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Database: UniProt
Entry: K9ZL69_ANACC
LinkDB: K9ZL69_ANACC
Original site: K9ZL69_ANACC 
ID   K9ZL69_ANACC            Unreviewed;       436 AA.
AC   K9ZL69;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Signal transduction protein with CBS domains {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=Anacy_4589 {ECO:0000313|EMBL:AFZ59941.1};
OS   Anabaena cylindrica (strain ATCC 27899 / PCC 7122).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=272123 {ECO:0000313|EMBL:AFZ59941.1, ECO:0000313|Proteomes:UP000010474};
RN   [1] {ECO:0000313|Proteomes:UP000010474}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27899 / PCC 7122 {ECO:0000313|Proteomes:UP000010474};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA   Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA   Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA   Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT   genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP003659; AFZ59941.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9ZL69; -.
DR   STRING; 272123.Anacy_4589; -.
DR   KEGG; acy:Anacy_4589; -.
DR   PATRIC; fig|272123.3.peg.4997; -.
DR   eggNOG; COG1253; Bacteria.
DR   HOGENOM; CLU_015237_4_0_3; -.
DR   OrthoDB; 9798188at2; -.
DR   Proteomes; UP000010474; Chromosome.
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; 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:UP000010474};
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        6..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        60..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..201
FT                   /note="CNNM transmembrane"
FT                   /evidence="ECO:0000259|PROSITE:PS51846"
FT   DOMAIN          220..281
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          284..340
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
SQ   SEQUENCE   436 AA;  47948 MW;  ECB01F0DD1DFE2E2 CRC64;
     MSSLSFEILT ILVLIFANGV FSMSEMAIVS ARKVRLQQLA NQGNLNAQAA LELAESPNHF
     LSIVQVGITL INILNGVFGG ATIAQRLEKY VQLVPFLADY SQPIAFGIVV LLITYLSLIV
     GELVPKRLAL NNPEGVASSV AIPMRALAAL ASPVVYLLSA STDAVLRLLG ITPSTEPQVT
     EEEIKILIEQ GTEAGTFEEA EQDMVERVFR LGDRPVTYLM TPRPDIVWLD LDDSLEENRH
     KMVESAYSRY PVCQEGLDNV LGIIPVTDLL ARSLRSEPLD LTLGLRQPVF VPESTRGLKV
     LELFKQTVTH MALVVDEYGV IQGLVTLNDI MSEIVGDVPA GPGQEEPQAV QREDGSWLVD
     GMLGIEEFLE LFGLEELGTE ERGNYQTLGG FVITHLGRIP AAADHFEWDS MRFEVMDMDG
     NRVDKVLVVP KINHNK
//
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