ID F6HSN3_VITVI Unreviewed; 873 AA.
AC F6HSN3;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=DNA ligase 6 {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=VIT_14s0006g02190 {ECO:0000313|EMBL:CCB57674.1};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB57674.1, ECO:0000313|Proteomes:UP000009183};
RN [1] {ECO:0000313|Proteomes:UP000009183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX PubMed=17721507; DOI=10.1038/nature06148;
RG The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase (DRMBL)
CC family. {ECO:0000256|ARBA:ARBA00010304}.
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DR EMBL; FN596245; CCB57674.1; -; Genomic_DNA.
DR AlphaFoldDB; F6HSN3; -.
DR STRING; 29760.F6HSN3; -.
DR PaxDb; 29760-VIT_14s0006g02190-t01; -.
DR EnsemblPlants; Vitvi14g01055_t001; Vitvi14g01055_P001; Vitvi14g01055.
DR Gramene; Vitvi14g01055_t001; Vitvi14g01055_P001; Vitvi14g01055.
DR eggNOG; KOG0967; Eukaryota.
DR eggNOG; KOG1361; Eukaryota.
DR HOGENOM; CLU_005138_3_0_1; -.
DR InParanoid; F6HSN3; -.
DR Proteomes; UP000009183; Chromosome 14.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0035312; F:5'-3' DNA exonuclease activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR GO; GO:0036297; P:interstrand cross-link repair; IBA:GO_Central.
DR CDD; cd16273; SNM1A-1C-like_MBL-fold; 1.
DR Gene3D; 3.40.50.12650; -; 1.
DR Gene3D; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR InterPro; IPR036599; DNA_ligase_N_sf.
DR InterPro; IPR011084; DRMBL.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR PANTHER; PTHR23240; DNA CROSS-LINK REPAIR PROTEIN PSO2/SNM1-RELATED; 1.
DR PANTHER; PTHR23240:SF35; DNA REPAIR METALLO-BETA-LACTAMASE FAMILY PROTEIN-RELATED; 1.
DR Pfam; PF04675; DNA_ligase_A_N; 1.
DR Pfam; PF07522; DRMBL; 1.
DR SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000009183}.
FT DOMAIN 273..374
FT /note="DNA repair metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF07522"
FT DOMAIN 778..870
FT /note="DNA ligase ATP-dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04675"
FT REGION 15..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..34
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 873 AA; 97423 MW; D9991C97D1DD785E CRC64;
MTLDSAHLFL NSHKSLSQHQ SPQPPPPPSL SFLSNHSPLP PIPTNFPQSK LIPKSRFVVD
GFRCSGDYSV TYFLSHFHSD HYSGLSPKWS NGIIFCSNTT ARLLVEVLGV SSLFVYPLAV
SQPVLIDGCE VALLDANHCP GAVQFLFKVP GVDGRFERYV HTGDFRFCES MKLEPCLGEF
VGSEAVFLDT TYCNPKFVFP SQDESVDYIV EAIERIGLEN KGLMKSVLFL VATYVIGKER
ILLEISRRRN CKIHVDGRKM SVLRVLGYED GGVFTEDESK SDVHVVGWNV LGETWPYFRP
NFVKMKEIMI ERGYSKVVGF VPTGWTYEVK RNKFAMRTKD SFEIHLVPYS EHSNYDELRE
YVKFLRPKRV IPTVGLDIEK LDSKHANAMR KHFAGLVDEM AIKHEFLKGF QRGCLEADEN
VENNTRTVLN KELDAEKHVT FSKRKTKEST ESGFLAVSSS SMQEPGSRDS TLLNDKGSEE
VIQELRDCLP IWVTQNQMLD LLSCSDGNVI EAVSNFYERE TEFREQVIGH TNSVCTSQTS
SLKDSVSLSK LGSVGSSPQK MEDIHGSQSY SLLNIRSSMK SSSLSSGKRK KNLDKKSIKK
GKVGSKPESG GSKQSTITRF FSKIASNDSQ SGDGISEQLS DNENSFPSEA ITSYEEQVEQ
FIKIVNVDES SRYYVSSILK KTKGDINMAL DIYYSKPEGN LGENEERLVV SSKSIQPECC
IQSCSSELEK KVSEKESGNI VEAKGLSRDT IAATLVSLPL EKYSPIEHAC WKLGQPAPYL
HLARTFDLVE GEKGKIKAAS MLCNMFRSLL ALSPEDVIPA VYLCTNKIAA DHENMELNIG
GSIVTSAMEE ACGTSRSKIR AMYNSLGDLG RKR
//
