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1.A.35.3.1
Divalent metal ion (Mg2+, Ca2+, Ni2+, etc.) transporter of 317 aas and 3 TMSs.  The cryo-EM structure shows a pentameric channel with an asymmetric domain structure and featuring differential separations between the trans-segments, probably reflecting mechanical coupling of the cytoplasmic domain to the transmembrane domain and suggesting a gating mechanism (Cleverley et al. 2015).

Accession Number:Q58439
Protein Name:CorA aka MJ1033
Length:317
Molecular Weight:37142.00
Species:Methanococcus jannaschii [2190]
Number of TMSs:3
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate Mg2+, Ca2+, Ni2+

Cross database links:

HEGENOM: HBG541091
RefSeq: NP_248027.1   
Entrez Gene ID: 1451930   
Pfam: PF01544   
KEGG: mja:MJ1033   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005886 C:plasma membrane
GO:0015087 F:cobalt ion transmembrane transporter activity
GO:0015095 F:magnesium ion transmembrane transporter act...
GO:0006824 P:cobalt ion transport
GO:0015693 P:magnesium ion transport
GO:0055085 P:transmembrane transport

References (4)

[1] “Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.”  Bult C.J.et.al.   8688087
[2] “Functional similarity between archaeal and bacterial CorA magnesium transporters.”  Smith R.L.et.al.   9573171
[3] “Cation hexaammines are selective and potent inhibitors of the CorA magnesium transport system.”  Kucharski L.M.et.al.   10748031
[4] “The CorA Mg2+ transporter is a homotetramer.”  Warren M.A.et.al.   15231793
Structure:
4CY4   4EGW   4EV6     

External Searches:

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  • 2° Structure (Network Protein Sequence Analysis)

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MITVIAIAKD GSIVEPKLDE ISFEDYRLIW IDCYDPKDEE LYKLSKKIGI SVSDLQIGLD 
61:	EQEIPRVEED EDFYLIIYKA PLFEEDITTT SLGIYIKNNL LLTIHSDKIK AIGRLHKLIS 
121:	TKKPRIVFER GIGFLLYHIL NEITRSYSRI LMNLEDELEE LEDKLLAGYD REVMEKILGL 
181:	RKTLVYFHKS LIANRDVLVL LKRKYLPITT KEDRENFEDL YYDTLQLIDM SATYREVLTS 
241:	MMDITLSLEN IKMNQIMKIL TMVTTIFAVP MWITGIYGMN FSYLPLANNP QGFWLVMALM 
301:	VVIIMIFVYI FRRSGWI