ID A0A2V0PT00_9CHLO Unreviewed; 238 AA.
AC A0A2V0PT00;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=signal peptidase I {ECO:0000256|ARBA:ARBA00013208};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208};
GN ORFNames=Rsub_13233 {ECO:0000313|EMBL:GBG00476.1};
OS Raphidocelis subcapitata.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Selenastraceae; Raphidocelis.
OX NCBI_TaxID=307507 {ECO:0000313|EMBL:GBG00476.1, ECO:0000313|Proteomes:UP000247498};
RN [1] {ECO:0000313|EMBL:GBG00476.1, ECO:0000313|Proteomes:UP000247498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-35 {ECO:0000313|EMBL:GBG00476.1,
RC ECO:0000313|Proteomes:UP000247498};
RX PubMed=29795299; DOI=10.1038/s41598-018-26331-6;
RA Suzuki S., Yamaguchi H., Nakajima N., Kawachi M.;
RT "Raphidocelis subcapitata (=Pseudokirchneriella subcapitata) provides an
RT insight into genome evolution and environmental adaptations in the
RT Sphaeropleales.";
RL Sci. Rep. 8:8058-8058(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences
CC from secreted and periplasmic proteins.; EC=3.4.21.89;
CC Evidence={ECO:0000256|ARBA:ARBA00000677};
CC -!- SIMILARITY: Belongs to the peptidase S26 family.
CC {ECO:0000256|ARBA:ARBA00009370}.
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:GBG00476.1}.
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DR EMBL; BDRX01000231; GBG00476.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V0PT00; -.
DR STRING; 307507.A0A2V0PT00; -.
DR InParanoid; A0A2V0PT00; -.
DR Proteomes; UP000247498; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR CDD; cd06530; S26_SPase_I; 1.
DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR InterPro; IPR019533; Peptidase_S26.
DR NCBIfam; TIGR02227; sigpep_I_bact; 1.
DR PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR Pfam; PF10502; Peptidase_S26; 1.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR PROSITE; PS00761; SPASE_I_3; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000247498}.
FT DOMAIN 79..189
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT REGION 205..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 238 AA; 25091 MW; 5831777DAE6819E1 CRC64;
MLRCGSNSLA ASGRAHAAPA LAPRAISRAH LAAGRPAGGA SPAAAGGAAA ARAAAARRAL
LHVARAQNRD SGEAGARSWR PPVAGDVVIF HPVEGVGRKS LLGDDVFIKR VVAVEGDSVE
VKGGKLYVNG APREEPFINE PPAYSLQKLV VPPHDVFVCG DNRNNSYDSH IWGPLPQENI
LGRAVFVYWP PQKVGSLPDY TEAIAQQAQQ QQQGQQGQQQ QQQQQQQQQK AQPAGAAS
//
