ID A0A1I0VQY3_9FIRM Unreviewed; 402 AA.
AC A0A1I0VQY3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Hemolysin, contains CBS domains {ECO:0000313|EMBL:SFA78751.1};
GN ORFNames=SAMN05216249_102147 {ECO:0000313|EMBL:SFA78751.1};
OS Acetitomaculum ruminis DSM 5522.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Acetitomaculum.
OX NCBI_TaxID=1120918 {ECO:0000313|EMBL:SFA78751.1, ECO:0000313|Proteomes:UP000198838};
RN [1] {ECO:0000313|EMBL:SFA78751.1, ECO:0000313|Proteomes:UP000198838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5522 {ECO:0000313|EMBL:SFA78751.1,
RC ECO:0000313|Proteomes:UP000198838};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the UPF0053 family.
CC {ECO:0000256|ARBA:ARBA00006337}.
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DR EMBL; FOJY01000002; SFA78751.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0VQY3; -.
DR STRING; 1120918.SAMN05216249_102147; -.
DR Proteomes; UP000198838; 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; 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:UP000198838};
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 69..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..175
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000259|PROSITE:PS51846"
FT DOMAIN 194..254
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 257..314
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 402 AA; 45580 MW; BE10EE1F43299198 CRC64;
MILLSAFFSS AETALTTVNM VRIRLLVDEG NKKAAIVAKI KDNSSHMLST ILIFNNIVNL
SASALTTTVA LELFGSQGVG IATGILTFII VEFSEITPKT IASINAEKMS LFYAPIIYML
MKIMVPVIFV IEMLSKFTMA VFGIKSDENQ GKITESELRT IVGVSNEEGI IENSEYDMIT
NVFDFGDSKA KDVMVPRINL TFVNIDSSYD ELIEIYRKNM FTRYPVYKES TDNVIGFINV
KDLILYGDFA DFKVKDILRE PFYTYELKNT AELFMEMKNS SNSAAIVLDE FGITAGMVTL
EDLLEEIVGE IKDEYDEYEE EEIHKISPKE YIVKGTTKID DFNEETEISI FSKAYDSMAG
YLLEQMEHLP VEGENFRNSE GILFIIRKMD NKRIDKIYIK LP
//
