ID A0A1W0AAG0_9STRA Unreviewed; 1431 AA.
AC A0A1W0AAG0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=THRCLA_00681 {ECO:0000313|EMBL:OQS07307.1};
OS Thraustotheca clavata.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Thraustotheca.
OX NCBI_TaxID=74557 {ECO:0000313|EMBL:OQS07307.1, ECO:0000313|Proteomes:UP000243217};
RN [1] {ECO:0000313|EMBL:OQS07307.1, ECO:0000313|Proteomes:UP000243217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQS07307.1,
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 -!- 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:OQS07307.1}.
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; JNBS01000252; OQS07307.1; -; Genomic_DNA.
DR STRING; 74557.A0A1W0AAG0; -.
DR OrthoDB; 52466at2759; -.
DR Proteomes; UP000243217; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16454; RING-H2_PA-TM-RING; 1.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46093; ACYL-COA-BINDING DOMAIN-CONTAINING PROTEIN 5; 1.
DR PANTHER; PTHR46093:SF17; MULTIPLE EGF-LIKE-DOMAINS 8; 1.
DR Pfam; PF13415; Kelch_3; 1.
DR Pfam; PF13854; Kelch_5; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF117281; Kelch motif; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000243217};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT TRANSMEM 1315..1337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1384..1425
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 1431 AA; 163423 MW; 939B91AE3FBD9715 CRC64;
MKTQLPSLSG TCDPLELTVR QMLYDVEVLL QNGIGENDAM KMYLDARKSL AKLKWNVVMA
ERLAYSVDEN GITRKNLLLQ ILPVSSEILE DKFHAIGMLL MEKTWKKIMT AENAKEVWDI
SVLVNYIKCL PTNEAWNLYV EKRKSNLKEI ADSSISLAQF SETAALFLRA DLNIICTECE
GTLISSFVWN EPIKDVAQRL SFLFDQAYGP ALKYILVRVV SQLTTDVNAW MHQNPTTSTN
ARPQVNFGDQ RFLMNKERSR EYRYAYKPHQ VTTPQNQTAI VSSMARLNVR LNSISASRSS
LSLHNNKEKG PKLMVLVADP TTYGIWRLIQ IERSSFGEGL TPPSLHRCLY VFFDELQSVS
AFCKRKNKYE FCVGWNVLAC IKGSSGHYWA NASIDCVKSE DSTCIVKIMS TSKLHDIPLS
IEQHIRIAPY DSRCRIHSGQ RWINLIEDLN CTINNMTHQL SPSIDILSLQ NCLWHTVSPA
LQPADYIFSR YLRTVLHFAR TTTKAIIPTA STLGHFELSG LYSITRIISN TPTEKPQFDD
YTLRAQAETF AVILRDVADS LQVWVVSGGY MEILRLYAQV FHEEIMMFAS TLTTHLTENN
LTVDIMIEGS VGLTLLLNAW RTTRRQLQTN GDGTAMHWTI ETLDKIERTL ESMIAMTLHY
IFTRITQETT SIYLPNIVEH AWQSTKPYFS DSRVTSGAQA AGFRLNRVVL RLITSSTMTS
EQPFAQTYLI DLCGSLCLHT TNALAELYTS ITPSRGRLDQ YRLDSLYIIM DIYSSLKATF
ELGASTGNLW MKQCSVILFD WLTRLAILFA PVNLVASHIS RTSSVKKSIP GAMGAFAALD
LQMKDIASTL GENSARGSMR YPWHLHCVVP FESIPNLCKL ELQWRVILEH SSLSRQETIH
WVHRRREFLS DEFPLLTAAE LETKKVLQAN VLSYGSLISQ LGFCSGLNPW TSVWQYDYGQ
YAPGPRAAHT LVMSNTDEMI VYGGIGDDEE SVYDDVWKFN LTAQLWKKLY PQNAQQPRKR
FHHTATMRES HSEMYIFGGM SVSRSSNTSA LRYSQNNDLW RLQLGIEPPQ WIREPCMNQD
QPSNRSEATA VTYQDQMYLF GGIHYDSTNG NGQSQDFNDI WTFDYQTKKW TQLVLGAQTL
PPARFSHTAN KITIDGSDYM VLFGGRCLTK DDGWALLGDT WLFSFRTSTW KQVQIEPAFK
RAYTSMVTVN NTMWLFGGYF KSDYSTNGYV YDDTILATLS NATLTQYYKN NESEDGKELP
SVRYLHRAVE YQGKMVIYGG RFQRALGDIW VQELNTSLFH PVTDVHELER SDMNALYIVC
VLFAVFTMLF VFTLVRFRIQ YIYPDTRTQP LPVRRGLTNE RLLELKTRKY QATSESTLTS
PDMCPICLAD YSGEDDIREL PCKHIFHVQC IDEWLKKNKT CPMCKLDIEA V
//
