ID K5VYZ6_AGABU Unreviewed; 720 AA.
AC K5VYZ6;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=SWIM-type domain-containing protein {ECO:0000259|PROSITE:PS50966};
GN ORFNames=AGABI1DRAFT_127415 {ECO:0000313|EMBL:EKM79729.1};
OS Agaricus bisporus var. burnettii (strain JB137-S8 / ATCC MYA-4627 / FGSC
OS 10392) (White button mushroom).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Agaricus.
OX NCBI_TaxID=597362 {ECO:0000313|EMBL:EKM79729.1, ECO:0000313|Proteomes:UP000008493};
RN [1] {ECO:0000313|Proteomes:UP000008493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB137-S8 / ATCC MYA-4627 / FGSC 10392
RC {ECO:0000313|Proteomes:UP000008493};
RX PubMed=23045686; DOI=10.1073/pnas.1206847109;
RA Morin E., Kohler A., Baker A.R., Foulongne-Oriol M., Lombard V., Nagy L.G.,
RA Ohm R.A., Patyshakuliyeva A., Brun A., Aerts A.L., Bailey A.M.,
RA Billette C., Coutinho P.M., Deakin G., Doddapaneni H., Floudas D.,
RA Grimwood J., Hilden K., Kuees U., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lucas S.M., Murat C., Riley R.W., Salamov A.A., Schmutz J., Subramanian V.,
RA Woesten H.A.B., Xu J., Eastwood D.C., Foster G.D., Sonnenberg A.S.,
RA Cullen D., de Vries R.P., Lundell T., Hibbett D.S., Henrissat B.,
RA Burton K.S., Kerrigan R.W., Challen M.P., Grigoriev I.V., Martin F.;
RT "Genome sequence of the button mushroom Agaricus bisporus reveals
RT mechanisms governing adaptation to a humic-rich ecological niche.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:17501-17506(2012).
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|ARBA:ARBA00001968};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH971389; EKM79729.1; -; Genomic_DNA.
DR RefSeq; XP_007329082.1; XM_007329020.1.
DR AlphaFoldDB; K5VYZ6; -.
DR STRING; 597362.K5VYZ6; -.
DR GeneID; 18826673; -.
DR KEGG; abp:AGABI1DRAFT127415; -.
DR eggNOG; ENOG502QTYC; Eukaryota.
DR HOGENOM; CLU_021047_1_0_1; -.
DR InParanoid; K5VYZ6; -.
DR OMA; CKHIKSL; -.
DR OrthoDB; 5489531at2759; -.
DR Proteomes; UP000008493; 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; PS50966; ZF_SWIM; 2.
PE 4: Predicted;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00325};
KW Reference proteome {ECO:0000313|Proteomes:UP000008493};
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 360..400
FT /note="SWIM-type"
FT /evidence="ECO:0000259|PROSITE:PS50966"
FT REGION 86..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 720 AA; 80458 MW; E51D91946C8F2EB1 CRC64;
MAQDELEEIN GIKPNIWLAD GEEHEVQLPP SKSKYKVKHT FDHFYCTCPA WRNQSGTPVN
ARTCKHIKSL LGEEYEEARI SLKNVNGAPA KSSKPKAKAT TSRTKPGSKR KRNDDDEEND
NDMGKSSKQT VVVKPKSKRS KVESKLEEAP LADSSDGQTS DQLAEINGIK PQVYLRDGEE
REVGRTKYKV KRTVDHYYWY DALREHLFAW RNQSRMAVDS RTCKHIKSLL GDTYEEARLQ
RRTSDSSEAK GDKPASKSKP ASKSEPSSKP PSKIASTTTS KPMSNSKEAL NLSAVEEDIE
MNDIEDGKKE ENGDAKIEED IKDVEGVDEL LEINGVKPKV LMKDGDEREV SSQSNPNSKY
KVKRTWDHYY CSCPAWRNQG GAPVNARTCK HLKGLLGEEY ENARLFLKNP DGPQPKVKSR
GKGKAKATGQ GEGDDDGKSV PQLLLANKWD LDNGIDPTGW WISEKLDGVR TYFDGKQMIS
RLGNPFTPPQ WFLDKLPKDV TLDGELWGGR GEFQSTVSVV KTLNSPHWKT IKFQIFDIPS
RGEEPFEARL SYLERLFGAE GSHKDEQIVV VSQTQATDRQ HVLDQLKYVE SLGGEGLMLR
KPESLYEGYR SATLLKIKTF YDAEAIVTGY IDGKGKHAGA TGALKCRMAS GKTFSVGSGL
SDKQRKSPPK IGSIIVYRFQ ELTRDGVPRF PTFVGIAADK DQPKDAEIPE HRLDGVKADA
//
