ID M7TY41_BOTF1 Unreviewed; 902 AA.
AC M7TY41;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=Putative fad binding domain protein {ECO:0000313|EMBL:EMR88591.1};
GN ORFNames=BcDW1_2930 {ECO:0000313|EMBL:EMR88591.1};
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR88591.1, ECO:0000313|Proteomes:UP000012045};
RN [1] {ECO:0000313|Proteomes:UP000012045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004448}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000256|ARBA:ARBA00006375}.
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DR EMBL; KB707785; EMR88591.1; -; Genomic_DNA.
DR AlphaFoldDB; M7TY41; -.
DR STRING; 1290391.M7TY41; -.
DR HOGENOM; CLU_321307_0_0_1; -.
DR Proteomes; UP000012045; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050614; F:delta24-sterol reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:1990547; P:mitochondrial phosphate ion transmembrane transport; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 2.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR044677; SLC25A3/Pic2/Mir1-like.
DR PANTHER; PTHR45671:SF10; PHOSPHATE CARRIER PROTEIN, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45671; SOLUTE CARRIER FAMILY 25 (MITOCHONDRIAL CARRIER PHOSPHATE CARRIER), MEMBER 3, LIKE-RELATED-RELATED; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF103506; Mitochondrial carrier; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00282}; Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00282};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 857..878
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 94..178
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 191..276
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT REPEAT 292..376
FT /note="Solcar"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00282"
FT DOMAIN 381..559
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 902 AA; 101561 MW; 3E1EF63EBD5D6083 CRC64;
MPSIFPSPDT LHDAFHSPNP YGRRNEPSIQ PRTAPVSKRP TPLQARSELY TAWSVVDDAK
NKANALSAEA TKEFDKASAA AQAKTGKIEL YSPKFYAACT FGGLLACGLT HTTVTPLDLV
KCRRQVDSKM YTGNFQAWGK IFRAEGFRGI MTGWGPTFFG YSAQGAFKYG GYEYFKKFYA
DLAGPENAYK YKTWLYLSAS ASAEFIADVA LCPFEAVKVR MQTTVPPFAK GTADGLSQII
SKEGYAGLYK GLYPLWGRQI PYTMMKFASF ETIVEMIYDR LPGQKSDYGK AAQTGVSFTG
GYLAGILCAI VSHPADVMVS KLNATRLPGE AFGAATGRIY KDVGFRGLWN GLPVRIVMIG
TLTGLQWMIY DYFKIFMGLP TTGGAAPVEK QEMDRHNEAI SIIASSVKQF YERKEAFRLY
HGSTNSTRDS NRRRDRMVDT SKLDRVLKVD TEKRTVLVEP NVPMDSLVTE TLRYGLVPPV
VMEFPGITTG GGFAGTSGES SSFKYGFFDR TVNWIEMVLA NGEIVSASKD VNSDLFYGAA
SSFGTLGVTT LIELQLIEAK TYVELTYINI QSMAQGIQKI EEISKDPNVD YLDGILFSKE
AGVICSGRLV DEITPSTRVQ CFTRNSDPWF YLHAKKVHDK SSGSVTEMIP LVDYLFRYDR
GGFWVARYAF RYFVTPFNRI TRRLLDYFMH TRVMYHALHQ SGLSKKYIIQ DVAIPYPRST
EFVEYLDKDF GQWPIWLCPL RQSGISSDSP LGLLAERKEN SSTPNMLLNF GVWGPGPNNR
DAFVSWNRKF EHKVRELGGQ KWLYAHAYYT EKEFDEIYNR KEYDALRAKY HATHLPSIYD
KVKVDIDSER KKLQASWSLW LLAIFWSIWP LSGLYGVYKA FLGGDYLLPK VHASSKTQKS
KD
//