ID G6FUY4_9CYAN Unreviewed; 323 AA.
AC G6FUY4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Peptidase M48 Ste24p {ECO:0000313|EMBL:EHC13064.1};
GN ORFNames=FJSC11DRAFT_2681 {ECO:0000313|EMBL:EHC13064.1};
OS Fischerella thermalis JSC-11.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae;
OC Fischerella.
OX NCBI_TaxID=741277 {ECO:0000313|EMBL:EHC13064.1, ECO:0000313|Proteomes:UP000004344};
RN [1] {ECO:0000313|EMBL:EHC13064.1, ECO:0000313|Proteomes:UP000004344}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSC-11 {ECO:0000313|EMBL:EHC13064.1,
RC ECO:0000313|Proteomes:UP000004344};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Sarkisova S., Bryant D.A., Brown I.,
RA Woyke T.J.;
RT "The draft genome of Fischerella sp. JSC-11.";
RL Submitted (SEP-2011) 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:EHC13064.1}.
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DR EMBL; AGIZ01000007; EHC13064.1; -; Genomic_DNA.
DR RefSeq; WP_009457360.1; NZ_AGIZ01000007.1.
DR AlphaFoldDB; G6FUY4; -.
DR GeneID; 60766750; -.
DR PATRIC; fig|741277.3.peg.2245; -.
DR Proteomes; UP000004344; 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:UP000004344};
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 295..322
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 323 AA; 36733 MW; 2136327B7F9CBE30 CRC64;
MATYTGISSE AFRHPLDRQA EQALRSLPGF DLVARKLMEF IYERPQLIYL MGNTIQVGPR
QYSTIYQIFR ECVRDLDIYP EPALFLSQNP QADSYALGQE HPYIVINTGI LDLLNEAEIR
AVLAHELGHI KCGHTILIQM AMGAMSAASA LGRFTFGIGN FVTPALIYAF FEWRRKAELS
ADRAALLLVD DLNTVMSSIM KTTGGSIKYA NECSLQELIR QSENYQVLDE DELNQVYKFL
VYSGSQSEML SHPFPVERLH YLQEWAVSTE YQQIKQGNYM RSPASGAVDV KATENAARNE
EIEKLRQKIA QLQREIDRMK KSD
//
