ID   W1P0C7_AMBTC            Unreviewed;      1115 AA.
AC   W1P0C7;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=CCHC-type domain-containing protein {ECO:0000259|PROSITE:PS50158};
GN   ORFNames=AMTR_s00003p00212560 {ECO:0000313|EMBL:ERN03282.1};
OS   Amborella trichopoda.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX   NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN03282.1, ECO:0000313|Proteomes:UP000017836};
RN   [1] {ECO:0000313|Proteomes:UP000017836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24357323;
RG   Amborella Genome Project;
RT   "The Amborella genome and the evolution of flowering plants.";
RL   Science 342:1241089-1241089(2013).
CC   -!- SIMILARITY: Belongs to the NEMF family.
CC       {ECO:0000256|ARBA:ARBA00008318}.
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DR   EMBL; KI394358; ERN03282.1; -; Genomic_DNA.
DR   RefSeq; XP_006841607.1; XM_006841544.2.
DR   AlphaFoldDB; W1P0C7; -.
DR   STRING; 13333.W1P0C7; -.
DR   EnsemblPlants; ERN03282; ERN03282; AMTR_s00003p00212560.
DR   GeneID; 18431419; -.
DR   Gramene; ERN03282; ERN03282; AMTR_s00003p00212560.
DR   KEGG; atr:18431419; -.
DR   eggNOG; KOG2030; Eukaryota.
DR   HOGENOM; CLU_003612_1_0_1; -.
DR   OMA; MFLEFFA; -.
DR   OrthoDB; 129892at2759; -.
DR   Proteomes; UP000017836; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:1990112; C:RQC complex; IBA:GO_Central.
DR   GO; GO:0043023; F:ribosomal large subunit binding; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0072344; P:rescue of stalled ribosome; IBA:GO_Central.
DR   GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   Gene3D; 2.30.310.10; ibrinogen binding protein from staphylococcus aureus domain; 1.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR   InterPro; IPR021846; NFACT-C.
DR   InterPro; IPR008532; NFACT_RNA-bd.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR15239; NUCLEAR EXPORT MEDIATOR FACTOR NEMF; 1.
DR   PANTHER; PTHR15239:SF6; RIBOSOME QUALITY CONTROL COMPLEX SUBUNIT NEMF; 1.
DR   Pfam; PF11923; NFACT-C; 1.
DR   Pfam; PF05670; NFACT-R_1; 1.
DR   Pfam; PF05833; NFACT_N; 2.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017836};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT   DOMAIN          947..962
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   REGION          188..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          690..731
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          799..901
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          915..934
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..212
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        816..857
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1115 AA;  125490 MW;  EB66D9C6B9E30601 CRC64;
     MVKVRMNTAD VAAEVKCLRK LIGMRCSNVY DLSPKTYMFK LMNSSGITES GESEKVLLLM
     ESGVRMHTTA YVRDKSTTPS GFTLKLRKHI RTRRLEDVRQ LGYDRVIVFQ FGLGSNAHYV
     ILELYAQGNI LLTDSDYVVM TLLRSHRDDE KGLAIMSRHR YPVEYCRVFE RTSFTKMKNA
     LTCSNSTEKD DFQSLEGDGH KTSNIDGKAM GTHKKAGDGV KIKKATLKTV LGESLGYGPA
     LSEHIILEAG LLPNMKVGNE NGATVDENTL RTLASAIDKF EDWLEDVISG ETVPEGYILM
     QSKTSGDRKG MSSQESSDQV YDEFTPILLN QFKSRQHMKM ETFDAALDEF YSKIESQKAE
     QQQKTKEGSA LLKLNKIRAD QENRVHTLKK EVDRCVALAE LIEYNLEDVD AAILAVRVAL
     ANGMDWEDLA RMVKEEKKSG NPVAGLIDKL HLERNCITLL LSNNLDDMDE EEKTRPADKV
     EVDLALSAHA NARRWYELKK RQENKQEKTI TAHEKAFKAA ERKTRLQLSQ EKTVAAISHM
     RKVHWFEKFN WFVSSENYLV ISGRDAQQNE MIVKRYMLKG DLYVHADLHG ASSTVIKNHK
     PEQPIPPLTL NQAGCFTVCH SQAWESKIVT SAWWVYPHQV SKTAPTGEYL TVGSFMIRGR
     KNFLPPHPLI MGFGILFRLD ESSLGSHLNE RRVRGEDEGL QDVEENGSRV EPMDSGSDEE
     NEVEKRSEEL NTNSDISINH SKITSNGPIA SAFESATSIE LDNKLFSKKE LSEPRMLPQL
     DVLIDRALEL GSKQIRGNLH GLQQDTQSDD QDEIPEEGKE AQRAKPYISK AERRKLRKGP
     ESGTGSTEEH GKKESNENHW SNPTPPKTIE NPKPTGGKVS RGQRGKLKKI KEKYAEQDEE
     ERKIRMELLA SAGRAQKDVN ESTEKRDGVT GNYSVSTTDH EDITKICYKC KRPGHLSREC
     PENIDDADNS TVTMHSGVDT EPSDRMLLEE DDIHEIGEEE KVKLNDVDYL TGNPLPNDIL
     LYAVPVCGPY SAVQTYKYRV KITPGMAKKG KAAKTAMNLF SHMPEATGRE KELMKACTDP
     ELVAAIIGNV KITAAGLTQL KQRQKKGKKN SKQDE
//