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Database: UniProt
Entry: A0A0C2PWY3_9CYAN
LinkDB: A0A0C2PWY3_9CYAN
Original site: A0A0C2PWY3_9CYAN 
ID   A0A0C2PWY3_9CYAN        Unreviewed;       323 AA.
AC   A0A0C2PWY3;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Peptidase M48 {ECO:0000313|EMBL:KIJ76109.1};
GN   ORFNames=SD81_16760 {ECO:0000313|EMBL:KIJ76109.1};
OS   Tolypothrix campylonemoides VB511288.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC   Tolypothrix.
OX   NCBI_TaxID=1245935 {ECO:0000313|EMBL:KIJ76109.1};
RN   [1] {ECO:0000313|EMBL:KIJ76109.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VB511288 {ECO:0000313|EMBL:KIJ76109.1};
RA   Tripathy S., Das S., Gupta A., Malar M.C., Adhikary S.P.;
RT   "Draft whole genome shotgun sequence of Tolypothrix campylonemoides
RT   VB511288.";
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:RU003983};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU003983};
CC   -!- SIMILARITY: Belongs to the peptidase M48 family.
CC       {ECO:0000256|RuleBase:RU003983}.
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:KIJ76109.1}.
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DR   EMBL; JXCB01000008; KIJ76109.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2PWY3; -.
DR   OrthoDB; 9810445at2; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07325; M48_Ste24p_like; 1.
DR   Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR   InterPro; IPR001915; Peptidase_M48.
DR   PANTHER; PTHR43221; PROTEASE HTPX; 1.
DR   PANTHER; PTHR43221:SF3; SLL1280 PROTEIN; 1.
DR   Pfam; PF01435; Peptidase_M48; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003983};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003983};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT   DOMAIN          63..265
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
FT   COILED          290..323
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   323 AA;  36881 MW;  08D2FF6434E37938 CRC64;
     MPTYKGISSE AFRHPLDRQA ELALRSLPGF DFVARKFVEF FVERPQLIYL MGNTIQVGPR
     QYSTIYQMFR ECVRDLDIYP EPALFLEQNP LANSYALGQE HPYIVINTGV LDLLNEAEIR
     AVLAHELGHI KCGHTILIQM AIWAMSAASA IGDLTFGIGN FVTQGLIYAF YEWRRKAELS
     ADRAALLVMD DLNPVMTSMM KVSGGSIKYA NECSLQEFIR QSEEYQALDA DGLNQIYKFL
     IYNGGRGTML SHPFAVERIH YLRQWAESEE YQQIKKGNYQ RATAAGAVNV EAQTAQNEEV
     ETLRRQIEEL QKEMDRIKRS KSE
//
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