ID A0A1Q9E5S7_SYMMI Unreviewed; 561 AA.
AC A0A1Q9E5S7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Thiol protease {ECO:0000313|EMBL:OLQ02775.1};
GN Name=SEN102 {ECO:0000313|EMBL:OLQ02775.1};
GN ORFNames=AK812_SmicGene14321 {ECO:0000313|EMBL:OLQ02775.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLQ02775.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLQ02775.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLQ02775.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT adaptations to a symbiotic lifestyle.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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:OLQ02775.1}.
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DR EMBL; LSRX01000254; OLQ02775.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9E5S7; -.
DR OrthoDB; 808912at2759; -.
DR Proteomes; UP000186817; Unassembled WGS sequence.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02248; Peptidase_C1A; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR013128; Peptidase_C1A.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR PANTHER; PTHR12411:SF741; CATHEPSIN K; 1.
DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000313|EMBL:OLQ02775.1};
KW Protease {ECO:0000313|EMBL:OLQ02775.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 215..272
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 301..531
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 561 AA; 61542 MW; 5250870D1CD1A799 CRC64;
MLGTSISWSW SYILEDLVQG KVFTHEDIEK GLGSLIGSFA AVPREIFRDP HKQNSPLAAE
SSWWGSRDAS ASDSKAYIGG WLAMDPNPDK SSVSPKQRIA VLEMLGSLVL MAFLIEKNDQ
GKRFLIIPLL SDKGTCPSSP RSVQGVMAWL RAIYPPQGLP SPEHLQEKLV CLVCEEQRSI
NMFQSFRILA FLACAASLRG EREKFTSEED DEAAYKQFRQ EFNRTADDSI AYMERLAHFR
RFRNAVARHN ARTDASWRAV VGPFADYTDA EFKALLGHRR TFRPEVKTAS SFLQTEPHKT
VASTVDWTDK LSSVRSVKGM VWFLGARFVF CSCWAVAAIG ALEMHAELAL QKASSALSSN
QVKDCSTNPK HCGGSGGCQG STSELAYDYI VKNGIALDST YGGDKNRDSS CQPHKPYLRI
AGFQPLPVNK LQPLMEAVST KGPVVVSIDA SGWNSYGGGI FDSCDKDAVV NHAVVLVGYG
KSKSENKEYW LIRNSWGEGW GEKGFIRLLR HSSDQGDAGY CGTDRNPKEG VGCDGGPPEI
PVCGMCGVLS DSVYPTGLQL A
//
