ID A0A090IHS2_9GAMM Unreviewed; 615 AA.
AC A0A090IHS2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Peptidase, family M3 {ECO:0000313|EMBL:CED60627.1};
DE SubName: Full=Putative peptidase {ECO:0000313|EMBL:SGZ09569.1};
GN ORFNames=MVIS_2697 {ECO:0000313|EMBL:CED60627.1}, NVI5450_3467
GN {ECO:0000313|EMBL:SGZ09569.1};
OS Moritella viscosa.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Moritellaceae; Moritella.
OX NCBI_TaxID=80854 {ECO:0000313|EMBL:CED60627.1, ECO:0000313|Proteomes:UP000032438};
RN [1] {ECO:0000313|EMBL:CED60627.1}
RP NUCLEOTIDE SEQUENCE.
RA Hjerde Erik;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000032438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hjerde E.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SGZ09569.1, ECO:0000313|Proteomes:UP000183794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NVI 5450 {ECO:0000313|EMBL:SGZ09569.1};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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|RuleBase:RU003435}.
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DR EMBL; LN554852; CED60627.1; -; Genomic_DNA.
DR EMBL; FPLD01000097; SGZ09569.1; -; Genomic_DNA.
DR RefSeq; WP_045110829.1; NZ_FRDV01000144.1.
DR STRING; 80854.MVIS_2697; -.
DR KEGG; mvs:MVIS_2697; -.
DR PATRIC; fig|80854.5.peg.2867; -.
DR HOGENOM; CLU_031103_0_0_6; -.
DR OrthoDB; 9773538at2; -.
DR Proteomes; UP000032438; Chromosome complete sequence.
DR Proteomes; UP000183794; Unassembled WGS sequence.
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 Gene3D; 1.10.1370.30; -; 2.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11804:SF84; SACCHAROLYSIN; 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 Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000032438};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 283..545
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 615 AA; 69372 MW; CDF7D97C98DF03CD CRC64;
MNPQNYFNQL NDDYLALHRR KEDLFWRTYM GTSDDHEGFA AAEAKLSAFI SDPSHIQTTR
CNLDVLLQLT DEDDELVQGL KGWLAFFDAN AIESAEGRDK MAALIRSESA LFTKRQDYLM
YCNDENGDKQ QASLTVLAAN IRTSNNEGVR QSAHQALLDL EQWVLNNGYI ELVKQRNDFA
RQQGFRNFFD YKVNKTEQMT PEQLFTILDD FELRTREGNL SSIQNLAEAK GDSAIQGHNF
SFMYAGDAAR QLDPYVPFSK SLRRWIESFG RLNIDYSQAD MTLDLLDRPG KYQNGFCHGP
IPSFYAEDKW QAGKINFTSN AKPDQIGSGY DGINTLFHEG GHAAHFANIK LNSPCFSQEF
APTSMAYAET QSMFCDSLLN DGDWLKQYAY NADGEVVPDD VIQALIAAKQ PFKAYQERSI
LVVPYFEWAV YSCDEELLTP EYLTTLARDT EQRILGLAAS PRPLLAVPHL LSQEAACSYQ
GYLLAHMAVY QTRAYFTKEF GYLTDNPAIG PLLAEHYWKP GNSISHDATL RSLTGEGFSA
AYLADTCNKT SEQAWLQEQA KIKAAQKRTR VQPAALNAKI SIVDGAETIA DNHISDGQLC
DDFETYITQR YGNNC
//
