ID A0A2I3STT5_PANTR Unreviewed; 891 AA.
AC A0A2I3STT5;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=PMS1 homolog 2, mismatch repair system component {ECO:0008006|Google:ProtNLM};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000080387.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000080387.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC {ECO:0000256|ARBA:ARBA00006082}.
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DR Ensembl; ENSPTRT00000088305.1; ENSPTRP00000080387.1; ENSPTRG00000048669.1.
DR GeneTree; ENSGT00940000155381; -.
DR InParanoid; A0A2I3STT5; -.
DR Proteomes; UP000002277; Unplaced.
DR Bgee; ENSPTRG00000048669; Expressed in dorsolateral prefrontal cortex and 11 other cell types or tissues.
DR GO; GO:0032389; C:MutLalpha complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; IBA:GO_Central.
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 DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277}.
FT DOMAIN 227..363
FT /note="DNA mismatch repair protein S5"
FT /evidence="ECO:0000259|SMART:SM01340"
FT DOMAIN 677..821
FT /note="MutL C-terminal dimerisation"
FT /evidence="ECO:0000259|SMART:SM00853"
FT REGION 390..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 891 AA; 98506 MW; 6491E1712929C97E CRC64;
MERAESSSTE PAKAIKPIDR KSVHQICSGQ VVLSLSTAVK ELVENSLDAG ATNIDLKLKD
YGVDLIEVSD NGCGVEEENF EGLTLKHHTS KIQEFADLTQ VETFGFRGEA LSSLCALSDV
TISTCHASAK VGTRLMFDHN GKIIQKTPYP RPRGTTVSVQ QLFSTLPVRH KEFQRNIKKE
YAKMVQVLHA YCIISAGIRV SCTNQLGQGK RQPVVCTGGS PSIKENIGSV FGQKQLQSLI
PFVQLPPSDS VCEEYGLSCS DALHNLFYIS GFISQCARGV GRSSTDRQFF FINRRPCDPA
KVFKIFLYLV NEVYHIYPFV VLKISVDSEC VDINVTPDKR QILLQEEKLL LAVLKTSLIG
MFDSDVNKLN VSQQPLLDVE GNLIKMHAAD LEKPMVEKQD QSPSLRTGEE KKDVSISRLR
EAFSLRHTTE NKPHSPKTPE PRRSPLGQKR GMLSSSTSDA ISDRGVLRPQ KEAASSSQGP
SDPTDRAEVE KDSGHGSTSV DSEGFSIPDT GSHCSSKCVA STPGDRGSQE HVDSQEKAPE
TDDCFSDVDC HSNQEDTGCK FRVLPQPTNL ATPNTKRFKK EEILSSSDIC QKLVNTQDVS
ASQVDVAVKI NKKVVPLDFS MSSLAKRIKQ LHHEAQQSEG EQNYRKFRAK ICPGENQAAE
DELRKEISKT MFAEMEIIGQ FNLGFIITKL NEDIFIVDQH ATDEKYNFEM LQQHTVLQGQ
RLIAPQTLNL TAVNEAVLIE NLEIFRKNGF DFVIDENAPV TERAKLISLP TSKNWTFGPQ
DVDELIFMLS DSPGVMCRPS RVKQMFASRA CRKSVSEESL AVSSAXXXXX XXXXHPTTSH
VGPACCYSAH RPRATAPPSS LFLSSSCNHG IPLRRFSSAR ANTAQTPESR S
//
