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DPOE_CRYNB
ID   DPOE_CRYNB              Reviewed;        2250 AA.
AC   P0CN27; Q55JX3; Q5K9M7;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=DNA polymerase epsilon catalytic subunit A;
DE            EC=2.7.7.7 {ECO:0000250|UniProtKB:P15436};
DE   AltName: Full=DNA polymerase II subunit A;
GN   Name=POL2; OrderedLocusNames=CNBK2100;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
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.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
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   -!- FUNCTION: DNA polymerase II participates in chromosomal DNA
CC       replication. {ECO:0000250}.
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:0000250|UniProtKB:P15436};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:P15436};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P15436};
CC   -!- SUBUNIT: Heterotetramer. Consists of 4 subunits: POL2, DPB2, DPB3 and
CC       DPB4 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The CysA-type zinc finger is required for PCNA-binding.
CC       {ECO:0000250|UniProtKB:P15436}.
CC   -!- DOMAIN: The CysB motif binds 1 4Fe-4S cluster and is required for the
CC       formation of polymerase complexes. {ECO:0000250|UniProtKB:P15436}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR   EMBL; AAEY01000052; EAL18192.1; -; Genomic_DNA.
DR   RefSeq; XP_772839.1; XM_767746.1.
DR   AlphaFoldDB; P0CN27; -.
DR   SMR; P0CN27; -.
DR   EnsemblFungi; AAW46304; AAW46304; CNK01430.
DR   EnsemblFungi; EAL18192; EAL18192; CNBK2100.
DR   GeneID; 4938907; -.
DR   KEGG; cnb:CNBK2100; -.
DR   VEuPathDB; FungiDB:CNBK2100; -.
DR   HOGENOM; CLU_000556_0_1_1; -.
DR   Proteomes; UP000001435; Chromosome 11.
DR   GO; GO:0008622; C:epsilon DNA polymerase complex; IEA:InterPro.
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:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; 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; IPR013697; DNA_pol_e_suA_C.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR029703; POL2.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10670; PTHR10670; 1.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   Pfam; PF08490; DUF1744; 1.
DR   SMART; SM01159; DUF1744; 1.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; DNA replication; DNA-binding; DNA-directed DNA polymerase; Iron;
KW   Iron-sulfur; Metal-binding; Nucleotidyltransferase; Nucleus; Transferase;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..2250
FT                   /note="DNA polymerase epsilon catalytic subunit A"
FT                   /id="PRO_0000410067"
FT   ZN_FING         2118..2159
FT                   /note="CysA-type"
FT                   /evidence="ECO:0000250|UniProtKB:P15436"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          235..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1990..2010
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           2190..2207
FT                   /note="CysB motif"
FT                   /evidence="ECO:0000250|UniProtKB:P15436"
FT   COMPBIAS        236..259
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         2118
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P15436"
FT   BINDING         2121
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P15436"
