ID A0A1V4KNJ2_PATFA Unreviewed; 1033 AA.
AC A0A1V4KNJ2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Presequence protease, mitochondrial {ECO:0000256|ARBA:ARBA00020167};
DE AltName: Full=Pitrilysin metalloproteinase 1 {ECO:0000256|ARBA:ARBA00032857};
GN Name=PITRM1 {ECO:0000313|EMBL:OPJ85347.1};
GN ORFNames=AV530_011777 {ECO:0000313|EMBL:OPJ85347.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ85347.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ85347.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ85347.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ85347.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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:OPJ85347.1}.
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DR EMBL; LSYS01002888; OPJ85347.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4KNJ2; -.
DR STRING; 372326.A0A1V4KNJ2; -.
DR Proteomes; UP000190648; 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 Hydrolase {ECO:0000313|EMBL:OPJ85347.1};
KW Protease {ECO:0000313|EMBL:OPJ85347.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000190648}.
FT DOMAIN 501..749
FT /note="Peptidase M16C associated"
FT /evidence="ECO:0000259|SMART:SM01264"
SQ SEQUENCE 1033 AA; 116944 MW; 109B1DAD921FC0FE CRC64;
MWSRYRAAGG LLSRGRSLVQ KSWRWRSVPA DERALQYRVG EQIHGFTVEQ VTAIPELFLT
AVKLSHDGTG ARYLHVARED SNNLFSIQFR TTPLDSTGVP HILEHTVLCG SQKYPCRDPF
FKMLNRSLST FMNAFTASDY TLYPFSTQNP KDFQNLLSVY LDAAFFPCLR QLDFWQEGWR
LEHENPTDPQ TPLVFKGVVF NEMKGAFTDN ERIFAQHLQN KILPDHTYGV VSGGDPLCIP
DLTWEQLKQF HATHYHPSNS RFFTYGNFPL EQHLKQIHEE ALVKFERIES NTDIPRQKLW
EKPREHSVTC GLDSFAADPS KQTTVSVSYL LTDITDTFET FTLSLLSSLL VDGPNSPFYK
ALIESGVGTD FSPDVGFNGS TREAYFSVGL QGIAERDIDT VKQIIARTID EVIVKGFEED
RIEALLHKIE IQLKHQSTSF GLALTSYIAS CWNQDGDPVE LLKIADKVSR FRQCLKENPT
FLQEKVKTYF KDNPHRLTLS MSPEKDYHDK QAKLETEKLE KKVKALSEEE KTQIFEKGLE
LIALQSKPQD TSCLPALKVS DIEPKIPFTV LETTLAADEI PVQYCAQPTN GVVYFRAVSS
LNTLPEELKP YVPLFCNVIT KMGCGALDYR EQAQKIELKT GGMSVSPHII PDDSHLDVYE
QGVLFSSLCL DRNLPDMMHL WSEIFNNPRF EEEEHFRVLV KKIAQELSNG VPDCGHLYAS
IRASKNLTPS GELQEMFSGM DQVKLMKRIA EMSDIKPILR KLPRIKKYLL NSDNIRCSVN
AAPQQISEVS KEVEKFIKSI GRSKKERKPV RPHVIEKSSE VKPVGSEMLT GLQITRKLVN
DPTFKPCQMK THFVLPFPVN YVGECIRTVP YTAADYASLR ILAQLMTAKF LHREIREKGG
AYGGGAKLSH SGIFTFYSYR DPNSLMTLKT FEKAVEWAKS GEFTQQDIDE AKLAVFAAVD
APIAPSDKGM GHFLYGISDE MKQSHREQLF AVNSDNLVDV SNKYLAAGKS TRGQAVLGPE
NADITKDPSW VKR
//