ID A0A1J5FSR0_9BACT Unreviewed; 411 AA.
AC A0A1J5FSR0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Hemolysin {ECO:0000313|EMBL:OIP60530.1};
GN ORFNames=AUK34_06350 {ECO:0000313|EMBL:OIP60530.1};
OS Ignavibacteria bacterium CG2_30_36_16.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1805221 {ECO:0000313|EMBL:OIP60530.1, ECO:0000313|Proteomes:UP000183261};
RN [1] {ECO:0000313|EMBL:OIP60530.1, ECO:0000313|Proteomes:UP000183261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_36_16 {ECO:0000313|EMBL:OIP60530.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
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:OIP60530.1}.
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DR EMBL; MNYQ01000100; OIP60530.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5FSR0; -.
DR STRING; 1805221.AUK34_06350; -.
DR Proteomes; UP000183261; 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 PROTEIN SLL0260; 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; 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}; 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..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 56..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..183
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000259|PROSITE:PS51846"
FT DOMAIN 261..318
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 411 AA; 46005 MW; 6901CFD2EBA25A3C CRC64;
MNDFFVLILL LLISGFLSGS ELAFVVANKL KIELRARKKS LPAMNAYFFS KNPQNLFPTI
LIANNIVNIA FASISTLFLT RTFGLGNVSI LIISTAVLLL FGELIPKYFS REAADSAVLA
SSIPLRIIYF ILYPFVKITS SLSGFLTKFS NVTGENINSL FGKEDIETLV KEGHEAGVVH
KNERDIISRV FELSEQRVYE AMRPRTDIVG VEINRSIDET LSIFIESSFS KLPVYDDSLD
NIKGVVYAYD VFKSPKSLSE ITREVIFVPE TKRSFEMLNE FLSKQVSIAI VIDEFGGTAG
IVTMEDIIEE LFGEIEDEYD VPEDLCRKIT PNTYIISGKV EIDYLNEKYS LNLPTGDFET
LGGYLISKLG RIPSQGEIIK IDDSEYLIAR ATPTKIDVVK VTLNLEIPES N
//