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UniProtKB/Swiss-Prot entry Q9V2F4


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DP2L_PYRAB
Primary accession number Q9V2F4
Secondary accession numbers None
Integrated into Swiss-Prot on April 27, 2001
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 55)
Name and origin of the protein
Protein name DNA polymerase II large subunit
Synonyms Pol II
EC 2.7.7.7
Contains Pab polC intein
     (Pab pol II intein)
Gene name
Name: polC
OrderedLocusNames: PYRAB01200
ORFNames: PAB2404
From
Pyrococcus abyssi [TaxID: 29292] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; Pyrococcus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=GE5 / Orsay;
DOI=10.1046/j.1365-2958.2003.03381.x; PubMed=12622808 [NCBI, ExPASy, EBI, Israel, Japan]
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.;
"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.";
Mol. Microbiol. 47:1495-1512(2003).
Comments
  • FUNCTION: Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase (By similarity).
  • CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
  • CATALYTIC ACTIVITY: Degradation of single-stranded DNA. It acts progressively in a 3'- to 5'-direction, releasing nucleoside 5'-phosphates.
  • SUBUNIT: Heterodimer of a large subunit and a small subunit (By similarity).
  • PTM: This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation (Potential).
  • SIMILARITY: Belongs to the archaeal DNA polymerase II family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AJ248283; CAB49044.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E75199; E75199.
RefSeq NP_125813.1; -.
3D structure databases
ModBase Q9V2F4.
Enzyme and pathway databases
BioCyc PABY272844:PAB2404-MON; -.
Ontologies
GO
GO:0008408; Molecular function: 3'-5' exonuclease activity (inferred from electronic annotation from HAMAP).
GO:0003677; Molecular function: DNA binding (inferred from electronic annotation from HAMAP).
GO:0003887; Molecular function: DNA-directed DNA polymerase activity (inferred from electronic annotation from HAMAP).
GO:0000738; Biological process: DNA catabolic process, exonucleolytic (inferred from electronic annotation from HAMAP).
GO:0006261; Biological process: DNA-dependent DNA replication (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00324; -; 1.
PBIL [Tree]
InterPro IPR003587; Hedgehog_hint_N.
IPR006141; Intein_splicing_site.
IPR004475; PolC_DP2.
IPR016033; PolC_DP2_N.
Graphical view of domain structure.
Pfam PF03833; PolC_DP2; 1.
Pfam graphical view of domain structure.
SMART SM00306; HintN; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR01445; intein_Nterm; 1.
TIGR00354; polC; 1.
PROSITE PS50818; INTEIN_C_TER; 1.
PS50817; INTEIN_N_TER; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9V2F4.
Genome annotation databases
GeneID 1495007; -.
GenomeReviews AL096836_GR; PYRAB01200.
KEGG pab:PAB2404; -.
NMPDR fig|272844.1.peg.131; -.
Phylogenomic databases
HOGENOM Q9V2F4; -.
Genome annotation databases
CMR Q9V2F4; PYRAB01200.
Other
ProtoNet Q9V2F4.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Autocatalytic cleavage; Complete proteome; DNA replication; DNA-binding; DNA-directed DNA polymerase; Exonuclease; Hydrolase; Multifunctional enzyme; Nuclease; Nucleotidyltransferase; Protein splicing; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1    954  954     DNA polymerase II large subunit, 1st part (Potential). PRO_0000007304
CHAIN   955   1139  185     Pab polC intein (Potential). PRO_0000007305
CHAIN   1140   1455  316     DNA polymerase II large subunit, 2nd part (Potential). PRO_0000007306
Sequence information
Length: 1455 AA [This is the length of the unprocessed precursor] Molecular weight: 165711 Da [This is the MW of the unprocessed precursor] CRC64: BB092E7BB2FE0D21 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MELPKEMEEY FEMLQREIDK AYEIAKKARA QGKDPSLDVE IPQATDMAGR VESLVGPPGV 

        70         80         90        100        110        120 
AKRIRELVKE YGKEIAALKI VDEIIEGKFG DLGSREKYAE QAVRTALAIL TEGIVSAPIE 

