ID A0A0B4H691_METMF Unreviewed; 328 AA.
AC A0A0B4H691;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=SURF1-like protein {ECO:0000256|RuleBase:RU363076};
DE Flags: Fragment;
GN ORFNames=MAJ_08778 {ECO:0000313|EMBL:KID95265.1};
OS Metarhizium majus (strain ARSEF 297).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium;
OC Metarhizium majus.
OX NCBI_TaxID=1276143 {ECO:0000313|EMBL:KID95265.1, ECO:0000313|Proteomes:UP000031176};
RN [1] {ECO:0000313|EMBL:KID95265.1, ECO:0000313|Proteomes:UP000031176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 297 {ECO:0000313|EMBL:KID95265.1,
RC ECO:0000313|Proteomes:UP000031176};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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}.
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:KID95265.1}.
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DR EMBL; AZNE01000082; KID95265.1; -; Genomic_DNA.
DR RefSeq; XP_014574259.1; XM_014718773.1.
DR AlphaFoldDB; A0A0B4H691; -.
DR HOGENOM; CLU_047737_3_0_1; -.
DR OrthoDB; 167824at2759; -.
DR Proteomes; UP000031176; 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:UP000031176};
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 292..311
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363076"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..48
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KID95265.1"
SQ SEQUENCE 328 AA; 37298 MW; 38CDD0E236829926 CRC64;
MNCPSSFLRG LRAGSIPPRL SQPTALATRR PPTRPTHRHG HRHRQLTTTP RRRLADKQAA
DDPGFTSILD APPQIVRAGK RHGPGIILLA LIPITAFALG TWQVQRLSWK TDLIAKFEDR
LVRDPLPLPP SVDPSAVHDF DYRRVRATGT FRHDQEMLIG PRMRDGKDGY MVVTPLERDG
GTTVLVNRGW ISKAHRDQRS RPDSLLPAGP VTVQGLLREP WKKNMFTPEN RPDRGQFYFP
DVKQMAELTG SQPVWIEVTM EPEFMRMMDF EARGIPYGRP AEVNLRNNHA QYIFTWYGLS
VATAIMLYMV LKKPASSITR RVQATKKF
//
