ID A0A165YS31_9AGAM Unreviewed; 540 AA.
AC A0A165YS31;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM50 {ECO:0000256|ARBA:ARBA00020799, ECO:0000256|RuleBase:RU365079};
GN ORFNames=PENSPDRAFT_747673 {ECO:0000313|EMBL:KZV76489.1};
OS Peniophora sp. CONT.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Peniophoraceae; Peniophora.
OX NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV76489.1, ECO:0000313|Proteomes:UP000077086};
RN [1] {ECO:0000313|EMBL:KZV76489.1, ECO:0000313|Proteomes:UP000077086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CONT {ECO:0000313|EMBL:KZV76489.1,
RC ECO:0000313|Proteomes:UP000077086};
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: Essential component of the TIM23 complex, a complex that
CC mediates the translocation of transit peptide-containing proteins
CC across the mitochondrial inner membrane.
CC {ECO:0000256|RuleBase:RU365079}.
CC -!- SUBUNIT: Component of the TIM23 complex.
CC {ECO:0000256|RuleBase:RU365079}.
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:RU365079}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004434, ECO:0000256|RuleBase:RU365079}.
CC -!- SIMILARITY: Belongs to the TIM50 family.
CC {ECO:0000256|ARBA:ARBA00006344, ECO:0000256|RuleBase:RU365079}.
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DR EMBL; KV424464; KZV76489.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165YS31; -.
DR STRING; 1314672.A0A165YS31; -.
DR InParanoid; A0A165YS31; -.
DR OrthoDB; 11362at2759; -.
DR Proteomes; UP000077086; Unassembled WGS sequence.
DR GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd07521; HAD_FCP1-like; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR PANTHER; PTHR12210; DULLARD PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR12210:SF3; MITOCHONDRIAL IMPORT INNER MEMBRANE TRANSLOCASE SUBUNIT TIM50; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00022792};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU365079};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU365079};
KW Reference proteome {ECO:0000313|Proteomes:UP000077086};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW ECO:0000256|RuleBase:RU365079};
KW Translocation {ECO:0000256|ARBA:ARBA00023010,
KW ECO:0000256|RuleBase:RU365079}; Transport {ECO:0000256|RuleBase:RU365079}.
FT DOMAIN 245..389
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT REGION 1..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..136
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 540 AA; 58320 MW; A117D85C949774E7 CRC64;
MHAALRSASR TALAHTRQPT PGIAHSVSVA RTLPGSSAVL GSRGYASKGK RTKKAAEQAA
GSRSSDVNSG PADAEASAAG HSPFEAPPPP ENAGSPSTAK AKAAAVEAAN ASSNSTSEAT
TPIPPAPAPS PQLLSLDVAP PDPTEGPGSG GRTGARSSKD SLSSIERRQR RLARLGMGVV
ALGLVGATVY LGREWEQEEL KERKLTEEAV AATRYGRTME RFTSLFDFFS KPAWTELLPP
PLPAPHQKPY TLLVSIDDLL VTSTWDRTHG WRTAKRPGVD YFLAYLSQFY EIVVFTTQAS
FTAMPIVEKL DPYGFSIAYK LYRESTRAGP DGPVKDLSYL NRPLDKVILL DAHPEHCTAQ
PENAVIIKPW KGQPGDKGLI EIIPFLESIG IYRPNDIRPI LKAYEGKDIP KEYAIKEAAE
KKALVEEWKA RGGGKGLSAG GFTFSSLFGG KEPKQAGPAL PETFLERARR EAQNIYLQEQ
KYLRDNKAEF DRLMKEDMEQ RQKEMGGTIF GMMTGMAAGG APPPGQEQAK DGQKPVEDKA
//
