ID A0A084W4H4_ANOSI Unreviewed; 2185 AA.
AC A0A084W4H4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFB45118.1, ECO:0000313|EnsemblMetazoa:ASIC013039-PA};
GN ORFNames=ZHAS_00013039 {ECO:0000313|EMBL:KFB45118.1};
OS Anopheles sinensis (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=74873 {ECO:0000313|EMBL:KFB45118.1};
RN [1] {ECO:0000313|EMBL:KFB45118.1, ECO:0000313|Proteomes:UP000030765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24438588; DOI=10.1186/1471-2164-15-42;
RA Zhou D., Zhang D., Ding G., Shi L., Hou Q., Ye Y., Xu Y., Zhou H.,
RA Xiong C., Li S., Yu J., Hong S., Yu X., Zou P., Chen C., Chang X., Wang W.,
RA Lv Y., Sun Y., Ma L., Shen B., Zhu C.;
RT "Genome sequence of Anopheles sinensis provides insight into genetics basis
RT of mosquito competence for malaria parasites.";
RL BMC Genomics 15:42-42(2014).
RN [2] {ECO:0000313|EnsemblMetazoa:ASIC013039-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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DR EMBL; ATLV01020332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KE525298; KFB45118.1; -; Genomic_DNA.
DR STRING; 74873.A0A084W4H4; -.
DR EnsemblMetazoa; ASIC013039-RA; ASIC013039-PA; ASIC013039.
DR VEuPathDB; VectorBase:ASIC013039; -.
DR VEuPathDB; VectorBase:ASIS006759; -.
DR OMA; TWRWAVR; -.
DR Proteomes; UP000030765; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18667; CD1_tandem_CHD3-4_like; 1.
DR CDD; cd18662; CD2_tandem_CHD3-4_like; 1.
DR CDD; cd17994; DEXHc_CHD3_4_5; 1.
DR CDD; cd00084; HMG-box_SF; 1.
DR CDD; cd15531; PHD1_CHD_II; 1.
DR CDD; cd15532; PHD2_CHD_II; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR012957; CHD_C2.
DR InterPro; IPR009462; CHD_II_SANT-like.
DR InterPro; IPR012958; CHD_N.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR009463; DUF1087.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45623:SF13; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF08074; CHDCT2; 1.
DR Pfam; PF06461; CHDII_SANT-like; 1.
DR Pfam; PF08073; CHDNT; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF06465; DUF1087; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01146; DUF1086; 1.
DR SMART; SM01147; DUF1087; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000030765};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 436..483
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 494..541
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 555..626
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 670..719
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 816..998
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1130..1292
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1407..1474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1634..1889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2163..2185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..83
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..421
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..786
