ID   A0A225NAV8_9RHOB        Unreviewed;       461 AA.
AC   A0A225NAV8;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Cytochrome C {ECO:0000313|EMBL:OWU67375.1};
GN   ORFNames=ATO3_26355 {ECO:0000313|EMBL:OWU67375.1};
OS   Marinibacterium profundimaris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Marinibacterium.
OX   NCBI_TaxID=1679460 {ECO:0000313|EMBL:OWU67375.1, ECO:0000313|Proteomes:UP000215377};
RN   [1] {ECO:0000313|EMBL:OWU67375.1, ECO:0000313|Proteomes:UP000215377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22II1-22F33 {ECO:0000313|EMBL:OWU67375.1,
RC   ECO:0000313|Proteomes:UP000215377};
RA   Lai Q., Li G., Shao Z.;
RT   "Oceanicola sp. 22II1-22F33 Genome Sequencing.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:OWU67375.1}.
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DR   EMBL; AQQR01000029; OWU67375.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A225NAV8; -.
DR   OrthoDB; 9792185at2; -.
DR   Proteomes; UP000215377; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd06198; FNR_like_3; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR013112; FAD-bd_8.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR47354:SF8; 1,2-PHENYLACETYL-COA EPOXIDASE, SUBUNIT E; 1.
DR   PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR   Pfam; PF08022; FAD_binding_8; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00409; PHDIOXRDTASE.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215377};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        40..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        70..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        113..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        148..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        186..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        211..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          236..335
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   461 AA;  50590 MW;  7018A3AE81A8435D CRC64;
     MIVATAITRD ATMTDTAHRD GNVSAPGLPT LPRLSLNSPL ALTGPVLVAL PCLLAALFGM
     NTYAPYGADA AFGIAVGAAA VVAMAQTLIL AARPPLVEPL FGGLDRMYRV HKWLGISAMV
     LMILHQQIEP DFERLVRETS LGDLGEEAGE LAFNALLALV AVSWFRRLPF IGLEIPYQLW
     RFSHRFMGAL FAIVVFHQFF VDMPAGVDPT FMLVLNAFGI AGVVAWIFTE LLAPHLRRRD
     FTVSQIRQTG DTTTLTLRPE GRAMRWRPGQ FAFFRAPEAG LSEPHPFTIA SAPRPDGTLT
     FSIRGLGGWT RSLPAILRTG TRVQVEGPYG RFNFRKGGAR QIWLAGGIGI TPFLAWAESL
     TEAESRDIHL IYCVPTQDEA IGVETLRAAV ARNPRFSFEV FVTARDGRLT AERLISATPF
     AVRQADLWFC GPTGLKDGVL KGLKAQGQTP RRVRFEQFEF A
//