ID S7MIG3_MYOBR Unreviewed; 200 AA.
AC S7MIG3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Mitochondrial genome maintenance exonuclease 1 {ECO:0000256|HAMAP-Rule:MF_03030};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_03030};
GN Name=MGME1 {ECO:0000256|HAMAP-Rule:MF_03030};
GN ORFNames=D623_10029082 {ECO:0000313|EMBL:EPQ04179.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ04179.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
CC -!- FUNCTION: Metal-dependent single-stranded DNA (ssDNA) exonuclease
CC involved in mitochondrial genome maintenance. Has preference for 5'-3'
CC exonuclease activity but is also capable of endoduclease activity on
CC linear substrates. Necessary for maintenance of proper 7S DNA levels.
CC Probably involved in mitochondrial DNA (mtDNA) repair, possibly via the
CC processing of displaced DNA containing Okazaki fragments during RNA-
CC primed DNA synthesis on the lagging strand or via processing of DNA
CC flaps during long-patch base excision repair. {ECO:0000256|HAMAP-
CC Rule:MF_03030}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03030}.
CC -!- SIMILARITY: Belongs to the MGME1 family. {ECO:0000256|HAMAP-
CC Rule:MF_03030}.
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DR EMBL; KE161494; EPQ04179.1; -; Genomic_DNA.
DR AlphaFoldDB; S7MIG3; -.
DR eggNOG; ENOG502QVKE; Eukaryota.
DR Proteomes; UP000052978; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0008297; F:single-stranded DNA exodeoxyribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043504; P:mitochondrial DNA repair; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.320.10; -; 1.
DR HAMAP; MF_03030; MGME1; 1.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR PANTHER; PTHR31340; MITOCHONDRIAL GENOME MAINTENANCE EXONUCLEASE 1; 1.
DR PANTHER; PTHR31340:SF3; MITOCHONDRIAL GENOME MAINTENANCE EXONUCLEASE 1; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
PE 3: Inferred from homology;
KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_03030};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03030};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03030};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_03030};
KW Reference proteome {ECO:0000313|Proteomes:UP000052978}.
FT DOMAIN 60..157
FT /note="PD-(D/E)XK endonuclease-like"
FT /evidence="ECO:0000259|Pfam:PF12705"
FT ACT_SITE 97
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03030"
FT ACT_SITE 110
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03030"
FT ACT_SITE 112
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03030"
SQ SEQUENCE 200 AA; 23053 MW; 6BC6B13F08B6060C CRC64;
MTSEQIFYLE RWKQRMILEL GEDGFAEYTS NLFLQGKQFH EALESILSPQ GNLKEGDENL
ESGYIESIQH ILKDVSGVQA LESAVQHETL KYVGLLDCVA EYQGNLCVID WKTSEKPKPL
IRNTFDNPLQ VVAYMGAINH DANYSFQVRC GLIVVAYKDG SPAHPHFMDT ELCSQYWTKW
LLRLEEYTKK EKNQNIQKPD
//