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DPOL_METJA
ID   DPOL_METJA              Reviewed;        1634 AA.
AC   Q58295;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=DNA polymerase;
DE            EC=2.7.7.7;
DE   Contains:
DE     RecName: Full=Mja pol-1 intein;
DE   Contains:
DE     RecName: Full=Mja pol-2 intein;
GN   Name=pol; OrderedLocusNames=MJ0885;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
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   -!- PTM: This protein undergoes a protein self splicing that involves a
CC       post-translational excision of the intervening region (intein) followed
CC       by peptide ligation. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR   EMBL; L77117; AAB98889.1; -; Genomic_DNA.
DR   PIR; E64410; E64410.
DR   AlphaFoldDB; Q58295; -.
DR   SMR; Q58295; -.
DR   STRING; 243232.MJ_0885; -.
DR   PRIDE; Q58295; -.
DR   EnsemblBacteria; AAB98889; AAB98889; MJ_0885.
DR   KEGG; mja:MJ_0885; -.
DR   eggNOG; arCOG00328; Archaea.
DR   eggNOG; arCOG00329; Archaea.
DR   eggNOG; arCOG03145; Archaea.
DR   HOGENOM; CLU_000203_6_4_2; -.
DR   InParanoid; Q58295; -.
DR   OMA; YAHNSYY; -.
DR   Proteomes; UP000000805; Chromosome.
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:0004519; F:endonuclease activity; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR   GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR   Gene3D; 1.10.132.60; -; 1.
DR   Gene3D; 3.10.28.10; -; 2.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.90.1600.10; -; 2.
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; IPR003586; Hint_dom_C.
DR   InterPro; IPR003587; Hint_dom_N.
DR   InterPro; IPR036844; Hint_dom_sf.
DR   InterPro; IPR027434; Homing_endonucl.
DR   InterPro; IPR006142; INTEIN.
DR   InterPro; IPR030934; Intein_C.
DR   InterPro; IPR004042; Intein_endonuc.
DR   InterPro; IPR006141; Intein_N.
DR   InterPro; IPR004860; LAGLIDADG_2.
DR   InterPro; IPR041005; PI-TkoII_IV.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF00136; DNA_pol_B; 3.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   Pfam; PF14528; LAGLIDADG_3; 1.
DR   Pfam; PF18714; PI-TkoII_IV; 1.
DR   PRINTS; PR00379; INTEIN.
DR   SMART; SM00305; HintC; 2.
DR   SMART; SM00306; HintN; 2.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF51294; SSF51294; 2.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF55608; SSF55608; 2.
DR   SUPFAM; SSF56672; SSF56672; 3.
DR   TIGRFAMs; TIGR01443; intein_Cterm; 2.
DR   TIGRFAMs; TIGR01445; intein_Nterm; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
DR   PROSITE; PS50818; INTEIN_C_TER; 2.
DR   PROSITE; PS50819; INTEIN_ENDONUCLEASE; 2.
DR   PROSITE; PS50817; INTEIN_N_TER; 2.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; DNA replication; DNA-binding;
KW   DNA-directed DNA polymerase; Nucleotidyltransferase; Protein splicing;
KW   Reference proteome; Repeat; Transferase.
