ID A0A1I7VZN1_LOALO Unreviewed; 820 AA.
AC A0A1I7VZN1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Zinc finger CCCH domain-containing protein 6 {ECO:0000313|WBParaSite:EN70_806};
OS Loa loa (Eye worm) (Filaria loa).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Loa.
OX NCBI_TaxID=7209 {ECO:0000313|Proteomes:UP000095285, ECO:0000313|WBParaSite:EN70_806};
RN [1] {ECO:0000313|Proteomes:UP000095285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease;
RA Nutman T.B., Fink D.L., Russ C., Young S., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Henn M.R.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Loa loa.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:EN70_806}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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DR AlphaFoldDB; A0A1I7VZN1; -.
DR STRING; 7209.A0A1I7VZN1; -.
DR WBParaSite; EN70_806; EN70_806; EN70_806.
DR eggNOG; KOG1040; Eukaryota.
DR Proteomes; UP000095285; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:InterPro.
DR Gene3D; 3.30.1370.210; -; 1.
DR InterPro; IPR045124; Su(sable)-like.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR13119:SF12; PROTEIN SUPPRESSOR OF SABLE; 1.
DR PANTHER; PTHR13119; ZINC FINGER CCCH DOMAIN-CONTAINING PROTEI; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR Pfam; PF14608; zf-CCCH_2; 2.
DR SMART; SM00356; ZnF_C3H1; 3.
DR SUPFAM; SSF90229; CCCH zinc finger; 3.
DR PROSITE; PS50103; ZF_C3H1; 3.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000095285};
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 226..253
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 256..283
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 284..305
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 226..253
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 256..283
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 284..305
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 32..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..55
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..820
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 820 AA; 89429 MW; E5DB6AB519CB7F29 CRC64;
MVDVAMAGSL EEYEFSGAVR KDVELESKKI AEVEVEDGEL PEEGEICDDD DAEGRDRETT
ENREAAQAVS PNVSLNQQSV RKPRDFDKEV ANARGAEGSM LNTWMTGVKQ RAKPGIATIA
SPTVDANEEY YGYGSNSPND GTGDKDYRNR GGDSTDKDYR WIRDEDGHRG PGDVNEFGDS
DYRGGSPKIE RRRRRSISPT YGGPKRPRHS PPVRGCYRGR GFRGRWGERQ ICKFFREGYC
RDGESCSYSH DAADSGRKAE LCKFYQQGFC KKGLQCPLLH GEYPCKAFHK GECSKDPCQF
SHLPLNNFTQ PIFDQMMKDD ELASRIAIPQ GPLKRRVLLP GGPSSSPGAQ PTVPAIVTVT
ADGGITGGVI PPPAVVVPTL SSGASVTIAQ PQLVIPPPLA ANPTPYPAFF PHHSIPATAV
VNPTSLSGAV PGLAPPQPVQ SATVILQQYS ASVEKRNSVE DEEDNSFNIN KMLEQITAKV
KKDNAIDDES PASPPMFNPD AVANESAPTI PETNIIAWKL HPIDDIPTPQ TNIDSQILQL
SLTDSGLRND PRIKKALASQ FDAFTNSLMN AAPPPLPQPA QIFVQQSNVA ATTSATQSTV
LSTLPKEESS VSRLSDPRMS TVNRDPRKRT AVSDPRVTAV GDSRLVSTAS PTLDPRLAPP
SSLIQVGQIP STSTLRVGID SAYGAAMQVT SQNRDQDHRL HPSGYENSHV EEHNVERVGS
YECRRGSGGS WMPQIRAAVD PRQVKRYIIG GYRSELNNSQ DRDERAVNRV RGEGTKSPSS
NSAAANVTTI PQAPLSLREK RKNNEYESPL SRIPEKTRWT
//
