ID A0A0L9UQX8_PHAAN Unreviewed; 1286 AA.
AC A0A0L9UQX8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 08-NOV-2023, entry version 30.
DE RecName: Full=MutL C-terminal dimerisation domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=LR48_Vigan06g060600 {ECO:0000313|EMBL:KOM45300.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM45300.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC {ECO:0000256|ARBA:ARBA00006082}.
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DR EMBL; CM003376; KOM45300.1; -; Genomic_DNA.
DR STRING; 3914.A0A0L9UQX8; -.
DR EnsemblPlants; KOM45300; KOM45300; LR48_Vigan06g060600.
DR Gramene; KOM45300; KOM45300; LR48_Vigan06g060600.
DR OMA; DHHAVEH; -.
DR Proteomes; UP000053144; Chromosome 6.
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 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 Gene3D; 3.30.1370.100; MutL, C-terminal domain, regulatory 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; IPR042121; MutL_C_regsub.
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:SF47; DNA MISMATCH REPAIR PROTEIN MLH3; 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 Reference proteome {ECO:0000313|Proteomes:UP000053144}.
FT DOMAIN 214..335
FT /note="DNA mismatch repair protein S5"
FT /evidence="ECO:0000259|SMART:SM01340"
FT DOMAIN 1048..1208
FT /note="MutL C-terminal dimerisation"
FT /evidence="ECO:0000259|SMART:SM00853"
FT REGION 565..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..877
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..927
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1286 AA; 145999 MW; 8141ED9590771991 CRC64;
MASIKPLQEA VRSSLRSGIF LFDFTRVVEE LVFNSLDARA TKVSVFVGVG RSYLKVVDNG
SGITRDGLEL VGERYATSKF LNLVDLNVTS ENFGFRGEAL ASISDVSVLE IVTRTHGRPN
GYQKVLKGCK CLYLGIDDDR KEVGTTVVVR DLFYNQPVRR KCIQSSPNKV LQSIKKCVMR
LALVRPNISF KVVDIEREDE LFCTHSASSP LSLITSGFGV EVTSSLHYLE VENDIIKLSG
YVSSPCNTSN IEGPIHKLLS QLAVRFEHLN SWTTDNEFRN KKRSRCHLGI AYLLDLSCPR
SMYDLAFEPS KTYVKFKDWT PILNFIEKVV KQFWEENIAS VEPSNQFAYM VEDQQEKAYV
SVISDVPDMS RFRNQNRKDC LDLFFSTSDK LIEDDYHQSN REDVRTSIDY LETAMFKEKQ
SIGDSLFQTG YSGNLLDDSH AKCISTVTRR QKSLLMHDSS SSLKGDNFFY SEIPAIESLN
DCVAFDAPSC SHGRKFHKEA DAISEAFQDD LHYDCNGHSF DVNINGDLQK PFLKGCSTPG
SILLKKDFFI NDGYEIQKDS FISKQNTGGG KDLNDVPFDE PSSSHGRKFD KEADVISESF
QDDLCYNYNG YRYDVNINGE LQKPFLKGCS ALGSILSKKD FSGNDNHELQ TDSFCSKQNT
GEDYRSGKDL YVHPFPEVKK KLKMSKNFDF LERPLAEENI LPSDLCYSAS QIGSSDSDDR
SLNFEWHPLY LKPSSQGHAL GFYRTTDIKD DIRGVSRCLK WIHHKNRFDE RENECNFSYN
TTWNTNQHHC ASSYANIGFN FDVAGDSGEI FNKLGDCHDF SDIHSTKRSD MLNKKLDWLL
PELCVKRCKM PNKDKGKTDK FRNSTVEENH ERSRRSISAP PFYRSKRRFF SLNHPSEIKA
KRQIDRVYNP GFNHEEASNS KDPQQPPVAR HESSKDLLLQ EFKINVKQTS KVLGAMQVND
ITEIEELDSF NIQNCAPFGE LLSKDVQDPI DYGTKWRNCS PDFTKNDRPA ANTQCRNNIL
DISSGLHLAG DSLIPETISK KCLEDAKVLH QVDKKFIPVV AGRTLVVIDQ HAADERIRLE
ELRQKVLSGE AKTVTYLHTE LELVLPEIGY QLLHSYSEQI KDWGWICNIH ANNSETFRRN
LDVIKRQETR ITLIAVPCIL GVKLNDVDLL EFLQQLADTD GSSTMPPSVI RLLNSKACRG
AIMFGDSLLP SECSLLVEEL KHTSLCFQCA HGRPTTVPLV NLEALHSQIA KLRLMNDSSS
KKWHGLRKHK LCVERVAQRL NSAMED
//
