ID A0A364LAN5_9EURO Unreviewed; 341 AA.
AC A0A364LAN5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 22-FEB-2023, entry version 13.
DE RecName: Full=SURF1-like protein {ECO:0000256|RuleBase:RU363076};
GN ORFNames=BHQ10_008783 {ECO:0000313|EMBL:RAO72771.1};
OS Talaromyces amestolkiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO72771.1, ECO:0000313|Proteomes:UP000249363};
RN [1] {ECO:0000313|EMBL:RAO72771.1, ECO:0000313|Proteomes:UP000249363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIB {ECO:0000313|EMBL:RAO72771.1,
RC ECO:0000313|Proteomes:UP000249363};
RX PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT "Differential ?-glucosidase expression as a function of carbon source
RT availability in Talaromyces amestolkiae: a genomic and proteomic
RT approach.";
RL Biotechnol. Biofuels 10:161-161(2017).
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:RAO72771.1}.
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DR EMBL; MIKG01000021; RAO72771.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364LAN5; -.
DR STRING; 1196081.A0A364LAN5; -.
DR OrthoDB; 167824at2759; -.
DR Proteomes; UP000249363; 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:UP000249363};
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 93..111
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363076"
FT TRANSMEM 305..324
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363076"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 341 AA; 39380 MW; B145C88809825433 CRC64;
MRPLLSSLSR ATSFPKTPLQ KGLQQQQQSQ IFDSVCLRCR RQQLQLHQRQ QQRNFNAGSR
RLHQQPADDP QWVSPIDRPS QIVRVGRRHG PGLILLALIP ITAFVLGTWQ VQRLDWKTKL
IAKFEDRLVK PPLPLPPRID PEVIPDFDYR RIVATGEYRH DQEMLIGPRM YEGEEGYVVI
TPLQRTTEPG RSGSENTVLV NRGWISKKFK DQKDRPEGLP QGEVVVEGLI RDPVKKNYFT
PDNRPDKGEF YFPDIEQMAQ LTGSQPVLIE ETMVPDLIES LNRTANGVPI GRPAQVNLRN
NHLQYIFTWY GLSVSTAIML WMVVRKRPNE ALRRVRQSKN M
//
