ID A0A1G4BLJ6_9PEZI Unreviewed; 1156 AA.
AC A0A1G4BLJ6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=cysteine dioxygenase {ECO:0000256|ARBA:ARBA00013133};
DE EC=1.13.11.20 {ECO:0000256|ARBA:ARBA00013133};
GN ORFNames=CORC01_02458 {ECO:0000313|EMBL:OHF02178.1};
OS Colletotrichum orchidophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX NCBI_TaxID=1209926 {ECO:0000313|EMBL:OHF02178.1, ECO:0000313|Proteomes:UP000176998};
RN [1] {ECO:0000313|EMBL:OHF02178.1, ECO:0000313|Proteomes:UP000176998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 309357 {ECO:0000313|EMBL:OHF02178.1,
RC ECO:0000313|Proteomes:UP000176998};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
CC -!- SIMILARITY: Belongs to the cysteine dioxygenase family.
CC {ECO:0000256|ARBA:ARBA00006622}.
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:OHF02178.1}.
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; MJBS01000014; OHF02178.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4BLJ6; -.
DR STRING; 1209926.A0A1G4BLJ6; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000176998; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0017172; F:cysteine dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd10548; cupin_CDO; 1.
DR CDD; cd16509; RING-HC_HLTF; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.30.70.2330; -; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR010300; CDO_1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014905; HIRAN.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45626:SF11; FAMILY HELICASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G06590)-RELATED; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF05995; CDO_I; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08797; HIRAN; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00910; HIRAN; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF51182; RmlC-like cupins; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Iron {ECO:0000256|PIRSR:PIRSR610300-51};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR610300-51};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000176998};
KW Thioether bond {ECO:0000256|PIRSR:PIRSR610300-50};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 596..762
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 917..955
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 989..1149
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 240..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 455..482
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 105
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT BINDING 107
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT BINDING 160
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT CROSSLNK 112..176
FT /note="3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-50"
SQ SEQUENCE 1156 AA; 128168 MW; 10DBFD80339311D7 CRC64;
MAVDILTKIT SAFGHNFKND VNRFDELVLG LKEALGPSSG LDSADVDVKE LMKLMEEYNT
TESEWIQFAF AEKSMGYTRN LVDEGNGKSN LLVLVWTPGK GSPIHDHGKA HCLMKILKGD
LTEIRYAFPE GNKEQPMQII SERTHKENAV AYMADELGVH RVCNKGSDFA VSLHLYTPPN
VAKGGCNIFN EKTNLSATDW WIASHILSHT LFQRVQENPC VDPTFQAGFA RDASTALGPI
WRGPISTHPA PEPGARTLRM PPKKRSIAVI DLVSSDGDDG SAPRPSKRAA GSRSVSGQAS
GRVYGSAPIN TQRHVSLGAV PGSSSQYAEY DDNLIDLTQA PDGPPRELYG FLDNKIVGVR
YYNGYASPGE VVVCLREPNN QYDSNAIRVC NVMGTQIGHL PRKVVEKLAP YVDGDEIAIE
AVLTGEKGMF DCPVRLQLYG TSNQVDRLAL EDKLKKDKLL KARELKQTRA EAEAQRKMLG
IKGSQSTIGL NAPAEPEVSL EDLAQASQAI SSHLRGDAVK SLVMDEEFLS KMPMAEQPAV
LESTLLPYQL QGLAWMTSKE SPQMPPQGSQ ESVQLWKWHP KSRNLYHNMA TNFVVQSAPK
LLSGGVLADD MGLGKTLQVI SLILTGGAGP TLIVAPLSVM SNWDQQIRRH VKQEHLPKIF
TYHGNNKATK NELAKYQVVI TSYNKLAQEG GQEKATTPLP PLMATNWRRV VLDEGHTIRN
AKTKAAIASR KLNAQSRWVL TGTPIINNIR DFQSLLQFLG INGGVEQPAI FTSVIARPLT
QGDETAETLL QLLMRDLCLR RKKDMKFVDL KLPAKKEYIH RIAFRPDEKN KYEALLSEAQ
IALEKFQNNT GGKGQFQSVL ERLLRLRQVC NHWTLCRKRI ANLLEALEGQ SVVVLNSENT
KILQEALRLF IETQEDCAVC LDTLSSPVIT HCKHVFCRGC ISKVIQTQHK CPMCRNQLDE
DALLEPAPEG GEEEDENFDA DAKSSKTEAL LKILQATTKD PKSKVIIFSQ WTSFLTIIQN
QLVEAGYKFT RIDGSMTAPK RDAAIHALDY DPDTRVMLAS LAVCSVGLNL VSADTVILAD
SWWAPAIEDQ AVDRVHRLGQ KRPTTVWRLV MEGTVEERVL DIQLEKRTLV GKAFQEKNKG
KKTQETRMAD LKKLLG
//
