ID A0A395HL19_ASPHC Unreviewed; 816 AA.
AC A0A395HL19;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Succinate dehydrogenase assembly factor 2, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03057};
DE Short=SDH assembly factor 2 {ECO:0000256|HAMAP-Rule:MF_03057};
DE Short=SDHAF2 {ECO:0000256|HAMAP-Rule:MF_03057};
GN ORFNames=BO97DRAFT_437905 {ECO:0000313|EMBL:RAL08133.1};
OS Aspergillus homomorphus (strain CBS 101889).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450537 {ECO:0000313|EMBL:RAL08133.1, ECO:0000313|Proteomes:UP000248961};
RN [1] {ECO:0000313|EMBL:RAL08133.1, ECO:0000313|Proteomes:UP000248961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101889 {ECO:0000313|EMBL:RAL08133.1,
RC ECO:0000313|Proteomes:UP000248961};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays an essential role in the assembly of succinate
CC dehydrogenase (SDH), an enzyme complex (also referred to as respiratory
CC complex II) that is a component of both the tricarboxylic acid (TCA)
CC cycle and the mitochondrial electron transport chain, and which couples
CC the oxidation of succinate to fumarate with the reduction of ubiquinone
CC (coenzyme Q) to ubiquinol. Required for flavinylation (covalent
CC attachment of FAD) of the flavoprotein subunit of the SDH catalytic
CC dimer. {ECO:0000256|HAMAP-Rule:MF_03057}.
CC -!- SUBUNIT: Interacts with the flavoprotein subunit within the SDH
CC catalytic dimer. {ECO:0000256|HAMAP-Rule:MF_03057}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000256|HAMAP-
CC Rule:MF_03057}.
CC -!- SIMILARITY: Belongs to the SDHAF2 family. {ECO:0000256|HAMAP-
CC Rule:MF_03057}.
CC -!- SIMILARITY: Belongs to the WD repeat G protein beta family. Ribosomal
CC protein RACK1 subfamily. {ECO:0000256|ARBA:ARBA00007253}.
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DR EMBL; KZ824319; RAL08133.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395HL19; -.
DR STRING; 1450537.A0A395HL19; -.
DR VEuPathDB; FungiDB:BO97DRAFT_437905; -.
DR OrthoDB; 1513008at2759; -.
DR Proteomes; UP000248961; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0045182; F:translation regulator activity; IEA:InterPro.
DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IEA:UniProtKB-UniRule.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 1.10.150.250; Flavinator of succinate dehydrogenase; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR HAMAP; MF_03057; SDHAF2; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR009038; GOLD_dom.
DR InterPro; IPR045223; RACK1-like.
DR InterPro; IPR005631; SDH.
DR InterPro; IPR036714; SDH_sf.
DR InterPro; IPR028882; SDHAF2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR19868; RECEPTOR FOR ACTIVATED PROTEIN KINASE C RACK1; 1.
DR PANTHER; PTHR19868:SF0; RECEPTOR OF ACTIVATED PROTEIN C KINASE 1; 1.
DR Pfam; PF01105; EMP24_GP25L; 1.
DR Pfam; PF03937; Sdh5; 1.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM01190; EMP24_GP25L; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR SUPFAM; SSF109910; YgfY-like; 1.
DR PROSITE; PS50866; GOLD; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 6.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_03057};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP-
KW Rule:MF_03057}; Reference proteome {ECO:0000313|Proteomes:UP000248961};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..816
FT /note="Succinate dehydrogenase assembly factor 2,
FT mitochondrial"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017298897"
FT DOMAIN 31..121
FT /note="GOLD"
FT /evidence="ECO:0000259|PROSITE:PS50866"
FT REPEAT 511..553
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 559..600
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 601..633
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 644..681
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 688..729
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 788..816
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 212..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 816 AA; 90589 MW; 30A2325ED8D873C9 CRC64;
MRSLLGLLFL LFAQLSTALK FDLSAVSGKN ERCIRNFVFK DQLVVVTAIV SGNKGDGQMV
NMHIKDALGN EHGRPKDIAG EVRQAFTAPA DTAFDVCFDN QLTTRHAIPN PYKSVELDVE
IGADARDWSS IQVQEKLKPV ETDLRRIEEM VAEIVSEMEY LRAREQKLRD TNESTNERVK
WFAFGTMGML VGLGAWQVVY LRAYFSVKKD RAPSTAPQHR ENNTNKPPNP NVPNTTSTMT
KDFPKVGAKS SPPDLVGAVD PNYKPADPYP GKVEHFTGGR EETGAQKPEL GVGEMEGITF
RVEPLRRQGE DVATMRARLL YQSRKRGILE SDLLLSTFAD VYLGKMNQEQ LQEYDRFLDE
NDWDIYYWAT QDPPADGGEE SPSSTAQGAQ DTVTETWKQT GAKSGEWAQT VGAYKAAYRP
VPSRWKNSDV LELLRAHVRD NSATGFQAAK SKKTGGGAGL GRMPNGWASR TTTSRAGTLS
QGQLLRPRSS LSPHRHPDSN MAEQLVLRGT LEGHNGWVTS LATSLENPNM LLSASRDKTL
IIWNLTRDEQ AYGYPKRSLE GHSHIVSDCV ISSDGAYALS SSWDKTLRLW ELSTGETTRK
FVGHTNDVLS VSFSADNRQI VSASRDRSIK LWNTLGDCKF TITDKGHSEW VSCVRFSPNP
QNPVIVSAGW DKLVKVWELA SCRLQTDHIG HTGYINTVTI SPDGSLCASG GKDGTTMLWD
LNESKHLYSL QAGDEIHALV FSPNRYWLCA ATASSITIFD LEKKSKVDEL KPEFIEKGKK
SREPECISLA WSADGQTLFA GYTDNKIRAW GVMSRA
//
