ID Q948Q3_PHYPA Unreviewed; 599 AA.
AC Q948Q3; A9SDD8; E1C9W5;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=GH3-like protein {ECO:0000313|EMBL:BAB71764.1, ECO:0000313|EMBL:CAD22056.2};
GN Name=PpGH3L1 {ECO:0000313|EMBL:BAB71764.1};
GN Synonyms=GH3-2 {ECO:0000313|EMBL:CAD22056.2}, gh3-2
GN {ECO:0000313|EMBL:CAD42871.1};
GN ORFNames=PHYPA_014192 {ECO:0000313|EMBL:PNR47072.1};
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:BAB71764.1};
RN [1] {ECO:0000313|EMBL:BAB71764.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11884681; DOI=10.1105/tpc.010388;
RA Imaizumi T., Kadota A., Hasebe M., Wada M.;
RT "Cryptochrome light signals control development to suppress auxin
RT sensitivity in the moss Physcomitrella patens.";
RL Plant Cell 14:373-386(2002).
RN [2] {ECO:0000313|EMBL:CAD22056.2}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Protonema {ECO:0000313|EMBL:CAD22056.2};
RX PubMed=15310072; DOI=10.1016/j.jplph.2003.12.010;
RA Bierfreund N.M., Tintelnot S., Reski R., Decker E.L.;
RT "Loss of GH3 function does not affect phytochrome-mediated development in a
RT moss, Physcomitrella patens.";
RL J. Plant Physiol. 161:823-835(2004).
RN [3] {ECO:0000313|EMBL:PNR47072.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c10_20960V3.1,
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 [4] {ECO:0000313|EMBL:PNR47072.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c10_20960V3.1,
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 [5] {ECO:0000313|EnsemblPlants:Pp3c10_20960V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the IAA-amido conjugating enzyme family.
CC {ECO:0000256|ARBA:ARBA00008068}.
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DR EMBL; AB061221; BAB71764.1; -; mRNA.
DR EMBL; AJ429070; CAD22056.2; -; mRNA.
DR EMBL; AJ496302; CAD42871.1; -; Genomic_DNA.
DR EMBL; ABEU02000010; PNR47072.1; -; Genomic_DNA.
DR RefSeq; XP_001764319.1; XM_001764267.1.
DR AlphaFoldDB; Q948Q3; -.
DR STRING; 3218.Q948Q3; -.
DR PaxDb; 3218-PP1S67_243V6-1; -.
DR EnsemblPlants; Pp3c10_20960V3.1; Pp3c10_20960V3.1; Pp3c10_20960.
DR EnsemblPlants; Pp3c10_20960V3.2; Pp3c10_20960V3.2; Pp3c10_20960.
DR Gramene; Pp3c10_20960V3.1; Pp3c10_20960V3.1; Pp3c10_20960.
DR Gramene; Pp3c10_20960V3.2; Pp3c10_20960V3.2; Pp3c10_20960.
DR eggNOG; ENOG502QTQD; Eukaryota.
DR HOGENOM; CLU_016249_2_1_1; -.
DR InParanoid; Q948Q3; -.
DR OMA; REYPIGQ; -.
DR OrthoDB; 5402445at2759; -.
DR Proteomes; UP000006727; Chromosome 10.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IBA:GO_Central.
DR InterPro; IPR004993; GH3.
DR PANTHER; PTHR31901; GH3 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR31901:SF5; JASMONOYL--L-AMINO ACID SYNTHETASE JAR1; 1.
DR Pfam; PF03321; GH3; 1.
PE 2: Evidence at transcript level;
KW Reference proteome {ECO:0000313|Proteomes:UP000006727}.
SQ SEQUENCE 599 AA; 67081 MW; 3E5A9939E540CF86 CRC64;
MALRIENPYY KLLDTDEEIV EDFELMSRNA RETQLELLRK ILERNANVEY LQRQGLNGRT
DEASFKACVP VSTYANIEAD VDRIADGDTS PICCVDPPTS FALSSGTTGG KCKLIPRTDA
LLAQAMKAGQ IGSVYRRRAF PRKHEGPPVV MSFQYAGRQF DTKSGLKAGT GTTNFYRSAA
FKNAKSAPFS ATSPVDIVLG YDVPQQMYCH LLCGLYRCQE VEQMSAIFAY MIVEPFRLLE
RVWRDICKDI REGTVNERVS DPELRSSVLK VLSPNPELAD LIERECAKGW SGIIERLFPN
INYIMSIFSG SMLPYVAPMR QYAGSVPLMN ADYGASEAWI GINLDPRCPA EDASFTIIPN
FAYFEFIPVN RDSAGYDSVE GDEIVGLTDV KVGQEYEIVL TTVGGLYRYR LGDIVKVTGF
FNSTPKVAFV CRKGVVLSVN TDKTDEEELR LVVGKASLLL KESNMELADY SSYTDQDSQP
GHYVIFWELR SHEHLDMDLL SECCKVLDQS FNNPYMRGRA ARTIGPLELA IVKEGAFARL
MEQFVRKNGV GASQYKVSRC FKNPATLKHF RDETIATLRS PDFPPELLAA WRPSTKIVG
//