ID A7SBN5_NEMVE Unreviewed; 487 AA.
AC A7SBN5;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Mitochondrial-processing peptidase subunit alpha {ECO:0000256|ARBA:ARBA00016741};
DE AltName: Full=Alpha-MPP {ECO:0000256|ARBA:ARBA00030006};
DE AltName: Full=Inactive zinc metalloprotease alpha {ECO:0000256|ARBA:ARBA00032315};
DE Flags: Fragment;
GN ORFNames=NEMVEDRAFT_v1g11103 {ECO:0000313|EMBL:EDO38902.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO38902.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO38902.1, ECO:0000313|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
CC -!- FUNCTION: Substrate recognition and binding subunit of the essential
CC mitochondrial processing protease (MPP), which cleaves the
CC mitochondrial sequence off newly imported precursors proteins.
CC {ECO:0000256|ARBA:ARBA00002123}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|RuleBase:RU004447}.
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DR EMBL; DS469617; EDO38902.1; -; Genomic_DNA.
DR RefSeq; XP_001630965.1; XM_001630915.1.
DR AlphaFoldDB; A7SBN5; -.
DR STRING; 45351.A7SBN5; -.
DR MEROPS; M16.985; -.
DR EnsemblMetazoa; EDO38902; EDO38902; NEMVEDRAFT_v1g11103.
DR GeneID; 5510507; -.
DR KEGG; nve:5510507; -.
DR eggNOG; KOG2067; Eukaryota.
DR HOGENOM; CLU_009902_5_2_1; -.
DR InParanoid; A7SBN5; -.
DR OMA; LKYHHSP; -.
DR OrthoDB; 7099at2759; -.
DR PhylomeDB; A7SBN5; -.
DR Proteomes; UP000001593; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IBA:GO_Central.
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; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR PANTHER; PTHR11851:SF49; MITOCHONDRIAL-PROCESSING PEPTIDASE SUBUNIT ALPHA; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001593}.
FT DOMAIN 49..198
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 205..405
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EDO38902.1"
FT NON_TER 487
FT /evidence="ECO:0000313|EMBL:EDO38902.1"
SQ SEQUENCE 487 AA; 54023 MW; 2E60CC1A976CEC8B CRC64;
RRWATNGQIP PLNEALPNVP PPPSGITEQV KWTRDHHETH VTTLPNGIKV ASEESFGQFS
TVGVVIDGGS RYEVDHPNGV THVIEKMAFQ STAKFPSHDD IMQELEPVGG MADCTSFRDA
IVYGTSSFTS GLPLAVEVLS EAVMRPQITS QEVDEQKMLV QFELENLEMR LDPEPILTDM
VHAAAYRNNT LGFPKLCPPQ NLPVINRETI MEFMKTYYQP DRMVIAGVNV DHEQLVELTK
KHFTDKPSWH TEGASVTPPD HSIAQYTGGI ITDHTAEPRV NPGPTPLPEL AHVSIGLEST
SYDDPDFFAF TVLNMLMGGG GSFSAGGPGK GMYSRLYLNV LNKYHWIYSA TAYNHSYSDS
GMFCIHASAH PTQLRDLVQV LVKEYFSLTK GLISEVELAR AKKQLQSMLM MNLESRVIVF
EDIGRQVLGL GERRSAGELY ECIENVTMDD ILRVSSRMLA SKPSVAAFGN LTFLPKYEDI
SAAFINK
//
