ID A0A0K3CMR9_RHOTO Unreviewed; 867 AA.
AC A0A0K3CMR9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=FGENESH: predicted gene_11.117 protein {ECO:0000313|EMBL:CTR09760.1};
GN Name=FGENESH: predicted gene_11.117 {ECO:0000313|EMBL:CTR09760.1};
GN ORFNames=BN2166_0056210 {ECO:0000313|EMBL:CTR09760.1};
OS Rhodotorula toruloides (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=5286 {ECO:0000313|EMBL:CTR09760.1, ECO:0000313|Proteomes:UP000199069};
RN [1] {ECO:0000313|EMBL:CTR09760.1, ECO:0000313|Proteomes:UP000199069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Single colony {ECO:0000313|EMBL:CTR09760.1};
RA Cajimat M.N.B., Milazzo M.L., Fulhorst C.F.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the NiCoT transporter (TC 2.A.52) family.
CC {ECO:0000256|ARBA:ARBA00010892}.
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DR EMBL; CWKI01000011; CTR09760.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K3CMR9; -.
DR STRING; 5286.A0A0K3CMR9; -.
DR Proteomes; UP000199069; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0015099; F:nickel cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR004688; Ni/Co_transpt.
DR InterPro; IPR011541; Ni/Co_transpt_high_affinity.
DR PANTHER; PTHR31611; HIGH-AFFINITY NICKEL TRANSPORT PROTEIN NIC1; 1.
DR PANTHER; PTHR31611:SF0; HIGH-AFFINITY NICKEL TRANSPORT PROTEIN NIC1; 1.
DR Pfam; PF01585; G-patch; 1.
DR Pfam; PF03824; NicO; 2.
DR SMART; SM00443; G_patch; 1.
DR PROSITE; PS50174; G_PATCH; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nickel {ECO:0000256|ARBA:ARBA00022596};
KW Reference proteome {ECO:0000313|Proteomes:UP000199069};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 436..459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 503..533
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 545..567
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 825..845
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 368..419
FT /note="G-patch"
FT /evidence="ECO:0000259|PROSITE:PS50174"
FT REGION 42..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 867 AA; 92108 MW; 159EF19846E31206 CRC64;
MAYHPPPPPR FIFSFNEADP DVATLPAPQK AALGFRRAGL GQRRTQYDGD DERVPDYGPT
TKRRGRMRFV PAKSSAFGVI PASEDGDEKL ETGYEGKGKG KAVEDVAEQD VQADGAVEEI
AVEPAASTSA GPSVQRRAPI PGSSVRGLYE SIVGLSVHSA PASTNPSPST SKRSTPSPPS
SPRSAAISSP SIPSTSTALY PVSSASSTSS VSSQTLKRSA SPPSSSLAQH ATTETADIVL
SSDSEDEDER PARRIRRDKR VKEEDSDSDD LVVIDPLTNL PEVPFRRSSS LPLPSSSSDT
SQPSTSRGTS SQTSPYGAFS AAAPSVKRLQ PLLIHQLLPP AISSSSDTDG KPAGFKPLVP
PTHYAIRPDS PGWQLLARQG WKEGQTLGPV TPEGEGRGLK VPLRPVEKHD RKGLGLGTGE
DGGGGKNGRK LTHEEILLLA GELVANVALW VAAACTFATN ETHKGVLSLC VVAWTLGLRH
GLDMDHIVAI DNATRSLVAI GQTPVTVGLF FSLGHSTIVI AMTLAIIIAT SAINKLPNVS
SVGGLIGVSI SASFLFLLAV INSVMLWQSL RVVRRRAALE AQQADALAIV PVLPSSGLPP
PALASPFSAD SPTDHKDAQL LADEPSPLPA NQPINEKEGD LDQKAELADE EKGSHAAGEL
QGLPAMTCIA RIGRPLFKLI NRPWKMYPIG VLFGLGFDTA SEMCAPPSPV RVHNSHSTGS
SLLGISALAS SSPHRLPSAQ LILLPLLFTA GMTAVDSLDS VFMLTAYTFP QRVEGPTKEA
EGGRWWDVRR WVLFERRLGE EEEQRRKEEA KERMGMLRRA DQDKLLGISV ALTVISIVVA
LLISITEFMG CAGCFRVQSS ASTDTRL
//
