ID A0A1L8D683_BOTAT Unreviewed; 409 AA. AC A0A1L8D683; DT 15-MAR-2017, integrated into UniProtKB/TrEMBL. DT 15-MAR-2017, sequence version 1. DT 22-NOV-2017, entry version 4. DE SubName: Full=BATXSVMPI1 {ECO:0000313|EMBL:JAV01877.1}; OS Bothrops atrox (Barba amarilla) (Fer-de-lance). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; OC Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops. OX NCBI_TaxID=8725 {ECO:0000313|EMBL:JAV01877.1}; RN [1] {ECO:0000313|EMBL:JAV01877.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tapajos National Forest {ECO:0000313|EMBL:JAV01877.1}; RC TISSUE=Venom gland {ECO:0000313|EMBL:JAV01877.1}; RA Amazonas D.R., Nishiyama M.Y.Jr., Gibbs H.L., Rokyta D.R., RA Junqueira-de-Azevedo I.L., Moura-da-Silva A.M.; RT "Transcriptomic analysis of venom glands from five Bothrops atrox RT snakes."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. 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; GEDR01000085; JAV01877.1; -; mRNA. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR CDD; cd04269; ZnMc_adamalysin_II_like; 1. DR Gene3D; 3.40.390.10; -; 1. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR InterPro; IPR034027; Reprolysin_adamalysin. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. PE 2: Evidence at transcript level; KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00276, KW ECO:0000256|SAAS:SAAS00517240}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276}; KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DOMAIN 193 389 Peptidase M12B. {ECO:0000259|PROSITE: FT PS50215}. FT ACT_SITE 330 330 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT METAL 329 329 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 333 333 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT METAL 339 339 Zinc; catalytic. {ECO:0000256|PROSITE- FT ProRule:PRU00276}. FT DISULFID 304 384 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DISULFID 344 368 {ECO:0000256|PROSITE-ProRule:PRU00276}. FT DISULFID 346 351 {ECO:0000256|PROSITE-ProRule:PRU00276}. SQ SEQUENCE 409 AA; 46041 MW; F636A91EF4CA894A CRC64; MIQVLLVTIC LAAFPYQGSS IILESGNVND YEVVYPRKVT ALPKGAVQPK YEDAMQYEFK VNGEPVVLHL EKNKGLFSKD YSEIHYSPDG REITTYPPVE DHCYYHGRIE NDADSTASIS ACNGLKGHFK LQGETYLIEP LKLSDSEAHA VFKFENVEKE DEAPKMCGVT QNWESYEPIK KASQSNLTPE QQRYVELFVV VDHGMFMKYN GNSDKIRRRI HQMVNIMKEI YSTMYIDIFL TGVEIWSNKD LINVQPAAPQ TLDSFGEWRK TDLLNRKSHD NAQLLTSTDF NGPTIGLAYV GSMCDPKRST GVIQDHSPIN LMVAVTMAHE LGHNLGISHD TGSCSCGGYS CIMSPVLSHE PSKYFSDCSY IQCWDFIMKE NPQCILNKRL RTDTVSTPVS GNQLLEAGE //