ID A0A0V1M583_9BILA Unreviewed; 969 AA.
AC A0A0V1M583;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Mitochondrial intermediate peptidase {ECO:0000313|EMBL:KRZ66979.1};
DE Flags: Fragment;
GN Name=MIPEP {ECO:0000313|EMBL:KRZ66979.1};
GN ORFNames=T10_7445 {ECO:0000313|EMBL:KRZ66979.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ66979.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ66979.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ66979.1};
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:KRZ66979.1}.
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DR EMBL; JYDO01000216; KRZ66979.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1M583; -.
DR Proteomes; UP000054843; 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; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR InterPro; IPR024969; EIF3F/CSN6-like_C.
DR InterPro; IPR000555; JAMM/MPN+_dom.
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; PF01398; JAB; 1.
DR Pfam; PF13012; MitMem_reg; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SMART; SM00232; JAB_MPN; 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:UP000054843};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..969
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006882298"
FT DOMAIN 46..182
FT /note="JAB1/MPN/MOV34 metalloenzyme"
FT /evidence="ECO:0000259|SMART:SM00232"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ66979.1"
SQ SEQUENCE 969 AA; 111497 MW; 0554DC483E19C265 CRC64;
LLVVVLRLLQ ALLLFKKSLV AWMMDAADTE HSLIKNNVIN NGASVEITLR PEVILHLSDH
FTRERVNGRN ENFQVYGALM GKQSGRFIEV TRSFPLTSVK MHSLFPNYDY LMDTMKSFGS
IYKDEIFVGW YVITGLNYFN ELDHQMHNVS MIVNENPIIL RFNPFDNLMR VLPIEFYESN
PAMTEFVLLS YSILYQKNEM ICIAHVSEQA VEKSSLPANN TLTRLNSQLS AIRLLMIRQK
LVIDYLQAVA SGTFPINHSI LRKISAHINS LLSVKMEYIE NDLYANEDDK NLLLSVQAMA
KLSLETSSGN NILDEFYCIA FYKHSLIDDG KVLFRLKSKY FQCLPFSSNA LGLFNVENLN
CSDGFLQLAN DVHAECNRLC AEAQSTNRKR KMAECVRLLH PDPNIVNAAD EAVYQLGALI
ERLNTSTDLF NVFRRAVEEE DIQPLDEVDR RVGELLLADF KMSGVHLPEL SRKKFVSFTE
ELFRLGSEFM RGCDNPVRIL TKDIAEPFAK YLTDVGDGFL ELHTPLLNYD DHRIRKFGYL
TYFQPSKYQE TKLKNLLHYR DAIATLVGYR SYADRAVQKL LLNNSSQVES FLKCTLDTVY
DQAMKERSEL AKFQDGLQPY IWDLPYLCYA AKDNLTQLNL SQLIPFLNRQ QVINNFSTLL
NYLYGVRIVE AEINPGEVWH DSVTKWLVQN EQSSTLGVIY CDWIDRRGKV SDSHFTIQCG
KQLPDGSYQQ PIVVLSFRCR DHCSDKAYFT LSQLENFLHE MGHALHSIFG RTRYQHVSGT
RCATDFAEVP SNLMENFMYN PKTLRMLTEQ ADGSSMPVEM IEKICRSRNM FGALELVQQI
LMSLCDLKLH QQGAEIENTV DFCRSLYSDV GFECLMPEQT AWQHRFSHFI PYGSKYHTYL
VAKAVSLLLW RQSFEKDPLN RQQGDRWRRL QSFGGERSVA DLLEEALGYC VSPSQLAHAL
RHQLDDTFS
//
