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Database: UniProt
Entry: A0A1I8PFM6_STOCA
LinkDB: A0A1I8PFM6_STOCA
Original site: A0A1I8PFM6_STOCA 
ID   A0A1I8PFM6_STOCA        Unreviewed;      2120 AA.
AC   A0A1I8PFM6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   Name=106086320 {ECO:0000313|EnsemblMetazoa:SCAU007637-PA};
OS   Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC   Muscidae; Stomoxys.
OX   NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU007637-PA, ECO:0000313|Proteomes:UP000095300};
RN   [1] {ECO:0000313|EnsemblMetazoa:SCAU007637-PA}
RP   IDENTIFICATION.
RC   STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU007637-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001665};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   RefSeq; XP_013106404.1; XM_013250950.1.
DR   STRING; 35570.A0A1I8PFM6; -.
DR   EnsemblMetazoa; SCAU007637-RA; SCAU007637-PA; SCAU007637.
DR   GeneID; 106086320; -.
DR   KEGG; scac:106086320; -.
DR   VEuPathDB; VectorBase:SCAU007637; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000095300; 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:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd18666; CD1_tandem_CHD1-2_like; 1.
DR   CDD; cd18659; CD2_tandem; 1.
DR   CDD; cd17993; DEXHc_CHD1_2; 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   InterPro; IPR040793; CDH1_2_SANT_HL1.
DR   InterPro; IPR025260; CHD1-like_C.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR023779; Chromodomain_CS.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
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   PANTHER; PTHR45623:SF14; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   Pfam; PF18375; CDH1_2_SANT_HL1; 1.
DR   Pfam; PF13907; CHD1-like_C; 1.
DR   Pfam; PF00385; Chromo; 2.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01176; DUF4208; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF54160; Chromo domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00598; CHROMO_1; 1.
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.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          419..513
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          538..599
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          638..808
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          938..1089
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1172..1275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1337..1368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1492..1635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1736..2120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..75
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..139
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..173
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..243
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..284
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..308
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..374
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1174..1191
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1199..1247
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1257..1275
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1549..1566
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1576..1592
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1593..1608
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1609..1627
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1747..1764
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1765..1809
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1875..1901
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1903..1955
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1965..2017
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2099..2120
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2120 AA;  237437 MW;  08D91EB6C8E8F625 CRC64;
     MSQEHNESLN SIGSEENDDT REDEHNDGSG SGSGSSSESD SDSDSSSSSS NSSGGGRSSP
     EPPDRDEEDD NARDGHNSQQ QQQHDSNYRL EQEEKQKQFA EAGLPPSAIE AQDDTKTNTN
     GYSDDNDSGS ESGSNSDSNS SNDDDDDDEK ASQQNDVRGR DGQGNHDAEH KQQNTTHNTT
     GTSFTSATTD NNTSHTTNDE DDSNDSNDSE DSNSDNEETQ TSQPMVTDET TTPPTTASEA
     IKQQHNSDEN EDEASDSAES AKSSNSSAHS ATESNSSSSS SSEDTEEDYQ PKRSARQARK
     PQPAAEKSKK PLKKKKRSQN WNSDESDESD EESEDSSPPP RRKPPAKQNK AQKRNKKSSA
     STDESGEDSK RFGTRRAAAT VSYKEDTDKT DSDDLVEIEY DESQAEAAAL AAEEDEKCET
     IERILYKRQG KKGCTGNQTT IYAIEESGCD PNDGVDENDL ENTEVQYLIK WKGWSYIHNT
     WESDATLKEQ KVKGMKKLDN FIKKELEQVY WMRHAGPEDI DYYECQKELQ NDLIKSYNNV
     DRIIARNVKP EGPVEYLCKW QSLPYAEATW EDGALVMRKW KRCVEQFEER ENSKCTPSRH
     CKVLKNRPKF YKIKNQPEFL SEGLVLRDYQ MDGLNWMLHS WCKENSVILA DEMGLGKTIQ
     TICFLYSLFK VHHLYGPFLC VVPLSTMTAW QREFDLWGPD MNVVTYLGDV KSREMIRQYE
     WTFDGSKRLK FNCILTTYEI VLKDKLFLGT LQWAALLVDE AHRLKNDDSL LYKSLKEFET
     NHRLLITGTP LQNSLKELWA LLHFIMPEKF VTWEDFELEH GNAADKGYTK LHQQLEPYIL
     RRVKKDVEKS LPAKVEQILR VEMTSLQKQY YKWILTKNFD ALRKGKKGST STFLNIVIEL
     KKCCNHAALI RPSEFELMGM PQDEALQTLL KGSGKLVLLD KLLCRLKETG HRVLIFSQMV
     RMLDILADYL QKRHFSFQRL DGSIKGEIRR QALDHFNAEG SQDFCFLLST RAGGLGINLA
     TADTVIIFDS DWNPQNDLQA QARAHRIGQK NQVNIYRLVT ARSVEEQIVE RAKQKMVLDH
     LVIQRMDTTG RTVLDRGSSG PSNHTPFNKD DLSAILKFGA EELFKDEQEN DEELVCDIDE
     ILRRAETRNE DPEMPGDDLL SAFKVASIAA FEEEPDAATK ENEANSQAAD EDDTKDWDDI
     IPENFRKIVE NEEKSKEMED LYLPPRRKTT ANQGDKKSKK GQADDSNDSD YDGGSDGSND
     ADGKSKRRGR PAMKEKIVGF NDAELRRFIR SYKKFPAPLE RLEAIACDAE LQEKPLAELK
     RIGQMLHDRC VQFLEEHKDD VPPAAPAKKP PNDPNAAPED AAAAKQKRSR ATYSVKLGGV
     SFNAKTLLSC EEELKPLNSV IPATINERLA WSLDVKTRPA NFDVEWGVIE DSKLLCGIYQ
     YGIGSWEQMK MDPSLNLTEK ILHNDDRKPQ AKHLQSRAEY LLKIIKKNLE TKKKGAETKK
     RKPRKQKEPK TAAAVGSAAA HSATPERKSR NVSEGDELSQ TGADSTPAPT EKKTRKERKE
     SSTKATVDPV DEAASNDVDA SNTSATTATA KKKNKTSSKE KDGTPKSSAK SKKSATSDST
     NKPMHFTANN EPRALEVLGD LDPNIFNECK EKMRPVKKAL KALDRPDTSL SSQEQIKNTR
     ESLMAIGKQI DVCLEAYSKD SEKKEWRSNL WYFVSKFTEF DAKKLFKMYK QMLKTSEGEA
     KQKSPPVAKA KSNSASPQKR PKDDSLNQNG SDEKNKSAAK KKKKDKEKEK EKDVEKVKDK
     TRDTPKSDRF TKIGNANKPP AAGGAAMHMN KNKRPQQAGG VNNSPMKRKR EDNESGAVGG
     IPNAAGGSDL KSMSFKRLNM DEQGRNRDDR KNRHRDDYYG SGNSHDGLNT SRGSIGSGNG
     DRHSSMNSPS TPNNRMHPSN SRLLPGNNPS PYGDSNSGGG GGGDRWGHNR DRYGGGNNDY
     NKRERYDGYN NRPGGYHRDH KDRDRDRRFD KRRYPPSHPP QHGYGNHYMG PNYYMPPNGG
     VPPGMGGGPH GGYSGAGRGG DPRYNHPAEW PREYPPDSYR RGAGGGPSGA VGGGGGQSGP
     PIPSSNSGDR RPPLPPTSQT
//
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