ID A0A2A2TA68_9CYAN Unreviewed; 326 AA.
AC A0A2A2TA68;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Peptidase M48 {ECO:0000313|EMBL:PAX45954.1};
GN ORFNames=CK510_29285 {ECO:0000313|EMBL:PAX45954.1};
OS Calothrix elsteri CCALA 953.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=987040 {ECO:0000313|EMBL:PAX45954.1, ECO:0000313|Proteomes:UP000218238};
RN [1] {ECO:0000313|EMBL:PAX45954.1, ECO:0000313|Proteomes:UP000218238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCALA 953 {ECO:0000313|EMBL:PAX45954.1,
RC ECO:0000313|Proteomes:UP000218238};
RA Gagunashvili A.N., Elster J., Andresson O.S.;
RT "Draft genome sequence of filamentous cyanobacterium Calothrix elsteri
RT CCALA 953.";
RL Submitted (AUG-2017) 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:PAX45954.1}.
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DR EMBL; NTFS01000629; PAX45954.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2TA68; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000218238; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000218238};
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 65..265
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT COILED 298..325
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 326 AA; 37125 MW; ED3FA2C805AA1710 CRC64;
MATYTGISSE AFRHPLDRQA EQALRSLPGF DFVARKFVEF FAERPQLVYL MGNTIQVGPR
QYSTIYHMFR ECVRDLDVYP EPTLFVEQNP QANSYALGKE HPCIVINTGI LDLLSEAEIR
AVLAHELGHI KCGHTILIQM AIWASRAASA IGEVTFGIGN FVSQGLLLAF YEWRRKAELS
ADRAALLVVE DLNTVMTTMM KISGGSDKFA NECHLQAFIK QSEEYQALDE DGLNQIYKFM
MYNGVIGSMQ SHPFPVERLH YIREWSNSEE YKNIRAGNYM RNPAEGAVDV KVNSNGGNNT
TNSESDQLRR QLEELQREID RIRRNQ
//