ID V5GRY7_KALBG Unreviewed; 1050 AA.
AC V5GRY7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Transcription initiation factor TFIID, subunit TAF6 {ECO:0000313|EMBL:EST08687.1};
GN ORFNames=PSEUBRA_SCAF15g05768 {ECO:0000313|EMBL:EST08687.1};
OS Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST08687.1, ECO:0000313|Proteomes:UP000019377};
RN [1] {ECO:0000313|Proteomes:UP000019377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA Goldman G.H.;
RT "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT high producer of endo-1,4-xylanase isolated from an insect pest of
RT sugarcane.";
RL Genome Announc. 1:E0092013-E0092013(2013).
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the AHA1 family.
CC {ECO:0000256|ARBA:ARBA00006817}.
CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00005404, ECO:0000256|RuleBase:RU004523}.
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DR EMBL; KI545857; EST08687.1; -; Genomic_DNA.
DR RefSeq; XP_016293676.1; XM_016435033.1.
DR AlphaFoldDB; V5GRY7; -.
DR STRING; 1365824.V5GRY7; -.
DR GeneID; 27417643; -.
DR eggNOG; KOG2282; Eukaryota.
DR eggNOG; KOG2936; Eukaryota.
DR HOGENOM; CLU_000422_11_2_1; -.
DR OMA; TMTACNT; -.
DR OrthoDB; 19999at2759; -.
DR Proteomes; UP000019377; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProt.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0001671; F:ATPase activator activity; IEA:InterPro.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd02773; MopB_Res-Cmplx1_Nad11; 1.
DR CDD; cd08892; SRPBCC_Aha1; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.30.530.20; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.15.10.20; Activator of Hsp90 ATPase Aha1, N-terminal domain; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR036338; Aha1.
DR InterPro; IPR015310; AHSA1-like_N.
DR InterPro; IPR013538; ASHA1-like_C.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
DR InterPro; IPR010228; NADH_UbQ_OxRdtase_Gsu.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR InterPro; IPR015405; NDUFS1-like_C.
DR InterPro; IPR023393; START-like_dom_sf.
DR NCBIfam; TIGR01973; NuoG; 1.
DR PANTHER; PTHR43105:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF09229; Aha1_N; 1.
DR Pfam; PF08327; AHSA1; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR Pfam; PF09326; NADH_dhqG_C; 1.
DR SMART; SM01000; Aha1_N; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF103111; Activator of Hsp90 ATPase, Aha1; 1.
DR SUPFAM; SSF55961; Bet v1-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00641; COMPLEX1_75K_1; 1.
DR PROSITE; PS00642; COMPLEX1_75K_2; 1.
DR PROSITE; PS00643; COMPLEX1_75K_3; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Initiation factor {ECO:0000313|EMBL:EST08687.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Protein biosynthesis {ECO:0000313|EMBL:EST08687.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019377};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 347..425
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 425..464
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 564..620
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 150..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1050 AA; 113417 MW; B83F55D739A255C6 CRC64;
MSTWNKHYHW KTKGCTPWAK NHITEATVGK QVTVGKSGHV KVDRLSSFEG DVELGNRKGK
LITIYDCAIA YAWSGSSDDG TEASGTITFP EVSHEIEDEG DEYRFETEMS TKSSAETNQL
YDAVRKELAP SLRPVFHAFR QTLIDAHAKD LGHDSPASTP GAATPTTTST STSTTPAAAA
PASATGAAPK PSKGSVSTSS SDVRVSSELA ISISDLWDLL TNPSRIPMWT RAPAQFEAKA
DADFALFGGN VTGKVISVDA PKQLIQKWRT PQFPQGHYGT LAVNLTEGGD STKLELVLSG
APSGDEEVVE KNLETYYIRG LKSMATSASF ATSASRRQAT PAPAPPKMVK LTINGKEIEV
EQGTALIQAC EKAGAQIPRF CYHERLMVAG NCRMCLVESK GAPKPLASCA FPAMPGQQIF
TDTPLVAKAR EGVMEFLLAN HPLDCPICDW GGECDLQDQS MRYGSDRSRF HEITGKRAVE
DKNMGPLVKT VMTRCIQCTR CVRYANDVAG VQDMGTTGRG NDLQIGTYIE KTMNSEMSGN
IIDLCPVGAL TSKPYAFHAR PWELKKTESV DVLDAVGSNI RVDSRGVQVM RILPRTNDDV
NEEWINDKTR FANDGLKYQR LTTPLIKQGD RFVPASWPEA LATIAEGLSS SGAKGDEIKA
VAGSLADVES MVVLKDLVNK LGSDNLATDQ VNGDQPPIYG SDFRSNYTFN TTIPGIEEAD
VLLLVGTNPR HEAAIVNTRI RKAYLHRELD VGLIGEKVDL TYEYDHVGTD GQAVKDLLSG
KGAFAKKFKE AKKPMIVVGS AVAEHPDGKA ILGNLAELVK ANKGKLLNGD WNGYNVLQRQ
ASRTGALDIG FTPSPAAAKT TPKFIYLLNA DDITPETIPR DAFVVYQGHH GDVGAQFADV
CLPGSAYTEK ATTYVNTEGR TQVTRAAVPP PGAAREDWKI VRALSEVMGA TVPYNDILDV
RDRMFEISPT LVRHEVAEPS TTSAPLAVEE LAKLAKSSIS GTPLLRPIEN FYQTDPISRA
SPTMAKCTAA FVEGQPMDKV DGKATLAAFN
//
