ID X6NRW1_RETFI Unreviewed; 1460 AA.
AC X6NRW1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETO29020.1};
GN ORFNames=RFI_08106 {ECO:0000313|EMBL:ETO29020.1};
OS Reticulomyxa filosa.
OC Eukaryota; Sar; Rhizaria; Retaria; Foraminifera; Monothalamids;
OC Reticulomyxidae; Reticulomyxa.
OX NCBI_TaxID=46433 {ECO:0000313|EMBL:ETO29020.1, ECO:0000313|Proteomes:UP000023152};
RN [1] {ECO:0000313|EMBL:ETO29020.1, ECO:0000313|Proteomes:UP000023152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24332546;
RA Glockner G., Hulsmann N., Schleicher M., Noegel A.A., Eichinger L.,
RA Gallinger C., Pawlowski J., Sierra R., Euteneuer U., Pillet L.,
RA Moustafa A., Platzer M., Groth M., Szafranski K., Schliwa M.;
RT "The Genome of the Foraminiferan Reticulomyxa filosa.";
RL Curr. Biol. 0:0-0(2013).
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:ETO29020.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ASPP01006306; ETO29020.1; -; Genomic_DNA.
DR EnsemblProtists; ETO29020; ETO29020; RFI_08106.
DR OrthoDB; 5405552at2759; -.
DR Proteomes; UP000023152; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005216; F:monoatomic ion channel activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 1.10.287.70; -; 2.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR46726; TWO PORE CHANNEL 3; 1.
DR PANTHER; PTHR46726:SF1; TWO PORE CHANNEL 3; 1.
DR Pfam; PF00520; Ion_trans; 2.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000023152};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 574..592
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 613..636
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 648..668
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 680..699
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 784..803
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 936..956
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 968..993
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1005..1022
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1028..1047
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1068..1090
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1158..1180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 294..327
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 465..527
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 826..861
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1272..1351
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1208..1239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1407..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1409..1423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1460 AA; 166562 MW; EA434772E90ED415 CRC64;
MRAKPPPPVI PSGSVGAKGK NSRGIAGLME YISRREGVGG DPSVMALLER INDTFNEHVP
DVQKMLDDRS EDIQRKMLRT AVVKRRAGKN DTQPNTNSNQ TTIQPHPHEN INIRRGTVKS
LRERFDHKAQ EKPATFRRTR KNTTTTLSIP DGNIRHRRRV SGGIDIQSLK QGHFSRQGSL
GSDVTSPAMA ALGGPSDIAN SSQLRLQLQH RESSHSRDSS SYEYSQTLIT TTEGEADPLD
QLRKILQKEP NARTDEDVDV MVDYFDNYRI MSEDIDIYSG KSTFRAFIQE TRYRKYQPNK
QIFEQGELGN EFYFILTGKV SVLVNEDVND TDNKDGASNN PDPNQQHEQH NDNQDDDDNE
RLPKDEQNPR LMSPPSATVT IHENDDNPDD DDDANENDPK KLNPKGGHGK GKESGRYVQP
RISAEEFVAR VEEEEKQNQP KQPTFGIWNA TSSSSLPKPP KRKEVAVLTS HDLFGELAVD
GKDSRRAATC ACQTIVEVAY WTRETYDRYI RPLKDNKRKA LQVLFDKNDN MLGEEELTQK
AALFLDDVMQ KRPLKMHRTS KWPQMVHHLT NSTWFTFSMY LTSMLLLGLI LLEPPCFGDY
REGGIYKSRI GPLLAVEWLF FFIFLMECLL RVYSFGSKWF LDTPVHKGRI VALTIFGLDL
LIATSMGGRS FRFSRVFRPM FLNIAVDILI MAVFARAGIH MFKFSKDLYV PYNFTNGLSP
YTDLKGNCDQ IQCFQDKSKC CNVDPTVFQS FDSFARGMAS LYVLMTTENY PDIFWPTWMN
GHFYWTYFLV FLLLVTFFLM NLFSAAMYDA FYHILSNVVW VEEERSESEA LQAAWTCLDR
NLSGKISLNK FKQLMKYLKP NYTDVQNNVL FSLLGAAHKD DEIDEEQFSI NIVSVMYLNI
TKVKPRAQSR KELLKKCPCC SKQLLFDIIR AFESQYYNAL KCLLIVLDCL VLLIYHDAYQ
ACWVIDTVMA FLFAVLTICE IVFVHSLTWR LFWPESLEEG LINKVEFVVG VVHLGSACIG
LYDDKAWITV FRFVALARAS FVAKFLFQNI RGLRSSMSHV LTRTFLRMLP VFFGLVFAFS
VGLMYVFTVV GMELFNDSNK YGKNRCDESG ALNHDPTATF CDAQMTIITL FHIFCSNNWN
VDMFSAVKHF NNNMAVSIYF ILFHFSGPIF MLNMLLAVFF EMYFEISQTL DSDLTAAFVD
EFDNITDKSK PKDERGDTQK QDEDKEGHSD NNAEGDQKHT TIELANNSKG NSTDANVDNN
GDVALKDIAK QLRTHLELRS FVLSDGQIFE KTFTGTQAVD YLVSNKLAPD KEEAVDTLTQ
LISQEMCAQR VDPGAPNEFE NIPNSHYKWI DDVDEESANI HIGLKQSYGG YQHIMKRTHT
IEKMQSEMTK APGGLKRART VGNLLVDNKK TPVPNTTGDK DNNANALDTE KANDSNEETV
HLYKTDQNQG PKKRQFFFVF
//
