ID C4JRS5_UNCRE Unreviewed; 574 AA.
AC C4JRS5;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
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=UREG_05164 {ECO:0000313|EMBL:EEP80322.1};
OS Uncinocarpus reesii (strain UAMH 1704).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX NCBI_TaxID=336963 {ECO:0000313|EMBL:EEP80322.1, ECO:0000313|Proteomes:UP000002058};
RN [1] {ECO:0000313|Proteomes:UP000002058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 1704 {ECO:0000313|Proteomes:UP000002058};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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}.
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DR EMBL; CH476617; EEP80322.1; -; Genomic_DNA.
DR RefSeq; XP_002584475.1; XM_002584429.1.
DR AlphaFoldDB; C4JRS5; -.
DR STRING; 336963.C4JRS5; -.
DR GeneID; 8438136; -.
DR KEGG; ure:UREG_05164; -.
DR VEuPathDB; FungiDB:UREG_05164; -.
DR eggNOG; KOG1691; Eukaryota.
DR eggNOG; KOG3326; Eukaryota.
DR HOGENOM; CLU_475036_0_0_1; -.
DR InParanoid; C4JRS5; -.
DR OMA; SITSHYE; -.
DR OrthoDB; 10631at2759; -.
DR Proteomes; UP000002058; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.150.250; Flavinator of succinate dehydrogenase; 1.
DR HAMAP; MF_03057; SDHAF2; 1.
DR InterPro; IPR009038; GOLD_dom.
DR InterPro; IPR005631; SDH.
DR InterPro; IPR036714; SDH_sf.
DR InterPro; IPR028882; SDHAF2.
DR PANTHER; PTHR12469; PROTEIN EMI5 HOMOLOG, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12469:SF2; SUCCINATE DEHYDROGENASE ASSEMBLY FACTOR 2, MITOCHONDRIAL; 1.
DR Pfam; PF01105; EMP24_GP25L; 1.
DR Pfam; PF03937; Sdh5; 1.
DR SMART; SM01190; EMP24_GP25L; 1.
DR SUPFAM; SSF109910; YgfY-like; 1.
DR PROSITE; PS50866; GOLD; 1.
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:UP000002058};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..574
FT /note="Succinate dehydrogenase assembly factor 2,
FT mitochondrial"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002939430"
FT DOMAIN 42..132
FT /note="GOLD"
FT /evidence="ECO:0000259|PROSITE:PS50866"
FT REGION 364..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 574 AA; 64419 MW; E5BDE84F89588C60 CRC64;
MGSSDSQLRS LLRTLFLLFI AISVSDALRF DLIADTHSGK HERCIRNFVS REQLVVVTAT
VSGTKGDGQV VNMHIKDSLG NEYGRPKDVV GETRQAFTSL GDASFDVCFS NVLSGRHSGA
LPFRTVELDV DIGADARDWD AIKVQEKLKP VEADLRHMEA LVAEIVTEMD YLRYREQKLR
DTNESTNERV KWFAYGTMDQ SILSKLYDFF TSLQCLYPLA MTGLHKRFTL WLEGDGFVNW
FLYFLRLTVS SRLILVCIAA VSNQSSSFQP LAGGCKHVKH TRRRLFGNGR NRGLEQATFT
ASRLLNLNNP DKQTIHKMNH AQSLCRYLGC LTPTRLPLRT GKVTRSALRY EQCTLHHRSL
STSSYLLNSN GPVRSGSSRR TDSQSKSGIP RKHELELGEM EGITFKVEPL RRTGEDVATM
RARLLYQSRK RGTLESDLLL STFAATNLST MSKSELEEYD RFLDENDWDI YYWATQEPPT
PGTESETSAT TGARPKDTVT ETWKSGAAKS GEWAQTVGAF KPAYRPVPER WANSDVLRLL
RQHVQDKSAL GDKSGAKATG GGLGRMPNIE VFNS
//
