ID A0A091HWL5_CALAN Unreviewed; 483 AA.
AC A0A091HWL5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Arylsulfatase K {ECO:0000256|ARBA:ARBA00035710};
DE EC=3.1.6.1 {ECO:0000256|ARBA:ARBA00035026};
DE EC=3.1.6.18 {ECO:0000256|ARBA:ARBA00035675};
DE AltName: Full=Glucuronate-2-sulfatase {ECO:0000256|ARBA:ARBA00035719};
DE Flags: Fragment;
GN ORFNames=N300_13697 {ECO:0000313|EMBL:KFO99549.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFO99549.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFO99549.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFO99549.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of the 2-sulfate groups of the 2-O-sulfo-D-
CC glucuronate residues of chondroitin sulfate, heparin and heparitin
CC sulfate.; EC=3.1.6.18; Evidence={ECO:0000256|ARBA:ARBA00035590};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aryl sulfate + H2O = a phenol + H(+) + sulfate;
CC Xref=Rhea:RHEA:17261, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16189, ChEBI:CHEBI:33853, ChEBI:CHEBI:140317; EC=3.1.6.1;
CC Evidence={ECO:0000256|ARBA:ARBA00034984};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
CC -!- SIMILARITY: Belongs to the sulfatase family.
CC {ECO:0000256|ARBA:ARBA00008779}.
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DR EMBL; KL217827; KFO99549.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091HWL5; -.
DR STRING; 9244.A0A091HWL5; -.
DR Proteomes; UP000054308; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16171; ARSK; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR047892; ARSK.
DR InterPro; IPR000917; Sulfatase_N.
DR PANTHER; PTHR46615; ARYLSULFATASE K; 1.
DR PANTHER; PTHR46615:SF1; ARYLSULFATASE K; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054308}.
FT DOMAIN 12..325
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO99549.1"
FT NON_TER 483
FT /evidence="ECO:0000313|EMBL:KFO99549.1"
SQ SEQUENCE 483 AA; 55561 MW; E9952A4FBCC7DB10 CRC64;
DGRLTFYPGN QTVDLPFINF MKRYGTVFLN AYTNSPICCP SRAAMWSGRF THLTESWNNF
KGLDPDYVTW MDLMEKYGYH TQKYGKLDYT SGHHSLSNRV EAWTRDVDFL LRQEGRPMVN
LTGDKKHVRV MEADWQTTDK AANWIKEEAI NLSQPFVLYL GLNLPHPYPS PYAGEHSGSS
TFLTSPYWLK KVTYEAIKIP KWSSLSEMHP VDYYSSYTKN CTGEFTTQEV RNIRAFYYAM
CAETDAMLGE IISALRDTGL LEKTVVIFTA DHGELAMEHR QFYKMSMYEG SSHVPLLVMG
PGVKEQQQVP DLVSLVDIYP TMLDIGRIPV PQNLSGYSLT PLLRGKDDNQ VTPPRPSWVL
SEFHGCDVNS STYMLRTGRW KYIAYSDGRS VLPQLFDLSA DPDELTNVAI KFPVIAHSLD
KTLRSVVDYP KVSSSVHEYN KREFISWKES LGQNYSDVIA NLRWHQDWLK EPKKYEAAID
RWL
//
