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Database: UniProt
Entry: A0A2K1JD68_PHYPA
LinkDB: A0A2K1JD68_PHYPA
Original site: A0A2K1JD68_PHYPA 
ID   A0A2K1JD68_PHYPA        Unreviewed;       480 AA.
AC   A0A2K1JD68;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PNR39476.1, ECO:0000313|EnsemblPlants:Pp3c15_14620V3.1};
GN   ORFNames=PHYPA_019754 {ECO:0000313|EMBL:PNR39476.1};
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:PNR39476.1};
RN   [1] {ECO:0000313|EMBL:PNR39476.1, ECO:0000313|Proteomes:UP000006727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c15_14620V3.1,
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:PNR39476.1, ECO:0000313|Proteomes:UP000006727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c15_14620V3.1,
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:Pp3c15_14620V3.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (DEC-2020) to UniProtKB.
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DR   EMBL; ABEU02000015; PNR39476.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K1JD68; -.
DR   STRING; 3218.A0A2K1JD68; -.
DR   PaxDb; 3218-PP1S104_101V6-2; -.
DR   EnsemblPlants; Pp3c15_14620V3.1; Pp3c15_14620V3.1; Pp3c15_14620.
DR   EnsemblPlants; Pp3c15_14620V3.2; Pp3c15_14620V3.2; Pp3c15_14620.
DR   EnsemblPlants; Pp3c15_14620V3.3; Pp3c15_14620V3.3; Pp3c15_14620.
DR   Gramene; Pp3c15_14620V3.1; Pp3c15_14620V3.1; Pp3c15_14620.
DR   Gramene; Pp3c15_14620V3.2; Pp3c15_14620V3.2; Pp3c15_14620.
DR   Gramene; Pp3c15_14620V3.3; Pp3c15_14620V3.3; Pp3c15_14620.
DR   OrthoDB; 3088759at2759; -.
DR   Proteomes; UP000006727; Chromosome 15.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd16514; RING-HC_LONFs_rpt2; 1.
DR   Gene3D; 1.20.58.1480; -; 1.
DR   Gene3D; 2.30.130.40; LON domain-like; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR003111; Lon_prtase_N.
DR   InterPro; IPR046336; Lon_prtase_N_sf.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR23327:SF42; LON PEPTIDASE N-TERMINAL DOMAIN AND RING FINGER PROTEIN C14F5.10C; 1.
DR   PANTHER; PTHR23327; RING FINGER PROTEIN 127; 1.
DR   Pfam; PF02190; LON_substr_bdg; 1.
DR   Pfam; PF13923; zf-C3HC4_2; 1.
DR   SMART; SM00464; LON; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00028; TPR; 2.
DR   SUPFAM; SSF88697; PUA domain-like; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS51787; LON_N; 1.
DR   PROSITE; PS50005; TPR; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006727};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   REPEAT          121..154
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          189..227
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          270..470
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51787"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   480 AA;  54827 MW;  32DCCB0337E72F6D CRC64;
     MANEDDVEDV KDLSLVDGEG ETSPEKNAAV EFLRRGNRDF RNSRFKEAIL CYTKALNANC
     LDQAMLYSNR CAAYCKYSQG IRLRPARTSE ESAMLELDPM TLGQLALKDS EKLVKLQSDN
     PKAYLRKATA QVLLEQYEAA VETYLSGLEI DPMNKPLQEG LREVKILMEG VEQNDSKRRK
     LKRSDDLDCT LCLKLLHQPI TTPCGHSFCR ACLLQALDHG NKCPMCRTVI FVSPKTYPVS
     VTLNNLIQRN FPEEFAERKA EMDAVSLAGG ETLPLFVMDV VLPMQQLMLN IFEPRYRLMI
     RRVVEGNHRM GMVRIEESGS LAEVACEVEI TECEPLPDGR FEIEVVGKRR FRMTETWEQD
     GYRVAKVQWL QDVVHPDGSP EKDELAQSVR TAADLVNAFI SRVRDIAVRS DRRLLEMLNR
     TEGMPSASDP ERFSFWVANL MNIPGRERLQ YLRITDTRER LTREITRLRS MPADSNCCIQ
//
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