ID G0RYP8_CHATD Unreviewed; 792 AA.
AC G0RYP8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Mitochondrial escape protein 2 {ECO:0000256|ARBA:ARBA00020222, ECO:0000256|RuleBase:RU367108};
GN ORFNames=CTHT_0007450 {ECO:0000313|EMBL:EGS24034.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS24034.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
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}.
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DR EMBL; GL988032; EGS24034.1; -; Genomic_DNA.
DR RefSeq; XP_006691276.1; XM_006691213.1.
DR AlphaFoldDB; G0RYP8; -.
DR GeneID; 18254783; -.
DR KEGG; cthr:CTHT_0007450; -.
DR eggNOG; ENOG502QS0P; Eukaryota.
DR HOGENOM; CLU_007861_0_0_1; -.
DR OMA; WTPEQAW; -.
DR OrthoDB; 1384689at2759; -.
DR Proteomes; UP000008066; 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 CDD; cd12433; RRM_Yme2p_like; 1.
DR Gene3D; 3.30.70.330; -; 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 InterPro; IPR034260; Yme2_RRM.
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.
DR PROSITE; PS50102; RRM; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
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:UP000008066};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176,
KW ECO:0000256|RuleBase:RU367108};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 128..218
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT COILED 717..744
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 792 AA; 88228 MW; 4A519ECC0BEAE491 CRC64;
MTLNLFPLKL SSVLLWSPWE TNRDLASLLG RPEVAPSGLF DPVGLVKQAI PKDLPIKITQ
VIPRLKESGA YVKFTYPPGI SPAEIEAKLV KSLIENPIKP WFSPFRGIKA SLVQGRPWLE
DLYRLPKGRL KVEFIPTGDG EPPGELSQES LYNLFRRYGK IADIVSQPPD SKVVPRYAYV
DFVLVRDAIM ARNCMHGFVL KEEGSKNPTR LRLSYEQRVK PHHFWSWISG HPKIVIPIIA
AVLAAFTVAV FDPIREFFVQ SHIQKSLDLT NSNLYKWLKR QTSDILSFKP RKEETAGLSA
LFTHHRELID TVQSSLLESG DTFVVVHGPR GSGARELIMN QVLHDRRDVL LIDCRQVMEA
RGEADIIKKL ASQVGYRPVF SWANNISSML DLAIQSTTGV KAGFSENLEA QIVKILQTTA
SALKNVSLSA RTKDDRDATL TDDAYLEAHP ERRAVVVIDN FLHKGDEKGI FYDRLSDWAA
ALVQSNIAHV IFLTTDTTYS KTLSRALPDR VFHQVRLSDL SPDVAKRFVI SQLNNQSQPQ
PGADDSRIKL SNQQLRSDLA ELDECISLLG GRVTDLQLLA RRLKAGQSPS KAVSDIIEQS
SIEILRFFLL STKPTTPSGA DKKWSAEQAW SLIKALATSP NEALPYNQVL LSPTFAYSTS
PDAASPEAAL EALANAELIT IHSRHGRPAT IKAGKPVYQA AFRKLLEDPV VKARMDLAML
TELVKIENKN IEKAEAELAV LGQAGAQNGS WGWGLAGERV KYLLGKVKAS QWRIEKWEGE
IKGLKKVLEK EV
//
