ID A0A024TT67_9STRA Unreviewed; 262 AA.
AC A0A024TT67;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=SURF1-like protein {ECO:0000256|RuleBase:RU363076};
GN ORFNames=H310_09997 {ECO:0000313|EMBL:ETV97209.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV97209.1};
RN [1] {ECO:0000313|EMBL:ETV97209.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETV97209.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU363076}.
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DR EMBL; KI913974; ETV97209.1; -; Genomic_DNA.
DR RefSeq; XP_008874455.1; XM_008876233.1.
DR AlphaFoldDB; A0A024TT67; -.
DR STRING; 157072.A0A024TT67; -.
DR EnsemblFungi; H310_09997-t26_1; H310_09997-t26_1-p1; H310_09997.
DR EnsemblProtists; ETV97209; ETV97209; H310_09997.
DR GeneID; 20087047; -.
DR VEuPathDB; FungiDB:H310_09997; -.
DR eggNOG; KOG1563; Eukaryota.
DR OrthoDB; 38481at2759; -.
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 Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363076};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363076}.
FT TRANSMEM 227..246
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363076"
SQ SEQUENCE 262 AA; 29492 MW; AE4EFFF5135BA2C1 CRC64;
MQKVGAVVFS SIVVGTAGMG VWQTNRYFWK LDVIEQRKKQ LDAPVIALPD TITAATASEG
FEFRPLKIEG SFVPGSAFYL YPRSPPIDMQ DTKGGRVSSG GYIYQLFQRL NGTSVIVNRG
WLPKPEMEAH MNAAAAFTAA PKLETIMGLM VQGEEEKTFS PPNEPEKRHF FWLDQPQLAR
AMGSTDYVPI LIDELAADED APRPAGEPIR KSKYNYLEFY MTPWKHATYA GIWFTLAILG
TGMVFTRFRP AARRVKQYPL QR
//