ID L0DDD2_SINAD Unreviewed; 566 AA. AC L0DDD2; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 27-MAR-2024, entry version 50. DE SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:AGA26681.1}; GN OrderedLocusNames=Sinac_2369 {ECO:0000313|EMBL:AGA26681.1}; OS Singulisphaera acidiphila (strain ATCC BAA-1392 / DSM 18658 / VKM B-2454 / OS MOB10). OC Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae; OC Singulisphaera. OX NCBI_TaxID=886293 {ECO:0000313|EMBL:AGA26681.1, ECO:0000313|Proteomes:UP000010798}; RN [1] {ECO:0000313|EMBL:AGA26681.1, ECO:0000313|Proteomes:UP000010798} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1392 / DSM 18658 / VKM B-2454 / MOB10 RC {ECO:0000313|Proteomes:UP000010798}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Chertkov O., RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C., RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., RA Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P., RA Eisen J.A.; RT "Complete sequence of chromosome of Singulisphaera acidiphila DSM 18658."; RL Submitted (FEB-2012) 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; CP003364; AGA26681.1; -; Genomic_DNA. DR RefSeq; WP_015245834.1; NZ_JH621478.1. DR AlphaFoldDB; L0DDD2; -. DR STRING; 886293.Sinac_2369; -. DR KEGG; saci:Sinac_2369; -. DR eggNOG; COG1164; Bacteria. DR HOGENOM; CLU_516473_0_0_0; -. DR OrthoDB; 9762795at2; -. DR Proteomes; UP000010798; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro. DR GO; GO:0008241; F:peptidyl-dipeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR Gene3D; 1.10.1370.30; -; 1. DR InterPro; IPR001548; Peptidase_M2. DR PANTHER; PTHR10514; ANGIOTENSIN-CONVERTING ENZYME; 1. DR PANTHER; PTHR10514:SF27; ANGIOTENSIN-CONVERTING ENZYME; 1. DR Pfam; PF01401; Peptidase_M2; 1. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. PE 4: Predicted; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Reference proteome {ECO:0000313|Proteomes:UP000010798}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}. FT SIGNAL 1..25 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 26..566 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5003940751" SQ SEQUENCE 566 AA; 64106 MW; D5F0217177D71023 CRC64; MLHRSAILTL TVLLMGISDI QAVSAAPEAT ADDVKAQRFV SDHVTRIRPL EQAAALAWWN ANVTGKDEDF ATKEEAQNRL DAALADPQRF SELKAIKQGH VADPVLKRQI EVLYLSYLEK QVDPQLLRKI TAKANAIEKA FNAYRATVDR HEMADSEVRK VLKESDDLPR RKAVWEASKG VGATVEADLK TLVALRNEAA HTLGFKNYHA MQLHLNEQSQ EQVLTLFDEL DALTRAPFHA AKAEIDTKLA DNFGLNVADL RPWHYHDPFF QETPAVFKTD LDEAYAKADI LDLCRKFYAG IGLPIEDVIG RSDLYEKPGK SPHAFCIDID REGDVRVLAN IVPNEYWMGT MLHELGHSVY SSKNIPRDLP YVLRTEAHIL TTEGVAMMFE KFSKDADWLQ QMGVKLADPR GFDEAGAKMR KNKLLIFSRW CQVMLRFEKA LYENPEQDLN ALWWDLVEKY QEVRRPEGRN APDYASKIHI VSAPAYYHNY MMGELFAAQV HHTIAREVLQ GVDPSKASYV GNPAVGRFLK ERLFGPGRSL TWDDLTRHVT GQSLNPKAFA LDFQSH //