ID A0A0F9XP27_TRIHA Unreviewed; 547 AA.
AC A0A0F9XP27;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Rhodanese domain-containing protein {ECO:0000259|PROSITE:PS50206};
GN ORFNames=THAR02_01477 {ECO:0000313|EMBL:KKP06426.1};
OS Trichoderma harzianum (Hypocrea lixii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=5544 {ECO:0000313|EMBL:KKP06426.1, ECO:0000313|Proteomes:UP000034112};
RN [1] {ECO:0000313|Proteomes:UP000034112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6776 {ECO:0000313|Proteomes:UP000034112};
RX PubMed=26067977; DOI=10.1128/genomeA.00647-15;
RA Baroncelli R., Piaggeschi G., Fiorini L., Bertolini E., Zapparata A.,
RA Pe M.E., Sarrocco S., Vannacci G.;
RT "Draft whole-genome sequence of the biocontrol agent Trichoderma harzianum
RT T6776.";
RL Genome Announc. 3:E0064715-E0064715(2015).
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:KKP06426.1}.
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DR EMBL; JOKZ01000026; KKP06426.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F9XP27; -.
DR OMA; YSPCAIP; -.
DR OrthoDB; 5473641at2759; -.
DR Proteomes; UP000034112; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR001307; Thiosulphate_STrfase_CS.
DR PANTHER; PTHR43031; FAD-DEPENDENT OXIDOREDUCTASE; 1.
DR PANTHER; PTHR43031:SF1; PHAGE SHOCK PROTEIN E-RELATED PROTEIN; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS00380; RHODANESE_1; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000034112}.
FT DOMAIN 462..542
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 547 AA; 59930 MW; A94B549976869393 CRC64;
MSKKVVIVGG VGGGMSAATR LRRLDESATI TVFEKGAYAG YANCGIPYAL GKVIKDDEAL
ILHTPKYFKE YFNIDVYLNT EVVEIDRTNE QVCTRTVGET EIRRVGYDKL ILSQGAEAVQ
PQIVGVDQSH VITLRTISDL QAIRSIMVER CVRDVCIIGG GFISLEAAEN LRKMKFGVSI
VEQWTHVLPS IDADIAQFLH TELKHNGVKL YLNDTARRIE DSHVVLASNG REIPAELVIL
AVGVRARTSL AKMAGLEVGT QGVKVESHME TSDEDIYAVG DMVETKHVIQ QQPRVVALGG
PANRQGRLAA DDIAGRPVHY RGNIGTIICQ VFDLTVGLAG LSVSALRDLG QEPLWVTVHP
PHHARYYPNA RPITIKTAFE KGTGRILGVQ AVGMAGVDKR IDVLATAMQA RMTVFDLEHL
ELSYAPPYSS AKDPVNMVGF VGSNLLRGDY QIVHAEDINI KNLHAWQVVD VRTPEEFATG
HLPGAINLPI ATLRNQKLEL DQSMPILVYC YVGYRGYLAY RILSQRGFSV VNLDGGLKTV
VEGGTRL
//
