ID A9SYI7_PHYPA Unreviewed; 449 AA.
AC A9SYI7;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=SP-RING-type domain-containing protein {ECO:0000259|PROSITE:PS51044};
GN ORFNames=PHYPA_027899 {ECO:0000313|EMBL:PNR29207.1};
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:PNR29207.1};
RN [1] {ECO:0000313|EMBL:PNR29207.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c23_10880V3.1,
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:PNR29207.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c23_10880V3.1,
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:Pp3c23_10880V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the NSE2 family.
CC {ECO:0000256|ARBA:ARBA00008212}.
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DR EMBL; ABEU02000023; PNR29207.1; -; Genomic_DNA.
DR RefSeq; XP_001771394.1; XM_001771342.1.
DR AlphaFoldDB; A9SYI7; -.
DR STRING; 3218.A9SYI7; -.
DR PaxDb; 3218-PP1S137_220V6-1; -.
DR EnsemblPlants; Pp3c23_10880V3.1; Pp3c23_10880V3.1; Pp3c23_10880.
DR EnsemblPlants; Pp3c23_10880V3.2; Pp3c23_10880V3.2; Pp3c23_10880.
DR Gramene; Pp3c23_10880V3.1; Pp3c23_10880V3.1; Pp3c23_10880.
DR Gramene; Pp3c23_10880V3.2; Pp3c23_10880V3.2; Pp3c23_10880.
DR eggNOG; KOG2979; Eukaryota.
DR HOGENOM; CLU_620227_0_0_1; -.
DR InParanoid; A9SYI7; -.
DR OrthoDB; 935506at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000006727; Chromosome 23.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IBA:GO_Central.
DR GO; GO:0061665; F:SUMO ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0016925; P:protein sumoylation; IBA:GO_Central.
DR CDD; cd16651; SPL-RING_NSE2; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR026846; Nse2(Mms21).
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR21330:SF1; E3 SUMO-PROTEIN LIGASE NSE2; 1.
DR PANTHER; PTHR21330; UNCHARACTERIZED; 1.
DR Pfam; PF11789; zf-Nse; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006727};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00452}.
FT DOMAIN 336..426
FT /note="SP-RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51044"
SQ SEQUENCE 449 AA; 50034 MW; AB0942A0CB909CA2 CRC64;
MENLGGKMVA LGEEVEEFFT DISQKETKAK IDNKMEYLDR LQMLRLAQGE GEPLLRKDNS
PGTDLSVDQQ SLAEEPAVFS STTEGKDEAF KHEAENFQIT KQIVRTAHIS QDEGELEEHV
AAIDHDRKPK ILIANEQDMG TKIREKQMGV NEESVEFKPA LVKKAVSELH GLTERQQKFL
QDFHVKFVLR GLEAAEDDQA RARQHSSHRV DLKIHADYGF GEASDIDITV KGQIDAKPSY
VTPRTLATTQ TSEPERAPQI RVIMDDVIDN LADVTICNLD PSAGCDSKPT PDFGNAMKDL
VDDDELSELQ GFTDREGRVG ECQCYGKAGK QMDEKDESDV QITNASYSVL NVVCPVSGVP
VVGLKDPVRS EGCEHVYDRA SALNYISSME KDGFCPCAVA GCRALLAEKK LVADSRLWQD
IEELRQIKAA LWESHMLQNF VNIEDSDED
//