FT   BINDING         2156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P15436"
FT   BINDING         2159
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P15436"
FT   BINDING         2190
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P15436"
FT   BINDING         2193
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P15436"
FT   BINDING         2205
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P15436"
FT   BINDING         2207
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P15436"
SQ   SEQUENCE   2250 AA;  255999 MW;  30EED4407247B80B CRC64;
     MPSRGSFRGR GRGSGSGFGS NTRFTGRRRG RGGGGGGGGV AYGIDRRPAT STNQANREDG
     TAATEKFEEV KVYDEIDEKI GFWRFESVRA EGEEKVGWLV NMHQTLVPSD VHPGGLAAVD
     YYFIQDDGGS FKVSIPYEPY FYLTCRGGTE SIVEEWLLKR YEGIIIRIER EKKWDLSLPN
     HLLSAPPVFL KLFFHNTADL QTIRRDLLPL ARSNSEKFTA VDAYADVVSA EAAANGHGDD
     ENRAWGAEDD TKKKKDKEPS ECIIEVREHD LAYHLRVAID LNIRVGLWYT VTSRTGVITL
     ERIPDRVKRA DPVVMAYDIE TTKQPLKFPD QQTDQIMMIS YMIDGMGYLI TNREIVGEDI
     DDFEYTPKDE YPGEFTVFNE PDEPAVIRRW FEHIRDSKPT VIATYNGDSF DFPFVDARAK
     IHGISMYEEI GFKPDIEEEY KSRSTMHMDC FRWVKRDSYL PQGSQGLKAV TTAKLGYNPI
     ELDPELMTPY AIEQPQILAQ YSVSDAVATY YLYMKYVHPF IFSLCNIIPL SPDEVLRKGT
     GTLCETLLMV EAYDAHIIMP NRHEDPHGVT YEGHLLASET YVGGHVEALE AGVFRSDIPT
     HFKIVPSAIQ ELIDDLDAAL RFSLIEEGQV KLEDVENYDE VKQQIQTALE TMRDEPNRFD
     NPLIYHLDVA AMYPNIMLSN RLQPDSVKEE ADCAVCDYNR PDKKCDRRME WAWRGEYFPA
     KRDEVNMVRY ALEQETFPPK RPYDPKRRFV DLTPTEQSAL LHKRLGDYSR KVYKKTHDTK
     IVTKTTIICQ RENSFYIDTV RAFRDRRYEY KGLHKTWKKN LDKAFEEGGA VATVDEAKKM
     IVLYDSLQLA HKCILNSFYG YVMRKGARWY SMEMAGITCL TGATIIQMAR QLVEQIGRPL
     ELDTDGIWCM LPGVFPEDFN FKLKNGKKFG ISYPCTMLNH LVHAQFTNDQ YHELVNNDSG
     TYNVKKENSI FFELDGPYKA MILPSSKEED KLLKKRYAVF NPDGSLAELK GFEVKRRGEL
     QMIKIFQSQI FDKFLLGKTT EECYAAVATV ADQWLDILQS KASSLHDDEL VDLIAENRSM
     SKTLAEYAGQ KSTSISTARR LAEFLGEQMV KDKGLSCRFI ISAKPNGAPV TERAVPVAIF
     TAEEPVKRHY LRKWLKDNSL TDFDLRTILD WDYYTERLGS VIQKLITIPA ALQKVPNPVP
     RIRHPDWLYK RIATKEDKFQ QHKITDMFTK LKDMEDLGDG QKKVGPKLAV VRRRNRKEQE
     KESEVEEVPP EPEYDYAGYI RIMKKKWRKQ RQEKARARKS GLRQDGTISS MLRTQTSSMN
     SKQWDVIQIA STNRPGEFKL WLAIDGTFQS VRLKVPREFY LNFKEDPEPQ MLATDRYEAV
     EVVRTLPRGQ PARHLYKLSV DEVLFMEGES HFSTLINNPN VDGAFELQVP LVVRALLSLG
     TSCALRSNIL GGLNRGLDKG FDLVDLERSG NLSRRKYLNE GRGIRYHFLF HAVADQRHII
     GLFSPDSTNA SIYLVDRAKN RQQLPNPLKF YTDRVERAER GVFSYPDMLD FTTSYHSSES
     SAFKALGKDL QAINHGLNVI ALCSPFEHSY YQAKAPVYSN FPFITYRLGK EEDPGLMWLL
     QTSRRMIGLY LRLSSWLKEQ IQIASHFDVP IGNLGADIAV FLADIEFARR LKQQDMLIWW
     SSTPRPDLGG SEEDANSSED LVSPHISNRG CYSSTVLEME VSDLAINAVL QSALVNEMEG
     SGTGSLAFDS ASHNLDEYAK GAVNTSVMLG DAVLSTQTFG VLKSMLRAWY ADKARAHVKG
     DSLSPAEIVV DQFWRWISSS TSSMFEPALH RFLHGLMRKT FLQLLAEFKR LGTQVVYADF
     GRVFLLTSKP DAGSAFAFAK YLVAAANSQE LFRHLIIDVA QFWNYLAWMD VANFGGVKVS
     PETAASREPP AKRFEISMDW NIQSFLPGTL QPVFERNVAS FIFSLYSAKR SSSDGREPLR
     VIHSLNIDQP GTEATSTMNP TKEKEKKAAS KSISQTLTRR LLSDIAAVKR QQAAVHLEPE
     EAYTLAFPDL PGARSKRINP TLELIKAITE VYSLASEHSI EVQILKRNLL DLIGVKEFSS
     DAAFNPPCES IEVPMVICKK CNAIRDVDLC RDPDRLPSVN PDSGEMLEPA RKNWVCHKCD
     SEYDRFQIEQ PLIEMVTKTI TNYQIQDVIC LKCSQTKSDN LAATCKCGGG FRTTSNRNEL
     KTKLKMIKSV CDYHKLPFAG SYVEETLSRW
 
 
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