ID B8MIN8_TALSN Unreviewed; 456 AA.
AC B8MIN8;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Cytochrome b-c1 complex subunit 2, mitochondrial {ECO:0000256|ARBA:ARBA00040751};
DE AltName: Full=Core protein II {ECO:0000256|ARBA:ARBA00041372};
GN ORFNames=TSTA_045860 {ECO:0000313|EMBL:EED15130.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED15130.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004443}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004443}; Matrix side
CC {ECO:0000256|ARBA:ARBA00004443}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. UQCRC2/QCR2 subfamily.
CC {ECO:0000256|ARBA:ARBA00038146}.
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DR EMBL; EQ962657; EED15130.1; -; Genomic_DNA.
DR RefSeq; XP_002485083.1; XM_002485038.1.
DR AlphaFoldDB; B8MIN8; -.
DR STRING; 441959.B8MIN8; -.
DR GeneID; 8107573; -.
DR VEuPathDB; FungiDB:TSTA_045860; -.
DR eggNOG; KOG2583; Eukaryota.
DR HOGENOM; CLU_009902_0_1_1; -.
DR InParanoid; B8MIN8; -.
DR OMA; APKFALY; -.
DR OrthoDB; 1330839at2759; -.
DR PhylomeDB; B8MIN8; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851:SF209; CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00022792};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745};
KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 48..183
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 194..373
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 456 AA; 48081 MW; FA083134E532A696 CRC64;
MMSKSSFGRT AQRALRTHRR AFASAASPST LYETTEAAGI KVANRELAGA TSLLAVVSKA
GSRYQPVPGF SDALARYAFQ STYKRSGLRI TREAELLGSN LTAKNTRENV VLQAKFLSAD
LPYFAELLAE VTSQTKYSGY EWAELVLPTI KLRQQVLFSN PETLALESAH ASAFHRGLGE
NTFATASTPF ESYFTEDGLA EFAQSAYAKP NISLVSVGPN SSEVSKWVNQ FFAGHSASPV
AGQFKVKDTV PSKFYGGEQR TSSKAGNAVV ISFPGSAQYG ASGFKAEADV LAALLGGEST
IKWSPGFSLL AKAVEGETGV SVSTKNYAYS DAGLFAITIS GKADGVATVS KRAAETIKQV
AAGEVPAEVI KKASALAKFR ALEASQVAET GVELTGSALI NGGKPYQISE LASSFEKVSP
QQVQDLAKSF VSGKASIAAV GDLHKLPFAE DLGLTI
//
