ID A0A1W0A708_9STRA Unreviewed; 907 AA.
AC A0A1W0A708;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Transmembrane protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=THRCLA_02094 {ECO:0000313|EMBL:OQS05820.1};
OS Thraustotheca clavata.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Thraustotheca.
OX NCBI_TaxID=74557 {ECO:0000313|EMBL:OQS05820.1, ECO:0000313|Proteomes:UP000243217};
RN [1] {ECO:0000313|EMBL:OQS05820.1, ECO:0000313|Proteomes:UP000243217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQS05820.1,
RC ECO:0000313|Proteomes:UP000243217};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the autoinducer-2 exporter (AI-2E) (TC 2.A.86)
CC family. {ECO:0000256|ARBA:ARBA00009773}.
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:OQS05820.1}.
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DR EMBL; JNBS01000413; OQS05820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W0A708; -.
DR OrthoDB; 51961at2759; -.
DR Proteomes; UP000243217; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR002549; AI-2E-like.
DR PANTHER; PTHR21716; TRANSMEMBRANE PROTEIN; 1.
DR PANTHER; PTHR21716:SF4; TRANSMEMBRANE PROTEIN 245; 1.
DR Pfam; PF01594; AI-2E_transport; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000243217};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 322..351
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 415..438
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 450..468
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 625..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..783
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..809
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..830
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 907 AA; 102291 MW; DED0C11D2948E01D CRC64;
MLLEYTIGTI IGNISTALVL ALVYFNFLLF EDYFRVIIWS VLFSQALRGA KEKICRILND
LSNAQDVQRN GLLYSICNKF WPYLMQGNDQ KKRIQELILD NGIFIFAMIG AVSIYVRMFS
WLSFLQVVIG ILAILAATLY VLDRRIFHYR YFISDEVLVS ALLLVGCCIV GCFVLLFLGT
ESYMEGNRAA MHITSWIQNN VVNDERTRNL WGEQVQNGKA MIASGLREIE GQYNTTMWFA
PLKALVYSYY DASDDKSTVT AASDVMNVTT VARIIDFPAN LTWTSVFTLA YSKFNLTSTD
VTDWTAKGFE ISSMAFGSVF QILFFVITFT IAFISIGIKA VFFVTSLFYL LCTTWDPIQR
FASDITSNTP DQPKAQALAN PLREAIEGVF FLPLKISSLH AIVTLVSLSM MANDFVYLGT
LITFFISIVP IIPAYLVCIP WVIALWSSTS FFKALLLFVI HYVAFSWIDQ VLYQKSLTAI
NPYVSALSVV FGVYVFGLEG VVFGPLLVWG VQYAYSVGIK GDPYFSDTMK VFSGFNDNIV
RRCSIDITSS NATEVTLIVP CVDSDTREQS IRFVVDKNGT YEDMLGEIRQ LLKVQRVQGL
YDTKNVLILS AKHIKQHEII RVEVEKKRNK TKNSSRKPTG KMSDAMSSTK RRRRASCDCY
TFRTYSLPNP QPPLPRTNSH SLNEPKSRNM HLPPSIQVND PRFQENCKKS FLTSFMGIQK
RLSMSSSPSH SVVRSDQDEE LANASTKSQA SDEAEFEPVT HDDSPAYIDD KDETHKKNNK
SQSDIIDTFH AITDSTEQHD NRSTDSANDN DEYPTEEVIN TERKSESTAD NAHPTRNPDL
NEFINSNESI TEVAPTADLK AVQVGYLVQE EMSRVPTTKE DQKNSSGKED VGRESSQVAL
QPVHILR
//
