ID A0A397T8C9_9GLOM Unreviewed; 809 AA.
AC A0A397T8C9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Mitochondrial escape protein 2 {ECO:0000256|ARBA:ARBA00020222, ECO:0000256|RuleBase:RU367108};
GN ORFNames=C1645_820450 {ECO:0000313|EMBL:RIA92615.1};
OS Glomus cerebriforme.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Glomus.
OX NCBI_TaxID=658196 {ECO:0000313|EMBL:RIA92615.1, ECO:0000313|Proteomes:UP000265703};
RN [1] {ECO:0000313|EMBL:RIA92615.1, ECO:0000313|Proteomes:UP000265703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 227022 {ECO:0000313|EMBL:RIA92615.1,
RC ECO:0000313|Proteomes:UP000265703};
RA Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT "Comparative genomics reveals the genomic features of Rhizophagus
RT irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT symbiotic lifestyle signature.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in maintaining the mitochondrial genome and in
CC controlling the mtDNA escape. Involved in the regulation of mtDNA
CC nucleotide structure and number. May have a dispensable role in early
CC maturation of pre-rRNA. {ECO:0000256|ARBA:ARBA00025276,
CC ECO:0000256|RuleBase:RU367108}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004434,
CC ECO:0000256|RuleBase:RU367108}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004434, ECO:0000256|RuleBase:RU367108}.
CC -!- SIMILARITY: Belongs to the YME2 family. {ECO:0000256|ARBA:ARBA00010320,
CC ECO:0000256|RuleBase:RU367108}.
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:RIA92615.1}.
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DR EMBL; QKYT01000122; RIA92615.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397T8C9; -.
DR STRING; 658196.A0A397T8C9; -.
DR Proteomes; UP000265703; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR018850; Mt_escape_2_C.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR039627; Yme2_C.
DR PANTHER; PTHR32198; MITOCHONDRIAL ESCAPE PROTEIN 2; 1.
DR PANTHER; PTHR32198:SF2; MITOCHONDRIAL ESCAPE PROTEIN 2; 1.
DR Pfam; PF10443; RNA12; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367108};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU367108};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792,
KW ECO:0000256|RuleBase:RU367108};
KW mRNA processing {ECO:0000256|RuleBase:RU367108};
KW Reference proteome {ECO:0000313|Proteomes:UP000265703};
KW RNA-binding {ECO:0000256|RuleBase:RU367108};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367108};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367108}.
FT TRANSMEM 289..313
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367108"
FT DOMAIN 193..259
FT /note="RRM"
FT /evidence="ECO:0000259|Pfam:PF00076"
FT DOMAIN 351..743
FT /note="Mitochondrial escape protein 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10443"
FT COILED 723..750
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 779..806
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 809 AA; 94173 MW; D246E7DADD6512CE CRC64;
MFRVLQNQTS NSRIIFSRND INCMNLPRSF VFSPPQKQQV LMRHKLFAFL AATPIEKVEK
GQLYFDNYDN MRITAPIRWP LDFRRFLAGP NEEKLLGKLK SGEWFPAENE LPYNFKIEGV
KIRKKEDGMF VNFTFRVDQA QKEMALEEII QRVQTFLKDK KDFLWFNINA HLVKGEPFID
DLIDRYPASR LRVEFQGPDV LTETLYKYLE PYGLIRDINL FPASSKDFSR YALVQYAKIR
SAICAKNCVH GIIVNGTRLN IIYDHPIKMY KLYIWITTHP TISTISLPLI PFIIVAAVVG
ITYGLDLVCY FFVKSRITYY HLYQRLRENT INRFTTFREK SGDEIFSFST KEQEDKLQNW
LKDPPESFIV LLGPANSGKS ALVNKIIRGR RNTLSIKCDD ILDSRNKNER ALELAKQVGC
SSVFNLVIPL SKLGTLLADE VIGHKIFGLP SSVDDPTKKV LDMIENALYQ TKYRSRKNSD
EEFPIVVIDA YMIKYKENHD LWELFVKFAT QLVEKKLAHV VFVSSNIGIT NHLKSQAPSM
EVKTLDLHEP DEVINLVDQY VRDKNIEIPE GLKEAVGKIG MHLTDLGLFI GKVRNGTNPN
DALNDLVSEA KADIYRIAFR DDIEHEMSKE WSDIQFWEIM KELSKKEFIF YDITKSSPLF
NDDDTPIKAM ERSGLISISQ LPNECSISII NPGKPLYQKA FAEISSDELF ETKMKYKTAQ
YYLLLENKKI KEYEDELEKL VKIDSKWNNK WSSKWSFKWL FGNGHEVIDY RVKYLLLLLK
KSLVRAKNHQ KQIDELKQNY ELILNRKGR
//
