ID A0A2P7YYT2_9ASCO Unreviewed; 360 AA.
AC A0A2P7YYT2;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 22-FEB-2023, entry version 12.
DE RecName: Full=SURF1-like protein {ECO:0000256|RuleBase:RU363076};
GN ORFNames=C7M61_000793 {ECO:0000313|EMBL:PSK41121.1};
OS [Candida] pseudohaemulonii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=418784 {ECO:0000313|EMBL:PSK41121.1, ECO:0000313|Proteomes:UP000241107};
RN [1] {ECO:0000313|EMBL:PSK41121.1, ECO:0000313|Proteomes:UP000241107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B12108 {ECO:0000313|EMBL:PSK41121.1,
RC ECO:0000313|Proteomes:UP000241107};
RA Munoz J.F., Gade L.G., Chow N.A., Litvintseva A.P., Loparev V.N.,
RA Cuomo C.A.;
RT "Candida pseudohaemulonii genome assembly and annotation.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably involved in the biogenesis of the COX complex.
CC {ECO:0000256|RuleBase:RU363076}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|RuleBase:RU363076}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU363076}.
CC -!- SIMILARITY: Belongs to the SURF1 family.
CC {ECO:0000256|RuleBase:RU363076}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PSK41121.1}.
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DR EMBL; PYFQ01000001; PSK41121.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P7YYT2; -.
DR STRING; 418784.A0A2P7YYT2; -.
DR EnsemblFungi; C7M61_000793_t1; PSK41121.1; C7M61_000793.
DR VEuPathDB; FungiDB:C7M61_000793; -.
DR OrthoDB; 167824at2759; -.
DR Proteomes; UP000241107; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR CDD; cd06662; SURF1; 1.
DR InterPro; IPR002994; Surf1/Shy1.
DR InterPro; IPR045214; Surf1/Surf4.
DR PANTHER; PTHR23427; SURFEIT LOCUS PROTEIN; 1.
DR PANTHER; PTHR23427:SF2; SURFEIT LOCUS PROTEIN 1; 1.
DR Pfam; PF02104; SURF1; 1.
DR PROSITE; PS50895; SURF1; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363076};
KW Mitochondrion {ECO:0000256|RuleBase:RU363076};
KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU363076};
KW Reference proteome {ECO:0000313|Proteomes:UP000241107};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363076};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363076}.
FT TRANSMEM 57..76
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363076"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363076"
SQ SEQUENCE 360 AA; 41574 MW; 6FCC94CF9B10BCD8 CRC64;
MISRLGIRVG GFGPKARPSS QFVFRRTVKT PTIDWKPIKS SVTNLARAEN QEKLKGFRRF
ILGLMIAMPV ITFWLGCWQV KRLKWKVDLI ARCEHLLAEP PLEGLPQQLD PSVIPEFEYR
RFKVRGHFDY SRELFLGPRI RNGELGYLLI TPFVRADGGK PILIERGWIA KEKVIPETRN
KGYLSHLAFP QGEIEIEAMF RTMPKKSKMQ YEHEPGTKLF HIPDVDAMAV ETGSLPIYAQ
MMYSLKDKQD WEGPSLNVEK KGSWKSLFSK DTTRKADHLP DSDTDTTLQY QEFEFVEQGV
PLAAIPKVNF TNNHMQYLIT WFGISIASTA LLFWTFYKKR STASAEKVLD AKRKDMKKHF
//
