ID A5GCU9_GEOUR Unreviewed; 1726 AA.
AC A5GCU9;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Peptidase S8 and S53, subtilisin, kexin, sedolisin {ECO:0000313|EMBL:ABQ24599.1};
GN OrderedLocusNames=Gura_0383 {ECO:0000313|EMBL:ABQ24599.1};
OS Geotalea uraniireducens (strain Rf4) (Geobacter uraniireducens).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geotalea.
OX NCBI_TaxID=351605 {ECO:0000313|EMBL:ABQ24599.1, ECO:0000313|Proteomes:UP000006695};
RN [1] {ECO:0000313|EMBL:ABQ24599.1, ECO:0000313|Proteomes:UP000006695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rf4 {ECO:0000313|EMBL:ABQ24599.1,
RC ECO:0000313|Proteomes:UP000006695};
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 Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Shelobolina E., Aklujkar M.,
RA Lovley D., Richardson P.;
RT "Complete sequence of Geobacter uraniireducens Rf4.";
RL Submitted (MAY-2007) 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; CP000698; ABQ24599.1; -; Genomic_DNA.
DR RefSeq; WP_011937325.1; NC_009483.1.
DR STRING; 351605.Gura_0383; -.
DR KEGG; gur:Gura_0383; -.
DR HOGENOM; CLU_240118_0_0_7; -.
DR OrthoDB; 5395460at2; -.
DR Proteomes; UP000006695; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 4.
DR CDD; cd04842; Peptidases_S8_Kp43_protease; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR011635; CARDB.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
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; IPR034058; TagA/B/C/D_pept_dom.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF07705; CARDB; 1.
DR Pfam; PF09136; Glucodextran_B; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00060; FN3; 8.
DR SMART; SM00409; IG; 3.
DR SUPFAM; SSF49265; Fibronectin type III; 6.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS50853; FN3; 7.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 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}; Reference proteome {ECO:0000313|Proteomes:UP000006695};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 1092..1181
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1183..1272
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1274..1362
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1365..1454
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1456..1545
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1547..1636
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1638..1726
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT ACT_SITE 244
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 287
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 467
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1726 AA; 180260 MW; 86C110D78435FE8D CRC64;
MCGQIKRCAS LSVFFIVLLY LGGSPAWAKE FSKHKVQING IVIDVKGKEP AVPEILEPRV
DKGRRKWVVQ FTGPIHEEEK AKVEELGCRL LDYLPDFAFL ATMDDTAKKA VKKLPYIEGV
VRFKPAHKLR EKLREKATAR PSGEKIRIHL RLDDPANVRD VLAVVQQMEG DVLDVGRDTL
RVAVDTTSIA KLAAIEEVSW IDEHFDMQLF NDTTRWVIQT DIPDNTEIWD QKIHGEGQII
GIGDTGLDYD MPWFRDPAGA PIGTGHRKIV GYDTTYGDDY DASTPGHGTH VTDTVAGDRT
PVDGLSNANG MAPKARVFIQ DLTPGGSNAV YPPDDLGLMF TAAYNVGARF HTNSWGNDDG
SYSSFAASAD RFLWEHKEFL ALFANGNAGP GLSTVGNPAT AKNVISVGAT YNGSSAENMA
SFSSNGPTAD GRIKPTVTAP GYGIISADSD GLKDSSNNGT LGMSGTSMAT PAVAGAAALV
RQYFIDGFHP LGIATPINAF TPSAALVKAV VVNSAQNMTG TGTGGPIPAT GQGWGRINLA
NALPFAGEAG RLAVVDEGGG LGTDKNWSRQ FLVPGGQPFK VTLVWTDYPG TIGAVKAIVN
DLDLAVSTPD GTVLTGNAFT NGESFAGGTP DRLNVEEQVL VQAPVPGIYT VSVTGYNVPY
APQPFALAIT GASGVTSRGT ISLDRQRYNS SSTLQIQIAD RDLNSDPTKV EQVPILVVST
AESSGETVVL TESAPNIAIF SGSIPIAAAP VVPGDGRLQG ADGDTITAIY HDANDGSGKS
ATVTAAAFVD NVPPAISNLA VTGITDTAAT ITWTTNEPAN SVLNYGDTPA MGGVSADKKL
ATEHSMRLTA LLEAATYHVA AKSTDEAGNT AGSSAILFTT LNLPPSLTVT SSEGSTTYQP
STVITGVCTD PSGVSSVTIN GTVANYRPSD GYYSLPVALQ VGDNGFTVAA TDTLGKTTSL
TITVTRLQPS DLFVQSVAGP PSAVQGSTIT ITDTVCNGGP GDATGFSVGF YLSSDQNLSS
DDMLIGSRNV ASIAAGTCPS GTTRAPIPPT APGGSLYLIA CADYTNRLVE TNKNNNTLAG
NQITLPNPQL APPSSINVPA GNTTGSFQVS WSPSNVSGVT YVLEYSKDNG AYTSAYNGTY
TWANLTVPAS GTYTFRVKAA KTGYTDSAYS ATRSCSVTLI CGAPASISVP SGNTTGSFQV
SWSPSNVSGV TYVLEYSKDN GAYTSAYNGT YTWANLTVPA SGTYTFRVKA AKTGYTDSAY
SATKSCSVTL ICGAPASISV PSGNTTGSFQ VSWSPSNVSG VTYVLEYSKD NGAYTSAYKG
TYTWANLTVP ASGTYTFRVK AAKTGYTDSA YSATKSCSVI LICGAPASIS VPSGNTTGSF
QVSWSPSNVS GVTYVLEYSK DNGAYTSAYN GTYTWANLTV PASGTYTFRV KAAKTGYTDS
AYSATKSCSV TLICGAPASI SVPSGNTTGS FQVSWSPSNV SGVTYVLEYS KDNGAYTSAY
SGTYTWANLT VPASGTYTFR VKAAKTGYTD SAYSATKSCS VTLICGAPAS ISVPSGNTTG
SFQVSWSPSN VSGVTYVLEY SKDNGAYTSA YKGTYTWANL TVPASGTYTF RVKAAKTGYT
DSAYSATKSC SVTLICGAPA SISVPASSTT GSFQVSWSRS NVSGVTYVLE YSKDNGAYTS
AFRGPYTWAN LTVPARGTYT FRVKATKTGY ADSAWKVSSS IVVNRK
//
