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Database: UniProt
Entry: A0A2K1L8W4_PHYPA
LinkDB: A0A2K1L8W4_PHYPA
Original site: A0A2K1L8W4_PHYPA 
ID   A0A2K1L8W4_PHYPA        Unreviewed;       522 AA.
AC   A0A2K1L8W4;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=C3H1-type domain-containing protein {ECO:0000259|PROSITE:PS50103};
GN   ORFNames=PHYPA_000881 {ECO:0000313|EMBL:PNR62457.1};
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:PNR62457.1};
RN   [1] {ECO:0000313|EMBL:PNR62457.1, ECO:0000313|Proteomes:UP000006727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c1_20290V3.1,
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:PNR62457.1, ECO:0000313|Proteomes:UP000006727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c1_20290V3.1,
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_20290V3.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (DEC-2020) to UniProtKB.
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DR   EMBL; ABEU02000001; PNR62457.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K1L8W4; -.
DR   STRING; 3218.A0A2K1L8W4; -.
DR   PaxDb; 3218-PP1S43_233V6-1; -.
DR   EnsemblPlants; Pp3c1_20290V3.1; Pp3c1_20290V3.1; Pp3c1_20290.
DR   EnsemblPlants; Pp3c1_20290V3.2; Pp3c1_20290V3.2; Pp3c1_20290.
DR   Gramene; Pp3c1_20290V3.1; Pp3c1_20290V3.1; Pp3c1_20290.
DR   Gramene; Pp3c1_20290V3.2; Pp3c1_20290V3.2; Pp3c1_20290.
DR   InParanoid; A0A2K1L8W4; -.
DR   OrthoDB; 200644at2759; -.
DR   Proteomes; UP000006727; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; IEA:InterPro.
DR   GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR   GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
DR   Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 3.
DR   InterPro; IPR045877; ZFP36-like.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   PANTHER; PTHR12547; CCCH ZINC FINGER/TIS11-RELATED; 1.
DR   PANTHER; PTHR12547:SF156; ZINC FINGER CCCH DOMAIN-CONTAINING PROTEIN 12-RELATED; 1.
DR   Pfam; PF00642; zf-CCCH; 3.
DR   SMART; SM00356; ZnF_C3H1; 3.
DR   SUPFAM; SSF90229; CCCH zinc finger; 3.
DR   PROSITE; PS50103; ZF_C3H1; 3.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000006727};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}.
FT   DOMAIN          157..184
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          229..257
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          319..347
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         157..184
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         229..257
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         319..347
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          92..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          190..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          285..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          351..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..319
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..406
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..477
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   522 AA;  55108 MW;  80DB7AFE1CA455EF CRC64;
     MDTTAAAELG MGEPVVGMDG AGFWDAGAPG LDQWGDNEDD ESVENDLSWD RAGPHGSAAV
     AQEYQQASHS GFGRGRAISG AEPTQKVLRT MPDGNRGPNH HNHSGNHQGF GGHGGGIQSG
     RGGSAAGGAG LADFGAVGSS SAGAGAVGRG RGMGSIFYKT KLCSRFRSGN CPYSTNCNFA
     HGMEELRKPP PGWEEFVASQ EFPPPPPSQP GGQGGSGSAA GSTDSQVRFH KTRPCKKYFG
     EGNCPYGEKC NFLHDEHSVP RAVREARDAA VAAASGAVVA ASPKVEMQLA PTTNGNTKEG
     EGGSSTPAGS ATPNARPSNW KTRLCNKWET TGHCPFEDKC HFAHGSDELQ RYGGGLPDSS
     APALSDSKSG GTPSQDTVAV SSYQRHQGGA SSARSGSKGK SNWRGPNEIS TIYGDWWIED
     DDWQRGATTT IHEAAEPESD VRGEVQRRTT FSVPSASTPK TVPFFRRSTG LEPSRQQNFT
     PINRCAIVAQ MDGEVNQQSF QYEGVKEDVY GSVLQPEQGW RR
//
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