ID H1VUN3_COLHI Unreviewed; 607 AA.
AC H1VUN3;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Arylsulfatase {ECO:0000256|PIRNR:PIRNR000972};
DE Short=AS {ECO:0000256|PIRNR:PIRNR000972};
DE EC=3.1.6.1 {ECO:0000256|PIRNR:PIRNR000972};
DE AltName: Full=Aryl-sulfate sulphohydrolase {ECO:0000256|PIRNR:PIRNR000972};
GN ORFNames=CH063_03200 {ECO:0000313|EMBL:CCF43942.1}, CH63R_10635
GN {ECO:0000313|EMBL:OBR06515.1};
OS Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF43942.1, ECO:0000313|Proteomes:UP000007174};
RN [1] {ECO:0000313|EMBL:CCF43942.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IMI 349063 {ECO:0000313|EMBL:CCF43942.1};
RA Ma L.-J., O'Connell R., van Themaat E.V.L., Stueber K., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Colletotrichum higginsianum IMI 34906.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
RN [3] {ECO:0000313|EMBL:OBR06515.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063 {ECO:0000313|EMBL:OBR06515.1};
RA O'Connell R., Zambounis A., Thon M., Dallery J.-F.;
RT "Resequencing and annotation of the Colletotrichum higginsianum genome.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000092177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000092177};
RX PubMed=28851275; DOI=10.1186/s12864-017-4083-x;
RA Dallery J.-F., Lapalu N., Zampounis A., Pigne S., Luyten I., Amselem J.,
RA Wittenberg A.H.J., Zhou S., de Queiroz M.V., Robin G.P., Auger A.,
RA Hainaut M., Henrissat B., Kim K.-T., Lee Y.-H., Lespinet O., Schwartz D.C.,
RA Thon M.R., O'Connell R.J.;
RT "Gapless genome assembly of Colletotrichum higginsianum reveals chromosome
RT structure and association of transposable elements with secondary
RT metabolite gene clusters.";
RL BMC Genomics 18:667-667(2017).
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|PIRNR:PIRNR000972};
CC -!- PTM: The conversion to 3-oxoalanine (also known as C-formylglycine,
CC FGly), of a serine or cysteine residue in prokaryotes and of a cysteine
CC residue in eukaryotes, is critical for catalytic activity.
CC {ECO:0000256|PIRSR:PIRSR000972-50}.
CC -!- SIMILARITY: Belongs to the sulfatase family.
CC {ECO:0000256|ARBA:ARBA00008779, ECO:0000256|PIRNR:PIRNR000972}.
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 EMBL; CACQ02006501; CCF43942.1; -; Genomic_DNA.
DR EMBL; LTAN01000007; OBR06515.1; -; Genomic_DNA.
DR RefSeq; XP_018155033.1; XM_018305609.1.
DR STRING; 759273.H1VUN3; -.
DR EnsemblFungi; CCF43942; CCF43942; CH063_03200.
DR GeneID; 28869716; -.
DR KEGG; chig:CH63R_10635; -.
DR VEuPathDB; FungiDB:CH63R_10635; -.
DR eggNOG; KOG3731; Eukaryota.
DR HOGENOM; CLU_006332_4_0_1; -.
DR OrthoDB; 1365192at2759; -.
DR Proteomes; UP000007174; Unassembled WGS sequence.
DR Proteomes; UP000092177; Unassembled WGS sequence.
DR GO; GO:0004065; F:arylsulfatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0018958; P:phenol-containing compound metabolic process; IEA:InterPro.
DR CDD; cd16147; G6S; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR012083; Arylsulfatase.
DR InterPro; IPR024607; Sulfatase_CS.
DR InterPro; IPR000917; Sulfatase_N.
DR PANTHER; PTHR43108; N-ACETYLGLUCOSAMINE-6-SULFATASE FAMILY MEMBER; 1.
DR PANTHER; PTHR43108:SF8; SD21168P; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR PIRSF; PIRSF000972; Arylsulf_plant; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR PROSITE; PS00523; SULFATASE_1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000972};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..607
FT /note="Arylsulfatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010965636"
FT DOMAIN 43..403
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT MOD_RES 87
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000256|PIRSR:PIRSR000972-50"
SQ SEQUENCE 607 AA; 67809 MW; 85E3854FA5D23669 CRC64;
MQFKTSVLAS AALLLSGNVA AAGDAQAPLA GSDRGAVPSS SRPNIVFVLT DDQDLHMNSL
EHIPLIQKRL IEQGTLYKKH YCTTAVCCPS RASLWTGKLA HNTNVTDLNP PYGGFPIFVK
NGHNENYLPI WLQNAGYNTF YTGKMFNAHT IWNYDSPHLK GWNSSDFLLD PNTYDYYNAT
FQRNHEKPVN HLGEYSTDLV AEKAYGFLDD AVEASKPFFL AIAPIAPHSN VNASILLPVK
GPDDNVPVSD DKFRVNFPLA AKRHEHLFTD AKVPRTDNFN PDKPSGADWI RRQPKLTDEN
VEYNDRHYQG RLRALQAVDE LVDGLVDRLE KHGILDNTYV FYTTDNGYHI SQHRLQPGKE
CGYEEDINIP LIVRGPGVPK GGVTEAVTAH VDLVPTILSL AGAPLRADFD GAPIPLSDKE
LNESPLTREH VNVEYWGWAI TESTFGFNGD DTKRIYNNTY KALRVVGEGY SLYYSVWCTN
EHELYDMTTD PGQLHNLLHA DEAALAAGAT VLGYPLKKVL PRLDSLLFVL KSCKGITCSQ
PWHALHPSGN VGSLREALAP RFDEFYTQQT RVQFDHCELG HIVEAEGPQF EHDGAVYWKG
SKWSDWT
//
