ID V8P931_OPHHA Unreviewed; 937 AA.
AC V8P931;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Presequence protease, mitochondrial {ECO:0000256|ARBA:ARBA00020167};
DE AltName: Full=Pitrilysin metalloproteinase 1 {ECO:0000256|ARBA:ARBA00032857};
DE Flags: Fragment;
GN Name=PITRM1 {ECO:0000313|EMBL:ETE70503.1};
GN ORFNames=L345_03689 {ECO:0000313|EMBL:ETE70503.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE70503.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE70503.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE70503.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- SUBUNIT: Monomer and homodimer; homodimerization is induced by binding
CC of the substrate. {ECO:0000256|ARBA:ARBA00011853}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. PreP subfamily.
CC {ECO:0000256|ARBA:ARBA00007575}.
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:ETE70503.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AZIM01000540; ETE70503.1; -; Genomic_DNA.
DR AlphaFoldDB; V8P931; -.
DR MEROPS; M16.009; -.
DR Proteomes; UP000018936; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR013578; Peptidase_M16C_assoc.
DR PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR PANTHER; PTHR43016:SF13; PRESEQUENCE PROTEASE, MITOCHONDRIAL; 1.
DR Pfam; PF08367; M16C_assoc; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SMART; SM01264; M16C_associated; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:ETE70503.1};
KW Protease {ECO:0000313|EMBL:ETE70503.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018936}.
FT DOMAIN 398..647
FT /note="Peptidase M16C associated"
FT /evidence="ECO:0000259|SMART:SM01264"
FT COILED 406..433
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE70503.1"
SQ SEQUENCE 937 AA; 106522 MW; 463FFF629A3256B2 CRC64;
LASSEVNTDF SLLVRSLNLE YTQLEFAKVT VVPEFSLTAV KLDHDKTGAQ YLHVAREDSN
NLFSVQFRTT PMDSTGVPHI LEHTVLCGSE RYPVRDPFFK MLNRSLSTFM NAFTASDYTL
YPFSTQNPKD FQNLLSVYLD AVFFPSLRLL DFWQEGWRLE HESPEDPRSP LTFKGVVFNE
MKGAFADNER VFSQHLQNKI LPDHTYAVVS GGDPLKIPDL SWEQLKHFHA THYHPSNARF
FTYGDFPLEL HLKQIHEEAL CKFQKIEPNT SVPPQQIWDK PREHYVTCAA DSLATDSKKQ
TMVSVSYLLA KNGFEKERID ALLHKIEIQM KHQSTRFGLV LASNIASCWN HEGDPVDLLK
IAEKVTQLRH CLKEDPRFLQ KKVKQYFKDN PHRLTLSMSP DAAFHDKQAA SEADKLKEKV
EALSEEEKKQ IYEKGLELLD LQSKPQDTSC LPALKVSDIE PRIPFTELEM AHTAEDVPVQ
YCAQPTNGIV YFRAISSLNT LPEELRPYVP LFCRVITKMG CGAFNYREQA LEIDLKTGGL
SVSPHINVDD SHLDMYEQGV IFSSLCLDRN LPDMMHLWTE IFNNPHFEDD EHFKVLVKMT
AQELSNGIPD SGHNYALIRA SRTLTLAGEL QEMFHGMEQR IAEMADIKSV LRKLPRIRKY
LLNSDNLRCA VNATPQQMPV VTRAVENFVL GIARSKKERK AVRPRIIEVM EETKLKYVYA
NVKPSDSKSA SSEAGSQIRR KLITDPTFQP CQMKTHFLLP FPVNYVGACV RTVPFTTPDY
ASLRLLARLM TAKFLHTEIR EKGGAYGGGA HISHNGIFNF YSYRDPNSMN TLAAFEKAAE
WARTGMFTQQ DIDEAKLAVF ASVDAPIAPS DKGMNNFLYG ISDEMKQRHR EHLFAVSRES
LIDAANKFLI AGKSTRGLAI LGPENPETAK DPSWVIR
//
