ID D8TIL2_VOLCA Unreviewed; 2638 AA.
AC D8TIL2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=ATP-dependent DNA ligase family profile domain-containing protein {ECO:0000259|PROSITE:PS50160};
GN ORFNames=VOLCADRAFT_86370 {ECO:0000313|EMBL:EFJ53264.1};
OS Volvox carteri f. nagariensis.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Volvox.
OX NCBI_TaxID=3068 {ECO:0000313|Proteomes:UP000001058};
RN [1] {ECO:0000313|EMBL:EFJ53264.1, ECO:0000313|Proteomes:UP000001058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=f. Nagariensis / Eve {ECO:0000313|Proteomes:UP000001058};
RX PubMed=20616280; DOI=10.1126/science.1188800;
RA Prochnik S.E., Umen J., Nedelcu A.M., Hallmann A., Miller S.M., Nishii I.,
RA Ferris P., Kuo A., Mitros T., Fritz-Laylin L.K., Hellsten U., Chapman J.,
RA Simakov O., Rensing S.A., Terry A., Pangilinan J., Kapitonov V., Jurka J.,
RA Salamov A., Shapiro H., Schmutz J., Grimwood J., Lindquist E., Lucas S.,
RA Grigoriev I.V., Schmitt R., Kirk D., Rokhsar D.S.;
RT "Genomic analysis of organismal complexity in the multicellular green alga
RT Volvox carteri.";
RL Science 329:223-226(2010).
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000256|ARBA:ARBA00007572}.
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DR EMBL; GL378323; EFJ53264.1; -; Genomic_DNA.
DR RefSeq; XP_002946269.1; XM_002946223.1.
DR STRING; 3068.D8TIL2; -.
DR GeneID; 9621668; -.
DR KEGG; vcn:VOLCADRAFT_86370; -.
DR eggNOG; KOG0967; Eukaryota.
DR eggNOG; KOG1361; Eukaryota.
DR InParanoid; D8TIL2; -.
DR OrthoDB; 961at2759; -.
DR Proteomes; UP000001058; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd07969; OBF_DNA_ligase_I; 1.
DR CDD; cd16273; SNM1A-1C-like_MBL-fold; 1.
DR Gene3D; 3.30.1490.70; -; 1.
DR Gene3D; 3.40.50.12650; -; 1.
DR Gene3D; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 2.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR InterPro; IPR036599; DNA_ligase_N_sf.
DR InterPro; IPR011084; DRMBL.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR PANTHER; PTHR45674:SF9; DNA LIGASE 3; 1.
DR Pfam; PF04679; DNA_ligase_A_C; 1.
DR Pfam; PF01068; DNA_ligase_A_M; 2.
DR Pfam; PF04675; DNA_ligase_A_N; 1.
DR Pfam; PF07522; DRMBL; 1.
DR Pfam; PF14555; UBA_4; 1.
DR SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 2.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
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:UP000001058}.
FT DOMAIN 2182..2450
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 626..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1485..1579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1925..1964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2092..2159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2239..2280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2562..2599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..1001
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1485..1517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2573..2596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2638 AA; 267197 MW; C1A9605A32DAAC7B CRC64;
