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Database: UniProt
Entry: M7NTG6_PNEMU
LinkDB: M7NTG6_PNEMU
Original site: M7NTG6_PNEMU 
ID   M7NTG6_PNEMU            Unreviewed;      1086 AA.
AC   M7NTG6;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   08-MAY-2019, entry version 39.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=PNEG_01633 {ECO:0000313|EMBL:EMR10381.1};
OS   Pneumocystis murina (strain B123) (Mouse pneumocystis pneumonia agent)
OS   (Pneumocystis carinii f. sp. muris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Pneumocystidomycetes; Pneumocystidaceae; Pneumocystis.
OX   NCBI_TaxID=1069680 {ECO:0000313|EMBL:EMR10381.1, ECO:0000313|Proteomes:UP000011958};
RN   [1] {ECO:0000313|Proteomes:UP000011958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B123 {ECO:0000313|Proteomes:UP000011958};
RX   PubMed=26899007; DOI=10.1038/ncomms10740;
RA   Ma L., Chen Z., Huang D.W., Kutty G., Ishihara M., Wang H.,
RA   Abouelleil A., Bishop L., Davey E., Deng R., Deng X., Fan L.,
RA   Fantoni G., Fitzgerald M., Gogineni E., Goldberg J.M., Handley G.,
RA   Hu X., Huber C., Jiao X., Jones K., Levin J.Z., Liu Y., Macdonald P.,
RA   Melnikov A., Raley C., Sassi M., Sherman B.T., Song X., Sykes S.,
RA   Tran B., Walsh L., Xia Y., Yang J., Young S., Zeng Q., Zheng X.,
RA   Stephens R., Nusbaum C., Birren B.W., Azadi P., Lempicki R.A.,
RA   Cuomo C.A., Kovacs J.A.;
RT   "Genome analysis of three Pneumocystis species reveals adaptation
RT   mechanisms to life exclusively in mammalian hosts.";
RL   Nat. Commun. 7:10740-10740(2016).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-
CC         COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7;
CC         Evidence={ECO:0000256|RuleBase:RU000442};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|RuleBase:RU000442};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU000442}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|RuleBase:RU000442}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EMR10381.1}.
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DR   EMBL; AFWA02000004; EMR10381.1; -; Genomic_DNA.
DR   RefSeq; XP_007873590.1; XM_007875399.1.
DR   STRING; 263815.XP_007873590.1; -.
DR   EnsemblFungi; EMR10381; EMR10381; PNEG_01633.
DR   GeneID; 19895327; -.
DR   OrthoDB; 20210at2759; -.
DR   Proteomes; UP000011958; Unassembled WGS sequence.
DR   GO; GO:0043625; C:delta DNA polymerase complex; IEA:EnsemblFungi.
DR   GO; GO:0000784; C:nuclear chromosome, telomeric region; IEA:EnsemblFungi.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:1904161; P:DNA synthesis involved in UV-damage excision repair; IEA:EnsemblFungi.
DR   GO; GO:1903459; P:mitotic DNA replication lagging strand elongation; IEA:EnsemblFungi.
DR   Gene3D; 1.10.132.60; -; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.90.1600.10; -; 1.
DR   InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR   InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR   InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR   InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR   InterPro; IPR042087; DNA_pol_B_C.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR025687; Znf-C4pol.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   Pfam; PF14260; zf-C4pol; 1.
DR   PRINTS; PR00106; DNAPOLB.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|RuleBase:RU000442};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000011958};
KW   DNA replication {ECO:0000256|RuleBase:RU000442};
KW   DNA-binding {ECO:0000256|RuleBase:RU000442};
KW   DNA-directed DNA polymerase {ECO:0000256|RuleBase:RU000442};
KW   Iron {ECO:0000256|RuleBase:RU000442};
KW   Iron-sulfur {ECO:0000256|RuleBase:RU000442};
KW   Metal-binding {ECO:0000256|RuleBase:RU000442};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU000442};
KW   Nucleus {ECO:0000256|RuleBase:RU000442};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011958};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN      123    461       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      525    956       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN      993   1065       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   COILED       60     83       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1086 AA;  125172 MW;  1F72C41661A57671 CRC64;
     MSKISKIKRK DIEVLQDIKN DLFMDNDIKK RRISEENSYD LEFITQKKAL KYKKTLRSFK
     NDLECIIQEL LENQQENKNE NQKWERPSLP LIDPINDDIY FQQIEIDDTM SVSGPILRLY
     GVTEQENSVL CTVTGFFPYF YVPSPQGFYE EHINSFKIAL ENTVNFSSKV INNIELVMRQ
     TIYGFHKDGK TQYIKITVND PKHIARVRNL FERGDINFNN MFPPQYITFE SNLPYALRFM
     IDTSITGMSW VKLPKTKYLI VDEKTSNCQL EVFIDWKDLE TFQPEGNWQK IAPLRILSFD
     IECAGRKGVF PEPEIDPVIQ IANVVTLYGE KTPFIRNVFT IDTCAQISGA QILSYADQKE
     LLLAWSKFIQ KTDPDVIIGY NIANFDIPYL IDRAKHLKVN DFPYFGRIIR QKCEINNTSF
     SSRAYGTRES RFTDISGRLQ LDMLQIMQRD YKLRSYTLNA VSSQFLNEQK EDVHHSIITD
     LQNGTSESRR RLAVYCLKDA YLPQRLMDKL MSLVNYIEIA RVTGVPFSYI LSRGQQIRIV
     SQLSRKAREK GFIIPNVKSE GIDEQYEGGT VIDPKKGYYN VPIATLDFTS LYPSIMQAHN
     LCYTTLISYK QIEILGFKKD RDYHVTPENY CFVKPHIRKG LLPQIFENLL AARQKAKLDL
     KNETEPFKKA VLDGRQLALK ISANSVYGFT GATNGKLPCL PISSSVTSYG RQMIEKAKDE
     IELKYTLENG YTHNAQVIYG DTDSVMIDFG VKDIAESMRL GCEAADYVTS KLIKPIKLEF
     EKVYFPYLLI SKKRYAGLYW TKPETFDKMD SKGIETIRRD NCRLVSTVIE TALRKLLIDR
     DIDDAQNYVK KVISELLQNK IDISNLVITK TLTKSDYVSK QAHVELAERI RKRDSGLAPT
     LGDRVAYIIV KGAKGDQTFL RSEDPIYVLE NNIPIDTKYY LDNQLSKPLL RIFEPILGEK
     ANSLLSGDHT RTISMTSPAI GGLVKFTVKT ATCIGCRIPL KNDSNAVVCN HCVGRTAELY
     QKQLNLVSDL EIRFAKLWTQ CQRCQSSLHQ DVLCTSKDCP IFYMRKKVQK DIKENIEILE
     RFNENW
//
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