ID A0A168P266_ABSGL Unreviewed; 365 AA.
AC A0A168P266;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM50 {ECO:0000256|ARBA:ARBA00020799, ECO:0000256|RuleBase:RU365079};
GN Name=ABSGL_07381.1 scaffold 8789 {ECO:0000313|EMBL:SAM01638.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM01638.1};
RN [1] {ECO:0000313|EMBL:SAM01638.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM01638.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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; LT553539; SAM01638.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168P266; -.
DR STRING; 4829.A0A168P266; -.
DR InParanoid; A0A168P266; -.
DR OMA; FYYGRPF; -.
DR OrthoDB; 11362at2759; -.
DR Proteomes; UP000078561; 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:UP000078561};
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 112..255
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT REGION 284..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 365 AA; 41053 MW; 9DB7C567D4C3335F CRC64;
MLRNTLATLG KSATRRSYSD KAAAQSLAEE ALKQKTGGQF KATLPKGDKK PAKAAGAKDS
YWKSIAIGTG ATTGALMGGL FYYGRPFADG REDKEMHQPM WDQLLPDPLP EPYRRPYTLV
INLDETLVYS TWSREHGWRH AKRPGVDYFL SYLSQFYEIV IFTSQPAMNA MPILDKLDPY
QYAMYRLYRD GTRYVDGQYI KDISHLNRDL SKVIIMDSNP HAFSLQPENG VALKPWKGEA
NDQGLLEYIP FLEAVALTNP TDIRPVLQSF GDSHIPEEWA KREADMNEQH RQQWLAEQQG
KPSNRNLGSL LRGGGAAGAP EGPPPTYLEQ MRAHVRETFA QEHEAMKGQP LMPPGQEQQQ
PGQGQ
//
