ID   A0A0E0DV64_9ORYZ        Unreviewed;      1414 AA.
AC   A0A0E0DV64;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=cysteine dioxygenase {ECO:0000256|ARBA:ARBA00013133};
DE            EC=1.13.11.20 {ECO:0000256|ARBA:ARBA00013133};
OS   Oryza meridionalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI05G23830.1};
RN   [1] {ECO:0000313|EnsemblPlants:OMERI05G23830.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI05G23830.1};
RA   Wing R.A., Panaud O., Henry R.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OMERI05G23830.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-cysteine + O2 = 3-sulfino-L-alanine + H(+);
CC         Xref=Rhea:RHEA:20441, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:61085; EC=1.13.11.20;
CC         Evidence={ECO:0000256|ARBA:ARBA00024284};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20442;
CC         Evidence={ECO:0000256|ARBA:ARBA00024284};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the DDB1 family.
CC       {ECO:0000256|ARBA:ARBA00007453}.
CC   -!- SIMILARITY: Belongs to the cysteine dioxygenase family.
CC       {ECO:0000256|ARBA:ARBA00006622}.
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DR   EnsemblPlants; OMERI05G23830.1; OMERI05G23830.1; OMERI05G23830.
DR   Gramene; OMERI05G23830.1; OMERI05G23830.1; OMERI05G23830.
DR   eggNOG; KOG1897; Eukaryota.
DR   eggNOG; KOG2073; Eukaryota.
DR   Proteomes; UP000008021; Chromosome 5.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0017172; F:cysteine dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0070483; P:detection of hypoxia; IEA:UniProt.
DR   CDD; cd20289; cupin_ADO; 1.
DR   Gene3D; 1.10.150.910; -; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR   InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR   InterPro; IPR018846; Cleavage/polyA-sp_fac_asu_N.
DR   InterPro; IPR012864; PCO/ADO.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR10644:SF3; DNA DAMAGE-BINDING PROTEIN 1; 1.
DR   PANTHER; PTHR10644; DNA REPAIR/RNA PROCESSING CPSF FAMILY; 1.
DR   Pfam; PF03178; CPSF_A; 1.
DR   Pfam; PF10433; MMS1_N; 1.
DR   Pfam; PF07847; PCO_ADO; 1.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008021}.
FT   DOMAIN          400..862
FT                   /note="Cleavage/polyadenylation specificity factor A
FT                   subunit N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10433"
FT   DOMAIN          1070..1383
FT                   /note="Cleavage/polyadenylation specificity factor A
FT                   subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03178"
FT   REGION          58..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1414 AA;  156738 MW;  52B9E4E1420FC55C CRC64;
     MDDAFSFSFS LIFPISTPLF PPPFSLLKSS LSFFSSPAAA RKIDLSLMPV QLGGGGKVAE
     PKDLAATDKD RPSSKKNRRR QKKPATSAAI SPPVAAMQTL FDTSREVFQD SLPGFVPPPQ
     AVARLAALLN DLKPHDVGIE PSMSCFKNVD SKGPPRVTYL HFYDCPKFSF GIFCLPKSAV
     IPLHNHPGMT VFCKILFGSM HLKSYDWAKS APDSDNNALE TSDGARLAKV NTDAVFDASS
     ETTVLYPENG GNLHCFTART ACAVLDVMGP PYNRADGRDC SYYDESPYLS SSGGDARYSW
     LKENHSTFEM KAAAAAAAAA AAAEMSVWNY VVTAHKPTSV THSCVGNFTG PNQLNLIVAK
     CTRIEIHLLT PQGLQPMIDV PIYGRIATLE LFRPHNETQD FLFIATERYK FCVLQWDGEK
     SELLTRAMGD VSDRIGRPTD NGQIGIIDPD CRLIGLHLYD GLFKVIPFDN KGQLKEAFNI
     RLEELQVLDI KFLYGCVKPT IVVLYQDNKD ARHVKTYEVA LKDKDFVEGP WSQNNLDNGA
     GLLIPVPAPL GGVIIIGEET IVYCNANSTF RAIPIKQSII RAYGRVDPDG SRYLLGDNAG
     ILHLLVLTHE RERVTGLKIE YLGETSIASS ISYLDNGVVY VGSRFGDSQL VKLNLQADPN
     GSYVEVLERY VNLGPIVDFC VVDLDRQGQG QVVTCSGAFK DGSLRVVRNG IGINEQASVE
     LQGIKGLWSL KSSFNDPYDM YLVVSFISET RFLAMNMEDE LEETEIEGFD AQTQTLFCQN
     AINDLLIQVT ANSVRLVSCT SRELVDQWNA PEGFSVNVAS ANASQVLLAT GGGHLVYLEI
     KDSKLVEVKH IQLEHEISCV DLNPIGENPQ YSSLAAVGMW TDISVRILSL PDLELIRKEN
     LGGEIVPRSV LLCTLEGVSY LLCALGDGHL FSFLLNASTG ELTDRKKVSL GTQPISLRTF
     SSKGTTHVFA SSDRPTVIYS SNKKLLYSNV NLKEVNHMCP FNTAAIPDSL AIAKEGELSI
     GTIDDIQKLH IRTIPLNEQA RRICHQEQSR TLAFCSFKHN QTSIEESETH FVRLLDHQTF
     EFLSIYQLDQ YEHGCSIISC SFSDDNNVYY CVGTAYVLPE ENEPSKGRIL VFAVEDGRLQ
     LIVEKETKGA VYSLNAFNGK LLAAINQKIQ LYKWTLREDG SHELQSECGH HGHILALYTQ
     TRGDFIVVGD LMKSISLLVY KHEESAIEEL ARDYNANWMS AVEMLDDEIY IGAENNYNIF
     TVRKNSDAAT DEERGRLEVV GEYHLGEFVN RLRHGSLVMR LPDSEMGQIP TVIFGTINGV
     IGIIASLPHE QYVFLEKLQS TLVKFIKGVG NLSHEQWRSF HNDKKTSEAR NFLDGDLIES
     FLDLSRNKME EVAKGMGVPV EELSKRVEEL TRLH
//