ID A4HAP3_LEIBR Unreviewed; 1264 AA.
AC A4HAP3;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Putative mitochondrial DNA polymerase I protein A {ECO:0000313|EMBL:CAM38475.1};
DE EC=2.7.7.7 {ECO:0000313|EMBL:CAM38475.1};
GN ORFNames=LBRM_20_1290 {ECO:0000313|EMBL:CAM38475.1};
OS Leishmania braziliensis.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC Leishmania braziliensis species complex.
OX NCBI_TaxID=5660 {ECO:0000313|EMBL:CAM38475.1, ECO:0000313|Proteomes:UP000007258};
RN [1] {ECO:0000313|EMBL:CAM38475.1, ECO:0000313|Proteomes:UP000007258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM38475.1,
RC ECO:0000313|Proteomes:UP000007258};
RX PubMed=17572675; DOI=10.1038/ng2053;
RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA Mottram J.C., Smith D.F., Berriman M.;
RT "Comparative genomic analysis of three Leishmania species that cause
RT diverse human disease.";
RL Nat. Genet. 39:839-847(2007).
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};
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DR EMBL; FR798994; CAM38475.1; -; Genomic_DNA.
DR RefSeq; XP_001564413.1; XM_001564363.1.
DR AlphaFoldDB; A4HAP3; -.
DR STRING; 5660.A4HAP3; -.
DR GeneID; 5414960; -.
DR KEGG; lbz:LBRM_20_1290; -.
DR VEuPathDB; TriTrypDB:LbrM.20.1290; -.
DR VEuPathDB; TriTrypDB:LBRM2903_200022100; -.
DR InParanoid; A4HAP3; -.
DR OMA; NIQSHDQ; -.
DR Proteomes; UP000007258; Chromosome 20.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR CDD; cd08638; DNA_pol_A_theta; 1.
DR Gene3D; 3.30.70.370; -; 1.
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; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR002298; DNA_polymerase_A.
DR PANTHER; PTHR10133; DNA POLYMERASE I; 1.
DR PANTHER; PTHR10133:SF27; DNA-DIRECTED DNA POLYMERASE; 1.
DR Pfam; PF00476; DNA_pol_A; 2.
DR PRINTS; PR00868; DNAPOLI.
DR SMART; SM00482; POLAc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE 4: Predicted;
KW Nucleotidyltransferase {ECO:0000313|EMBL:CAM38475.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007258};
KW Transferase {ECO:0000313|EMBL:CAM38475.1}.
FT DOMAIN 1015..1217
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT REGION 22..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..930
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1264 AA; 138295 MW; A7EF848785503CBF CRC64;
MDPFQRTADV TRYSFRVVPM THRNSTAGAK PSGSACSIPG GSPSSPSARG GAPAFGNLAS
GLPQCETTAW RQPSFREPLE SEETTRNVDK WRQFGLQMGT AVASQALPPL EQQQGQRLQP
QTIVCHRPEQ DTSTNSSLLY RQNTRFHSAE AQNEVQLRRQ CRLNRAAALA LPPHDEQSSA
HASPWPLPEA SSRVRAVVKS ALDNDDVVVL SDDGEHHTDG ENTVCQRQTV KPPPRSVSRT
DIRSPAPATL SQHAPDTSDG ACADVTRQLQ AELAKLSEKV QHSSEAQRCG PPKRNGGGEP
SLWAAKHWGG KKRRRETKTT HHNDGDEEAE AREGSERDET SAAMQGRSTS STDARRKLTA
RRRDCASTDT AADVSTEKRK RKTRGHGGDD AIFHGVSNQT LQTMLTPRTL FSLASSEAGG
SAMSNLQSEP AAVATISVPY VYLQDSAEGL FSDVRRALND PDRIQAPPLF VGVLALSGNR
NATTTLASVE CRTNFTYYGS GAKTAKHRVS CCFSSPDPVR SHQHVELVLI RWKDDMYGLP
AQTVGLTFLC RILTELPGVE LITFNAQVLL VALLAYCKGT LWSYCVSDVR VMAWMAQLHM
ASTLPKPPSP AYALAGEGSA TTVTGASDTD SSVLYDYGQL LLHVCGGKLP PNVQLEKTSP
VERLSPARGS FAESTGTAVA TTPAPPLTPA QRQLAHQVYY LATVYRSLYG LLGSKGLLQA
FLRQEKRIAP LLALLKYNGM PVDLHEVRRY QMSCETEMAR QRGLAHKLVP ELGEEFNIQS
HDQCRKALYE VLQLGKYLVQ SESAEAVGTT GLIITKGGRL STAEDTLRAL ARHHEFPACL
LRYRKVSKLM QTYIEGMMSY AVVRSRSKTS PPLSRDGVGT ETETSGAREG QQQLYDDDER
AVAERPSLLR EGVDVNDDSP FVDRRLHAGN NRHSPSGAEP RPARNQRNGE EEAYTMQADE
VILPATGYAT LHPNFLQEGT DTGRLSCVEP NLQNLPRNGI TSTEEEGEED LLGFRRCFVA
AAGCVLLSID YQQIELRVLA HLCGDPALVK ALTSSADIHQ TIAEVVFKKK PVSTEERSLA
KRVVFGVLYG AGPKTLATHM GVTVDRALHI TSLLTNAFPG INTYHRRVIA ETRANGFVRT
LSGRLRYLPD ICSTVLSRRS YAERQAFNSV VQGSAADVMK MAMLAVSKEV LQRYDRSDVS
LLSQIHDEMV FMVRKEHLRT VVPLLSSAMS HAMQLLVPLS VTVKFGTSLG DLQEWSVEHD
LGVG
//
