ID F0W079_9STRA Unreviewed; 1934 AA.
AC F0W079;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=APS kinase/ATP sulfurlyase/pyrophosphatase fusion protein putative {ECO:0000313|EMBL:CCA14450.1};
GN Name=AlNc14C3G526 {ECO:0000313|EMBL:CCA14450.1};
GN ORFNames=ALNC14_005930 {ECO:0000313|EMBL:CCA14450.1};
OS Albugo laibachii Nc14.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA14450.1};
RN [1] {ECO:0000313|EMBL:CCA14450.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21750662; DOI=10.1371/journal.pbio.1001094;
RA Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L.,
RA Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., Maclean D.,
RA Jones J.D.;
RT "Gene gain and loss during evolution of obligate parasitism in the white
RT rust pathogen of Arabidopsis thaliana.";
RL PLoS Biol. 9:e1001094-e1001094(2011).
RN [2] {ECO:0000313|EMBL:CCA14450.1}
RP NUCLEOTIDE SEQUENCE.
RA MacLean D.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Sulfur metabolism. {ECO:0000256|ARBA:ARBA00004678}.
CC -!- SIMILARITY: Belongs to the PPase family.
CC {ECO:0000256|ARBA:ARBA00006220}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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DR EMBL; FR824048; CCA14450.1; -; Genomic_DNA.
DR EnsemblProtists; CCA14450; CCA14450; ALNC14_005930.
DR HOGENOM; CLU_001841_0_0_1; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004427; F:inorganic diphosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0000103; P:sulfate assimilation; IEA:InterPro.
DR CDD; cd02027; APSK; 1.
DR CDD; cd00412; pyrophosphatase; 1.
DR Gene3D; 2.60.40.3120; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.90.80.10; Inorganic pyrophosphatase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.10.400.10; Sulfate adenylyltransferase; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR InterPro; IPR002891; APS_kinase.
DR InterPro; IPR025980; ATP-Sase_PUA-like_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR040626; Pepdidase_M14_N.
DR InterPro; IPR000834; Peptidase_M14.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR008162; Pyrophosphatase.
DR InterPro; IPR036649; Pyrophosphatase_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR024951; Sulfurylase_cat_dom.
DR NCBIfam; TIGR00455; apsK; 1.
DR PANTHER; PTHR11055; BIFUNCTIONAL 3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE SYNTHASE; 1.
DR PANTHER; PTHR11055:SF1; PAPS SYNTHETASE, ISOFORM D; 1.
DR Pfam; PF01583; APS_kinase; 1.
DR Pfam; PF01747; ATP-sulfurylase; 1.
DR Pfam; PF18027; Pepdidase_M14_N; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR Pfam; PF14306; PUA_2; 1.
DR Pfam; PF00719; Pyrophosphatase; 1.
DR SUPFAM; SSF50324; Inorganic pyrophosphatase; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00387; PPASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Kinase {ECO:0000313|EMBL:CCA14450.1}; Lyase {ECO:0000313|EMBL:CCA14450.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 238..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 516..683
