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Database: UniProt
Entry: A0A250XUK5_9CHLO
LinkDB: A0A250XUK5_9CHLO
Original site: A0A250XUK5_9CHLO 
ID   A0A250XUK5_9CHLO        Unreviewed;       145 AA.
AC   A0A250XUK5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   22-FEB-2023, entry version 20.
DE   RecName: Full=Peptidase M48 domain-containing protein {ECO:0000259|Pfam:PF01435};
DE   Flags: Fragment;
GN   ORFNames=CEUSTIGMA_g13937.t1 {ECO:0000313|EMBL:GAX86530.1};
OS   Chlamydomonas eustigma.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=1157962 {ECO:0000313|EMBL:GAX86530.1, ECO:0000313|Proteomes:UP000232323};
RN   [1] {ECO:0000313|EMBL:GAX86530.1, ECO:0000313|Proteomes:UP000232323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2499 {ECO:0000313|EMBL:GAX86530.1,
RC   ECO:0000313|Proteomes:UP000232323};
RA   Hirooka S., Hirose Y., Kanesaki Y., Higuchi S., Fujiwara T., Onuma R.,
RA   Era A., Ohbayashi R., Uzuka A., Nozaki H., Yoshikawa H., Miyagishima S.Y.;
RT   "Acidophilic green algal genome provides insights into adaptation to an
RT   acidic environment.";
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:GAX86530.1}.
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DR   EMBL; BEGY01000349; GAX86530.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A250XUK5; -.
DR   STRING; 1157962.A0A250XUK5; -.
DR   OrthoDB; 3080668at2759; -.
DR   Proteomes; UP000232323; Unassembled WGS sequence.
DR   GO; GO:0016020; C: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   Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR   InterPro; IPR001915; Peptidase_M48.
DR   PANTHER; PTHR10120; CAAX PRENYL PROTEASE 1; 1.
DR   PANTHER; PTHR10120:SF24; CAAX PRENYL PROTEASE 1 HOMOLOG; 1.
DR   Pfam; PF01435; Peptidase_M48; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW   Membrane {ECO:0000256|SAM:Phobius};
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:UP000232323};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT   TRANSMEM        42..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..134
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:GAX86530.1"
SQ   SEQUENCE   145 AA;  16591 MW;  FBD5DC91C81C504D CRC64;
     YGFWKNKRIV LYDTLLNHCS EEQVVAVLAH ELGHWKLGHT PVLFTVNQFV MLFSFSLFTF
     IRNSQVIQFC QNLVSRTFEF QADGFAVSQG VGGHLREALL KLEEENKSAM NVDPLYSSFH
     YSHPPLAERL KAIDVGVSEQ KKKDS
//
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