ID R7S2Z7_PUNST Unreviewed; 958 AA.
AC R7S2Z7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=DNA ligase/mRNA capping enzyme {ECO:0008006|Google:ProtNLM};
GN ORFNames=PUNSTDRAFT_92533 {ECO:0000313|EMBL:EIN04603.1};
OS Punctularia strigosozonata (strain HHB-11173) (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Corticiales; Punctulariaceae; Punctularia.
OX NCBI_TaxID=741275 {ECO:0000313|EMBL:EIN04603.1, ECO:0000313|Proteomes:UP000054196};
RN [1] {ECO:0000313|Proteomes:UP000054196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-11173 SS5 {ECO:0000313|Proteomes:UP000054196};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|ARBA:ARBA00001968};
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DR EMBL; JH687553; EIN04603.1; -; Genomic_DNA.
DR RefSeq; XP_007387996.1; XM_007387934.1.
DR AlphaFoldDB; R7S2Z7; -.
DR GeneID; 18886516; -.
DR KEGG; psq:PUNSTDRAFT_92533; -.
DR eggNOG; ENOG502QTYC; Eukaryota.
DR HOGENOM; CLU_308186_0_0_1; -.
DR OMA; CKHIKSL; -.
DR OrthoDB; 5489531at2759; -.
DR Proteomes; UP000054196; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd07896; Adenylation_kDNA_ligase_like; 1.
DR CDD; cd08041; OBF_kDNA_ligase_like; 1.
DR Gene3D; 3.30.1490.70; -; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR InterPro; IPR029319; DNA_ligase_OB.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR007527; Znf_SWIM.
DR PANTHER; PTHR47810; DNA LIGASE; 1.
DR PANTHER; PTHR47810:SF1; DNA LIGASE B; 1.
DR Pfam; PF01068; DNA_ligase_A_M; 1.
DR Pfam; PF14743; DNA_ligase_OB_2; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
DR PROSITE; PS50966; ZF_SWIM; 4.
PE 4: Predicted;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00325};
KW Reference proteome {ECO:0000313|Proteomes:UP000054196};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00325};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00325}.
FT DOMAIN 35..75
FT /note="SWIM-type"
FT /evidence="ECO:0000259|PROSITE:PS50966"
FT DOMAIN 229..269
FT /note="SWIM-type"
FT /evidence="ECO:0000259|PROSITE:PS50966"
FT DOMAIN 409..449
FT /note="SWIM-type"
FT /evidence="ECO:0000259|PROSITE:PS50966"
FT DOMAIN 580..620
FT /note="SWIM-type"
FT /evidence="ECO:0000259|PROSITE:PS50966"
FT DOMAIN 773..858
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 85..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..540
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 958 AA; 104332 MW; 4E07DD42ED8A09B8 CRC64;
MAQDELAEIA GVKPLRVLAD GEEVEAKSQS SKSVYKVKRT ADHYHCTCPA WRNQKGVTVD
ARTCKHLRAI LGDAYEDARI AAKGGAATGA AKAKGGAKRK KAADEEVEAD GGEEDEKPAL
RSSKRVKTAS GSNPPSKAKP PSKPKPASRA KRTLKVEEPD ADGDEEDPME VDGPQAEGDE
KAVAADELSE DEMACIDGVR PAVYLKDGEE KEVQSQSKGK GKAAGGTVYK IKRTWDHYYC
SCPAWRNQKG VVTEARTCKH LRATLGDAYE DARIARKQAQ GAPGVTGAPD ASKAGSKPAL
KRGKLASTSK AKPESAASKP ASSTRATRGS QRETIEEEEA EDAEGEVKEE EGASDHGGDA
EGERAAADDA DELAVVGGVR PAVYLKDGEE KEVQSQSKGK GKAASGTVYK IKRTWDHYYC
SCPAWRNQKG VVTEARTCKH LRATLGDAYE DARIARKQAQ GAPGVTGAPD ASKVTSKPAS
KSGKPASLSK TKPQSVASSS RATRESNREA IQEEEAEDAE DEIKEEDEVD EVEEVEEDEK
PNDSPGLADE LACINGVRPK VYMKDGDERE EKSMTSSSVY KIKRTWDHYY CTCPAWRNQG
GMPVNARSCK HLRAVLGDEY EDARLTLKNP HGFKPASKGK GKAKPRSKKT KGDGGEDEDE
DEDADADDNA GTRRVPELLL ANKWDLEKGP DPTGWWMSEK LDGVRTYYDG VANKMYSRLG
NAFTPPDWFL DKLPKDITLD GELFGGRGEF QNTVSIVKTV NSPHWQGISF QIFDVPSMGE
EPFEDRLAFL ERTFGENGEK RQAQIEVVKH ERAESREHVM SKLEEVERLG GEGLMLRKPG
SLYEGRRSST LLKIKSFYDA EARVVGYVPG KGKYKGMTGA LQCVMASGKK FAVGTGMSDK
LRQNPPKVGT IVVYRFQELT RDSVPRFPSY VGEAVDKTEP KDAEVPEHRK VVTGGDDA
//
