ID A0A1V9X5B3_9ACAR Unreviewed; 1095 AA.
AC A0A1V9X5B3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=C2H2-type domain-containing protein {ECO:0000259|PROSITE:PS50157};
GN ORFNames=BIW11_12744 {ECO:0000313|EMBL:OQR68694.1};
OS Tropilaelaps mercedesae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Laelapidae;
OC Tropilaelaps.
OX NCBI_TaxID=418985 {ECO:0000313|EMBL:OQR68694.1, ECO:0000313|Proteomes:UP000192247};
RN [1] {ECO:0000313|EMBL:OQR68694.1, ECO:0000313|Proteomes:UP000192247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR68694.1};
RX PubMed=28327890; DOI=10.1093/gigascience/gix008;
RA Dong X., Armstrong S.D., Xia D., Makepeace B.L., Darby A.C., Kadowaki T.;
RT "Draft genome of the honey bee ectoparasitic mite, Tropilaelaps mercedesae,
RT is shaped by the parasitic life history.";
RL Gigascience 6:1-17(2017).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQR68694.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MNPL01023496; OQR68694.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9X5B3; -.
DR STRING; 418985.A0A1V9X5B3; -.
DR InParanoid; A0A1V9X5B3; -.
DR OrthoDB; 3081573at2759; -.
DR Proteomes; UP000192247; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 9.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24394:SF29; GM08392P; 1.
DR PANTHER; PTHR24394; ZINC FINGER PROTEIN; 1.
DR Pfam; PF00096; zf-C2H2; 6.
DR Pfam; PF12874; zf-met; 2.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Reference proteome {ECO:0000313|Proteomes:UP000192247};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 661..689
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 689..717
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 721..748
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 749..776
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 778..805
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 806..833
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 834..861
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 862..889
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 890..917
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 918..948
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 395..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1095 AA; 119637 MW; 0246C82769153198 CRC64;
MSAESSSEMS ASSAAGFRPM EISAQDGSSH VAEIGYAASV DKVARSSGLE QTLEYRGQNF
NFQFASGEGQ TGGMVQDVAG IVHEAGLFEQ GRQFEGQIFQ GHSGVKDSEF SFATEQPVPE
FTSTQPLEFI ERASLGDKRS LAKTSETGQQ QTSNVIIYLP SNVQICGPTS ASPADGEPFG
QQEFCSDSGQ VVNFIGNMAD MKSATIPGAA VGKTHLAKTL SAPVAGVSAD PPATCIGNFL
RENTTPEAQE SVKDEVKFLP APPEMPTLTS LAPLNPALKQ RLGKDANSRN EKKLTSALLT
LFFDERSSSY QRELVDVLKP LVKMLELLEA SPIDAEAMRR MLGSLVALVA SLQGIIVADR
RRSVMTHYGI DELHSMEQEG VELFGADFLM RHGFAPRKET GKASKRDSKK QPPLVRTREP
PNGIILPSKR KRKDKRGKKD TTESDNDADG CSDEIAQIII LDDSTDRQQP FPQSVLHKDT
GRQDQLQTQK GQRDLLPANE NCSALRSKRP KTEGREQDQQ LPQGVSKEQQ VRKTRLPRTR
QSDLGQLPAI TKSSNDDAAQ CSEHQSVIDE VRVSADSGVD TTMDFACLDE HPNKSAGQQG
LMLVDVTASS SPTMASKVRQ DADGLIRTMK AAETDAGAAA TAVTRPTRPR ANSKQTEIPS
GKCSFCELSF AKRLHLAQHL KQTHADQLPQ CEICNRRFAF ETILRQHLEE KHSQDVTGQR
DECKHCGKTF SDKDRLQAHL FVHTGTKQFE CSICSRRCLT KAHLDQHMAA HGRGEERFYC
ERCDKPFAKK TNYNHHLRLH SGEKNFECDL CHKRFATRQY LHIHLRSHSA EKPFTCDICG
RGFQFQHVLV DHVRTHTGET PFVCEVCGIS FKVKRTLKRH MKTHGDERPH TCHICQRGFK
VKATLREHMK THSNEKPYQC HECGLAYKRN VELRKHACPA RQHLHQTPAM ITTTVPPAVA
ARLPTAIQLA VSSQATSLSG TLTSAATAQT PVVATLNSSS GASALGVPVG GGLLVANGCD
GDPVQVQLDE VTEGSVNECQ PDPAAHQSLQ TVIPVRTAQS GPDGTTTTII LQPMGAVGAT
TAAGANFTGI HFINL
//
