ID A0A2R5G5T9_9STRA Unreviewed; 1395 AA.
AC A0A2R5G5T9;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 28-JUN-2023, entry version 19.
DE SubName: Full=Lateral signaling target protein 2-like {ECO:0000313|EMBL:GBG26407.1};
GN ORFNames=FCC1311_026282 {ECO:0000313|EMBL:GBG26407.1};
OS Hondaea fermentalgiana.
OC Eukaryota; Sar; Stramenopiles; Bigyra; Labyrinthulomycetes;
OC Thraustochytrida; Thraustochytriaceae; Hondaea.
OX NCBI_TaxID=2315210 {ECO:0000313|EMBL:GBG26407.1, ECO:0000313|Proteomes:UP000241890};
RN [1] {ECO:0000313|EMBL:GBG26407.1, ECO:0000313|Proteomes:UP000241890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sedici K., Godart F., Aiese Cigliano R., Sanseverino W., Barakat M.,
RA Ortet P., Marechal E., Cagnac O., Amato A.;
RT "Sequencing, de novo assembly and annotation of complete genome of a new
RT Thraustochytrid species, strain FCC1311.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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:GBG26407.1}.
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DR EMBL; BEYU01000020; GBG26407.1; -; Genomic_DNA.
DR EnsemblProtists; GBG26407; GBG26407; FCC1311_026282.
DR InParanoid; A0A2R5G5T9; -.
DR Proteomes; UP000241890; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd05121; ABC1_ADCK3-like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 3.30.1050.10; SCP2 sterol-binding domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR004147; ABC1_dom.
DR InterPro; IPR001466; Beta-lactam-related.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003033; SCP2_sterol-bd_dom.
DR InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR43173; ABC1 FAMILY PROTEIN; 1.
DR PANTHER; PTHR43173:SF3; ABC1 FAMILY PROTEIN; 1.
DR Pfam; PF03109; ABC1; 1.
DR Pfam; PF00144; Beta-lactamase; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF02036; SCP2; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55718; SCP-like; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000241890};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 363..382
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 389..411
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 149..201
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 208..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1395 AA; 152783 MW; 950E2AA7C8A7BDD3 CRC64;
MAAATMDQRR AQLASFFAHL DEELAGSSGL PETVVDLVVT GAHGGSWRVE TKNGRGSARL
LTQAEAAGAP KPACRVETDL RTLDKLANGE MRPAMALLRG KVSYSGSYGV LRELQGPFRR
AAEKVMAELG PDSVPIATFV LDKNNPAWES DAERCKLCLA RFTFWTRQHH CRRCGAAVCG
NCSSHQIKGY RACSACWQQQ LELQRQQRKD GQASQLATET PSQFRATTPA SQRDDEVAAN
ILPYQRLIEH IRGLQARSIA AAVETSSMAI RPLLLRIRKL EGAVELHAKA SLPALATRLA
TFLLPKLLLT GALALAWAYP NNLFSLGFMA YCWNRPLLLG LSWLPFRPEP LQVLSTLFST
RPIAATIVLT GVTVLNCVRF FFGRLLRIYS TAFVVIFSYY TTYLVAVRAM GMGTTASTRI
FQSLDLIMAP FACNEILALR SVFVKFGQYI GSRADIIPPR WATVLAKLQD DLPADRFKYV
ERCIEQEFGH KIEKLFESFE PEPMASASIA QVHRAVLRPN VIPTISTPLE VAVKVQHEGI
EAIMLSDVVA FRRIIRLIAW LNPRFAIAKT LLRAWETEMV KELDFNVESS NLATVRRNLR
QVGLIADADD DYLDAACRGS HVLVPRPVRG LVGRRAFCMT FIQGFKITDL EQLALFGVDR
AALVRRVVQS YGCMIFVDGF TSADPHPGNL MVSVSDDGMA RPVLLDFGMV VTLEDPTRVG
YCRLVNSIAN ISVSGLAEAI ASIGYKNSQS DVHPERDLEF FAHLLRDTGD RKSQRQSQAQ
FRKRRKAQRA ADLERDPAKE GRYFSGFPDS LIFLFRVLGL IRGLCTTLDA PISYVDILGD
YAKLGLMHYK MQEAADAATQ RSSPQALPPA VQTPRSPQFL QGKVAQLLSR AQSDASHELA
LPESHGFAAD TFLGAQVCVM MGEKVVVDTF AGVQDELSPV RVSSSTVFPL MDLTRVVLVV
DILDLIDKGT LDPKDPICKH WSDFADKSVT IEDLLSYASN IRDIVPATTS VNSLRDYSSL
KAKLQDTSAM RSRRDVDRSK AHYTIFTSGY IMAGLLEAVK ENSIDAIYAQ RVAQSSFEEV
HLCASSMASS GRCAELSNGF AGFVRSMAMG GGTAAAASFS AERPERKAES GRKDLPSEAS
SLTRTQKTTW SAKNAASRPE EVNVERSSSQ EGAFKGFTTR KTEIQMGKET DGEKNNAALN
LPAASLDSGS EHDDDDAEQK EDVNVDAEID ADDEEDTESP LPPGVKLPNG ALLDPCCVNA
SALRESSVPS FGAFGTARGL ASVAASFFHK PASGKLVNRL SHGPLRTETS PLYGEMAWSL
GLQVFIMPDT GIRMLVHHAF GGSMLVLVPE LKVCVSVLVN CLTLDRTVTR DILVLVCKEL
NITVGGVDQL FGGMF
//