MASQALPPHK VIPGTGGTIV VDAFRYAHPG IKAYFLTHAH SDHYTGLSDS WCCGPIYCSE
TTARLVAHLC GVDPAYLKPL PMRQPVMVAE SGCPPPPPPP PPPPPPPPPP PPPPPPPPPP
PPPPPPPPPP PPPPPPPNPP RCAPGVEVTL VDANHCPGAV QLLFRLPASG ARYLHTGDMR
FCAAMATCPL LAAWRGCEAV LLDTTYCSPK HTFPLQVLGL GVWPGRQVLA EESVDYLVST
LGTLLDEDGR AAAAAAEEAA VAVAAGRGDG GGDGGCLTAA AGETAGRMLS QVAAEAGAGA
TPAAAAVPAV VLSGPAVGSG GNGGAGGVED PAATTTVAAA PAPASNAAPS NSSASGKGVF
TVGGGGRIAE TPAAEAAEAA EAAEAAEAGG GSAVSAAVGG GGRGGPFRRL YLVSTYVIRK
ERILLAIRQR CGVRVYVSET KLAVLSLLGL PEQQLADTFT TDPRVTPVHV VPWGTLGETW
PFFRPNFVNM QRIAEEMGAP AVVGFCPTGW LYEMKRTAFP VRTRGSLSVH LVPYSEHSSY
SELREYVRWL RPQRVIPTVG VGGDDGERNR AAMLKHFRTL VDETASKAKF LAGMRGRATA
TAGAAAAINP SGPHPALADT EVEGTATMPW TPSQPQQPLA VPPGPIPSER SVGRQLQLHA
GVEGPMCRGS EAQLQSGGRG VSGSRTAAGR RGPGDRWGRQ QRGGKKKVGS SGSGGGGGGA
GGVGRGCPVV KEVIVIASSS SSGSDSGISG RDGGSDGCEG EELVQEEEEE REVRNSGRAA
RSCDGGGSGG DDSRGAAELV LHSAERPTPM LPPSLPLLPL QRQQHQQSVK QLGRYGSGDD
CGGDGCGGVC GNPHEPDFNG FGAGEANSGR NGDNQCSGGG GGRGGSGEGG GGGTLVKPEA
EVGCAQNVGI CGALEEGLGE VEEVEVKNEA EGTGPGGGVG GSGGGGGGGG GGGGEVGNDR
PSGEAGARSR GEAPQGCADT GPPESSQPAS PSPSPSSLSS SLQQLMAVLG SGANLQEAQR
LLAATRNDVA AAANLYFDGG LPPLPSPSVG VGGGGGGGRR SAGAKSSIRS RTPATAATAV
ATGGGAARPS KKARLSHPQG SAATAAAAAA AGRSKGLQGR PVQRSIASFL VRPCGGNVGG
VAGAAGGAAN GGDGTVGGGS STSGGAGLHG KDVAVSGGAP IGVHDTPAAA LPQESRCTVA
VVGAGGEATS ATAAPSAGAA AAPGHQHYPW GTTAGCLHTR PILGTAPTAP TAGAVNAYTA
LLATREDEDR EVAEEKRYSV DCAESTAPDE FLALPSMPLS AGAVPQGGSK SEAGPGVSAG
GVAAAAVTGL SGPALYAPPA GAYMNVPAAG PALDFIGTQS AAPDAGLGSA DVAAAPLRSR
RHGRLAAAAV PAAVVAIPQF RAVYTACAGA VDDLSAGGGG GLDWVESIGA GDGDVAANDA
AKILSDSRGD RDGADGVPYS RRWCGFVGSC CGWCRVADVY GEHAGHPSST QTLQGSQNQK
QQQQQQQQHQ RTLHSFLSNP RGGGGRRGTA ANRHLEHDSA AAAAAAKMRH SGMASHHHHH
QQQGRQPHPQ QQQQHRHERS TANLVEDLQR QDRQLGHLET QTAQAAAAAV ARNSGFVAEA
EQQQQQLPPR RQQLKLTVTS EATTAAEAGE EEDANVEAGG LAEGAPAAAA AAATAVPETI
AAAAAATAAP APAPAPPIGA ALDELRAAVL LPLGKYDPVR HACWGPARAP TPYLHVALSL
AAIDSTPKRL AIADALTNMF RSILALAATP AEDLVAVLYL VTGRIAPEYE KMELSVGGAT
VSGALMAATG VSATGLRQLY RQFGDLGDVA QACRRKQSTL RSPQPLLVGR LLQQLRAIAA
DRGSGVAARR QAAVLGMLRA CRDCEVKYLT RTLISNLRVG ANWRSVLGPL GRAVLVHQHQ
AKGEEEAEAA AADTTRTMAA AAAGPGPSNG LRGSGGGGGG GGAPSKADLD SAAAAVVAAY
HLCPDFEVLV PALLEGGVEG LRSRCVLTPG VPIKPMLAKI CGGVADGLMQ LGPGVPFLAE
YKYDGVRAQI HLLPDGRVLI FSRNGEDRTE AFPDVSCVLD AEVVAVQWLG PGQQPEEEDK
EEDGEQEQQE GGGGEQSAGG ESEPRTAAAA PRSGDGGGGA GGGDGNGGGS SRTATPATAD
VAPYRLRAFQ ELATRARGPV EEHQVTVQVC VFVFDLLFWN GKALLDRPLR ERRALLPAAL
PGMSPGRVML ATAAEMEPLR EAPPPPAPAA ERKGKGKGKG ATAAAAAKGG DDEDAAAAAA
AAEPVRLWPA PGEPGARRVE DVGPVLAAAP SARRPGRAAA AGAAAVPQRA PASAAAASAA
AGSDGVVDLV DDGSDGKEDE AAAAAAPSAS DAVYDMLLQA FNAGAEGLML KRLDGGAAYE
PSRRSESWIK IKRDYVEGLR DSVDVVPIGA WYGQGRKVKW FSPVLLAVYD PVREEFQSLC
RCMSGFSDEF YTAARERLGA VTIPGPKPYY NTAERPSVWF EPTEVWELRG AAAFGLTDPR
SVGVSLVSRS FIRVREDKRP EDATTPQDIC DLYDKQTRKV VVRAGGAGRT RRQDATSRGH
EGGGGSGDRA ETETEAGTKR AVTAVAGSGG GFKTKKLTRE WPAHRSIGKL LPWPCCTR
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