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Database: UniProt
Entry: A9SK04_PHYPA
LinkDB: A9SK04_PHYPA
Original site: A9SK04_PHYPA 
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
//
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