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Database: UniProt
Entry: A0A368GI65_ANCCA
LinkDB: A0A368GI65_ANCCA
Original site: A0A368GI65_ANCCA 
ID   A0A368GI65_ANCCA        Unreviewed;       137 AA.
AC   A0A368GI65;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Protein-tyrosine sulfotransferase {ECO:0000256|ARBA:ARBA00013262, ECO:0000256|RuleBase:RU365018};
DE            EC=2.8.2.20 {ECO:0000256|ARBA:ARBA00013262, ECO:0000256|RuleBase:RU365018};
GN   ORFNames=ANCCAN_11298 {ECO:0000313|EMBL:RCN42750.1};
OS   Ancylostoma caninum (Dog hookworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=29170 {ECO:0000313|EMBL:RCN42750.1, ECO:0000313|Proteomes:UP000252519};
RN   [1] {ECO:0000313|EMBL:RCN42750.1, ECO:0000313|Proteomes:UP000252519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Baltimore {ECO:0000313|EMBL:RCN42750.1,
RC   ECO:0000313|Proteomes:UP000252519};
RA   Mitreva M.;
RT   "Draft genome of the hookworm Ancylostoma caninum.";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the O-sulfation of tyrosine residues within acidic
CC       motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as
CC       cosubstrate. {ECO:0000256|RuleBase:RU365018}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + L-tyrosyl-[protein] = adenosine
CC         3',5'-bisphosphate + H(+) + O-sulfo-L-tyrosine-[protein];
CC         Xref=Rhea:RHEA:16801, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:11688,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:58339,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:65286; EC=2.8.2.20;
CC         Evidence={ECO:0000256|ARBA:ARBA00000411,
CC         ECO:0000256|RuleBase:RU365018};
CC   -!- SIMILARITY: Belongs to the protein sulfotransferase family.
CC       {ECO:0000256|ARBA:ARBA00009988, ECO:0000256|RuleBase:RU365018}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RCN42750.1}.
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DR   EMBL; JOJR01000181; RCN42750.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A368GI65; -.
DR   STRING; 29170.A0A368GI65; -.
DR   Proteomes; UP000252519; Unassembled WGS sequence.
DR   GO; GO:0008476; F:protein-tyrosine sulfotransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR026634; TPST-like.
DR   PANTHER; PTHR12788; PROTEIN-TYROSINE SULFOTRANSFERASE 2; 1.
DR   PANTHER; PTHR12788:SF7; PROTEIN-TYROSINE SULFOTRANSFERASE-RELATED; 1.
DR   Pfam; PF13469; Sulfotransfer_3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000252519};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365018}.
SQ   SEQUENCE   137 AA;  16466 MW;  274CCE0B9DCB2889 CRC64;
     MFKTWNIQFT RMFNECERMK EACLKVYYER LVQQTAKEAR RILKFLGVPW SEDVLRHQDK
     IGKEVKLNPI EYSTSQVKEK IYKKALTSWF GYFPDNILND INTIAPMLRQ LGYDTSARKP
     SYAKFAEDDF YEKWNNK
//
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