ID A9T365_PHYPA Unreviewed; 1020 AA.
AC A9T365;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=PHYPA_017366 {ECO:0000313|EMBL:PNR42536.1};
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:PNR42536.1};
RN [1] {ECO:0000313|EMBL:PNR42536.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c13_14550V3.1,
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:PNR42536.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c13_14550V3.1,
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:Pp3c13_14550V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; ABEU02000013; PNR42536.1; -; Genomic_DNA.
DR RefSeq; XP_001773034.1; XM_001772982.1.
DR AlphaFoldDB; A9T365; -.
DR PaxDb; 3218-PP1S158_52V6-1; -.
DR EnsemblPlants; Pp3c13_14550V3.1; Pp3c13_14550V3.1; Pp3c13_14550.
DR EnsemblPlants; Pp3c13_14550V3.3; Pp3c13_14550V3.3; Pp3c13_14550.
DR Gramene; Pp3c13_14550V3.1; Pp3c13_14550V3.1; Pp3c13_14550.
DR Gramene; Pp3c13_14550V3.3; Pp3c13_14550V3.3; Pp3c13_14550.
DR eggNOG; KOG0167; Eukaryota.
DR HOGENOM; CLU_004912_0_1_1; -.
DR InParanoid; A9T365; -.
DR OMA; VKMIMAK; -.
DR OrthoDB; 467211at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000006727; Chromosome 13.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd21037; MLKL_NTD; 1.
DR CDD; cd16664; RING-Ubox_PUB; 1.
DR Gene3D; 1.20.930.20; Adaptor protein Cbl, N-terminal domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 4.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR036537; Adaptor_Cbl_N_dom_sf.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR045210; RING-Ubox_PUB.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45958; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR PANTHER; PTHR45958:SF5; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF00514; Arm; 2.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00185; ARM; 8.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50176; ARM_REPEAT; 3.
DR PROSITE; PS51698; U_BOX; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006727}.
FT DOMAIN 263..337
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REPEAT 379..421
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 544..586
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 585..616
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
SQ SEQUENCE 1020 AA; 111074 MW; 2BBECD9A530B0D17 CRC64;
MKDDTGMDNA TVALYSEVLA RIPKEVELVE ESAKGVLIGK ESFRVLSRYL ESIRSVLQEL
TGKKVSDPAA MQVTLISLEQ EIVKLKNIID KFSSKSKFYL ILKCQDFLKE IEDVTHELGY
CLNSVPVANS DLAVEIQEMM SKLSSDMRKA QFKPATVEEA IINEIKVGIH DQQSNSKYAN
YLLLQIARAV GVSTNPSSLK LELDSLKKEK EDARSRENQE EYRYLEQIIA ILSCADAATS
ASEKGLNYQK KRGLGGWGGH PLPPLQSFYC PITHEIMEEP VDIASGQTYE RYAIEKWFSA
GNSNCPITKV ELENLQIKLN LALKKSIQEW KERNIAISIA ATKPKLQSTS ESEICSALRM
LLDLSEEKGI HRYWIALEGL IPCLVQLLSS SQRTVRKETL EVLRSLSIDN KENKEHIAAA
GAIKLVVKSL ARDLGEGRQA VALLRELSKD PEICEKIGKV QGCILLLVTM LNAENPHAVT
DAKELLNDLA NNDQNVVQMG EANYFGPLTQ RLNEGPDMAK ILMANALSRM GLTDQSKAAL
AAQGAIPPLV SMISIGKLEA KTAALGALKN LSTLPDNRDT MIEAGVIPPL LQLLFSVTSG
MTSLKENAAA TLANLAMAST TAEDKIDHHY NILESDKTMV HLLSLLNIEG AVIRGHLLRA
LLGMSSIPNA REVRTKMRKV GAIQLLLPFC EDTVEDVRIH ALKLLKCLSS EGAGKDIADH
LGPSYIRALV KLLGDSSGDE EKLAAVGIIS NLPTTSAQMT DILLQADALA AIVNLLIPSR
GLKSSPRAVR NALSESATGA LLRFTSPENP NVTAHRQKAA DLDAIPRLVT ILQTGTPLAK
CRAAIALGHF SLSSDSLASI DNVPQSCLLW CRPATPAGCC IHGGPCTVKS TFCLVMAQAV
LPLVQALEEQ EDGADDAALT ALRTLLLNDA TLENGVKVIA QAQGIRPIVR LLTVGSVDVK
EKAVWMLEKI FRIEEYKVEF GSAAQMPLID LTQNGSIVTR PLAAKILAHL NILHSQSTYF
//
