ID A0A093R352_PYGAD Unreviewed; 925 AA.
AC A0A093R352;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 {ECO:0000313|EMBL:KFW65484.1};
GN ORFNames=AS28_00851 {ECO:0000313|EMBL:KFW65484.1};
OS Pygoscelis adeliae (Adelie penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; Pygoscelis.
OX NCBI_TaxID=9238 {ECO:0000313|EMBL:KFW65484.1, ECO:0000313|Proteomes:UP000054081};
RN [1] {ECO:0000313|EMBL:KFW65484.1, ECO:0000313|Proteomes:UP000054081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS28 {ECO:0000313|EMBL:KFW65484.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase
CC family. {ECO:0000256|ARBA:ARBA00010594}.
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DR EMBL; KL224913; KFW65484.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093R352; -.
DR STRING; 9238.A0A093R352; -.
DR Proteomes; UP000054081; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR CDD; cd16018; Enpp; 1.
DR CDD; cd00091; NUC; 1.
DR Gene3D; 4.10.410.20; -; 2.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 3.40.570.10; Extracellular Endonuclease, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
DR InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
DR InterPro; IPR020821; Extracellular_endonuc_su_A.
DR InterPro; IPR044925; His-Me_finger_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR020436; SMB_chordata.
DR InterPro; IPR036024; Somatomedin_B-like_dom_sf.
DR InterPro; IPR001212; Somatomedin_B_dom.
DR PANTHER; PTHR10151; ECTONUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR10151:SF21; ECTONUCLEOTIDE PYROPHOSPHATASE_PHOSPHODIESTERASE FAMILY MEMBER 2; 1.
DR Pfam; PF01223; Endonuclease_NS; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR Pfam; PF01033; Somatomedin_B; 2.
DR PRINTS; PR00022; SOMATOMEDINB.
DR SMART; SM00892; Endonuclease_NS; 1.
DR SMART; SM00477; NUC; 1.
DR SMART; SM00201; SO; 2.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR SUPFAM; SSF54060; His-Me finger endonucleases; 1.
DR SUPFAM; SSF90188; Somatomedin B domain; 2.
DR PROSITE; PS00524; SMB_1; 2.
DR PROSITE; PS50958; SMB_2; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054081};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 55..98
FT /note="SMB"
FT /evidence="ECO:0000259|PROSITE:PS50958"
FT DOMAIN 99..143
FT /note="SMB"
FT /evidence="ECO:0000259|PROSITE:PS50958"
FT REGION 318..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..363
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 925 AA; 106101 MW; 4F40B84FEEA9D517 CRC64;
MAKKGCVHSH QVISLFAFAF GVNVCMGFTT NRFRRSEEWD EGPVSVLSDS PWISTSGSCK
NRCFELQEAE PPGCRCDNLC KSYNSCCFDF DELCLKTARG WECTKDRCGE TRNDDNACHC
SEDCLSRGDC CTNYQVICKG ETHWVDDDCE EIKAPECPAG FVRPPLIIFS VDGFRASYMK
KGNKVMPNIE KLRSCGTHSP YMRPVYPTKT FPNLYTLATG LYPESHGIVG NSMYDPVFDA
SFSLRGREKF NHRWWGGQPI WITAAKQGVK AGTFFWSVVI PHERRILTIL QWLTLPDNER
PYVYAFYSEQ PDAAGHRYGP FNSEESSYGS PLTPPKRPKR KLPPKRRQER PVAAPKKRRR
KVRRVDQYAA EARRKKMMVN PLREIDKTVG QLMDGLKQLK LHRCVNVIFV GDHGMEDTTC
ERTEFLSNYL TNVEDIILLP GSLGRIRPRS SNNLKYDPKV IVANLTCRKP DQHFKPYLKQ
HLPKRLHYAY NRRIEDVHLL VDRKWHVARK AVDVYKKPTG KCFFHGDHGY DNKINSMQTV
FIGYGPTFKY KTKVPPFENI ELYNIMCDLL GLKPAPNNGT HGSLNHLLRA NVYKPTVPDE
VAKPLYPVAL PSASDFDIGC TCDDKVVTLI LFLFSILEKN KLDELNKRFH VKGTEEKHLL
YGRPAVLYRT KYNILHHHDF ESGYSETFLM PLWTSYTISK QAEVSGVPEH LASCVRPDLR
ISPGNSQSCT AYRGDKQLSY GYLFPPQLSS SAEAKYDAFL ITNIIPMYPA FKKVWNYFQR
VLVKRYATER NGVNVISGPI FDYDYDGLHD TPDKIKQFVE GSAIPVPTHY YTIITSCLDF
TQPADKCDGP LSVLSYILPH RPDNDETCNS LEDESKWVED LLKMHTARVR DIEQLTSLDF
FRKTSRSYTE ILSLKTYLHT FESEI
//
