ID A0A0P7BR28_9HYPO Unreviewed; 826 AA.
AC A0A0P7BR28;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=DNA polymerase lambda {ECO:0000256|ARBA:ARBA00016513};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=AK830_g2708 {ECO:0000313|EMBL:KPM43870.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM43870.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM43870.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM43870.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00024632};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family.
CC {ECO:0000256|ARBA:ARBA00008323}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPM43870.1}.
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DR EMBL; LKCW01000026; KPM43870.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7BR28; -.
DR STRING; 78410.A0A0P7BR28; -.
DR OrthoDB; 49764at2759; -.
DR Proteomes; UP000050424; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd00141; NT_POLXc; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 1.10.150.110; DNA polymerase beta, N-terminal domain-like; 1.
DR Gene3D; 3.30.210.10; DNA polymerase, thumb domain; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR002054; DNA-dir_DNA_pol_X.
DR InterPro; IPR019843; DNA_pol-X_BS.
DR InterPro; IPR010996; DNA_pol_b-like_N.
DR InterPro; IPR028207; DNA_pol_B_palm_palm.
DR InterPro; IPR018944; DNA_pol_lambd_fingers_domain.
DR InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf.
DR InterPro; IPR037160; DNA_Pol_thumb_sf.
DR InterPro; IPR022312; DNA_pol_X.
DR InterPro; IPR002008; DNA_pol_X_beta-like.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR029398; PolB_thumb.
DR PANTHER; PTHR11276:SF43; DNA POLYMERASE IV; 1.
DR PANTHER; PTHR11276; DNA POLYMERASE TYPE-X FAMILY MEMBER; 1.
DR Pfam; PF14792; DNA_pol_B_palm; 1.
DR Pfam; PF14791; DNA_pol_B_thumb; 1.
DR Pfam; PF10391; DNA_pol_lambd_f; 1.
DR Pfam; PF14716; HHH_8; 1.
DR PRINTS; PR00869; DNAPOLX.
DR PRINTS; PR00870; DNAPOLXBETA.
DR SMART; SM00483; POLXc; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF47802; DNA polymerase beta, N-terminal domain-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81585; PsbU/PolX domain-like; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS00522; DNA_POLYMERASE_X; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000050424};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 171..266
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 56..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 548
FT /note="Nucleophile; Schiff-base intermediate with DNA; for
FT 5'-dRP lyase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR622312-50"
SQ SEQUENCE 826 AA; 92548 MW; BE93403ECF3A6790 CRC64;
MASLQEKTAF FSQLQPLYSD DEFDAEEQGE RKRCRSFFKA TPVPVRQEPV VLDLTKDEPP
KARATPRRVA SAPTPFPSGG AQVIKGTPMA AFRRKGRLGS LLDAQSPDVI LVDDTPIPES
TRPAQRRISR SDSTPAFPSK RLLGVAREDS PSPSIAMKKR KREPVLKLRP EREQVFKGLS
FFYVPDNDIA PARRLRIAKA REFGATWTRN PGDATHIVVE KSIAFKDVEG VLKSASKALP
PKVVNEDYPI DCIQFKALLE WNQKKYQLAG QPVVECESAA SIAPSSSNES VLSLQLKPPP
ANPKRWDFAP LSGTPTRSEE SPEPSRVVLT PILTDSQPVI LDLEAVVESP PNASDSEEWE
AGGTDANNQG PADDKATKNV SSIQRDTQNL RMENAGSRDE PNDELTEYIN LMQQYKDLPL
DVDEDDTHSV LDTADGSDAV ETSGSEGERV KKCRLAKRKT RSGRKKMAYE ERFSCNTAGA
KDAKAGNPNT RTMEVLQLMA DYYDRVNDHW RTTAYRRAIS TLKRQDAKVT TEEEALLLPS
IGQRLAQKIE EIVTTDRLQR LEYAQDESMA KPLQLFLGIY GVGNRQAQQW IAQGFRTLED
LKGKANLTRN QLVGVNHYDD LNTRIPRREV EALGAVVQKA SQEVDPKIQL IIGGSYRRGA
ESSGDIDFIV TKPNTESSGD LRPALDELVR RLEADKFLVV RLASSRTDSE GSKWHGCCVL
PRLAGGFNDD ESYRPTWRRI DFLLVPESEM GAALLYFTGN DIFNRSMRLL ASKKGMRLNQ
RGLYRDVMRG PQRAKVTEGE LVEGRDERRI FEILGVKWRE PHERWC
//
