ID A0A2D0SFK8_ICTPU Unreviewed; 1194 AA.
AC A0A2D0SFK8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=DNA polymerase subunit gamma-1 {ECO:0000256|ARBA:ARBA00015350};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
DE AltName: Full=Mitochondrial DNA polymerase catalytic subunit {ECO:0000256|ARBA:ARBA00031966};
GN Name=polg {ECO:0000313|RefSeq:XP_017341251.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017341251.1};
RN [1] {ECO:0000313|RefSeq:XP_017341251.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017341251.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Involved in the replication of mitochondrial DNA. Associates
CC with mitochondrial DNA. {ECO:0000256|ARBA:ARBA00025629}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000256|ARBA:ARBA00024632};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC {ECO:0000256|ARBA:ARBA00007705}.
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DR RefSeq; XP_017341251.1; XM_017485762.3.
DR AlphaFoldDB; A0A2D0SFK8; -.
DR STRING; 7998.ENSIPUP00000005846; -.
DR Ensembl; ENSIPUT00000006113; ENSIPUP00000005846; ENSIPUG00000004036.
DR GeneID; 108275148; -.
DR KEGG; ipu:108275148; -.
DR CTD; 5428; -.
DR OMA; LWLWDED; -.
DR OrthoDB; 5403095at2759; -.
DR Proteomes; UP000221080; Chromosome 14.
DR GO; GO:0005760; C:gamma DNA polymerase complex; IEA:InterPro.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006264; P:mitochondrial DNA replication; IEA:InterPro.
DR CDD; cd08641; DNA_pol_gammaA; 1.
DR Gene3D; 3.30.420.390; -; 2.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR InterPro; IPR002297; DNA-dir_DNA_pol_A_mt.
DR InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR041336; DNApol_Exo.
DR InterPro; IPR047580; POLG_palm_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR PANTHER; PTHR10267; DNA POLYMERASE SUBUNIT GAMMA-1; 1.
DR PANTHER; PTHR10267:SF0; DNA POLYMERASE SUBUNIT GAMMA-1; 1.
DR Pfam; PF18136; DNApol_Exo; 1.
DR PRINTS; PR00867; DNAPOLG.
DR SMART; SM00482; POLAc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion nucleoid {ECO:0000256|ARBA:ARBA00023271};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 829..1104
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT REGION 470..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 407..434
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1194 AA; 136381 MW; 4FD09C6409672D1A CRC64;
MLRLVSPRRS WRCPSAALQR RKCSASAEPK VQERSTQTRV NPLNIQMLSR NLHEQIFRSS
TVEYSSEDIE RSIRHLEKHK LWGKEASLLS DVELKLPNMY GKNIDEHFCK LAQKQSLPYL
EAAGQLQQAQ LPDMPPQWAW EVGWVRYLQN GEHIKVDFPE ENALVFDVEV CMAEGHCPTL
AVAVSPNAWY SWCSKRLIEE RYSWSSQLTL ADLIPLETAA NSSRPPGGHW QERLVVGHNV
SFDRAHIKEQ YLLKGSKMRF LDTMSLHMAI SGLTGFQRSL WMASRYGKRQ GLHEVKQHMK
KLRRRPEGPV IGSWDWVNIS SINNLADVHA LYVGGDPLEK EARNIFVKGS MSDIRSNFQE
LMQYCAMDVL ATHEVFIQQL SLFLERCPHP VTFAGMLEMG VCYLPVNQSW DRYLEDAQDT
YDELQREMKK SLMILADDAC QLLQDDRYKE DPWLWDLEWD VQEFKQKKMT VSKKKKAKQE
AEKAAAASSS GNLEKDWDED PGPPEEEEGM KDPSRELLER LKGTVSCLPK RRQHMPAHPG
WYRKLCLRMS EEEDWSPGAI LISLQMRVTP KLMGLTWDGF PLHYTEKHGW GYLVPGRRDN
LETTEDTEGP ICPYRAIENV YKEYCEQKGK EQPQCLDSLP SDDLMLTDSS VWQTVEELSR
LEVVSEDEIL PRTVRAKKAT SIDSANECPY HHGNGPYNDV NIPGCWFFKL PHKDGNENNV
GSPFSKDFLS KMEDGTLQAG RGGTNAARAL EINKMISFWR NAHKRISSQM VVWLRRGELP
RTVMRHDDYN EEGQYGAILP QVVTAGTVTR RAVEPTWLTA SNARRDRVGS ELKAMVQVPP
GYHLVGSDVD SQELWIAAVL GESHFAGMHG CTAFGWMTLQ GKKSQGTDLH SCTADAVGIS
REHAKVFNYG RIYGAGQPFA ERLLMQFNHR LSQNEAASKA RQMYALTKGL RRYHPSEEGE
WLIKELGVDV KRDEDGTVSR EELGRISKLL HQRSRNKRKW DIFGRRVWSG GTESEMFNKL
ESIAHSKQPA TPVLGCRISR ALEPAAVKEE FITSRVNWVV QSSAVDYLHL MLVAMKWLME
EYDIDGRFCI SIHDEVRYLV KSEDRFRAAL ALQIANLLTR CMFAYKLGMN DLPQSVAFFS
AVDIDQCLRK EVVMDCVTPS NPTGLERRFG LAQGEALDIY QIIEITKGSL AKGR
//
