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Database: UniProt
Entry: A0A091LAK0_CATAU
LinkDB: A0A091LAK0_CATAU
Original site: A0A091LAK0_CATAU 
ID   A0A091LAK0_CATAU        Unreviewed;       925 AA.
AC   A0A091LAK0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 {ECO:0000313|EMBL:KFP52917.1};
GN   ORFNames=N323_01906 {ECO:0000313|EMBL:KFP52917.1};
OS   Cathartes aura (Turkey vulture) (Vultur aura).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Accipitriformes; Cathartidae; Cathartes.
OX   NCBI_TaxID=43455 {ECO:0000313|EMBL:KFP52917.1, ECO:0000313|Proteomes:UP000053745};
RN   [1] {ECO:0000313|EMBL:KFP52917.1, ECO:0000313|Proteomes:UP000053745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N323 {ECO:0000313|EMBL:KFP52917.1};
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; KL310128; KFP52917.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091LAK0; -.
DR   Proteomes; UP000053745; 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:UP000053745};
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..365
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;  105976 MW;  457826CA7B5A80E1 CRC64;
     MAKKGCVHSH QVISLFAFAF GVNVCMGFTT NRFRRSEEWD EGPVSVLSDS PWISTSGSCK
     NRCFELQEAE PPGCRCDNLC KSYNSCCFDF DELCLKTARG WECTKDRCGE TRNDDNACHC
     SEDCLSRGDC CTNYQVVCKG ETHWVDDDCE EIKAPECPAG FVRPPLIIFS VDGFRASYMK
     KGNKVMPNIE KLRSCGTHSP YMRPVYPTKT FPNLYTLATG LYPESHGIVG NSMYDPVFDA
     SFSLRGREKF NHRWWGGQPI WITAAKQGVK AGTFFWSVVI PHERRILTIL QWLTLPDNER
     PYVYAFYSEQ PDAAGHRYGP FNSEESSYGS PLTPPKRPKR KLPPKRRQER PVAAPKKRRR
     KVHRVDQYAA EARRKKMMVN PLREIDKTVG QLMDGLKQLK LHRCVNVIFV GDHGMEDTTC
     ERTEFLSNYL TNVEDIILLP GSLGRIRPRS SNNLKYDPKV IVANLTCRKP DQHFKPYLKQ
     HLPKRLHYAY NRRIEDVHLL VDRKWHVARK AVDVYKKPTG KCFFHGDHGY DNKINSMQTV
     FIGYGPTFKY KTKVPPFENI ELYNVMCDLL GLKPAPNNGT HGSLNHLLRA NVYKPTVPDE
     VAKPLYPVAL PSASDFDIGC TCDDKVVILI LFLFSILEKN KLDELNKRFH VKGTEEKHLL
     YGRPAVLYRT KYNILHHHDF ESGYSETFLM PLWTSYTISK QAEVSGVPEH LASCVRPDLR
     ISPGNSQSCA AYRGDKQLSY GFLFPPQLSS SAEAKYDAFL ITNIIPMYPA FKKVWNYFQR
     VLVKRYATER NGVNVISGPI FDYDYDGLHD TPDKIKQFVE GSAIPVPTHY YAIITSCLDF
     TQPADKCDGP LSVLSYILPH RPDNDESCNS LEDESKWVED LLKMHTARVR DIEQLTSLDF
     FRKTSRSYTE ILSLKTYLHT FESEI
//
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