ID A0A0E1RWA6_COCIM Unreviewed; 1221 AA.
AC A0A0E1RWA6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=DNA mismatch repair protein {ECO:0000256|PIRNR:PIRNR037677};
GN ORFNames=CIMG_08825 {ECO:0000313|EMBL:EAS30079.2};
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410 {ECO:0000313|EMBL:EAS30079.2, ECO:0000313|Proteomes:UP000001261};
RN [1] {ECO:0000313|Proteomes:UP000001261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2] {ECO:0000313|Proteomes:UP000001261}
RP GENOME REANNOTATION.
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
CC -!- FUNCTION: Component of the post-replicative DNA mismatch repair system
CC (MMR). Heterodimerizes with MSH2 to form MutS beta, which binds to DNA
CC mismatches thereby initiating DNA repair. MSH3 provides substrate-
CC binding and substrate specificity to the complex. When bound, the MutS
CC beta heterodimer bends the DNA helix and shields approximately 20 base
CC pairs. Acts mainly to repair insertion-deletion loops (IDLs) from 2 to
CC 13 nucleotides in size, but can also repair base-base and single
CC insertion-deletion mismatches that occur during replication. After
CC mismatch binding, forms a ternary complex with the MutL alpha
CC heterodimer, which is thought to be responsible for directing the
CC downstream MMR events, including strand discrimination, excision, and
CC resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch
CC repair functions. {ECO:0000256|ARBA:ARBA00025373}.
CC -!- SUBUNIT: Heterodimer consisting of MSH2-MSH3 (MutS beta). Forms a
CC ternary complex with MutL alpha (MLH1-PMS1).
CC {ECO:0000256|ARBA:ARBA00025902}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family.
CC {ECO:0000256|PIRNR:PIRNR037677, ECO:0000256|RuleBase:RU003756}.
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DR EMBL; GG704913; EAS30079.2; -; Genomic_DNA.
DR RefSeq; XP_001241662.2; XM_001241661.2.
DR AlphaFoldDB; A0A0E1RWA6; -.
DR STRING; 246410.A0A0E1RWA6; -.
DR GeneID; 4560406; -.
DR KEGG; cim:CIMG_08825; -.
DR VEuPathDB; FungiDB:CIMG_08825; -.
DR InParanoid; A0A0E1RWA6; -.
DR OMA; TPMMAQY; -.
DR OrthoDB; 168255at2759; -.
DR Proteomes; UP000001261; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0030983; F:mismatched DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006298; P:mismatch repair; IEA:InterPro.
DR Gene3D; 1.10.1420.10; -; 2.
DR Gene3D; 3.40.1170.10; DNA repair protein MutS, domain I; 1.
DR Gene3D; 3.30.420.110; MutS, connector domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N.
DR InterPro; IPR017261; DNA_mismatch_repair_MutS/MSH.
DR InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
DR InterPro; IPR007861; DNA_mismatch_repair_MutS_clamp.
DR InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
DR InterPro; IPR016151; DNA_mismatch_repair_MutS_N.
DR InterPro; IPR036187; DNA_mismatch_repair_MutS_sf.
DR InterPro; IPR007860; DNA_mmatch_repair_MutS_con_dom.
DR InterPro; IPR036678; MutS_con_dom_sf.
DR InterPro; IPR045076; MutS_family.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11361:SF148; DNA MISMATCH REPAIR PROTEIN MSH6; 1.
DR PANTHER; PTHR11361; DNA MISMATCH REPAIR PROTEIN MUTS FAMILY MEMBER; 1.
DR Pfam; PF01624; MutS_I; 1.
DR Pfam; PF05188; MutS_II; 1.
DR Pfam; PF05192; MutS_III; 1.
DR Pfam; PF05190; MutS_IV; 1.
DR Pfam; PF00488; MutS_V; 1.
DR PIRSF; PIRSF037677; DNA_mis_repair_Msh6; 1.
