ID A0A0Q9T9I3_9ACTN Unreviewed; 463 AA.
AC A0A0Q9T9I3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Hemolysin {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASG94_18280 {ECO:0000313|EMBL:KRF32410.1};
OS Nocardioides sp. Soil805.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736416 {ECO:0000313|EMBL:KRF32410.1, ECO:0000313|Proteomes:UP000051356};
RN [1] {ECO:0000313|EMBL:KRF32410.1, ECO:0000313|Proteomes:UP000051356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil805 {ECO:0000313|EMBL:KRF32410.1,
RC ECO:0000313|Proteomes:UP000051356};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF32410.1, ECO:0000313|Proteomes:UP000051356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil805 {ECO:0000313|EMBL:KRF32410.1,
RC ECO:0000313|Proteomes:UP000051356};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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:KRF32410.1}.
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DR EMBL; LMSU01000004; KRF32410.1; -; Genomic_DNA.
DR RefSeq; WP_056927910.1; NZ_LMSU01000004.1.
DR AlphaFoldDB; A0A0Q9T9I3; -.
DR STRING; 1736416.ASG94_18280; -.
DR OrthoDB; 110231at2; -.
DR Proteomes; UP000051356; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma 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; PTHR43099:SF6; UPF0053 PROTEIN RV1842C; 1.
DR PANTHER; PTHR43099; UPF0053 PROTEIN YRKA; 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 4: Predicted;
KW CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW ProRule:PRU00703}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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 DOMAIN 1..202
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000259|PROSITE:PS51846"
FT DOMAIN 221..279
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 285..342
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 400..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 463 AA; 49825 MW; 96F7169937E0E637 CRC64;
MTPWLLLLVS FALIAVCGVF VAAEFSFVTV DRSTVERAAS GGDASAAGVQ RALKSLSTQL
SGAQVGITVT NLAVGFLAEP AIATLVRDPL TAAGLPDGWV PPISVAIGLT LGTILTMLFG
EMVPKNLALA KPLETARATQ GFMRGFTAAS RWPIKVLNNS ANTLVRRLGI EPQEELRSAR
SSEELASLVQ RSADQGTLDA ETAELMERSV EFGTRTAGEI MTPRVRTTTV EEGDRASTVI
ELARQTGLSR FPVLDQEDAV VGTVHVKHAV ALPVHERATT RIKHIMVKPT VVPDSLRLDP
LLALLRGDGF QMAIVLDEYG GHAGIVTLED VVEEIVGDIS DEHDRLGARA RQRRDGAWSL
SGLLRPDEVE DATGIELPDH EDYDTIGGLV MQRLGKIPHA GDRVEVPVPD RSDPDEPRED
LATLTVERMD GLRIDRLELR LVTLDELSVE PTDPASGEGD DRG
//