ID D8SQU2_SELML Unreviewed; 536 AA.
AC D8SQU2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SELMODRAFT_424715 {ECO:0000313|EMBL:EFJ13319.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ13319.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; GL377634; EFJ13319.1; -; Genomic_DNA.
DR RefSeq; XP_002985741.1; XM_002985695.1.
DR AlphaFoldDB; D8SQU2; -.
DR MEROPS; S08.006; -.
DR EnsemblPlants; EFJ13319; EFJ13319; SELMODRAFT_424715.
DR Gramene; EFJ13319; EFJ13319; SELMODRAFT_424715.
DR KEGG; smo:SELMODRAFT_424715; -.
DR HOGENOM; CLU_000625_4_5_1; -.
DR InParanoid; D8SQU2; -.
DR OMA; HYVITES; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04852; Peptidases_S8_3; 1.
DR Gene3D; 2.60.40.2310; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034197; Peptidases_S8_3.
DR InterPro; IPR045051; SBT.
DR InterPro; IPR041469; Subtilisin-like_FN3.
DR PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR PANTHER; PTHR10795:SF812; SUBTILISIN-LIKE PROTEASE SBT4.1; 1.
DR Pfam; PF17766; fn3_6; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 42..365
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 440..483
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT REGION 104..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 48
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1"
FT ACT_SITE 113
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1"
FT ACT_SITE 325
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1"
SQ SEQUENCE 536 AA; 56441 MW; DAC6F1C2686640A5 CRC64;
MPEVLNIYPS KTLHSLTTHS WDFLGLAMPA KSSHAGSPST DVIVGLLDTE SESFKDTDMG
PVPARWKGTC VNPPGTKANE TVNCNKKLVG ARYYNGAKVS TGPYKNSRDS VGHGTHTSST
AAGSLVPHAS KRGLAPGTAR GGAPNARIAM YKVCWTDSCE EVDIAAGFDD AINDGVDVLS
ISLGGYPAVY SVDVIAIGAY HAVERGIMVS CAGGNSGPFT GSVSNGAPWI FTVGASTIDR
EINEDAKIAA NRKSRILRGT TIPYKPAPVV AEFSSRGPHT ISPDIIKPDV TAPGVEILAA
WPSNIPDTDN GKEVFVEYTF LSGTSMACPH VSGTIAYLKS IHPTWSPAAI KSAVMTTAIT
KDNTNKTIID PSTNKAATVF DVGNGEIQPA KAVDPGLVYD TDPLDYITYL CNSGYTSKQI
QNITGDSSSK CPKNDTSFSL NYPSIAVLLD GSSKTVERTV TNVGNPSATY TASVGSAKGI
SISQQAELHK RRTEADLQRH RLRQGIHNGG SPSAEMEASR ISPGKMECTL CAARSP
//
