ID Q5KLX6_CRYNJ Unreviewed; 1989 AA.
AC Q5KLX6;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 2.
DT 27-MAR-2024, entry version 122.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN OrderedLocusNames=CNB03700 {ECO:0000313|EMBL:AAW41897.2};
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684 {ECO:0000313|EMBL:AAW41897.2, ECO:0000313|Proteomes:UP000002149};
RN [1] {ECO:0000313|EMBL:AAW41897.2, ECO:0000313|Proteomes:UP000002149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565 {ECO:0000313|Proteomes:UP000002149};
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J., Koo H.L., Krzywinski M.I., Kwon-Chung J.K.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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|RuleBase:RU000442};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966,
CC 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|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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DR EMBL; AE017342; AAW41897.2; -; Genomic_DNA.
DR RefSeq; XP_569204.1; XM_569204.1.
DR STRING; 214684.Q5KLX6; -.
DR PaxDb; 214684-Q5KLX6; -.
DR EnsemblFungi; AAW41897; AAW41897; CNB03700.
DR VEuPathDB; FungiDB:CNB03700; -.
DR eggNOG; KOG0968; Eukaryota.
DR HOGENOM; CLU_000203_3_1_1; -.
DR InParanoid; Q5KLX6; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000002149; Chromosome 2.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016035; C:zeta DNA polymerase complex; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0042276; P:error-prone translesion synthesis; IBA:GO_Central.
DR CDD; cd05778; DNA_polB_zeta_exo; 1.
DR CDD; cd05534; POLBc_zeta; 1.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1.
DR Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR030559; PolZ_Rev3.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR025687; Znf-C4pol.
DR PANTHER; PTHR45812; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR45812:SF1; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
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; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|RuleBase:RU000442};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication {ECO:0000256|RuleBase:RU000442};
KW DNA-binding {ECO:0000256|RuleBase:RU000442};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU000442};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000442};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU000442};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000442};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442}; Nucleus {ECO:0000256|RuleBase:RU000442};
KW Reference proteome {ECO:0000313|Proteomes:UP000002149};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000442};
KW Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT DOMAIN 1140..1317
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 1383..1829
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1887..1956
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1850..1878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..747
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..894
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..925
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1989 AA; 222472 MW; C6D3F8C33990B04B CRC64;
MEDTAVVNQG PSSSLPVGSS QSLSLSSPRL RVKITHIVSD QAAPIPTLRQ HYAPSRLATA
IPLGNLPHSV PVIRIFGTTS SSQKICANIH LCYPYFFVPY PMDSQDPLRP ERVVKLCQRF
AVSLNHAICL ALRQNPTSAA NNTNYGGGVD PKHLHVVSVI LVKGTPFYGY HLGFDYFLKI
NLANPARLHI ALEQLRKPNV LGREWQPHEA HLNHVLQFMC DFDLYGCGWL ELGGGTFREP
VPEADPFDSL SETVTDGTLG LLNCRTIPTS MLYPPGLSPA KDSFTSLEID ILPHQILNRQ
RLMPRLLHHD FIELLHKPLD PNEKLVPAVA ELWEDERRRR AAKGLGTGTN DMMPGSGGMD
GRSMEELGYR GNQVDGKKNK GGDWKISDEL WAILEERMGA ERKRKGKLTF QKYSRDVSAG
REGEKLQWDK WIMTTFDALS AHWPKQAKKV TKTTQMSRKS HMTLPADTSS IYYGSSQDKN
ALFGESTSVT LEEPGMDSRL EKEDEEINPF EAFAMTQASQ HPQPVPELSQ HVQAVPFKEV
EDSDQYYVGE DEGDIDEYKQ AEGARVHAQE TDKIRATQMA SEMEGHYDEY DDKELEELFR
QTVAAGLGIQ SVPTTPHKPK DQDQEGNSRW SGWTPTSKGS SKSSVGTFES RKRKRNQRLL
EDAGLGDLST IIDRSSLSLS PLKNPYDERG HGVSTPENAN TPSREMATPS SLMRNAFAKS
RQQSPNLSPA KRSESSRSKH LRSDTVILPL ERKNPGAITS SPSLSPRDKV IDGDHGNLQR
KLAEAKKPLQ GQFPSASAKK NLVVGPEPGQ EVVQLSLPPA GAGLYEPVAN VVSPVVSNSS
RPIGLVESHL SSTLLNPSFR DKTSDLPLSA TLLNAPSAKP ALSPTFQDPS ANDERLPISP
SIVATHRDDR EAKVRPHKRV KLTEPGHASQ ESLLPLIRNF SHPSHGDRHR SPQNAASDHQ
ENLSSCLASK AWQYYILPPQ RHEIADTMEL HGVSTVDYQP PFFGQLADVP KRSKTLAGRV
FNLKSHSVRN LQKFESTIGS GPLLENAKGK ERAKAGWLKT NSDNDSVGKV RWNLGWEYAP
RPPSKREVKR WCEKIEDKAK IAREKYEEKT SQLAHPTQKS KYGFKYSQKG KVRDSSGDPQ
NMSILTMEVF AQSRGTLLPD PEKDAVTAIF YCYSNTDDDL PDTTIYPGYH AGYVVTSALA
NPARLRLDDI PFEIVEDELA LINWVIDIVK FWDPDVLAGW ELHNSSWGYL AARASGEFAM
DMMDQISRII SGRTGPRNDG YSAHHSSTFK VVGRHTLNIW RICRSEINLT QYTFENVVFH
LLHQRIPHYS PSSLTALWKS KYPSHACRVL KYFFQRTVMC MEILDQAEII TKTAEFARVF
GVDFASVLTR GSQYKVESFI FRIAKPESFV LVSPSKQQVG LQNAPFAVPL IAEPESKYYT
HPVIVLDFQS LYPSIMIAYN ICYSTCLGRV EMFKGTNKFG FTNLKVTEGL LELLKDYLTV
TPNGMIFVKP AIRKSLLAKM LGEILDTRVM IKHAMKGARG DKSLTAMHNA RQLGLKLMAN
VTYGYTSATY SGRMPCIEIA DSIVQTGRET LEKAQELIHS RVDWDARVVY GDTDSLFVAL
PGRSKEQAFK IGYDIANAVT ALNPKPVKLK FEKVYMGSVL MAKKRYVGFK YEHPDDTEPS
FDAKGIETIR RDGFPAQQKM EEVCLKLLFR TQDLSKVKEF CLKEWTKILQ GHVSMQDFII
AKEVRLGTYS EKGIPPPGAA VAYRRILKDP RDEPQYAERV PYLISNADGR RLIDRARMPE
ELLSSRSLSI DAEYYIRNLL IPPLSRIFNL VGADVEEWYD SMPKTKRLGK YDKAGGKMTN
RGNGKGKQGE AKGRGSRIDS HFRSSHCVVC GIESSDVLCH PCRLDPSTTS HALLSRLHIA
QDKLIVLQKI CASCSSVPPA EKILCDSIDC PNTFARVAAE REVEDLEDVG ELLLELKLED
ERPEIDLSW
//
