ID A0A0D2HIR6_9EURO Unreviewed; 1552 AA.
AC A0A0D2HIR6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Flavodoxin-like domain-containing protein {ECO:0000259|PROSITE:PS50902};
GN ORFNames=Z520_01944 {ECO:0000313|EMBL:KIY01806.1};
OS Fonsecaea multimorphosa CBS 102226.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIY01806.1, ECO:0000313|Proteomes:UP000053411};
RN [1] {ECO:0000313|EMBL:KIY01806.1, ECO:0000313|Proteomes:UP000053411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 102226 {ECO:0000313|EMBL:KIY01806.1,
RC ECO:0000313|Proteomes:UP000053411};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- COFACTOR:
CC Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC Evidence={ECO:0000256|ARBA:ARBA00001929};
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000256|ARBA:ARBA00010429}.
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DR EMBL; KN848064; KIY01806.1; -; Genomic_DNA.
DR RefSeq; XP_016635928.1; XM_016772458.1.
DR STRING; 1442371.A0A0D2HIR6; -.
DR GeneID; 27707690; -.
DR VEuPathDB; FungiDB:Z520_01944; -.
DR OrthoDB; 5474937at2759; -.
DR Proteomes; UP000053411; Unassembled WGS sequence.
DR GO; GO:0009337; C:sulfite reductase complex (NADPH); IEA:InterPro.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:InterPro.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 2.
DR HAMAP; MF_01540; CysI; 1.
DR InterPro; IPR011786; CysI.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR InterPro; IPR045169; NO2/SO3_Rdtase_4Fe4S_prot.
DR InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR PANTHER; PTHR11493:SF47; SULFITE REDUCTASE [NADPH] SUBUNIT BETA; 1.
DR PANTHER; PTHR11493; SULFITE REDUCTASE [NADPH] SUBUNIT BETA-RELATED; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF01077; NIR_SIR; 1.
DR Pfam; PF03460; NIR_SIR_ferr; 2.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00397; SIROHAEM.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 2.
DR SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 2.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053411}.
FT DOMAIN 808..957
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT REGION 217..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1552 AA; 170611 MW; A5A5D956FE01AE1C CRC64;
MGSVASPAEA VARIAYLAND VVLSVQPSLS TDSEFSYHLS RFVANNAKNF VSKSLPEIVP
VRQNADPLLS AYTPLQAGKL VSVTAPSSIL LNSVPHLYKL AQYPVVLHVA LATPNPDFSE
ISSIRQCGFT FLQSETLQEA QDIALTAHAL AVRSGKGVIH FYDPSNSVQD HPIPIESREL
VQALLGTGVK ASHTGETEQT LYANSGRTAT VTDLGLPEVT PSQAPAPTAR EALSPVAAPT
SANGHTDLSS AASSSSRRQS SSGSTAPSSI ATTVETPVSR ALSATDIFNY VSEIWAAISH
ITGRSYSAIE YSGPPDAEAA LYIFGSTGVF VDVLDADDVP ADLSSLGIIT ARLYRPWLGS
AVLLDSIPKT IQKIAVLEQI RRKTTKWGPS FLDLLSSLNP GAGGQSAISL VQYRLGQIDA
STALQALRGI FQNLAPAITP RKHSRRRGYS QAAAVSIQNL SIGHELEPVV DSFVPEQPEA
ENAYLKILDQ LFSTRLYIAN LLDKKNAGVS STIAASPEYG FGSLLARAER RQEFVKEVEG
AARSNQFITE SPKQWLSRWA LNANDSVKAN EIAPEVVARL STDGSRLASS LLDQKAFFPK
EAQWLIGSDA WAYDLGNSGV HHVLASGANV NLLIIDSEPY SERAAADAMR RKKDIGLYAM
NFGNAYVASV AVYSSYTQVL QAMIEAERFN GPSVVLAYLP YNKETDSPLT VLQETKKAVD
MGYWPLYRWD PSNEEKGEPS FSLDSERIKR ELEEFLRRDN QLTQVMNRHP QFAASLSESY
GSEVRKLQKR KAKDAYEQML EGLYGAPLTV LFASDNGNAE GLAKRLGNRG KARGLKTMVF
AMDDYPLEDL PNEENVVFIT STAGQGEFPQ NGRAFWEGIK DAADLDLSNI HYSVFALGDS
HYWPRKEDKI FYNKPGKDLD TRIQFLGGKL LTAIGLGDDQ DPDSFQTGYQ EWEPRLWQAL
NVANVEGLPE EPPPLTNEDI KIASNYLRGT IAEGLADTST GAISASDQQL TKFHGTYQQD
DRDLRDERKA QGLEPAYSFM IRCRLPGGVA TPSQWVQMDA IASAHGNETI KLTTRQTFQF
HGVIKSKLKP AMRAINKALM TTIAACGDIN RNVMCSSLPT LSEYHQEVHA VSKRISDHLL
PSTTAYHEIW LKDDTTGEKT QVAGDAVQDF EPLYGPTYLP RKFKITIAIP PHNDTDVYAH
DVGLIAIRSK DNGHLEGFNI LAGGGMGVTH NNKKTYPRLG YMMGYVPADV AHLVCEKIML
VQRDNGDRKN RKHARLKYTM DDMGNEVFKS KVQELLTPLG ITFDTPRPYK FDSNIDTFGW
LRDEKGMNHF TFFIENGRVE DTADFSMRTG LREIAKIHKG EFRLTGNQHL ILSNVTDEAK
PAIAELMKKY KLDNTQFSGM RLSSSACVAF PTCGLAMAES ERYLPTLISK LEACLEENGL
SQDSIVMRMT GCPNGCARPW VAEAAFVGKA YGAYNMYLGG GYHGQRLNKL YRSSIKEDEI
LEIMQGLLGR YAKERTQGER FGDWTIRAGV INETTEGKNF HDNTAEEESD AE
//