ID A0A178EKR0_9PLEO Unreviewed; 941 AA.
AC A0A178EKR0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 08-NOV-2023, entry version 24.
DE RecName: Full=DNA mismatch repair protein S5 domain-containing protein {ECO:0000259|SMART:SM01340};
GN ORFNames=IQ07DRAFT_529607 {ECO:0000313|EMBL:OAL55769.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL55769.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL55769.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL55769.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC {ECO:0000256|ARBA:ARBA00006082}.
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DR EMBL; KV441637; OAL55769.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178EKR0; -.
DR STRING; 765867.A0A178EKR0; -.
DR InParanoid; A0A178EKR0; -.
DR OrthoDB; 1369806at2759; -.
DR Proteomes; UP000077535; 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:UP000077535}.
FT DOMAIN 229..357
FT /note="DNA mismatch repair protein S5"
FT /evidence="ECO:0000259|SMART:SM01340"
FT REGION 443..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..737
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 941 AA; 104138 MW; D4C71F89AC79424F CRC64;
MADGAPPIPL PGIMALKATT AQQISSGQLL VDPSSVVKEL IENALDARAK SIFIDISANA
LESIQVKDDG HGIPAEDRAL ACRRYCTSKI RDYDDLKEVG GKWLGFRGEA LASIAEMSDS
LSITSRVEGE PVAVRLKYGR NGELTSSEKD SHPVGTTVKV TGFFKHLPVR QQTALQNSTK
FLAKIRKLVQ AYSLARPHVR LRFHVLKAKS GNYDLIYAPK ADASVEDAVV KVISKDCASQ
CDSITLEKNG FLIRAFLPKS TANGSKISTH GAFISIDARP VANNRGLTKQ IVKNFVDALR
KSNHSLATVK MPFMYMNIAC PPGSYDANIE PAKDDVIFDE SSLLIEAVEE LLDTFYTTVI
MDMETTQSSP PVNRSRIDDA AVILSATEAR VLSRNEVPVR ASDLSTSEVQ HSPSRWASTM
YGISIEDGKF AEEGNIAIVE EEEDLRSAEA SNPWTIAKMN APAKPRKAPL NMQRPSPTKN
QSDKPNERSS SVFESPARQT LPYAPLTPQS SPTKSLPIPS GHSEPVTNAR RLETRPAVYH
SSQNPVPPVF EVFPYPASEP GEAISSVPPS PHRETEKQRG YINKPFVPPL QRNDETRTSH
IQALNTFTFS QPPQKKQRNR RPKDAQHLPE NSLPPLMHEP APAGQVTLRA PQPDDVDIRS
YFGRDKRQAD DVLEHPTGGF QFTPINSQST SSQLRSRPRP LHIPTKPQGM TSPPHNRPES
RPRRLRSDKL ERTKSSRLPL ERVPAGYRIH DVVLQTTTSI VAILRASRGL DMQRNGLRWG
TSVQEATSVF TEAAHESRIR TWVLRLDQML DQRWQRVDGV DTRGALHESM QVGLDGKKAT
GVVDDVHVNV LELPGVRVSA VPDAIHNNLE EDGVQDANKA QKLIDIGKQG EEYGMVDFDM
AQFVDFDAEE EMEAVGALKD QKRNESDECY DDIDDDMLMD L
//