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1450..1472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1634..1662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1663..1692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1702..1722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1730..1753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1770..1798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1799..1813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1823..1841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2185 AA; 241945 MW; 796A2BD48FFD529D CRC64;
MASDEEIDES IAEEDGGLAD EGVDASLAAD ADDASDEEVN AKGATQADED DDYEPEDSRK
KKKGKKRKAR SSDEKRGRKK KKRKKNDSGD ESDQKQSDDG GGSSAAASAA AAAAAAAAAQ
AESDYEARPK RGRDRKKGSS SSSSRGVASE VSEKKSAVVE EKEKMPSIQE VCSSFDLTDV
KIEYSEEDFE NLVTFKMFQT HVRPILTKEN PKVPMAKLMM LVAAKWREFC TQNPHIPSEE
AGGEAKEEEA APATPEYVPK SSRSRSKMEN KHEDMVYDDE DDEDEEEVER ERTRKSKKGK
SGGGGGGGGS SSNKKGGGSS SSGGRKQKVP TLKIKFGKRK NASSDEEQDA SGASERDSDA
EFEKMLQQSE SEKPEKPERG ESSSGLGATE GAGDDTSDPP VRKKAKTKIG NKSKKKSKSK
KSKFPDGGEE GEHEHQDYCE VCQQGGEIIL CDTCPKAYHL VCLDPELEDT PEGKWSCPTC
EAEGPADDDD DEHQEFCRVC KDGGELLCCD NCPSAYHTFC LNPPLDDIPD GEWRCPRCSC
PPLPGKVQKI LTWRWTDKPI INPDEPSTSK GTGGGGGPTR RREYFVKWAE KSYWHCDWIT
ELQLDVHHPL MFRYYTRKYD MEEPPKLEEA LDEQDNRYKR IQRMRDIQGD VNETELEEKF
YRYGVKPEWL MVHRVINHRT MRDGRTLYLV KWRELPYDQA TWEDEEEDIP GLKMTIEYYL
DLRANCSQDI GGGSGGGGGG GGGSSSSKKN KKKRGGSRRI RELEEEERTT GLKRYTPPPE
KPTTDLKKKF EVQPPYLDET GMRLHPYQLE GINWLRYSWA NGTDTILADE MGLGKTIQTA
TFLYSLYKEG HCRGPFLVAV PLSTIINWER EFETWAPDFY CITYVGDKES RAVIRENELS
FEEGAVRGGK ASRIRASSIK FNVLLTSYEL VSIDAACLGS IDWSVLVVDE AHRLKSNQSK
FFKVLNAYNI AYKLLLTGTP LQNNLEELFH LLNFLNKNKF NELGDFQNEF ADISKEEQVK
RLHEMLGPHM LRRLKADVLK NMPTKSEFIV RVELSPLQKK YYKYILTRNY EALNPKGGGG
ACSLINIMMD LKKCCNHPYL FAAAAEEATL GPGGNYELQS LTKAAGKLVL LEKMLKLLKS
QGHRVLIFSQ MTKMLDILED FLEGLGYKYE RIDGGITGSI RQEAIDRFNA PGAPQFCFLL
STRAGGLGIN LATADTVIIY DSDWNPHNDI QAFSRAHRIG QANKVMIYRF VTRNSVEERV
TQVAKRKMML THLVVRPGMG GKGTNFTKQE LDDILRFGTE ELFKEDGKDE EAIHYDDKAV
AELLDRSNKG VEEKENWANE YLSSFKVASY STKEDVEEET ETEVIKQEAE NSDPAYWVKL
LRHHYEQHQE DLSRSLGKGK RVRKQVNYTD GGVIQADPVK EDSTWQENVS DYNSDYSGNS
DEDRDEDDEE SELGRRSRRR IERKEAERDN RPLPPLLARV GGNIEVLGFN ARQRKSFLNA
IMRYGMPPQD AFHSQWLVRD LRGKSERIFK AYVSLFMRHL CEPGADNAET FADGVPREGL
SRQHVLTRIG VMSLIRKKVQ EFEHINGYYS MPELIKRPCE PVKIALPIVA PGTSGEVPGT
SAAAAAAVGE SSKSATTSTS ATPATSAAPS PAPNSTAGGK DDESTGDNGK ESDKDKEKSE
PASEEVKKEP SAAAGGEGEA TASSAEDKKK DVEAKVEPTG DEPMDTTEGA DGDGEEKKKL
AVKKEDTTAT EEGESSKKPA VVATEVKSEE TTAAADEMKK ESDGKDEKEK EKDEEKASAA
ASGTTSPAAS SGEGGSSAAK VGGLVEEDKK SSDASAGKKA ADDDDDDDDD EVKIVEDSST
IPPAVKKESA GKSTPPAAAA PVPIDDDDDD VVIVKDDDEE VKKPAPVKEN LEVHKRAFMF
NIADGGFTEL HTLWINEEKA AVPGREYEIW HRRHDYWLLA GIVTHGYGRW QDIQNDIRFA
IINEPFKMDV GKGNFLEIKN KFLARRFKLL EQSLVIEEQL RRAALLNLAQ DPAHPAMALN
ARFAEVECLA ESHQHLSKES LAGNKPANAV LHKVLNQLEE LLSDMKSDVS RLPATLARIP
PVAQRLQMSE RSILSRLAAT GNTVQQNPPL SQFPAGYQGT TLPGFAAAAA ANFATFRPTF
SVPGQPTNFP SGAGASTSGS SASGK
//
