ID A0A158NR79_ATTCE Unreviewed; 963 AA.
AC A0A158NR79;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=C3H1-type domain-containing protein {ECO:0000259|PROSITE:PS50103};
GN Name=105623248 {ECO:0000313|EnsemblMetazoa:XP_012060037.1};
OS Atta cephalotes (Leafcutter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012060037.1, ECO:0000313|Proteomes:UP000005205};
RN [1] {ECO:0000313|Proteomes:UP000005205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA Weinstock G.M., Gerardo N.M., Currie C.R.;
RT "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT insights into its obligate symbiotic lifestyle.";
RL PLoS Genet. 7:e1002007-e1002007(2011).
RN [2] {ECO:0000313|EnsemblMetazoa:XP_012060037.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (APR-2016) to UniProtKB.
CC -!- FUNCTION: May be involved in the turnover of nuclear polyadenylated
CC (pA+) RNA. {ECO:0000256|ARBA:ARBA00043866}.
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DR EMBL; ADTU01023815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01023816; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01023817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012060037.1; XM_012204647.1.
DR AlphaFoldDB; A0A158NR79; -.
DR STRING; 12957.A0A158NR79; -.
DR EnsemblMetazoa; XM_012204647.1; XP_012060037.1; LOC105623248.
DR GeneID; 105623248; -.
DR KEGG; acep:105623248; -.
DR eggNOG; KOG2135; Eukaryota.
DR InParanoid; A0A158NR79; -.
DR OrthoDB; 5406435at2759; -.
DR Proteomes; UP000005205; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR CDD; cd12257; RRM1_RBM26_like; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR002483; PWI_dom.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR045137; RBM26/27.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR14398; RNA RECOGNITION RRM/RNP DOMAIN; 1.
DR PANTHER; PTHR14398:SF0; ZINC FINGER PROTEIN SWM; 1.
DR Pfam; PF14605; Nup35_RRM_2; 1.
DR Pfam; PF01480; PWI; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Reference proteome {ECO:0000313|Proteomes:UP000005205};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00723}.
FT DOMAIN 327..355
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 327..355
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 79..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 650..685
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 748..792
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 139..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..406
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..955
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 963 AA; 107670 MW; 000FC8BC4DBA2B9E CRC64;
MIIDNPDVFK AWLTAVLEPL CDADPAALAK YVYALVKKDK TLEELRGDMV EQLDVFLQKE
TKNFVELLFK TLETQDYVFP PPKSDPDGGG TPPGVNPSAP VVSSSTEKII DATIPLVPII
TNPPAPLQIN GSAPAVISKR ETRKSDSDKD KEKEKRSRSR SGRMRSRTRS RSRSWERDRR
RSRSREHIRR DRERDRSRPW RNESPPISTR RHDRRRTRSR STSPIRPRIR DGPDSRDHRA
RFRNRSPTPL RSRSRSRSIE RKKIDRFERI EVDRTERIEG SPGGGTPTQD SNHGDVDMRL
STTSQSIQSV VAVAGSIPNN QTSSFQQQAK RRCRDFDEKG YCMRGDLCPY DHGTDPVVLE
DVALSRVLSF GPHSAQAPGT VPVPTVPEPP QGPNGNPPPP HLPLASLPPS HLRNHHSNMD
VFAEYNPDAP SMEPRMPWGR HPQSAPGIYG RGQRELISVP VIPHTNSSEI THTQSNPLKR
KQTFDFNRLG PKQRVVHNPA NCSLELKKVP RSLNNITQLN NHFSKFGKIV NIQVNFGGDP
EAALVTFQLP AEAKSAYRSA EAVLNNRFIK VFWHNNVNNN AAGGAIENVP PGCRPSVKER
LGAAVTLSTK TEDNEYVPTR RSTEEQVTQA LVPTSPKAAV IPTREDKVLA IKKTQEILAA
KETLKKKQEE KRKEAIKLTA DLRKRKQELL DKHLIELRAL IDKAEKNPEQ KESIMPTIKT
MQQSVDNLRK DLAANGQIGG NKSQVKSREQ AQKEILDAEL DLMTAQQEGQ DAGELQKRLN
ELRAQAAALG LNTNPGVGRG AKVSRVARGT HTISFRGRGR GSFAHVSVDH RPTSLLVSGY
ETEEKAEVLA HFQQFGEIVN QIVDDATPSI VINFKSRKEA EVALVKGRTF QDRLLSITWV
SGHHLHRGGA GTNSSASIQL SSRSEQTAPT ADEDIDLEGT EALLLEENEE EEDEDGESRS
WRR
//