       130        140        150        160        170        180 
GIANVKIKRN TWADNSEYLA LYYAGPIRSS GGTAQALSVL VGDYVRRKLG LDRFKPSEKH 

       190        200        210        220        230        240 
IERMVEEVDL YHRAVTRLQY HPSPEEVRLA MRNIPIEITG EATDDVEVSH RDVPGVETNQ 

       250        260        270        280        290        300 
LRGGAILVLA EGVLQKAKKL VKYIDKMGIE GWEWLKEFVE AKEKGEPKEE GKEESLAEST 

       310        320        330        340        350        360 
LEETKVEVDM GFYYSLYQKF KEEIAPSDKY AKEVIGGRPL FSDPSKPGGF RLRYGRSRAS 

       370        380        390        400        410        420 
GFATWGINPA TMILVDEFLA IGTQLKTERP GKGAVVTPVT TIEGPIVKLK DGSVLRVDDY 

       430        440        450        460        470        480 
NLALKVREDV EEILYLGDAV IAFGDFVENN QTLLPANYCE EWWILEFVKA LKEIYEVHLE 

       490        500        510        520        530        540 
PFTENEEESI EEASDYLEID PEFLKEMLRD PLRVKPPVEL AIHFSEVLGI PLHPYYTLYW 

       550        560        570        580        590        600 
NSVEPKDVEK LWRLLKNYAE IEWSNFRGIK FAKKIVISQE KLGDSKRTLE LLGLPHTVRD 

       610        620        630        640        650        660 
GNVIVDYPWA AALLTPLGNL NWEFMAKPLY ATIDIINENN EIKLRDRGIS WIGARMGRPE 

       670        680        690        700        710        720 
KAKERKMKPP VQVLFPIGLA GGSSRDIKKA AEEGKVAEVE IAFFKCPKCG HVGPEHLCPN 

       730        740        750        760        770        780 
CGTRKELLWV CPRCNAEYPE SQAEGYNYTC PKCNVKLRPY AKRKIRPSEL LNRAMENVKV 

       790        800        810        820        830        840 
YGVDKLKGVM GMTSGWKMPE PLEKGLLRAK NDVYVFKDGT IRFDATDAPI THFRPREIGV 

       850        860        870        880        890        900 
SVEKLRELGY THDFEGKPLV SEDQIVELKP QDIILSKEAG RYLLKVAKFV DDLLEKFYGL 

       910        920        930        940        950        960 
PRFYNAEKME DLIGHLVIGL APHTSAGIVG RIIGFVDALV GYAHPYFHAA KRRNCFPGDT 

       970        980        990       1000       1010       1020 
RILVQIDGVP QKITLRELYE LFEDERYENM VYVRKKPKRE IKVYSIDLET GKVVLTDIED 

      1030       1040       1050       1060       1070       1080 
VIKAPATDHL IRFELEDGRS FETTVDHPVL VYENGRFIEK RAFEVKEGDK VLVSELELVE 

      1090       1100       1110       1120       1130       1140 
QSSSSQDNPK NENLGSPEHD QLLEIKNIKY VRANDDFVFS LNAKKYHNVI INENIVTHQC 

      1150       1160       1170       1180       1190       1200 
DGDEDAVMLL LDALLNFSRY YLPEKRGGKM DAPLVITTRL DPREVDSEVH NMDIVRYYPL 

      1210       1220       1230       1240       1250       1260 
EFYEATYELK SPKELVGVIE RVEDRLGKPE MYYGLKFTHD TDDIALGPKM SLYKQLGDME 

      1270       1280       1290       1300       1310       1320 
EKVRRQLEVA KRIRAVDEHG VAEKILNSHL IPDLRGNLRS FTRQEFRCVK CNTKFRRPPL 

      1330       1340       1350       1360       1370       1380 
NGKCPVCGGK IVLTVSKGAI EKYLGTAKML VTEYNVKNYT RQRICLTERD IDSLFENVFP 

      1390       1400       1410       1420       1430       1440 
ETQLTLIVNP NDICQRLVMA RTGEVNKSGL LENLSNGSKK TEKAEKAEKP RKKSDEKPKK 

      1450 
KRVISLEEFF SRKSK 

Q9V2F4 in FASTA format

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