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Database: UniProt
Entry: A0A0M4ET91_DROBS
LinkDB: A0A0M4ET91_DROBS
Original site: A0A0M4ET91_DROBS 
ID   A0A0M4ET91_DROBS        Unreviewed;       795 AA.
AC   A0A0M4ET91;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   08-NOV-2023, entry version 31.
DE   SubName: Full=Pms2 {ECO:0000313|EMBL:ALC40432.1};
GN   ORFNames=Dbus_chr2Rg11 {ECO:0000313|EMBL:ALC40432.1};
OS   Drosophila busckii (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC40432.1, ECO:0000313|Proteomes:UP000494163};
RN   [1] {ECO:0000313|EMBL:ALC40432.1, ECO:0000313|Proteomes:UP000494163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole larvae {ECO:0000313|EMBL:ALC40432.1};
RA   Zhou Q., Bachtrog D.;
RT   "Ancestral chromatin configuration constrains chromatin evolution on
RT   differentiating sex chromosomes in Drosophila.";
RL   Submitted (AUG-2015) 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; CP012524; ALC40432.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M4ET91; -.
DR   SMR; A0A0M4ET91; -.
DR   STRING; 30019.A0A0M4ET91; -.
DR   OMA; RCSKIRS; -.
DR   Proteomes; UP000494163; Chromosome 2r 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:0006298; P:mismatch repair; IEA:InterPro.
DR   CDD; cd16926; HATPase_MutL-MLH-PMS-like; 1.
DR   CDD; cd03484; MutL_Trans_hPMS_2_like; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.1540.20; MutL, C-terminal domain, dimerisation subdomain; 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; IPR014790; MutL_C.
DR   InterPro; IPR042120; MutL_C_dimsub.
DR   InterPro; IPR037198; MutL_C_sf.
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:SF52; MISMATCH REPAIR ENDONUCLEASE PMS2; 1.
DR   Pfam; PF01119; DNA_mis_repair; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF08676; MutL_C; 1.
DR   SMART; SM01340; DNA_mis_repair; 1.
DR   SMART; SM00853; MutL_C; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF118116; DNA mismatch repair protein MutL; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   Reference proteome {ECO:0000313|Proteomes:UP000494163}.
FT   DOMAIN          229..386
FT                   /note="DNA mismatch repair protein S5"
FT                   /evidence="ECO:0000259|SMART:SM01340"
FT   DOMAIN          699..795
FT                   /note="MutL C-terminal dimerisation"
FT                   /evidence="ECO:0000259|SMART:SM00853"
FT   COILED          634..698
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   795 AA;  88662 MW;  CC3B3179A9DFFA4A CRC64;
     MSDIKEEEAA IPKATDAASG NIKAIAKDTV HKICSGQAMA IKELVENSID AGATLVEINL
     RDQGLQGLEV SDNGSGVEEA NLDGMTAKYH TSKIRDFVDL LGVETFGFRG EALSSLCALT
     DMCIQTRHAS TDVALKVELD HDGKIKKRSP CARGVGTTVT LNNLFVTLPV RRRDFTRNIK
     KEFNKMCQIL QAYCLVTKGV RIICSNQTPK GAKTVVMQTH GAQDVLANIT SVFGTRQAAD
     LVPLKSPFEQ GALNEIGLRA ELESASDVAE ITCTQFNAED IEQLNQADFQ LEGYISSCRH
     GAGRSSKDRQ YFFINARPCE PKNIAKVMND LYHRYNVQQQ PFIYLNVVTA RADVDVNLTP
     DKRQLLLNNE KILLLALKKS LLNTFGALPS TFQMQNVSIV SMLEPKPKIK EETVNESAKE
     DEIDVPISSS QGFMDVLSQW RRTGDTKGVA PPAPAKRPCE ETAEITARAM KMQKIQDFLT
     QEAPKPRQLL SDEEDEELQD ALKLDKVKTS LDTSIVSLKQ LQQESAAYDE LMKPAKDTAQ
     LERQESSLNT TYDELLKPAK ATRIDCKTQT PIKTLKISKV APAALEQQAQ TKQEFELSSS
     QTTTEFSDDE IEMPTHIELD GDSDNEAAPA SVASGELRTS LAEIRQQLQA VEQQQQQRKQ
     RAKLQRLRFK SEINPQQNQN AEAELEKEIG KADFARMQIV GQFNLGFIIV KLDDDLFIVD
     QHAADEKFNF ETLQRTTQLE HQRLTRPQPL ELTAVNEMIL LDNLQVFEKN GFKFEIDETG
     VNIIYIESPN IAHVL
//
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