ID A0A0Q9A2T0_9FLAO Unreviewed; 592 AA.
AC A0A0Q9A2T0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Cytochrome C peroxidase {ECO:0000313|EMBL:KRD12912.1};
GN ORFNames=ASE21_03110 {ECO:0000313|EMBL:KRD12912.1};
OS Flavobacterium sp. Root901.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1736605 {ECO:0000313|EMBL:KRD12912.1, ECO:0000313|Proteomes:UP000051400};
RN [1] {ECO:0000313|EMBL:KRD12912.1, ECO:0000313|Proteomes:UP000051400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root901 {ECO:0000313|EMBL:KRD12912.1,
RC ECO:0000313|Proteomes:UP000051400};
RX PubMed=26633631; DOI=.1038/nature16192;
RA Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E., Rott M.,
RA Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M., Huttel B.,
RA McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL Nature 528:364-369(2015).
RN [2] {ECO:0000313|Proteomes:UP000051400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root901 {ECO:0000313|Proteomes:UP000051400};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000051400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root901 {ECO:0000313|Proteomes:UP000051400};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRD12912.1}.
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DR EMBL; LMJB01000001; KRD12912.1; -; Genomic_DNA.
DR RefSeq; WP_057121091.1; NZ_LMJB01000001.1.
DR AlphaFoldDB; A0A0Q9A2T0; -.
DR STRING; 1736605.ASE21_03110; -.
DR OrthoDB; 9805202at2; -.
DR Proteomes; UP000051400; Unassembled WGS sequence.
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 Gene3D; 1.20.1420.20; M75 peptidase, HXXE motif; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR004852; Di-haem_cyt_c_peroxidsae.
DR InterPro; IPR038352; Imelysin_sf.
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:KRD12912.1};
KW Peroxidase {ECO:0000313|EMBL:KRD12912.1}.
FT DOMAIN 294..403
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 446..584
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 592 AA; 66568 MW; 190C0A25C2EAB632 CRC64;
MKKIYCLLFL VAFAACQKKD KHQEINKLFQ EDIRLLIEKA AQLKQSVESD SAEAQIQEQF
LEAHQGYKKV ELLSEYYSPA VSKSINGPAI PEFEENDNIT VNPEGFQVIE ELVFPKYDKK
NKKELLQEIG VLSANLIRLE KVANSNELTD AHVFDAMRLE VYRIITLGIT GFDSPVVLNS
LPEASISLET IEKYYRVYLE NKEISSAPQV LGILEKGKKY LQSNNNFNAF DRAYFIKEIL
NPLSKGLFKT QAELGIPLMK EQKGLKVTSQ TLFDKDAFDP DAFSGFPDYK TTPEKIALGK
KLFNDPILSG NNTRSCASCH HAEKAFTDGL EKAVSLDGKS MIQRNTPTLA NIAFQRVFFA
DSRVSYLEDQ AIAVIKNENE MHGSLEKSAL AIQKKAQYVK DFKTAFAKGE INEFTIKNAL
GSYIRSLSHY DAKFDHYMQN KTSFAADEKA GFNLFAGKAK CATCHFIPLT NGTVPPNFDK
SESEILGVPD KNKKLDGDLG KFVITQAAIH KHSFKTPTIR NIELTAPYMH NGVYKTLEEV
IDFYDQGGGL GLGFDLPNQT LPEDKLNLTV KEKKQLIAFM KTLTDKKFLK KS
//