FT /note="ATP-sulfurylase PUA-like"
FT /evidence="ECO:0000259|Pfam:PF14306"
FT DOMAIN 692..907
FT /note="Sulphate adenylyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01747"
FT DOMAIN 1313..1437
FT /note="Cytosolic carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18027"
FT DOMAIN 1468..1570
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|Pfam:PF00246"
FT REGION 1802..1902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1802..1823
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1825..1849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1858..1884
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1934 AA; 218685 MW; A2BC3168B6AA4BF8 CRC64;
MVVSNICRIV YWLLENPFVL LDARRGITTL DQEFLDFLEE MESFYQIILT KIDAVRAEWP
MLTFDTMPLL ITLGQFGVDQ IDCERHTLAT ESFRTFDCHL LEGEVRRTAT FTEFPSDPAT
EMPFSFWRDF VDIGQIQAFS IRLTESLFVL IVVLEYRSNS PTRGKPPCGS SIINSFDSWR
SSTLFRAHSK APLAPQAHVY RPVEQEDSDE NEESRSLQLN RNFCGQFVTP RRSILQSFLR
LTCLLPTFLL VLTYLYLYAT QNETGSCALH REHVLQNHSK NSNLFRAPSE IPLSERFARL
GQKGATVWFT GLPGSGKSTI GKALERLLLQ KRAHVIQLDG DNLRLGLNQD LSFSNADRKE
SVRRAGEVAA LFSEAGVIAL VTLISPFRED RDYIREMHRK KGIPFYEVFV DVNISVAIER
DPKGLYARAI KGEIKEFTGI SSPYEPPTQP DIHLETATMS VEEEAEILMR YITAQGILTW
KEVSKEYPGI AVADGVNSKS EFEMKYPSDP VVQNASSTYK DLEQYPRVLL RHEDVHWLQV
IGEGWASPLK GFMREGVYLQ SLHFSSALCA VKTTGGGPLS LSPSNFQSNC TLSKAERVSF
PVPIVLPIHS TTKNHIGKAT KVVLVSPVGE ELAILHDPEI YSHRKDERIA RTFGNSDTQH
PVIQEILHAG DLLLGGEVEM LQRVRYNDGL DAYRLTPTEL RQRFQQMKAD VVVAFQTRNP
THAGHVYLMD SARKQLIHQG FKNPVLWLSP LGGWTKDDDV PLDVRLKQHE AVLSAGVLNV
SSTVLAIWPS PMIYAGPKEV QWHAKSRRNA GASVFIVGRD PAGIKSHGKD LYDQDHGRFV
LHVAPGLEDL QLMSFDKVYY DVNDQQMKPM EKGREADFLS ISGSRMRTMA EKGLSKCSGD
MVPKLWKENP NCVPPSFMVD SGWQIMVNYY KHRSFNWLRF SIQQSKPFLD ATRSFQVVGT
FGQPDYKLFF QDTNKKLISP WHDIPLRIPE KHLYNFVVEI PKGVMYKMEV NKESAHNPIM
QDTTHNGTRG RSFLYGVPFF NYGMFPQTWE NPQARNTDGN GGDNDPLDVL EIGSRKLPMG
SVNPVKILGS LALIDQGEVD HKILVLSIDD PEANHINSVD DLEPGVLEYI IDWLRNYKTA
EGYPVNRFTQ EHPLTPKEAE EIVLSNHDHW KALRNGSIEN RAFFNPCVIL CMTSIEKRIT
GRPKSCAGKL LDIPPPLPLF SFPPETRQPL TGTNTRPAHL PIHRHPNTLP SASAPTDACE
FLPGKHPIEP TLVDHSFTTE EEGYVAHRVH IYEYNEPAIQ SQSNAPADTL RFDSLFESGN
LLRVYRVFRQ AEDQEYELLL HPDVGNSAYR QWFYFQTQNG YTNVEYTFHI INLAKSGALF
GNGLQPLVYS SIQASGWKHQ GSHIHYEASK SEMSPARCNT LSFRYTFQYD HDKVYFACLQ
PYTFTDLCEY CDNLEQDRER SPYLKRSELC LTLAGNVCDL LTITSPARSR GTPYDQRRIV
VISARVHPGE ANSSWMVKGM IDHLTSSSFE AQVLREHYIF KIVPMLNPDG VILGNSRVGL
AGWDLNRKWS NPVERLFPTV FHLKKLIASH QAHGRVAVYC DLHGHSLHHN IFMYGCYKHK
LAARNFKVAG PTLGTDPRVF PMILAKDSPF FFYKSCDFRV HKSKLHTGRV VVHNELGVVH
SYTLEASFCG PDYGPRKHTQ FSALDLEAMG RDWCESLLRY MRLLGYVGRS TELWRGVKIA
EDQKGFMMED SGAGLADLVV LIDIQDDDEH EERLSQTDAE GLDLSDIDEF TPEREDLAIL
GSERNTGKEV ASHRPKKPAK PNGKISELKQ NTKAVVRHSA SSSKMPTESA QAPKMVRTAI
TKEKKKSIPK RSQNLHETHD SVTKVRRSQS IGSTPKRPSV VKSGIVSKSQ IVHGVNPARL
VPGIGHIELP EVAK
//