FT   CHAIN           1..425
FT                   /note="DNA polymerase, 1st part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000007317"
FT   CHAIN           426..794
FT                   /note="Mja pol-1 intein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000007318"
FT   CHAIN           795..882
FT                   /note="DNA polymerase, 2nd part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000007319"
FT   CHAIN           883..1358
FT                   /note="Mja pol-2 intein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000007320"
FT   CHAIN           1359..1634
FT                   /note="DNA polymerase, 3rd part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000007321"
FT   DOMAIN          552..693
FT                   /note="DOD-type homing endonuclease 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
FT   DOMAIN          1163..1295
FT                   /note="DOD-type homing endonuclease 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
SQ   SEQUENCE   1634 AA;  191710 MW;  84A1FAFAB1F97DDD CRC64;
     MGMSMGKIKI DALIDNTYKT IEDKAVIYLY LINSILKDRD FKPYFYVELH KEKVENEDIE
     KIKEFLLKND LLKFVENIEV VKKIILRKEK EVIKIIATHP QKVPKLRKIK ECEIVKEIYE
     HDIPFAKRYL IDNEIIPMTY WDFENKKPVS IEIPKLKSVA FDMEVYNRDT EPNPERDPIL
     MASFWDENGG KVITYKEFNH PNIEVVKNEK ELIKKIIETL KEYDVIYTYN GDNFDFPYLK
     ARAKIYGIDI NLGKDGEELK IKRGGMEYRS YIPGRVHIDL YPISRRLLKL TKYTLEDVVY
     NLFGIEKLKI PHTKIVDYWA NNDKTLIEYS LQDAKYTYKI GKYFFPLEVM FSRIVNQTPF
     EITRMSSGQM VEYLLMKRAF KENMIVPNKP DEEEYRRRVL TTYEGGYVKE PEKGMFEDII
     SMDFRCHPKG TKVVVKGKGI VNIEDVKEGN YVLGIDGWQK VKKVWKYEYE GELINVNGLK
     CTPNHKIPLR YKIKHKKINK NDYLVRDIYA KSLLTKFKGE GKLILCKDFE TIGNYEKYIN
     DMDEDFILKS ELIGILLAEG HLLRRDIEYF DSSRGKKRIS HQYRVEITVN EDEKDFIEKI
     KYIFKKLFNY ELYVRRKKGT KAITLGCAKK DIYLKIEEIL KNKEKYLPNA ILRGFFEGDG
     YVNTVRRAVV VNQGTNNYDK IKFIASLLDR LGIKYSFYTY SYEERGKKLK RYVIEIFSKG
     DLIKFSILIS FISRRKNNLL NEIIRQKTLY KIGDYGFYDL DDVCVSLESY KGEVYDLTLE
     GRPYYFANGI LTHNSLYPSI IISYNISPDT LDCECCKDVS EKILGHWFCK KKEGLIPKTL
     RNLIERRINI KRRMKKMAEI GEINEEYNLL DYEQKSLKIL ANSILPDEYL TIIEEDGIKV
     VKIGEYIDDL MRKHKDKIKF SGISEILETK NLKTFSFDKI TKKCEIKKVK ALIRHPYFGK
     AYKIKLRSGR TIKVTRGHSL FKYENGKIVE VKGDDVRFGD LIVVPKKLTC VDKEVVINIP
     KRLINADEEE IKDLVITKHK DKAFFVKLKK TLEDIENNKL KVIFDDCILY LKELGLIDYN
     IIKKINKVDI KILDEEKFKA YKKYFDTVIE HGNFKKGRCN IQYIKIKDYI ANIPDKEFED
     CEIGAYSGKI NALLKLDEKL AKFLGFFVTR GRLKKQKLKG ETVYEISVYK SLPEYQKEIA
     ETFKEVFGAG SMVKDKVTMD NKIVYLVLKY IFKCGDKDKK HIPEELFLAS ESVIKSFLDG
     FLKAKKNSHK GTSTFMAKDE KYLNQLMILF NLVGIPTRFT PVKNKGYKLT LNPKYGTVKD
     LMLDEVKEIE AFEYSGYVYD LSVEDNENFL VNNIYAHNSV YGYLAFPRAR FYSRECAEIV
     TYLGRKYILE TVKEAEKFGF KVLYIDTDGF YAIWKEKISK EELIKKAMEF VEYINSKLPG
     TMELEFEGYF KRGIFVTKKR YALIDENGRV TVKGLEFVRR DWSNIAKITQ RRVLEALLVE
     GSIEKAKKII QDVIKDLREK KIKKEDLIIY TQLTKDPKEY KTTAPHVEIA KKLMREGKRI
     KVGDIIGYII VKGTKSISER AKLPEEVDID DIDVNYYIDN QILPPVLRIM EAVGVSKNEL
     KKEGAQLTLD KFFK
 
 
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