(data stored in ACNUC7421 zone)

SWISSPROT: C6WGN1_ACTMD

ID   C6WGN1_ACTMD            Unreviewed;       447 AA.
AC   C6WGN1;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 50.
DE   SubName: Full=Ferric reductase domain protein transmembrane component domain {ECO:0000313|EMBL:ACU34347.1};
GN   OrderedLocusNames=Amir_0380 {ECO:0000313|EMBL:ACU34347.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34347.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34347.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
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DR   EMBL; CP001630; ACU34347.1; -; Genomic_DNA.
DR   RefSeq; WP_012783010.1; NC_013093.1.
DR   ProteinModelPortal; C6WGN1; -.
DR   STRING; 446462.Amir_0380; -.
DR   EnsemblBacteria; ACU34347; ACU34347; Amir_0380.
DR   KEGG; ami:Amir_0380; -.
DR   eggNOG; ENOG4105F2R; Bacteria.
DR   eggNOG; COG4097; LUCA.
DR   HOGENOM; HOG000252445; -.
DR   OMA; AMHRTRP; -.
DR   OrthoDB; POG091H05VQ; -.
DR   Proteomes; UP000002213; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR017927; Fd_Rdtase_FAD-bd.
DR   InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR001221; Phe_hydroxylase.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   Pfam; PF01794; Ferric_reduct; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00410; PHEHYDRXLASE.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
DR   PRODOM; C6WGN1.
DR   SWISS-2DPAGE; C6WGN1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|SAAS:SAAS00124020};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213};
KW   Transmembrane {ECO:0000256|SAM:Phobius, ECO:0000313|EMBL:ACU34347.1};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     21     41       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     53     73       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     85    110       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    130    152       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    164    182       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    194    214       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      219    319       FAD-binding FR-type.
FT                                {ECO:0000259|PROSITE:PS51384}.
SQ   SEQUENCE   447 AA;  47994 MW;  943700B4F760743C CRC64;
     MTTLQAQAPA VRPRAAARTG LHAVLGANAA VVAVLFAQAG FGSNALILLG RLTGLYAALV
     LAFQLLLVAR LPWFDRRLGM DRLTAWHRVT GISVVWLLVA HVVFITTGYA QLASLPPLDE
     LVHLATTVEG VLRAVVAVVL VLVVGGASAR WARRRLAYET WHFIHLYAYL AVVLAFSHQV
     AAGTTFTSSP LATAYWWALW GAALAAVLVG RVGLPLWRNL RHRLRVAAVV PESDDVVSIH
     ITGRDLDKLP ARAGQFFLWR FLERGRWWQA NPFSLSAAPD GRSLRLTAKA LGAGSASLRS
     LKPGTRVFAE GPYGAFTALH RTRPNALLIA GGVGVTPVRA LLEEIGGHAV VVYRVSERRD
     AVLLDELRGL ARAKGAVLHV VTGATADHAP DAQPLGARAL GAAVPDVRER DVFVCGPSRM
     TDAVLASLRE LGVPANQVHA ERFTLAR
//

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