Protein data for FEN_METAC:

Description:
Flap structure-specific endonuclease (EC 3.1.-.-).

Molecular weight: 38164

View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):

DNA repair( GO:0006281 )


Important dates:
12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
07-MAR-2006, entry version 25.

Phylogenetic order:
Archaea Euryarchaeota Methanomicrobia Methanosarcinales Methanosarcinaceae Methanosarcina.

To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html

Links to references in other databases for protein FEN_METAC:

DatabasePointerAdd. info#1Add. info#2
EMBLAE011112AAM07354.1-
HSSPO936341B43
GenomeReviewsAE010299_GRMA4004.1
BioCycMACE188937:MA4004-MONOMER-.1
HAMAPMF_00614-1.
InterProIPR000513Exo_N_I.
InterProIPR008918HhH2.
InterProIPR006086XPG_I.
InterProIPR006085XPG_N.
InterProIPR006084XPGC_Rad.
PfamPF00867XPG_I1.
PfamPF00752XPG_N1.
PRINTSPR00853XPGRADSUPER.
SMARTSM00279HhH21.
SMARTSM00484XPGI1.
SMARTSM00485XPGN1.
PROSITEPS00841XPG_11.

General information about the databases mentioned above

Keywords:
Complete proteome; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease.

References:
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C2A / ATCC 35395 / DSM 2834;
RX MEDLINE=21929760; PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P.,
RA FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A.,
RA Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R.,
RA Linton L., McEwan P., McKernan K., Talamas J., Tirrell A., Ye W.,
RA Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M.,
RA Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A.,
RA Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K.,
RA Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C.,
RA Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T.,
RA Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E.,
RA Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic
RT and physiological diversity.";
RL Genome Res. 12:532-542(2002).

Feature:
CHAIN 1 338 Flap structure-specific endonuclease.
/FTId=PRO_0000154052.
METAL 154 154 Magnesium 1 (By similarity).

Comments:
-!- FUNCTION: Endonuclease that cleave the 5'overhanging flap
structure that is generated by displacement synthesis when DNA
polymerase encounters the 5'end of a downstream Okazaki fragment.
Has 5'endo-/exonuclease and 5'pseudo-Y-endonuclease activities.
Cleaves the junction between single and double-stranded regions of
flap DNA (By similarity).
-!- COFACTOR: Binds 2 magnesium ions per subunit (By similarity).
-!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1
subfamily.
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Sequence length: 338

     MGTDIGDLLQ KRKIELSDLS NRVVAVDAFN TLHQFLSIIR QRDGSPLVNS RGKVTSHLSG
     LLYRTASLVE AGIKPVFIFD GKPPDLKSET LSRRKEVRET SLEKWENAKA EGDLEAAYKY
     AQASSRVDQE IVEDSKYLLG IMGIPWIQAP CEGEAQAAHM VLKKDADYVA SQDYDSFLFG
     APKVVRNMAV TGKRKLPGKN VYVDVELEVI ELEETLRALE INRDQLIDIA ICVGTDYNKG
     LEKVGPKTAL KLIKKHGDIH AVLREKDMEI EGLDRIRKLF THPEVTEDYE IKWTKPDSEK
     LIKFLCEEND FSTDRVEKAA ERLKAASGAR QKTLDQWF