ID A0A167Q4Z2_CALVF Unreviewed; 924 AA.
AC A0A167Q4Z2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Mitochondrial escape protein 2 {ECO:0000256|ARBA:ARBA00020222, ECO:0000256|RuleBase:RU367108};
GN ORFNames=CALVIDRAFT_544474 {ECO:0000313|EMBL:KZO99417.1};
OS Calocera viscosa (strain TUFC12733).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1330018 {ECO:0000313|EMBL:KZO99417.1, ECO:0000313|Proteomes:UP000076738};
RN [1] {ECO:0000313|EMBL:KZO99417.1, ECO:0000313|Proteomes:UP000076738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUFC12733 {ECO:0000313|EMBL:KZO99417.1,
RC ECO:0000313|Proteomes:UP000076738};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV417272; KZO99417.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167Q4Z2; -.
DR STRING; 1330018.A0A167Q4Z2; -.
DR OrthoDB; 1384689at2759; -.
DR Proteomes; UP000076738; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
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 InterPro; IPR018850; Mt_escape_2_C.
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.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Exonuclease {ECO:0000313|EMBL:KZO99417.1};
KW Hydrolase {ECO:0000313|EMBL:KZO99417.1};
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 Nuclease {ECO:0000313|EMBL:KZO99417.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076738};
KW RNA-binding {ECO:0000256|RuleBase:RU367108};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 388..872
FT /note="Mitochondrial escape protein 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10443"
FT REGION 133..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 845..872
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 924 AA; 102425 MW; CB6BB4820AC0130F CRC64;
MLRPLVGIRR LPFARQHVLL ARRLIPRRTL ATSAENDTTD VVRNEGLPDD PPKEPFGRKD
AWIYLSGVFP IRFGVWDFRY IIARLEKEDI IDQINSLIGD FNKYNFQVLA VEGTQKDGGV
FIHFEYDSSL SPSASSTATG TPGTSPPSPP IQGLSDFDRL KEIEVGLRKE VEKKGGLPTW
KRYGTAHVWL VRGKPWREDL YRFPSPQLKV EFDGPDVDHE SLYDILRPYG RIADMSVPVP
VPAGTLRSST VRFIKTQSAT IARNCLHGIA VAPHAHDLGA IHGIPADGKL TRLRLIYEKA
IKDHMFRDWI SNHPRIVLPV AAFLLATLTY TIFDPVRAWF VEAKVLDWFD YRNYSVVRWL
KRNTIERLSF DTTKVTPTPS ASSAWRERQD AARDITAFLG EQPSNFALVT GPEGSGKGVM
VAHALSSGNR HALTIDCAEL CKATSDAALI SELAKQTGYW PIFSMLSSIN NLLDLASVGL
IGQKAGFSTS IDQQMKQVLE VVGKGLEGVS KHHKAQVARR EEYAKNEASE KEQEEARSEL
IRLGAWHDGR IDCVAGNGIM SELGFGDELL RESDYDAAPA SSQAIFAASE PVEGEEKKKL
DEEKADLGAL PVVVMKNWAL KGAKKDELWD VLSAWAAALV ENKVAQVIFV SDNSSAPKNI
AKALPSKPIT TITLTDATAE SALGFVTEKL KEAGVQDDLS ADDCIEVRRL GGRLTDLESF
VYKVRNGLTI AEAVEDIISR NVAEVRKNAF GDDAEDASNL PWTTEQAWGI FKRLAEEEEI
PYADVLLDYP FKGNETALRE LEHDEFINIT QLNGRPNTIR AGKPVFYSVF QRLTSDKTFA
AMQDIAYNEK AMAAAESAIR SAEQELNTLT NIGVDTGLKG WILGATGVEA RASWLLRKIE
TNEKKLEILD AQNDKLKALL KKGE
//
