ID A0A163HTE4_DIDRA Unreviewed; 1602 AA.
AC A0A163HTE4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=MutS protein homolog 3 {ECO:0000256|ARBA:ARBA00029792};
GN ORFNames=EKO05_006817 {ECO:0000313|EMBL:KAF9706330.1}, ST47_g3408
GN {ECO:0000313|EMBL:KZM25458.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM25458.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM25458.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM25458.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
RN [2] {ECO:0000313|EMBL:KAF9706330.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9706330.1};
RA Syme R.A., Farfan-Caceres L., Lichtenzveig J.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAF9706330.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9706330.1};
RX PubMed=32345704; DOI=10.1534/g3.120.401265;
RA Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA Debler J.W., Oliver R.P., Lee R.C.;
RT "Reference Genome Assembly for Australian Ascochyta rabiei Isolate
RT ArME14.";
RL G3 (Bethesda) 10:2131-2140(2020).
RN [4] {ECO:0000313|EMBL:KAF9706330.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9706330.1};
RA Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA Debler J.W., Oliver R.P., Lee R.C.;
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MSH3
CC subfamily. {ECO:0000256|ARBA:ARBA00007094}.
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:KZM25458.1}.
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DR EMBL; RYYQ01000013; KAF9706330.1; -; Genomic_DNA.
DR EMBL; JYNV01000127; KZM25458.1; -; Genomic_DNA.
DR STRING; 5454.A0A163HTE4; -.
DR OrthoDB; 168255at2759; -.
DR Proteomes; UP000076837; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
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; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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; 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; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR InterPro; IPR036678; MutS_con_dom_sf.
DR InterPro; IPR045076; MutS_family.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11361:SF122; DNA MISMATCH REPAIR PROTEIN MSH3; 1.
DR PANTHER; PTHR11361; DNA MISMATCH REPAIR PROTEIN MUTS FAMILY MEMBER; 1.
DR Pfam; PF00743; FMO-like; 2.
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 Pfam; PF13450; NAD_binding_8; 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; SSF51905; FAD/NAD(P)-binding domain; 2.
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};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000076837}.
FT DOMAIN 972..988
FT /note="DNA mismatch repair proteins mutS family"
FT /evidence="ECO:0000259|PROSITE:PS00486"
FT REGION 1..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1169..1184
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1602 AA; 179130 MW; F6A7643A0CCFED07 CRC64;
MAPKSSQPPL SASQRTKQQS ISSFFAPKPS QAPKAAPSSA PKPASPATDG ANRNDHGDET
SPLGHSILSR KRTVSNSGDD GESPKRVRIA ESEDARPSLD QATEASLNTP KAMTRTDRTS
RFLFSSSPPP RDENAAAQEE DAAATQRERE RLHEKFVKKL GRPDSFAELR RRNKVLTEEE
ANGEGEGEDE DEEQEAPKPA KGKKGAATKK PASKLTPMDK QYLEIKRKHL DTIIVMEVGY
KFKFFGEDAR TASKELGIVC IPGKFRYDEH PSEAHLDRFA SASFPVHRLQ VHVKRLVKAN
HKVGVVRQIE TAALKAAGDN RNTPFVRKLT NLYTKGTYVD DVEGLETAAE SPAGGAQSTG
YLLCITETNA NGWGTDEKVQ VGLVAVQPAT GDIIYDDFED GFMRSEIETR LLHIAPAEFL
VVGDLSKATD KLIQHLSASK TNVFGDRSRV ERVEKPKTMA AQAYGHISNF YADKMKSSQG
GGSSSQGAIL DKVHQLSEHV TICLSAMITY LSEYGLEHVF DLTKYFQPFS ARSYMLLNGN
TLSSLEIYQN QTDYTAKGSL FWTMDRTKTR FGQRLLRKWV GRPLIDKERL EERITAVEEL
KNGENTIPFD KLKFLLGRTR TDLEKVLIRI YYKKCTRPEL LAALQTLQDI SGQYLQVKSP
EQSGFSSTLL SEAVSNIPKI YDDLNKFLEK INASAAKADD KYGFFQEEHE AEDINDLKLS
IASVEDDLNT HRKEAAAKLG ITKVDYVTVA GIEYLIEVKR KSPQEKKVPA SWQQISATKA
TLRFHTPEVK RMCQERDQYK ESLAAACDAA FMRLLDDISA KYQELRDCVH SIATLDALFS
LAILANQPGY VKPTFTDEIE LNISGGRHPM VEQLLLDSYV PNDLQLSHSA TRALLVTGPN
MGGKSSYVRS AALIAIMGQI GSYVPATEAR LGMLDAVFTR MGAFDNMLKG ESTFMVELNE
TSDILRSATS RSLIILDELG RGTSTFDGVA IAEAVLDYVI RDIQGLTLFI THYQHLSKLH
SRFTNGELKN VHMSFEERDG GREVVFLYEV AEGTSHRSYG LNVARLAKVP EKVIDVASVK
SSELEDNMTA CKMGNLSRLM KGIMNDNSEQ SLDRLVESIE QLSVAVIGAG AAGAAAAAAL
DAEDAFDIIQ VFERRETPGG TWIYDPDPAP PTQLRPGGMP PDTDPPLKVP QSLPAAVKPT
EQQRFDRTPI YEGLTTNVPE IIMSLSDERF AYGPFAPHWV PKQYIQNYFA SHHVDRYLVL
NTTVEDVTRA HEKWILILRK YDPVQKVDIW WSEQFDALIV ANGHYSIPYI PQVSGLDTYI
QRFPTRITHS KFYRSPTHYP NQRILIIGNS ASGHDITTQI AQSGSVELPV YQSRRSRNRW
DGSSPPPGVE WKPMVSSYDA ESGAVHFADG SRLTNIDVVI YCTGYKPSFP FWNSKANGGL
LYDYRKDKLQ DFYQHTFSAR FPQSLGIVGL PRVLTFRSFE YQAIALARIF CGREARPLPS
GKEIREWEDK RVQKCKEEGR SFHTILWDDG ETMEWFRYLY QLAGLPLLEG KGRVPPVLGE
RERWAYDNIK KYPEPGKGSR KYGIGEEGWV ATDEERDSAW FV
//
