ID A0A0K9NWD5_ZOSMR Unreviewed; 680 AA.
AC A0A0K9NWD5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Putative Magnesium and cobalt efflux protein corC {ECO:0000313|EMBL:KMZ61081.1};
GN ORFNames=ZOSMA_54G00100 {ECO:0000313|EMBL:KMZ61081.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ61081.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
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:KMZ61081.1}.
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DR EMBL; LFYR01001529; KMZ61081.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9NWD5; -.
DR STRING; 29655.A0A0K9NWD5; -.
DR OMA; GSDNQDD; -.
DR OrthoDB; 1256at2759; -.
DR Proteomes; UP000036987; 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; 1.
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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU01193}; Reference proteome {ECO:0000313|Proteomes:UP000036987};
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 155..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 271..294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 146..332
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000259|PROSITE:PS51846"
FT DOMAIN 351..412
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 418..476
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 680 AA; 76708 MW; 8322F863BDAE272C CRC64;
MDYAAVIGLS FSSTAFHGRY SLRHTIVSSL RPPNFFNPKR FSKTPLLNPP SLLLLRDRRV
RPVDCLRAVG SVRGGEEEDG MEGKTIPVWF KVGGLVAVLA LAMFVVRCKS VVAADGVVRD
LKERVLGMRW WDPDLFKNMW PKVLLILKLF KEQGLVLFFL LGLSGFFSMS ETAITTLWPW
KVRELAEKEP ENGVFKILRN DVNRFLTTIL IGTTVASIAA TAIFTDAVTA IFGEAGITAA
TAVMTVAVLL LTEITPKSIG IHNATDVAKI VVRPIALLSV ILYPVGKVAT YLSMGIQKML
GLKARSEPYV TENELKLMLR GAELSGAIEE EEQDMIENVL MIKDTVVREV MTPLVDVVAI
DANVKLIDFQ KLWVTKQYSR VPVFEQRVDN IVGIAFAMDM LEYVEQVEKL DEFTVLDIVH
NPTYFVPDSM SVWNLLREFR IRKVHMAVVL NEYGGTIGIV TLEDVVEEIV GEIFDENDSK
EEIHRKTGFV VMLQDGSFLV DANTSMDQLS EELNIELPED HQYETVSGFI CESFGCIPNK
GSKMKVRLEK SIEEENDDDV EFHHQNNKER EKHQIFEIEI LEANARRVES VVFKPINDGD
VSVELTGRDE KRLVSTKVVK RRKKHNSDMD YNPNTIDEFE EPLSIKNSEI GDTLLQETLN
YGVIKDEEQS SDQLPNSNQQ
//
