ID R4KLY4_9FIRM Unreviewed; 428 AA.
AC R4KLY4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Serine protease inhibitor {ECO:0000313|EMBL:AGL02557.1};
GN ORFNames=Desgi_3203 {ECO:0000313|EMBL:AGL02557.1};
OS Desulfoscipio gibsoniae DSM 7213.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfallaceae;
OC Desulfoscipio.
OX NCBI_TaxID=767817 {ECO:0000313|EMBL:AGL02557.1, ECO:0000313|Proteomes:UP000013520};
RN [1] {ECO:0000313|EMBL:AGL02557.1, ECO:0000313|Proteomes:UP000013520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7213 {ECO:0000313|EMBL:AGL02557.1,
RC ECO:0000313|Proteomes:UP000013520};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Parshina S.,
RA Plugge C., Muyzer G., Kuever J., Ivanova A., Nazina T., Klenk H.-P.,
RA Brambilla E., Spring S., Stams A.F., Woyke T.;
RT "Complete sequence of Desulfotomaculum gibsoniae DSM 7213.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the serpin family.
CC {ECO:0000256|RuleBase:RU000411}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003273; AGL02557.1; -; Genomic_DNA.
DR RefSeq; WP_006524089.1; NC_021184.1.
DR AlphaFoldDB; R4KLY4; -.
DR STRING; 767817.Desgi_3203; -.
DR KEGG; dgi:Desgi_3203; -.
DR eggNOG; COG4826; Bacteria.
DR HOGENOM; CLU_023330_2_1_9; -.
DR OrthoDB; 9764871at2; -.
DR Proteomes; UP000013520; Chromosome.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR CDD; cd19589; serpin_tengpin-like; 1.
DR Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1.
DR Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 1.
DR InterPro; IPR023795; Serpin_CS.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR InterPro; IPR036186; Serpin_sf.
DR InterPro; IPR042178; Serpin_sf_1.
DR InterPro; IPR042185; Serpin_sf_2.
DR PANTHER; PTHR11461:SF211; ACCESSORY GLAND PROTEIN ACP76A-RELATED; 1.
DR PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; Serpins; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00284; SERPIN; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000013520}.
FT DOMAIN 60..424
FT /note="Serpin"
FT /evidence="ECO:0000259|SMART:SM00093"
SQ SEQUENCE 428 AA; 48633 MW; F119B9140D0FCD25 CRC64;
MIPFHVKFTG IALVILFFII GCGNAATAVQ FEKQAELKKI EKPSVFHEDK LYTACNTSGI
QLLQKISAAN EGKNTIFSPV SFATLMAVLN NGAASKTRCE INALINPEQL SPAELNEKYC
HTINHLINTG YRENGNQTTV VELANSLWIQ EDLRVKDDFL NTSNTYYDTE AYNVNFKDNS
TINAMNRWIE DKTYGRIQNH ITEFDPPPVM VAFNSLYFNG KWQNPFDQSK TQKEDFHLNN
GDIAKVEMMN AEKRMQYYED DQIQAGKFDY YGCGMLVILP KGDTDNYFSN LSYAEIQKAN
NNLENMKVKI KFPKFNFKQK NKLADHLKTM GLESAFDYKN ADFTAIADRS DRFNLYINDI
SQECFINVDE EGTEAAALTS VFLAGSGMPR DNVPPEFYLN KPFIFVISDD WTGLILFAGK
VENPLENV
//
