ID Q10Z63_TRIEI Unreviewed; 1154 AA.
AC Q10Z63;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Peptidase S8 and S53, subtilisin, kexin, sedolisin {ECO:0000313|EMBL:ABG52461.1};
GN OrderedLocusNames=Tery_3359 {ECO:0000313|EMBL:ABG52461.1};
OS Trichodesmium erythraeum (strain IMS101).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Trichodesmium.
OX NCBI_TaxID=203124 {ECO:0000313|EMBL:ABG52461.1};
RN [1] {ECO:0000313|EMBL:ABG52461.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMS101 {ECO:0000313|EMBL:ABG52461.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Richardson P.;
RT "Complete sequence of Trichodesmium erythraeum IMS101.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
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DR EMBL; CP000393; ABG52461.1; -; Genomic_DNA.
DR AlphaFoldDB; Q10Z63; -.
DR KEGG; ter:Tery_3359; -.
DR eggNOG; COG0823; Bacteria.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_276069_0_0_3; -.
DR OrthoDB; 9798386at2; -.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR001846; VWF_type-D.
DR PANTHER; PTHR46580:SF3; ATP_GTP-BINDING PROTEIN-RELATED; 1.
DR PANTHER; PTHR46580; SENSOR KINASE-RELATED; 1.
DR Pfam; PF13517; FG-GAP_3; 3.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF00094; VWD; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00216; VWD; 1.
DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 2.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS51233; VWFD; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 573..767
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 273
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 310
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 509
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1154 AA; 125871 MW; CC6829282442E27E CRC64;
MMTTPSSRRV QNSRNNPPVA DKNKITVYEN STDTPLGITA PTDPDGDPLT IRVIGLPRLG
TVTKADGTEV KRRDKLTSEE LVGLEYDAPN NYNGKGNAGG FFYFVNDGTS NRLGSTRITI
NPLPEDFKPG EVIVKLKDVD NKTSSKKIES FRDNLDIEVI STIEGIGVEL WKLPNSTNVQ
EFVEEYSSRP EFDIQPNFTN TKLFTPNHPD DPDYNVLEGS SPPGLGRLWG LNNKGQTGGT
DDADINAPEA WGFTTTPVVS PTVNSTVRVA VIDTGVDVNH PDLTGNLNLD LAANTIFGDD
PEDVTDNHGH GTHVAGIIGA VGNNQTGVVG VNWDVEIVPI KAFDDIDGDG VPEATDMAIL
EAINYAINVA KVDIINASWG KLPDNDNDDN DDIAELWKNV IDNDTDDESQ PPPSPPPLFV
AAAGNQGVDI DDPENAVYPA SIDSQNIISV AATDHDDNLS SFSNFGASVD LAAPGGSDIP
GNGPGSSTDP RNIYSTLPNN DYGYSAGTSA AAAYVSGAAA LMLGTRRARN EKTGQPDLST
LQLEEKLRNA ITPINGLPTA TGGRLNLYNG IDQEGIGWGD VHFTTFDGRK YDLQSFGDFI
MAETARNDDD WVVQTRQQPW AKNSSVAVNT AFATRVDGKT VVFNQKFPNN RLQVGGVDFP
LASGETKNIG DSKIERDGNK YTITYAGNDG IIDVDDAKLT AFDNGDHINI HISDFATMQG
LLGNNDGNPN NDFALSDDTQ KSNNVTAKTI HQEHGEYWRV PSEDKEQKGD RKSLFEDSAE
VIGIPKRFLT LDGFPKNDVA AVNAKVKKAG ITDKDRADAV AFDLLATEDE TFLTSAVEFF
KSVDEANNPD VQAPVQFDFN ADGVADILWR EEKGRRARSD IWFMNDDGTL NKSTPLVNYY
SRWDVAGVGD FNADGVADIL WRHKKYGFNY IWLMNDEGTF NSRLHIKRLS SSWNVEGVAD
FNGDGVEDIF WRNKSQNQIW FMNDEGKVNN RASLDSLGTS WDVAGVGDFN GDGVEDILLR
DTKGSNEIWF MNDQGEVDNR DRLSRLSSRW DVAGVGDFNS DGVEDILWRD TKGSNQIWLM
NDQGKVQSSV DPGSYDSAWD VAGVAEFNGD GVADILWRDE NNGSNRIWLM NNDGTRNQIV
DPGSLGSTWD VVGM
//
