ID D2Z5E5_9BACT Unreviewed; 417 AA.
AC D2Z5E5;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=CBS domain containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=Dpep_0664 {ECO:0000313|EMBL:EFC90692.1};
OS Dethiosulfovibrio peptidovorans DSM 11002.
OC Bacteria; Synergistota; Synergistia; Synergistales;
OC Dethiosulfovibrionaceae; Dethiosulfovibrio.
OX NCBI_TaxID=469381 {ECO:0000313|EMBL:EFC90692.1, ECO:0000313|Proteomes:UP000006427};
RN [1] {ECO:0000313|EMBL:EFC90692.1, ECO:0000313|Proteomes:UP000006427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11002 {ECO:0000313|EMBL:EFC90692.1,
RC ECO:0000313|Proteomes:UP000006427};
RX PubMed=21304695;
RA Labutti K., Mayilraj S., Clum A., Lucas S., Glavina Del Rio T., Nolan M.,
RA Tice H., Cheng J.F., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Goodwin L., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Spring S., Goker M.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Permanent draft genome sequence of Dethiosulfovibrio peptidovorans type
RT strain (SEBR 4207).";
RL Stand. Genomic Sci. 3:85-92(2010).
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:EFC90692.1}.
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DR EMBL; ABTR02000001; EFC90692.1; -; Genomic_DNA.
DR RefSeq; WP_005659593.1; NZ_ABTR02000001.1.
DR AlphaFoldDB; D2Z5E5; -.
DR STRING; 469381.Dpep_0664; -.
DR PaxDb; 469381-Dpep_0664; -.
DR eggNOG; COG1253; Bacteria.
DR OrthoDB; 9798188at2; -.
DR Proteomes; UP000006427; 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; 1.
DR Pfam; PF01595; CNNM; 1.
DR Pfam; PF03471; CorC_HlyC; 1.
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; 1.
DR PROSITE; PS51846; CNNM; 1.
PE 4: Predicted;
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:UP000006427};
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 6..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 94..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..188
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000259|PROSITE:PS51846"
FT DOMAIN 271..328
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 417 AA; 45846 MW; 6BFE1B00070AE111 CRC64;
MATGTLFSAL ITFVLLFALS AFFSASETAF SSVNKIRLRR FVEEERPGAS SAMELAKDFN
RTVSAILIGG NIVDILITSA ATAVLTSMFG PMGAVYATVL MTILIILFGE ILPKALVKDR
AEPFALASAP MVKFFVSVLN PVCTLTSRIT SALRHGRTGG TLIPTVTHDE LLSIVDTMGG
EGTLPLSERE LVENAVNFNG LEVWEVQTPR VDLFAIEVDD DPSVVTGLIV ANHYSRIPIY
QSSIDNIVGI LYEKDYLAAV TSGKKPVIRD MMKRPILIAG SASLMDSLKI LRSSHTHMAV
VLDEYGGTSG IVTLEDLLEE LVGELYDEHD DIKENVTKIE ENVYMANGDI YIKRLFEAFL
DVPYEPETDA TTLSGWLLEQ FKTLPETGAE VKWENFSFQV SKLSGQRIHK VRITRQP
//
