ID A0A1S3JI48_LINUN Unreviewed; 649 AA.
AC A0A1S3JI48;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Adenosine deaminase 2-like {ECO:0000313|RefSeq:XP_013410067.1};
GN Name=LOC106173475 {ECO:0000313|RefSeq:XP_013410067.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013410067.1};
RN [1] {ECO:0000313|RefSeq:XP_013410067.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013410067.1};
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR RefSeq; XP_013410067.1; XM_013554613.2.
DR AlphaFoldDB; A0A1S3JI48; -.
DR STRING; 7574.A0A1S3JI48; -.
DR EnsemblMetazoa; g3135.t1; g3135.t1; g3135.
DR EnsemblMetazoa; XM_013554613.2; XP_013410067.1; LOC106173475.
DR GeneID; 106173475; -.
DR KEGG; lak:106173475; -.
DR InParanoid; A0A1S3JI48; -.
DR OMA; AICRTIY; -.
DR OrthoDB; 2952433at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0019239; F:deaminase activity; IEA:InterPro.
DR CDD; cd00603; IPT_PCSR; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR001365; A_deaminase_dom.
DR InterPro; IPR006330; Ado/ade_deaminase.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11409; ADENOSINE DEAMINASE; 1.
DR PANTHER; PTHR11409:SF39; ADENOSINE DEAMINASE 2; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR Pfam; PF01833; TIG; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..649
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010259077"
FT DOMAIN 268..508
FT /note="Adenosine deaminase"
FT /evidence="ECO:0000259|Pfam:PF00962"
FT DOMAIN 541..635
FT /note="IPT/TIG"
FT /evidence="ECO:0000259|Pfam:PF01833"
SQ SEQUENCE 649 AA; 73897 MW; 3A9689AF89544F44 CRC64;
MLAFCVCLVV FFASVGAKTP FMSEYEFSRQ RDELMAKEWM FAGHAMDLTD DEKIVDNYLE
YLKWQEFMAT KDRFPPSVGL ESVLDHIVNS KVFKTLKKFP KGGNMHLHEN HVLSKSKMLD
IVYSSDDYEH LYVAVNVSNN YKWRLDFFLN PPQGWEKVKG NPKYTKEKLL PHMHLLGSMT
EYAKENPTNS GQRWKETNPM FSRLGSKVIA NANIKEKYLQ GILDAAVEEN VQYLETRTSI
YGRLYVLDPD PKYTSKRGKR YIDTSDGELE IQQSIKTIDA FIKKNPHFIG LRKIANSFRR
NTMKGMYADM EKAVRMHLKY PNYIAGFDMV GEEDRGNSLL YFMEDFLKLY DNATGESRVP
FYLHNGETNW PDDLLTASNA NDPVGTLQNT YEAVLLGAKR VGHGLGYFKH PYLLDLLKQH
QTAIEVCPVS NQLLGYTADL RNHPAINFIR MGVPVILGAD DPATFGYNYF TADWYEAFMG
WGLRLPDLKK LAINSLHYSA MTTKEKVSAI NEKWKPAYSK FIADIKREAC SIDFSNTTNE
PFIARIFPRE GPMKASSKVH VFGRNFEQAI CQGVVCNFDN TVTSGSYVSG QQLSCQVPDF
KSLGKTDVGE SVSVRLRVSL DGGATFRSYS SQFTYVSQLK DGTSEPFIG
//