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Database: UniProt
Entry: A0A067TYM1_GALM3
LinkDB: A0A067TYM1_GALM3
Original site: A0A067TYM1_GALM3 
ID   A0A067TYM1_GALM3        Unreviewed;       289 AA.
AC   A0A067TYM1;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=mRNA 3'-end-processing protein {ECO:0000256|RuleBase:RU369008};
GN   ORFNames=GALMADRAFT_83466 {ECO:0000313|EMBL:KDR85089.1};
OS   Galerina marginata (strain CBS 339.88).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Strophariaceae; Galerina.
OX   NCBI_TaxID=685588 {ECO:0000313|EMBL:KDR85089.1, ECO:0000313|Proteomes:UP000027222};
RN   [1] {ECO:0000313|Proteomes:UP000027222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 339.88 {ECO:0000313|Proteomes:UP000027222};
RX   PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA   Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA   Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA   LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA   Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA   Hibbett D.S., Grigoriev I.V.;
RT   "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT   white-rot/brown-rot paradigm for wood decay fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
CC   -!- FUNCTION: Component of the cleavage factor I (CF I) involved in pre-
CC       mRNA 3'-end processing. {ECO:0000256|RuleBase:RU369008}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU369008}.
CC   -!- SIMILARITY: Belongs to the CPSF4/YTH1 family.
CC       {ECO:0000256|ARBA:ARBA00008907, ECO:0000256|RuleBase:RU369008}.
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DR   EMBL; KL142367; KDR85089.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067TYM1; -.
DR   STRING; 685588.A0A067TYM1; -.
DR   HOGENOM; CLU_024513_0_0_1; -.
DR   OrthoDB; 33612at2759; -.
DR   Proteomes; UP000027222; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0031124; P:mRNA 3'-end processing; IEA:UniProtKB-UniRule.
DR   Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 2.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR   InterPro; IPR045348; CPSF4/Yth1.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR23102:SF24; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 4; 1.
DR   PANTHER; PTHR23102; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 4-RELATED; 1.
DR   Pfam; PF00642; zf-CCCH; 2.
DR   Pfam; PF14608; zf-CCCH_2; 1.
DR   Pfam; PF18345; zf_CCCH_4; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SMART; SM00356; ZnF_C3H1; 4.
DR   SUPFAM; SSF90229; CCCH zinc finger; 2.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   PROSITE; PS50103; ZF_C3H1; 5.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}; mRNA processing {ECO:0000256|RuleBase:RU369008};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU369008};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027222};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU369008};
KW   RNA-binding {ECO:0000256|RuleBase:RU369008};
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          41..70
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          89..116
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          117..145
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          149..168
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          169..195
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          256..271
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   ZN_FING         41..70
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         89..116
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         117..145
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         149..168
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         169..195
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          193..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          268..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..216
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   289 AA;  32079 MW;  17D560EEAFE2CE02 CRC64;
     MVSANPLAGP SALRDVINPQ FHQNNFPAEA HIKTELGLKL DKDDQICRLA LTPAGCPLGP
     LHCPLRHTTP SVQNFQPPRQ LPTHPRERER LSTVCKHWLR GLCKKGDACE FLHEYNLRRM
     PECWWFAKYG YCSAGDECLY AHPKERRVEC PDYNRGFCKL GPACPRKHIR KVACQSYLTG
     FCPLGPDCPR GHPKPNLPPP KAYEPPSPPS AKDLGPPPPG YGRYADFDRG AGGSAPGGPG
     SAMTGPPRRN LDEVLCFKCG EKGHYANHCR NRNVPGNRGG SERIKRYGE
//
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