ID S2J1F7_MUCC1 Unreviewed; 428 AA.
AC S2J1F7;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM50 {ECO:0000256|ARBA:ARBA00020799, ECO:0000256|RuleBase:RU365079};
GN ORFNames=HMPREF1544_09808 {ECO:0000313|EMBL:EPB83424.1};
OS Mucor circinelloides f. circinelloides (strain 1006PhL) (Mucormycosis
OS agent) (Calyptromyces circinelloides).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=1220926 {ECO:0000313|EMBL:EPB83424.1, ECO:0000313|Proteomes:UP000014254};
RN [1] {ECO:0000313|Proteomes:UP000014254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1006PhL {ECO:0000313|Proteomes:UP000014254};
RG The Broad Institute Genomics Platform;
RA Cuomo C., Earl A., Findley K., Lee S.C., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome sequence of Mucor circinelloides f. circinelloides 1006PhL.";
RL Submitted (MAY-2013) 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; KE124071; EPB83424.1; -; Genomic_DNA.
DR AlphaFoldDB; S2J1F7; -.
DR STRING; 1220926.S2J1F7; -.
DR VEuPathDB; FungiDB:HMPREF1544_09808; -.
DR eggNOG; KOG2832; Eukaryota.
DR InParanoid; S2J1F7; -.
DR OMA; FYYGRPF; -.
DR OrthoDB; 11362at2759; -.
DR Proteomes; UP000014254; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|RuleBase:RU365079};
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:UP000014254};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW ECO:0000256|RuleBase:RU365079};
KW Translocation {ECO:0000256|ARBA:ARBA00023010,
KW ECO:0000256|RuleBase:RU365079};
KW Transmembrane {ECO:0000256|RuleBase:RU365079};
KW Transmembrane helix {ECO:0000256|RuleBase:RU365079};
KW Transport {ECO:0000256|RuleBase:RU365079}.
FT TRANSMEM 73..92
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365079"
FT DOMAIN 143..286
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT REGION 42..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 371..399
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 51..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..428
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 49048 MW; 40A349ADCE7B7780 CRC64;
MFRRTALRFQ KTATAALKRN YTSETPNSSA HKLAEEALAQ KVGTATKSRA TLPKGDKKPT
KAKGEKDNSY KEIALATGVV TGLGLGGLFY YGRPFEDGRP DKYVEENALS AAYKRCVDRF
NEFQQGMNEP MWDKLLPEPL PEPYRRAYTL VINLDETLVY STWDKEHGWR HAKRPGVDYF
LSYLSQFYEI VIFTSQSSMN AMPLLDKLDP YQYAMYRLYR EATRYVDGKY VKDLSHLNRD
LSKVIIMDSN PDSFSMQPEN GIALKPWKGE VKDQGLLEYI PFLEAVALTT PEDIRPVLKS
FEGQYIPIEW AKREQEMNKM HRLQWEQEQA KKKTSRNLGS LLGGGGAAAQ VEGPPPTYLE
QMRKHVRETF ASEFEQQKKS QEEAMAQDME RQMEMMKEMK MSVWDLMTQA ASGQPLAPPP
PPSTEEQK
//
