ID A0A0L0CBX7_LUCCU Unreviewed; 1732 AA.
AC A0A0L0CBX7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=ZAD domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=FF38_05233 {ECO:0000313|EMBL:KNC29742.1};
OS Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Luciliinae; Lucilia.
OX NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC29742.1, ECO:0000313|Proteomes:UP000037069};
RN [1] {ECO:0000313|EMBL:KNC29742.1, ECO:0000313|Proteomes:UP000037069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS {ECO:0000313|EMBL:KNC29742.1,
RC ECO:0000313|Proteomes:UP000037069};
RC TISSUE=Full body {ECO:0000313|EMBL:KNC29742.1};
RX PubMed=26108605; DOI=10.1038/ncomms8344;
RA Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT interventions.";
RL Nat. Commun. 6:7344-7344(2015).
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:KNC29742.1}.
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DR EMBL; JRES01000634; KNC29742.1; -; Genomic_DNA.
DR STRING; 7375.A0A0L0CBX7; -.
DR EnsemblMetazoa; KNC29742; KNC29742; FF38_05233.
DR OMA; NTANNCA; -.
DR Proteomes; UP000037069; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1800.20; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 2.
DR InterPro; IPR012934; Znf_AD.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24404:SF49; RH47711P-RELATED; 1.
DR PANTHER; PTHR24404; ZINC FINGER PROTEIN; 1.
DR Pfam; PF07776; zf-AD; 1.
DR SMART; SM00868; zf-AD; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR PROSITE; PS51915; ZAD; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01263}; Reference proteome {ECO:0000313|Proteomes:UP000037069};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU01263};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 18..101
FT /note="ZAD"
FT /evidence="ECO:0000259|PROSITE:PS51915"
FT DOMAIN 295..323
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 325..352
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 354..381
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 200..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1384..1404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1498..1557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1591..1616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1702..1732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..687
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..839
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..856
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..879
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..913
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..947
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1095
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1150
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1511..1545
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1713..1732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
SQ SEQUENCE 1732 AA; 193691 MW; 95BCDAFE41E59ED7 CRC64;
MERFAIKIDK KLKANLYKIC RLCGIDNPDM VPILTDKPEN TAIDVEAEME MAEKINLLLG
LSVTKDDKMP QSMCYLCVDK INDFYEFREM CYSTNAQTRK LLGLKNVKKP TVDIKPKVEI
KEESIVPTNN TANNCAANNK ANRKRKPEEV ALKEEIPATP VVLPKKKLRF TAAAETSIKE
EVPMITKKKL RFTATNDEAT STAAVGNKKT KTTLTEESKW KKESSPPEPA ITAAFSNKKL
KMSAPSPKEL AAKKTKQKFG KTAELDVKEE IKEEIKEEET SASAAKIPPG PKLKFGCNIC
KERFAAKNNL DAHTRTTHIP KIERFVCTAC NEVLSKSFDI KNHQLWHKLS KTPYVCGCCG
ESILNTYAFS RHLREHAFET PPALLVLDRE CPQCHTSYAT NYLYNIHICA VKTKRCAGCN
RLQRNDAEYI KHSAQCAKVY LNYSKHIMPS VEALEDAVRI KNENDVEAAA EEMARLSGVP
LDMAPVVQLT RLSSPIIMAA NQCVSMTGLD DAASTSSKRS GKKGVSKKDL KRVDELLKST
LDALVSIKHE PEVHVEPETP CAGVHSDNDE QNESHMSDHI GGLDDYHHNA DDSDYENEPA
NTDAASIAPN SETYVANETT SVEQIKIKQE IDEINEENAN KIGGGGLKLK IKKEHGQLNS
SIIEQQKSSE KRAEKRKKKK KHKDKEKEKQ KLSKELQDEQ LSQDSNGHNN TEDNIAAATT
IRIKTEPQDG TDVADIQSVA STIQIRPQPE ATIMTSIPMM QFQIACVSSG VEFNGGAASA
VVETSQRMAS TNHEVEPEDV KPNREELDRM MKISHVSSGI AMETDDKEEQ HMDHDGNDDE
GNGGDVDEGE ETDYHEESNE DDHHDDNNES AQHQHIDEDQ EAEEEAEDEH DKDIDKTSED
TGIDNEYIIA KKIKKPLNKN KLTSKPKVKP TPSLTKSRNK ACKSTAKPSN MPVLQITAVR
SGVTLEPTAS CASDFIPIFI KPEPQNRGYS DEQPLVETPT QIQTVQPQEL TDELSNTHTI
EEKSYISSID FNNITIKQEK DIEINDVHIS QKSVKSYADF NGIKRKRKPQ RRTHGIKDRT
LKKDEKLANT DENMEADEEH ATDDEVDEEE NDDEEETEEV EEEEEEDDEE EEAEEEEDEE
EVETDFEEER EYRELEYPPA LEKEAANETE EKQNEDPKSK TISEKQMDVS VKENMSDSNQ
VKESNMPQPS FVIASVCSQV AIGSSEDIHK STSGMDNMKH TQGINNHNDK LLKEVSVAEA
KDDPNKSQTL EINHDLKKAL GASENSNIAM ETPSIGISNA AMTFNGPQIE NTQLFPTTLP
STDQQENIQA SEMSLQLGQP YELRADQEIT QAPQLTQNVV ESLPCHAPLT QTDQLDIIHP
QCAEQNSQEN IESQTKSQEN PLNDVDSQGI QQLEQENKAQ DQQHPQSHTS QDLQPVFKIS
SITSAAALDV TPQVSNNPLS NKNDDDQEIL KDNQEETAII EGVVEQAKEL NLEAQPVTAE
LPQNMHDNEM EVDDDNYDNE EDDEDEEEEE EDDVNEDENE LNDGNNVNDD DSSTLCNNNL
EERQNYQNQE VLTQIRPAAL ALHPYLEDIS SSSNSLLSNS LSQTPPPTVT SLSISSQPAC
STTATSASAE RRLLNTEETE NILNESSDAL SRRSSIVAAT SAAATVGQPL TPSHLAQQLP
PHMPTFNFDN INEIAENNNN ANIEREQLQD GQHHYHQQQL QQQNQQQTRN TQ
//
