ID A0A1G8SYB2_9ACTN Unreviewed; 431 AA.
AC A0A1G8SYB2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Hemolysin, contains CBS domains {ECO:0000313|EMBL:SDJ34218.1};
GN ORFNames=SAMN05421874_101498 {ECO:0000313|EMBL:SDJ34218.1};
OS Nonomuraea maritima.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=683260 {ECO:0000313|EMBL:SDJ34218.1, ECO:0000313|Proteomes:UP000198683};
RN [1] {ECO:0000313|EMBL:SDJ34218.1, ECO:0000313|Proteomes:UP000198683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5681 {ECO:0000313|EMBL:SDJ34218.1,
RC ECO:0000313|Proteomes:UP000198683};
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}.
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DR EMBL; FNFB01000001; SDJ34218.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8SYB2; -.
DR STRING; 683260.SAMN05421874_101498; -.
DR OrthoDB; 110231at2; -.
DR Proteomes; UP000198683; 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 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:UP000198683};
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 57..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 88..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..184
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000259|PROSITE:PS51846"
FT DOMAIN 203..263
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 271..328
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 431 AA; 46728 MW; B11EFAACDF644B24 CRC64;
MNAWLLLAIA LVIVGGLIAS AETALTRISR VRAEEFVREA RRGAERLQAI VTDPPRYLNL
LLLLRLSCEL VATVIATLLF IDLMDDQGWA YVCAAAVMIV TSYVVVGVMP RTLGRQHAEP
VALASAPAVY GLTRIFGPLP KLLILLGNAL TPGKGFRDGP FTSEAELRDL VDLAEERRVI
EPDEREMIHS VFELGDTLVR EVMVPRTDMV YIERGKTLNQ ALSLALRSGF SRIPVVGENE
DDVVGMAYLK DVARKIHEGG NGGGGETVES IMRPAAYVPE SKPIDQLMRE MQARQTHIAI
VIDEYGGTAG LVTIEDVLEE IVGEITDEYD QEAPRVEPMP DGGLRVTARM PVDELGELFD
TEIEVDDVET VGGLLAHALG RVPIAGSHAE VAGLSLTAES LAGRRNRIST VVVRRAETPS
GDVVPAAAER D
//