ID A0A178AX55_9PLEO Unreviewed; 458 AA.
AC A0A178AX55;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=IQ06DRAFT_292690 {ECO:0000313|EMBL:OAL01903.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL01903.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAL01903.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL01903.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; KV441710; OAL01903.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178AX55; -.
DR STRING; 765868.A0A178AX55; -.
DR InParanoid; A0A178AX55; -.
DR OrthoDB; 1330839at2759; -.
DR Proteomes; UP000077206; 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:0016787; F:hydrolase activity; 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 Hydrolase {ECO:0000313|EMBL:OAL01903.1};
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:UP000077206};
KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 54..188
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 202..378
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 458 AA; 49029 MW; 9E91D4E1A5F4D2E7 CRC64;
MFSRQTACRG VQRASRQHAL RQTQRRGLAA PASGSFQYEA GEAKGVKFAS RDFAGPTTTL
ALVAKAGTRY QPLPGLTEGL ANFAFRATER RSTLRIVREA ELLGATLNAH HSRENLILEA
KFLRDDLPYF VELLGEVVSQ SKYQPHVYAE EVLPLIDFAH KRFLASVTDM ATNSAHSLAF
HRGLGNPTAS ASQTPYTKYL DAATIKWFSE SAYAKPNFAV VANGAEHGEF SKWVNQFFDG
VPAQPKEQLT VGTEQTKYVG GEERIAHDGG NAMVIAFPGS SSFTGKFYKP ELAVLGSLLG
GQSAIKWSPG FTILGNAAAP GVKVKTTSAI YSDAGLLYTT ITGSAKGVAE TAKASVDAIK
KIAAGEVSSE QISKAKAAAK FKELEHGQDI RAGLELTGNG LIHNTKAYQI DEVAKAIDGV
SEEAVKTAAK QLLEQRASVA SVGDLFVLPY ADELGLKV
//
