ID A0A1V3R5T2_9FLAO Unreviewed; 419 AA.
AC A0A1V3R5T2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Hemolysin {ECO:0000313|EMBL:OOG71803.1};
GN ORFNames=B0E44_09230 {ECO:0000313|EMBL:OOG71803.1};
OS Flavobacterium sp. A45.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1945862 {ECO:0000313|EMBL:OOG71803.1, ECO:0000313|Proteomes:UP000188437};
RN [1] {ECO:0000313|EMBL:OOG71803.1, ECO:0000313|Proteomes:UP000188437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A45 {ECO:0000313|EMBL:OOG71803.1,
RC ECO:0000313|Proteomes:UP000188437};
RA Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA Frostegard A.;
RT "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT isolation strategy.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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:OOG71803.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MUNX01000080; OOG71803.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3R5T2; -.
DR STRING; 1945862.B0E44_09230; -.
DR OrthoDB; 9798188at2; -.
DR Proteomes; UP000188437; 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:SF33; UPF0053 PROTEIN YEGH; 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; 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:UP000188437};
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 55..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..191
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000259|PROSITE:PS51846"
FT DOMAIN 273..330
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 419 AA; 47891 MW; 8E65235190F90311 CRC64;
MEIGIIILCL ILCAFFSGME TAFVSSNKIY LELEKKQDGF LSKILTKLIE KPSKFIAAML
IGYNVAFVVY GFFMGKMLMS RLLLFDLHFS GFTGLLIQTV ISASVVVMTA EFLPKVFFQI
YANSLIKFLA IPAFFFYKLF YFISTFLIWI SDFVLKRFFK TEGDQVQLYF SKVELGNYIN
EQMSTVEDHE EVDSEIQMFR NALDFSGVKA RDVMTPRTEI AAVDIKESLE NLKELFIDTG
YSKMVIYQNS LDDIIGYVHS FDLFKKPSSI KEIVIPVEFI PEAIYVKDAM SLLTKKRKSM
AVVLDEYGGT SGILTIEDIV EELFGEIEDE HDLEEELVEK ELEDGAFLFS ARLDVEYLNH
TYKLAIPESD SYGTLGGFIV NFTKGIPQKG DEITIENYHF VIDEATNKKI ELVKMTIKD
//