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Database: UniProt
Entry: L0DK53_SINAD
LinkDB: L0DK53_SINAD
Original site: L0DK53_SINAD 
ID   L0DK53_SINAD            Unreviewed;       479 AA.
AC   L0DK53;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=Cytochrome c peroxidase {ECO:0000313|EMBL:AGA29220.1};
GN   OrderedLocusNames=Sinac_5068 {ECO:0000313|EMBL:AGA29220.1};
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:AGA29220.1, ECO:0000313|Proteomes:UP000010798};
RN   [1] {ECO:0000313|EMBL:AGA29220.1, 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.
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DR   EMBL; CP003364; AGA29220.1; -; Genomic_DNA.
DR   RefSeq; WP_015248326.1; NZ_JH621480.1.
DR   AlphaFoldDB; L0DK53; -.
DR   STRING; 886293.Sinac_5068; -.
DR   KEGG; saci:Sinac_5068; -.
DR   eggNOG; COG1858; Bacteria.
DR   HOGENOM; CLU_034652_3_2_0; -.
DR   OMA; TGCTTCH; -.
DR   OrthoDB; 9772811at2; -.
DR   Proteomes; UP000010798; Chromosome.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 2.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR004852; Di-haem_cyt_c_peroxidsae.
DR   PANTHER; PTHR30600; CYTOCHROME C PEROXIDASE-RELATED; 1.
DR   PANTHER; PTHR30600:SF10; METHYLAMINE UTILIZATION PROTEIN; 1.
DR   Pfam; PF03150; CCP_MauG; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 2.
DR   PROSITE; PS51007; CYTC; 2.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00433}; Oxidoreductase {ECO:0000313|EMBL:AGA29220.1};
KW   Peroxidase {ECO:0000313|EMBL:AGA29220.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010798};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..479
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003940914"
FT   DOMAIN          136..268
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          290..435
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   REGION          27..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          446..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   479 AA;  51329 MW;  7CA4E4875555B2BC CRC64;
     MLARFGSVTR LALAAALLTL GGCGGTGTEK EEAASAPSPS GALDAAAAKA TDTNSADLPA
     KLVTPDRAVD PKKLVDVVEQ EVKGGENASP SPESILWLPT DQAKVKDEPL TVQVPKGLSP
     LILNVNVPAS NPLTKAKFEL GKQLYFDPRV SLDGTISCAT CHNPEKGWTD QLKFSIGIDG
     QTGGRNAPTV VNTVYGKTMF WDGRAPSLEG QAQGPIQNPI EMGKQSYEDI VKRLRTIPSY
     KEQFATVFGS DVTLDGMAKA IATFERVAAL SGNSRYDKYN SGDDLAALSE SEKRGMVLFG
     LRLRSEDEFK PNVTLKKADC TSCHTGSNFT NEQFHNIGVG WNTEKNDFAD YGRFVISPIG
     SKNNAELGAF KTPTVREIEK TGPYMHDGSM KTLEEVVEHY NKGGNPNPAL DKDIKKLNLT
     DSEKADVVAF LKALTGEEIK VALPTLPPGA DGKTPDPQAA LTPPPLKTVS NVFHPDVQQ
//
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