ID A0A6J2PKV2_COTGO Unreviewed; 562 AA. AC A0A6J2PKV2; DT 07-OCT-2020, integrated into UniProtKB/TrEMBL. DT 07-OCT-2020, sequence version 1. DT 10-FEB-2021, entry version 3. DE SubName: Full=cytosolic purine 5'-nucleotidase isoform X1 {ECO:0000313|RefSeq:XP_029286683.1}; GN Name=nt5c2 {ECO:0000313|RefSeq:XP_029286683.1}; OS Cottoperca gobio (Frogmouth) (Aphritis gobio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Notothenioidei; Bovichtidae; Cottoperca. OX NCBI_TaxID=56716 {ECO:0000313|Proteomes:UP000504630, ECO:0000313|RefSeq:XP_029286683.1}; RN [1] {ECO:0000313|RefSeq:XP_029286683.1} RP IDENTIFICATION. RG RefSeq; RL Submitted (OCT-2020) to UniProtKB. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR017434-2}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR017434-2}; CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family. CC {ECO:0000256|ARBA:ARBA00009589}. 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 RefSeq; XP_029286683.1; XM_029430823.1. DR Proteomes; UP000504630; Genome assembly. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1000; -; 2. DR InterPro; IPR036412; HAD-like_sf. DR InterPro; IPR008380; HAD-SF_hydro_IG_5-nucl. DR InterPro; IPR023214; HAD_sf. DR InterPro; IPR016695; Pur_nucleotidase. DR PANTHER; PTHR12103; PTHR12103; 1. DR Pfam; PF05761; 5_nucleotid; 1. DR PIRSF; PIRSF017434; Purine_5'-nucleotidase; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR02244; HAD-IG-Ncltidse; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR017434-2}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR017434-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000504630}. FT REGION 531..562 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 548..562 FT /note="Acidic" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 52 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR017434-1" FT ACT_SITE 54 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR017434-1" FT METAL 52 FT /note="Magnesium" FT /evidence="ECO:0000256|PIRSR:PIRSR017434-2" FT METAL 54 FT /note="Magnesium; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR017434-2" FT METAL 351 FT /note="Magnesium" FT /evidence="ECO:0000256|PIRSR:PIRSR017434-2" FT BINDING 127 FT /note="Allosteric activator 1" FT /evidence="ECO:0000256|PIRSR:PIRSR017434-3" FT BINDING 154 FT /note="Allosteric activator 2" FT /evidence="ECO:0000256|PIRSR:PIRSR017434-3" FT BINDING 354 FT /note="Allosteric activator 2" FT /evidence="ECO:0000256|PIRSR:PIRSR017434-3" FT BINDING 436 FT /note="Allosteric activator 1; via carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR017434-3" FT BINDING 453 FT /note="Allosteric activator 2" FT /evidence="ECO:0000256|PIRSR:PIRSR017434-3" SQ SEQUENCE 562 AA; 65198 MW; 46F01AF7841AC5A4 CRC64; MTTSWSDRLQ NYADLPANMD GVTMKKYRRE PYHRVFVNRS LAMEKIKCFG FDMDYTLAVY KSPEYESLGF ELTVERLVSI GYPQELLSFV YDPSFPTRGL VFDTMYGNLL KVDAYGNILV CVHGFNFLRG PEIRERYPNK FIQRDDTERF YILNTLFNLP ETYLFACLVD FFSNCDRYTS CESGFKNGDL FMSYKSMFQD VRDAVDWVHF KGTLKEKTVE NLEKYVVRDG KLPLLLSRMN EVAKVFLATN SDYKYTDKIM NYLFDFPHGP KPGTSHRPWQ SYFDLILADA RKPLFFGEGT VLRQVDTTTG RLKIGTYTGP LQHGIVYSGG SSDIVCDLLG AKGKDIVYIG DHIFGDILKS KKRQGWRTFL VIPELAQELH VWTDKSSLFE ELQGLDIFLA ELYKHLDSSS NERPDISTIQ RRVKKVTHDM DMCYGMMGSL FRSGSRQTLF ASQVMRYADL YAASFINLLY YPFSYLFRAA HVLMPHESTV EHAHVDIDME SPLATRNRTH CSDCKDLECK RNQLTRSFSE IKPPNLFPQT PQEITHCHDE DDDEEEEEEE EE //