQDAVSAMR
TMDMSVEGVF RKNGNIKRLR ELTEEIDAKG GDAVDLTRES PVQVAALLKK FLRELPDPVM
TFKLHKLFIT GAKIPDEDKR RRVLHLTCCL MPKVHRDTME VLFTFLNWVS SFHTVDEDTG
SKMDIHNLAT VIAPNILYSS TKSPDMDSSF LAIEAVHSLI ECNESMCEVP EDLQSILADS
SMFDLNAELT TKEILKRVGE LGKIPQATVV GPGQQANRNS GSRSSAPVVA RIESDPASYQ
AESSVRHVGG NNGELGPPQP PYAGHPNAST DSHGSDRGSP SRYRENRSSQ FQRPGVGVTG
AG
//
