ID A0A0V0UXJ5_9BILA Unreviewed; 625 AA.
AC A0A0V0UXJ5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Mitochondrial intermediate peptidase {ECO:0000313|EMBL:KRX55996.1};
GN Name=cops6 {ECO:0000313|EMBL:KRX55996.1};
GN ORFNames=T09_8245 {ECO:0000313|EMBL:KRX55996.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX55996.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX55996.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX55996.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX55996.1}.
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DR EMBL; JYDN01000132; KRX55996.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0UXJ5; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06457; M3A_MIP; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR InterPro; IPR033851; M3A_MIP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR11804:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 1.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 185..616
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 625 AA; 72067 MW; 7354D40EB14BB5A3 CRC64;
MVSRSLPTTY MQNATDSVQK LKAQIGRGKW WKFLTICRTK FAQLLIWQAE CVRLLHPDPK
IVNAADEAVY QLGVLIERLN TSTELYNIFR RSVEEGDILP LDEVDLRVGE LLLADFEMSG
VHLPELSRRK FVSFTEDLFR LGSEFMRCCD SPVRILTSDI AEPFAKYLTD VGDGFSELHS
ALLNYNDHRV RKFGYLTYFQ PSKYQETKLK NLLHYRDAIA TLVGYRSFAD RAVQKLLLNN
SSKVESFLKC TLDTVYDQAM KERSELAKFQ DGRQPYVWDL PYLCYTAKDN LTQLSFSELV
PFLNRQQVIN NLSIMLNYLY GVQIVEAEIN PGEVWHDSVT KWLVQNEQGS TLGVIYCDWI
DRRGKVSDSH FTIQCGKQLS DGSYQQPVVV LSFRCRDRCS DKAYFTLSQL ENFLHEMGHA
LHSIFGRTRY QHVSGTRCAT DFAEVPSNLM ENFMYNPKTL LMLTKQADGS SMPDETIEKI
CRSRNIFGAL ELVQQILMSL CDLKLHEQGA EIENTVEFCR SLYSDVGFEC LMPEQTAWQH
RFSHFIPYGS KYHIYLVAKA ASSLLWRQSF EKDPLNRQQG DRWRRLQSFG GERSVADLLE
EALGYCVSPS QLAHALRHQL DDTFS
//
