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2.A.113.2.1 High affinity Nickel transporter of 556 aas and 8 or 9 TMSs in a 1 + 4 +3 or 4 TMS arrangement. TMS 1 is N-terminal. distant from the others. Then there are 4 TMSs followed by a hydrophilic regiion with one peak of very weak hydrophobicity. This is followed by 3 clear TMSs.
Accession Number:	G0Q1C5
Protein Name:	High-affinity nickel-transporter
Length:	554
Molecular Weight:	57621.00
Species:	Streptomyces griseus XylebKG-1 [649189]
Number of TMSs:	8
Substrate	nickel(2+)

UniProt (Universal Protein Resource)
CDD Search (Conserved Domain Database)

Predict TMSs (Predict number of transmembrane segments)

FASTA formatted sequence

1:	MNNTLRRTLT TLAAGALVAV ANVASAPAAT AHPLGNFSVN YHTGLVLRPD RIDAHVVVDH 
61:	AEISALQERS AIDTDHDGKV SDDESRVHAE KTCSDLSGQL HLSVGGTQAE WRRSSATLVY 
121:	ENGEAGLRTS RLTCSLTSQA DLTERAGIRA ETGYDTRRVG WHEMTATGQG VRITRTDVPA 
181:	TSTTRELRQY PADPLASPLD QRSATLRSEP GQGHAAVPAV VADLPGAGVI GGVLAKVTGA 
241:	FDSLVGAREI TLPVGLLALF LALVLGASHA AMPGHGKTIM AAYLAGRRGT RRDALTVGAT 
301:	VTLTHTAGVL VLGLALPVST HLAGETVLMW LGAASGLLVT GIGLWLLTGA VRGRPQHNHH 
361:	HHGPGHSHSH SHDDHGHGHG HHHDHDHGDD SPHHHGPVSP ASARDSAPAG GLRATPAVAT 
421:	LTPPDHEHHP TNTSTAPREA QRTSRTGLIG MGIAGGLVPS PSALVVLLGA VALGRTAFGV 
481:	LLVIGYGFGM AATLTLAGLL LVRLRERIES HDRARTFRHN PVLRKLARTG PVITSVLVIA 
541:	VGLGLMLRAA AGTG

2.A.113.2.1
High affinity Nickel transporter of 556 aas and 8 or 9 TMSs in a 1 + 4 +3 or 4 TMS arrangement. TMS 1 is N-terminal. distant from the others. Then there are 4 TMSs followed by a hydrophilic regiion with one peak of very weak hydrophobicity. This is followed by 3 clear TMSs.

Cross database links:

External Searches:

Analyze:

2.A.113.2.1High affinity Nickel transporter of 556 aas and 8 or 9 TMSs in a 1 + 4 +3 or 4 TMS arrangement. TMS 1 is N-terminal. distant from the others. Then there are 4 TMSs followed by a hydrophilic regiion with one peak of very weak hydrophobicity. This is followed by 3 clear TMSs.

Cross database links:

External Searches:

Analyze:

2.A.113.2.1
High affinity Nickel transporter of 556 aas and 8 or 9 TMSs in a 1 + 4 +3 or 4 TMS arrangement. TMS 1 is N-terminal. distant from the others. Then there are 4 TMSs followed by a hydrophilic regiion with one peak of very weak hydrophobicity. This is followed by 3 clear TMSs.