ID G1XAW7_ARTOA Unreviewed; 911 AA.
AC G1XAW7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=DNA mismatch repair protein S5 domain-containing protein {ECO:0000259|SMART:SM01340};
GN ORFNames=AOL_s00078g64 {ECO:0000313|EMBL:EGX49575.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX49575.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX49575.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
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:EGX49575.1}.
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DR EMBL; ADOT01000133; EGX49575.1; -; Genomic_DNA.
DR RefSeq; XP_011121629.1; XM_011123327.1.
DR AlphaFoldDB; G1XAW7; -.
DR STRING; 756982.G1XAW7; -.
DR GeneID; 22893124; -.
DR eggNOG; KOG1978; Eukaryota.
DR HOGENOM; CLU_326773_0_0_1; -.
DR InParanoid; G1XAW7; -.
DR OMA; MIHEIPQ; -.
DR OrthoDB; 1369806at2759; -.
DR Proteomes; UP000008784; 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 CDD; cd16926; HATPase_MutL-MLH-PMS-like; 1.
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; IPR002099; MutL/Mlh/PMS.
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 NCBIfam; TIGR00585; mutl; 1.
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 Pfam; PF13589; HATPase_c_3; 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:UP000008784}.
FT DOMAIN 223..357
FT /note="DNA mismatch repair protein S5"
FT /evidence="ECO:0000259|SMART:SM01340"
FT REGION 412..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 911 AA; 100551 MW; 77FCCD4176B146F8 CRC64;
MIHEIPQESV RRLGSTQVIT DPITVIKELV ENALDAGATS IIVEASSDLV SHIQIKDNGC
GIDPNDRNLM AKPHCTSKIS KFDDLLDVTT LGFRGEALAS LANVSGLLTI ITRVKNEAMA
VACEIASDGS LKTISPVSAP IGCTVKVTNL FSKFPVRKST LEKTAAKYLG RIRPLLLSYY
LTHPQTRLQF RCVAAPQGNK GKKKIETKYD VVFTASSTKE QAVIKAFGAE SNRHGQWIES
KAEDGDVHVE AFIVKPDADT NPISKKGVCV AYKNRPLSIT RNQGLAHSIY SLYKKQTKLA
FTARSVDAPT EPLLFLNILS SVGKVDVNIE PAKDDVLFES NEKVIGCIKE CFEQVYGTEE
EFRRKGRTND DFSSEATNDS VVPSEFPIEQ TLQKAPTFVP EISGTAEQLL AETRSHAPSS
SPPIKISSST IRAQHQKPLG RNQTAPEEVE EDIPLTYSEI SQGRPNTRKQ EDGWSFSMYG
SGIDEDEDAD FVDIEEIMKG TERQQAAREE DSRRDKSISN PWTISKMNSR VTQQEKQADI
PQAASAARSP TVPLPSFPFQ TQGREIRSCN PGIPNAMEIA SLSSALAIAN TPTSNTPITR
ISERGNLWYP NFGSDNNTSS PNRRKRCLIP ERLSEAASTS SSRTAQQSAH LPGAQKPVRK
SAGPIDTWIG ANKATEESHT SSLAGDDHES ATPLPISVFF GTPDLGTSSR PGDGGRGIFP
SASDRMREER RATNPQIDEE WKEEISSSEN DEPHQPEFEP PKNSRASASK LLISTGRSNP
TKLPSTYKVS NKSSKPQPGT SKFLRDVEED DVFPRKMKLL VTTLPKFDLR SLRFRARLIE
DDLYDDEYET GETCPNELEL KKPFFCFLKK YVDGADYSDD TELELLQEDI LDGREFDLSF
QNLASRQFAT A
//
