ID A0A2C9UYU3_MANES Unreviewed; 180 AA.
AC A0A2C9UYU3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=signal peptidase I {ECO:0000256|ARBA:ARBA00013208};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208};
GN ORFNames=MANES_11G054400 {ECO:0000313|EMBL:OAY36855.1};
OS Manihot esculenta (Cassava) (Jatropha manihot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY36855.1, ECO:0000313|Proteomes:UP000091857};
RN [1] {ECO:0000313|EMBL:OAY36855.1, ECO:0000313|Proteomes:UP000091857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY36855.1};
RA Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA Stites J., Rounsley S., Rokhsar D.S.;
RT "WGS assembly of Manihot esculenta.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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 S26B family.
CC {ECO:0000256|ARBA:ARBA00011035}.
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DR EMBL; CM004397; OAY36855.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9UYU3; -.
DR STRING; 3983.A0A2C9UYU3; -.
DR EnsemblPlants; OAY36855; OAY36855; MANES_11G054400.
DR Gramene; OAY36855; OAY36855; MANES_11G054400.
DR OMA; IPVVWFP; -.
DR OrthoDB; 1114626at2759; -.
DR Proteomes; UP000091857; Chromosome lg11.
DR GO; GO:0005787; C:signal peptidase complex; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006465; P:signal peptide processing; IBA:GO_Central.
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; IPR015927; Peptidase_S24_S26A/B/C.
DR InterPro; IPR019533; Peptidase_S26.
DR InterPro; IPR001733; Peptidase_S26B.
DR NCBIfam; TIGR02228; sigpep_I_arch; 1.
DR PANTHER; PTHR10806; SIGNAL PEPTIDASE COMPLEX CATALYTIC SUBUNIT SEC11; 1.
DR PANTHER; PTHR10806:SF35; SIGNAL PEPTIDASE I; 1.
DR Pfam; PF00717; Peptidase_S24; 1.
DR PRINTS; PR00728; SIGNALPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000091857};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 19..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..143
FT /note="Peptidase S24/S26A/S26B/S26C"
FT /evidence="ECO:0000259|Pfam:PF00717"
SQ SEQUENCE 180 AA; 19992 MW; DC3C53BD6EA221A2 CRC64;
MGWIGDTVDS IKSIQIRQLL TQAVSLGMIV TSALIIWKGL MCITGSESPV VVVLSGSMEP
GFKRGDILFL HMSKDPIRAG EIVVFNVDGR EIPIVHRVIK VHERQETGEV EVLTKGDNNY
GDDRLLYAQG QLWLQRHHIM GRAVGFLPYV GWVTIIMTEK PIIKYILIGA LGLLVITSKD
//
