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Database: UniProt
Entry: A0A097ECK1_9SPHN
LinkDB: A0A097ECK1_9SPHN
Original site: A0A097ECK1_9SPHN 
ID   A0A097ECK1_9SPHN        Unreviewed;       512 AA.
AC   A0A097ECK1;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Ribonuclease BN {ECO:0000313|EMBL:AIT05300.1};
GN   ORFNames=MC45_01455 {ECO:0000313|EMBL:AIT05300.1};
OS   Sphingomonas taxi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1549858 {ECO:0000313|EMBL:AIT05300.1, ECO:0000313|Proteomes:UP000033200};
RN   [1] {ECO:0000313|EMBL:AIT05300.1, ECO:0000313|Proteomes:UP000033200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55669 {ECO:0000313|EMBL:AIT05300.1,
RC   ECO:0000313|Proteomes:UP000033200};
RA   Zhou Y., Ma T., Liu T.;
RT   "Using Illumina technology Improving SMRT sequencing Genome Assembly by
RT   RASTools.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; CP009571; AIT05300.1; -; Genomic_DNA.
DR   RefSeq; WP_038658644.1; NZ_CP009571.1.
DR   AlphaFoldDB; A0A097ECK1; -.
DR   STRING; 1549858.MC45_01455; -.
DR   KEGG; stax:MC45_01455; -.
DR   eggNOG; COG2303; Bacteria.
DR   HOGENOM; CLU_008878_4_0_5; -.
DR   Proteomes; UP000033200; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR46056; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   PANTHER; PTHR46056:SF4; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000033200}.
FT   DOMAIN          188..219
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   512 AA;  54872 MW;  EC80DEE12D34468A CRC64;
     MTSKRYGAHE VVDAVVIGTG AGGAPLTARL AQAGLSVVAL EAGRPFRPDD HVADEVAADI
     YWMEERLSGG ATPTAFGSNN SGMGVGGSTL HWGAFCPRPD PRDLQLKTMT GQGADWPINH
     AELIRYIAEV EQFTGVSGPD DYPWDATRRY AYPPVARNAA ADAMARGCAA VGMTATDAPA
     ALVSRDRDQP HWGQRQACVN CGTCHQGCRT AAKTSMDTTY LPLALAHGTE IRAGARVVSF
     EFDCSGRIGA VVYQQDGEEH RQRCSTVFLC AGGVETPRLL LNLGIANSSG QVGRNFMAHV
     ATQIWGRFDA DMRMNRGYPS SLISEDMMRP GDADCAGGYL IQSLGVLPVN LATGLARGAG
     MWGERLQALL RGYNRMAGIG INGECLPHAD NRLMLADEVD AYGHRKARID FSYHANEQAI
     DRHARRTLTR IWEAAGARDI VAVDRSAHTI GTCRMGTDGD AAVVDPDGRS FDLPNLLICD
     NSVFPSALAA NPALTIMALS LRTADRFLAS RH
//
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