ID A0A061QKA7_9PROT Unreviewed; 425 AA.
AC A0A061QKA7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:GAK34658.1};
GN ORFNames=AQ1_02560 {ECO:0000313|EMBL:GAK34658.1};
OS alpha proteobacterium Q-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1492281 {ECO:0000313|EMBL:GAK34658.1, ECO:0000313|Proteomes:UP000027360};
RN [1] {ECO:0000313|EMBL:GAK34658.1, ECO:0000313|Proteomes:UP000027360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Q-1 {ECO:0000313|EMBL:GAK34658.1,
RC ECO:0000313|Proteomes:UP000027360};
RX PubMed=22447601; DOI=10.1128/AEM.00084-12;
RA Suzuki M., Eda Y., Ohsawa S., Kanesaki Y., Yoshikawa H., Tanaka K.,
RA Muramatsu Y., Yoshikawa J., Sato I., Fujii T., Amachi S.;
RT "Iodide oxidation by a novel multicopper oxidase from the
RT alphaproteobacterium strain Q-1.";
RL Appl. Environ. Microbiol. 78:3941-3949(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the UPF0053 family. Hemolysin C subfamily.
CC {ECO:0000256|ARBA:ARBA00006446}.
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:GAK34658.1}.
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DR EMBL; BAYV01000104; GAK34658.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061QKA7; -.
DR STRING; 1492281.AQ1_02560; -.
DR OrthoDB; 9797674at2; -.
DR Proteomes; UP000027360; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR CDD; cd04590; CBS_pair_CorC_HlyC_assoc; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR002550; CNNM.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR044751; Ion_transp-like_CBS.
DR InterPro; IPR005170; Transptr-assoc_dom.
DR PANTHER; PTHR22777; HEMOLYSIN-RELATED; 1.
DR PANTHER; PTHR22777:SF17; UPF0053 INNER MEMBRANE PROTEIN YFJD; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01595; CNNM; 1.
DR Pfam; PF03471; CorC_HlyC; 1.
DR SMART; SM00116; CBS; 2.
DR SMART; SM01091; CorC_HlyC; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS51846; CNNM; 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW ProRule:PRU00703};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU01193}; Reference proteome {ECO:0000313|Proteomes:UP000027360};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU01193};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|PROSITE-
KW ProRule:PRU01193}.
FT TRANSMEM 61..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 92..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..190
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000259|PROSITE:PS51846"
FT DOMAIN 209..271
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 276..333
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 425 AA; 46656 MW; 73DC03A0855DFC34 CRC64;
MLMAHLPALI GIFILLCLSA FFSGSETALT AASRARIHRL ARDGDHRAQR VEKLIEDKER
LIGAILLGNN LVNILASALA TYVFIAMVGE GGVVYATLVM TALVLIFAEV LPKSYAISNP
DGMALAVGSV IAILVLLFSP VVNLVRQIVR GTLSVFGVDL ESGEAILSAR DEIRGAIDLG
ASEGGIRKAH RDMLDSILDL DEISIEDVMI HRKNMALIDG AMPPAEIVDE VIKSPYTRLP
VYEEDAENII GVLHAKDVLR ALKAVGDPAA INICEIMTDA WFVPETTSLR EQLNRFLSRR
AHFALVVDEY GSIQGLVTLE DILEEIVGDI SDEFDHMIHG VKKLADGWVQ VDGTMTLRDL
NRRFDWSLPD ADASTLAGLV IFESEIIPIV GQRFNFHGFE FEIIGRRRNQ ITQIKIRPKP
SETTA
//