DR SMART; SM00534; MUTSac; 1.
DR SMART; SM00533; MUTSd; 1.
DR SUPFAM; SSF55271; DNA repair protein MutS, domain I; 1.
DR SUPFAM; SSF53150; DNA repair protein MutS, domain II; 1.
DR SUPFAM; SSF48334; DNA repair protein MutS, domain III; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR037677};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|PIRNR:PIRNR037677};
KW DNA repair {ECO:0000256|PIRNR:PIRNR037677, ECO:0000256|RuleBase:RU003756};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR037677};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR037677};
KW Reference proteome {ECO:0000313|Proteomes:UP000001261}.
FT DOMAIN 1055..1071
FT /note="DNA mismatch repair proteins mutS family"
FT /evidence="ECO:0000259|PROSITE:PS00486"
FT REGION 1..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 790..824
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..207
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1221 AA; 137031 MW; AD726F060802A010 CRC64;
MPESSRVPKN SMAGTQTMKG QKSILGFFQP KSSPCTPPAT SRTQNVKDEP ASSPAPRPSH
NRTKASQLSG TQSSHRAPNL TPSPSSDAVE PVSDDLNIEQ STVQQLKGSP EAVDVSLPSP
ATSANGRDGE QAENQELPSA TPSRRAKKTV DYWESDEEDV VKPPTRRSAV GRANKKRRTV
ATSEDEEEFQ PDESIGDFDD LDDFIVPDES DQEMRPSRKR KRSSNPKPTK PSTPISAPQD
DMDVDLDIPN SASGTAKKWT YDPNDTECRQ HRTTLAPLSS KSLGKKKEKA HLTEPEKRYP
WLANILDMDK NPPGHPDYDP RTLYIPPLAW SRFSPFEKQY WEIKQKFWDT VVFFKKGKFY
ELYENDATIG HQLFDLKLTD RVNMRMVGVP ESSLEYWANQ FVAKGFKIAR VDQSESALGK
EMRERDDKKK GDKVIKRELS CVLTAGTLVD GAMLQDDMST YCVAVKEALV DDLPAFGVSF
VDTATGQFFL TEFTDDVDMT KFETLVAQTR PQELLLEKGF MSPKALRILK NNTNPTTIWN
YLKPEREFWD ASTTRRELDA SEYFVSVDQD NIEAWPEVLR QARDNELVIS SFGALIQYLR
MLKIERDLIT IGNFTWYDPI RKASSLVLDG QTLINLEVFA NSYDGGQDGT LFQLLNRCIT
PFGKRMFKQW VCHPLMDSKK INARLDAVDA LNADSSIRDQ FSSQLTKMPD LERLISRVHA
GTCKCQDFVR VLEGFEQIDY TMSLLKQTGS GDGVIGHLIS SMPDMDGLLQ YWKTAFDRVK
AKDSGIFVPK AGVEEDFDAS TQRIEEIEAK LDQLLKRVRR ELNSSAIIYR DNGKEIYQLE
VPVKVRNIPK SWDQMSATKQ AKRYYFPELR GLIRKLQEAQ ETHNQIVKEV TSRFYARFDE
NYQTWLAAVK ITARLDCLIG LAKASTAIGY PSCRPVFVDS DRSVLEFQEL RHPCMLATVG
DFIPNDVKLG GNTASINLLT GANAAGKSTV LRMTCTAVIM AQIGCYVPCA SARLTPVDRI
MSRLGANDNI FGAQSTFFVE LSETKKILSE ATSRSLVILD ELGRGTSSYD GVAVAQAVLH
HVATHIGALG FFATHYHSLA AEFEGHPEIS PRRMRIHVDE EDRRVTFLYK LEDGVAEGSF
GMHCASMCGI PTKVIETAEV AAKEWEHTSR LKESVERKKG SGLVGLGWWS DIAWILKDDD
FVRDSADGKG MEVLLKAIEN M
//
