ID A0A2T4BSG8_TRILO Unreviewed; 775 AA.
AC A0A2T4BSG8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=M440DRAFT_1472909 {ECO:0000313|EMBL:PTB72244.1};
OS Trichoderma longibrachiatum ATCC 18648.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=983965 {ECO:0000313|EMBL:PTB72244.1, ECO:0000313|Proteomes:UP000240760};
RN [1] {ECO:0000313|EMBL:PTB72244.1, ECO:0000313|Proteomes:UP000240760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18648 {ECO:0000313|EMBL:PTB72244.1,
RC ECO:0000313|Proteomes:UP000240760};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC {ECO:0000256|ARBA:ARBA00006278}.
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DR EMBL; KZ679142; PTB72244.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4BSG8; -.
DR STRING; 983965.A0A2T4BSG8; -.
DR Proteomes; UP000240760; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000293; F:ferric-chelate reductase activity; IEA:UniProt.
DR GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR PANTHER; PTHR32361:SF9; FERRIC REDUCTASE TRANSMEMBRANE COMPONENT 3-RELATED; 1.
DR PANTHER; PTHR32361; FERRIC/CUPRIC REDUCTASE TRANSMEMBRANE COMPONENT; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000240760};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023065}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..775
FT /note="FAD-binding FR-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015439713"
FT TRANSMEM 158..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..367
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 379..397
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 418..582
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 187..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 775 AA; 86706 MW; 089917B94FE36A2A CRC64;
MIATRYLLRI SLLLVGLFSS HALSSSIDVD QECVSAVFSI LGGLNFVGIG YGSYYVSNCQ
NPLKVASIYA VSKTYCPSSD LDPGLNYVRS LCRLYGGAEL LPEAEVAANL TDEAISSFPV
LDQTDDAVLT NLTMPVLISK AWFDLGFKTE LTCINNRYAM YGFWGTVLLF GTFHRLITHL
LESRVIPSST DPEDTESADS RAKSRTGTKS LANLYSRIRN GLTTPSVFPP YHRQLLFGCT
IPTRIELFIV ASYWIVSFVL CCVNYRAFEG NLYWPKVAPQ LWRYIADRTG VMAYANLPLI
WMFSGRNNIF IWLTGWQFGT FNLFHRHIAR IATLQAIMHS VGYTAFYYTA GFGMSLATIS
MSFIVFFSFS WFRRMIYESF LLIHIVLSVV VIVALFYHTS IFDGQYDPYL WPLVAIWSFD
RFLRIVRVVY CNLHVRLRKT TLQRSIAAIA YDQDANIITV QINTHVKPGP GQHYYLYQPF
RLKGWENHPF TLAHWSQPGG PAGSTDVHSR TVDGSVVTSF EANSPHGAIE GEHLLSFWIR
PYDGWTRHLR DLCLKSQTKS QLPAIHKETV LLEGPYGMAE PLWAYDEVLL FAGGSGIATM
VPYILDHIAR TTASDKTKRT RTRGLTLVWS NRSQAFIKRI AQRELAAALG REDIECMFYC
TNTAKESLDS LPLTPKDEIS AEKGCGGIAE SSVLKGKEET DVSESTDGAS LSIRMGRPDI
GVMIEKAAAS ASESGSRLAV FACGPGEMAD AARAATYRAM RQSHSVEYFE EAFGW
//
