ID A0A1J9QY22_9PEZI Unreviewed; 1132 AA.
AC A0A1J9QY22;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 08-NOV-2023, entry version 24.
DE SubName: Full=Dna mismatch repair protein {ECO:0000313|EMBL:OJD32898.1};
GN ORFNames=BKCO1_35000106 {ECO:0000313|EMBL:OJD32898.1};
OS Diplodia corticola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD32898.1, ECO:0000313|Proteomes:UP000183809};
RN [1] {ECO:0000313|EMBL:OJD32898.1, ECO:0000313|Proteomes:UP000183809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD32898.1,
RC ECO:0000313|Proteomes:UP000183809};
RA Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA Esteves A.C.;
RT "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT hemibiotrophic lifestyle of Diplodia corticola.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC {ECO:0000256|ARBA:ARBA00006082}.
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:OJD32898.1}.
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DR EMBL; MNUE01000035; OJD32898.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9QY22; -.
DR STRING; 236234.A0A1J9QY22; -.
DR OrthoDB; 1369806at2759; -.
DR Proteomes; UP000183809; Unassembled WGS sequence.
DR GO; GO:0032300; C:mismatch repair complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR GO; GO:0061982; P:meiosis I cell cycle process; IEA:UniProt.
DR GO; GO:0006298; P:mismatch repair; IEA:InterPro.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR014762; DNA_mismatch_repair_CS.
DR InterPro; IPR013507; DNA_mismatch_S5_2-like.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR038973; MutL/Mlh/Pms-like.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR PANTHER; PTHR10073; DNA MISMATCH REPAIR PROTEIN MLH, PMS, MUTL; 1.
DR PANTHER; PTHR10073:SF41; MISMATCH REPAIR PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_8G05820)-RELATED; 1.
DR Pfam; PF01119; DNA_mis_repair; 1.
DR SMART; SM01340; DNA_mis_repair; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00058; DNA_MISMATCH_REPAIR_1; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW Reference proteome {ECO:0000313|Proteomes:UP000183809}.
FT DOMAIN 339..463
FT /note="DNA mismatch repair protein S5"
FT /evidence="ECO:0000259|SMART:SM01340"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..62
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..1010
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1132 AA; 120678 MW; A485CFEAFFF7FD9C CRC64;
MPVPSAATAN ADDDDDEATS HHPHHHHHSS APPPPRPPPP SPGTRNSTTA PPPPPPLPPH
PSSTTSSSTS IRPLPPQTAR ALRSSLTIVD PASAVKELVD NALDAGATSV GVEVSGGGTG
AAGLDLVVVR DNGRSVPPVG EDRVLLGRRH CTSKVRWGAG CAGEMQMVGG LGEGGGGTSG
GAGGGGSGGN PAVLGFRGEA LASLVEVCEK VEVTVRCEGE RVGEVLRLGR EGEDLQGVAP
RKVGAPVGTT VRAEGFFERW PVRRQAALKE AEKGGGGGGV MRRIKGLLQG YALARPAVRL
SLKVVKGRGI KNGKEGGWTY APKPGLGLGG GRERVADAVL KVVGKGAAAQ CIYAAQELNG
YRFEAFLPRA DAEGKEISGL GQFLSVDARP VSTARGTLSL IAKAFRDRLK KANPALENVK
EPFLRLDIGC PPGSYDPNVE PSKSDLLFDE PKAVLSALED FLDIFYSSAG PQMETAKIHE
SKVPTQREIS LVEDTVTAPD SEAQKSDDDV TTYSDIFDEF VMIPATDVAH PPASSDSIAA
TLRSNTEMED VEDPRPKRRR TWKSNMYDFD EDDVLVDDGN GDAQGNPDVD LADEDTEEAM
GHVTVSNPWT MAKMNAKIPK PSVASSPEVA HMRKQNTEPQ LELPTSTPPE SRISLGGAYL
PTPQASSPNY GQSASVARCG GFGGTNLTQS PATPSATFAK SPNSHLPFPQ NSSRQVDDDG
FVPVPPQPVG GGTVNSAKTA TPKRSRLGGP GNARSGRRGI NKPFKPPINP ERDSWFSYTP
SQRPKRSTVF LRKNKIPAAG GDDARNEYVM SGGADGGGLS DGHDRDIRHW MASNTTRVGR
TQSDNGPGIH EDAASIQDSS VASEETRPAL QQRLPATPEE LRIRNFDFNM KAPAPFPRIT
QSRLTVQNRP SATSQRDETE EHTRQETADT AATAQPLRRS FRRHAAARPP PIVEKALYAN
EEIAKQPLQS HPQLGQSERQ QQQHSGTGTG LVPLRRLSTR QQSRRRTTSS LPLERVPDGA
QMQNVALIIL SSAAAALSTK RTTYSALQED DVALSWGASG DLKSPFAKAG DDDVTAYTAV
VQSWADRLGN LLMRFRLDGV EGHGVELRQD LSFVLMDAVE RYRRGQVMME AS
//
