ID A9SK04_PHYPA Unreviewed; 700 AA.
AC A9SK04;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 110.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=PHYPA_000605 {ECO:0000313|EMBL:PNR62181.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR62181.1};
RN [1] {ECO:0000313|EMBL:PNR62181.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c1_13190V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [2] {ECO:0000313|EMBL:PNR62181.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c1_13190V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=29237241; DOI=10.1111/tpj.13801;
RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA Schmutz J., Rensing S.A.;
RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT structure and evolution.";
RL Plant J. 93:515-533(2018).
RN [3] {ECO:0000313|EnsemblPlants:Pp3c1_13190V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; ABEU02000001; PNR62181.1; -; Genomic_DNA.
DR RefSeq; XP_001766701.1; XM_001766649.1.
DR AlphaFoldDB; A9SK04; -.
DR STRING; 3218.A9SK04; -.
DR PaxDb; 3218-PP1S86_153V6-1; -.
DR EnsemblPlants; Pp3c1_13190V3.1; Pp3c1_13190V3.1; Pp3c1_13190.
DR EnsemblPlants; Pp3c1_13190V3.2; Pp3c1_13190V3.2; Pp3c1_13190.
DR EnsemblPlants; Pp3c1_13190V3.3; Pp3c1_13190V3.3; Pp3c1_13190.
DR EnsemblPlants; Pp3c1_13190V3.4; Pp3c1_13190V3.4; Pp3c1_13190.
DR Gramene; Pp3c1_13190V3.1; Pp3c1_13190V3.1; Pp3c1_13190.
DR Gramene; Pp3c1_13190V3.2; Pp3c1_13190V3.2; Pp3c1_13190.
DR Gramene; Pp3c1_13190V3.3; Pp3c1_13190V3.3; Pp3c1_13190.
DR Gramene; Pp3c1_13190V3.4; Pp3c1_13190V3.4; Pp3c1_13190.
DR eggNOG; KOG0297; Eukaryota.
DR HOGENOM; CLU_006994_2_1_1; -.
DR InParanoid; A9SK04; -.
DR OMA; XSIIDST; -.
DR OrthoDB; 21736at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000006727; Chromosome 1.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16504; RING-HC_COP1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR042755; COP1.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR44080; E3 UBIQUITIN-PROTEIN LIGASE COP1; 1.
DR PANTHER; PTHR44080:SF1; E3 UBIQUITIN-PROTEIN LIGASE COP1; 1.
DR Pfam; PF00400; WD40; 2.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00504; Ubox; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006727};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 53..90
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REPEAT 485..527
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 571..611
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 221..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 139..203
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 228..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 700 AA; 77924 MW; 70CE05309CE6EB28 CRC64;
MEGGTCTQGS IGPHVPSVAA VKQEPRTGSW SSQDNKCELA MASKPALDKD FLCPICIQTM
KDAFLTACGH SFCYTCIMTH LSNKSNCPCC GQYLTNNQLF PNFLLNKLLR KASASQLVSN
ASPAEHLRLA LQQGVDLPVK ELDSLMHLLS DKKRKAEQEE AEANMEILLE FLHRSRQQKN
EELNLLQGDL QFLKEDISTV EKQRQDLLHI TEKNALKIRM IAGGPSSSRP DTLATNENTS
KGEATSQSRG GQFGASVPSN LPPASLKRDY RGRVTSIGTY KEMIGGDVSL SKSQSELKAL
TPSPAVLTMA KKRRVVAQIE VLQEAYLQRR RKVAQVHRQE QKVHETIVRK DEEVNSARAD
LYSSGLDDFQ SVLTAFTRYS RLSVIAELRH GDLFHSSNIV SSIEFGRDDE LFATAGVSRR
IKIFEFATVV NEFAGVHCPV VEMSTRSKLS CLSWNKYIKS HIASSDYEGI ITVWDVNRRQ
SITEYEEHEK RAWSVDFSRT DPTMLVSGSD DGKVKIWCTR QESSVINIDM KANICCVKYN
PGSSNYVAVG SADHHIHYFD VRNSHLPLYV FNGHRKAVSY VKFLSPNELA SASTDSTLCL
WDVKENCPIR TLKGHTNEKN FVGLTVNSEY IACGSETNEV FVYHKAMSKP ASWHRFGSED
AGESDDDTSH FISAVCWKSE SPTMLAANSQ GTIKVLVLAP
//