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Database: UniProt
Entry: Q54KQ4_DICDI
LinkDB: Q54KQ4_DICDI
Original site: Q54KQ4_DICDI 
ID   Q54KQ4_DICDI            Unreviewed;      1872 AA.
AC   Q54KQ4;
DT   24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 128.
DE   SubName: Full=SNF2-related domain-containing protein {ECO:0000313|EMBL:EAL63860.1};
GN   ORFNames=DDB_G0287171 {ECO:0000313|EMBL:EAL63860.1};
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689 {ECO:0000313|EMBL:EAL63860.1, ECO:0000313|Proteomes:UP000002195};
RN   [1] {ECO:0000313|EMBL:EAL63860.1, ECO:0000313|Proteomes:UP000002195}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4 {ECO:0000313|EMBL:EAL63860.1,
RC   ECO:0000313|Proteomes:UP000002195};
RX   PubMed=15875012; DOI=10.1038/nature03481;
RG   The Dictyostelium discoideum Sequencing Consortium;
RA   Eichinger L., Pachebat J.A., Glockner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M., Spiegler S., Tivey A., Sugano S.,
RA   White B., Walker D., Woodward J., Winckler T., Tanaka Y., Shaulsky G.,
RA   Schleicher M., Weinstock G., Rosenthal A., Cox E.C., Chisholm R.L.,
RA   Gibbs R., Loomis W.F., Platzer M., Kay R.R., Williams J., Dear P.H.,
RA   Noegel A.A., Barrell B., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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:EAL63860.1}.
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DR   EMBL; AAFI02000098; EAL63860.1; -; Genomic_DNA.
DR   RefSeq; XP_637376.1; XM_632284.1.
DR   AlphaFoldDB; Q54KQ4; -.
DR   SMR; Q54KQ4; -.
DR   STRING; 44689.Q54KQ4; -.
DR   PaxDb; 44689-DDB0233435; -.
DR   GeneID; 8625998; -.
DR   KEGG; ddi:DDB_G0287171; -.
DR   dictyBase; DDB_G0287171; -.
DR   eggNOG; KOG0298; Eukaryota.
DR   HOGENOM; CLU_001726_1_1_1; -.
DR   InParanoid; Q54KQ4; -.
DR   OMA; PTCVHRF; -.
DR   PhylomeDB; Q54KQ4; -.
DR   Reactome; R-DDI-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR   PRO; PR:Q54KQ4; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0006974; P:DNA damage response; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   CDD; cd16449; RING-HC; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR048686; SHPRH_helical_1st.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR45865:SF1; E3 UBIQUITIN-PROTEIN LIGASE SHPRH; 1.
DR   PANTHER; PTHR45865; E3 UBIQUITIN-PROTEIN LIGASE SHPRH FAMILY MEMBER; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF21325; SHPRH_helical-1st; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002195};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          762..905
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1565..1609
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          1686..1842
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          327..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          589..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1368..1391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1121..1148
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        42..104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..356
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..418
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        589..635
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1872 AA;  216509 MW;  3D91FA6F4C164425 CRC64;
     MNEINSEDEK EINYHQQNGS QGDETRNSSE SQNKRKKIQP KRLSQGQLNE KSWSNQQQQP
     HQQNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNYI IIDNDDTPMS TTPEYENEDT
     KNINDNINEL PETQKLSMGF KKRKTTYHGI LVNFEKDNSL FNKSNNNNNN GENININIGE
     VMIYSDSQIK FDKPLYLYYK YGNVGTKSDG FFTNWENSKS ISTFTADSPS NVFYCLTNLK
     ANHFINLVFL PVRDNNNSNK SRGTLISMQV YLIKESFEEY NNDPTSTHTN RSFKTVMNYF
     LKIKDLEQME IENQLLKELE EENLLHAESE KEIEKEKEKE KEKEKEKEKE IEKEQDIEMV
     DEPDNQDSSN NDHNNSLSTI DSDIFSDNNN SNSNSNSNSN SNSNSNSNSN SNSNNNNNNN
     REKKKRFIFN ITELYDNVKM DSDAVEISKS KFNGQMISTL KPYQLKAVNW MLNRELNPKI
     DFSPLSHNNK YNNNNNNNNN NNNNINNDII HPIWSRFLVD KREFFYNQFT GRLTLKEVLL
     SDKKDDLSLM GGILADEMGL GKTVEFLGLV LSHPKPDKNV IIINPPKPII NKNNNNNNNN
     NNNNNNNNNN NNNNNNNNNN NNKNNNNINN NQNNNNNEEE EEEDDNNNNN EIKKKKRKII
     KKEIILNQGE FKRLNGDIIS CICGKDEESH KRGNWVKCNS CNKFQYSSCV WASNPRYRGI
     SKFYFCTRCV TVPRDPSLTH QDDQEEYENR WDETTLVGSR ATLIVAPNTI FTQWQEEIVK
     HTNGLKVYIY NGIYKDKINP FQLADYDLVL TTYDVLSDDS ICLTQISAGK QLRYTKIPTP
     KSALKCIKWW RICLDEAQMV ESSSQTKYKK LALGLESHYR WCLTGTPIQR SLDDMFGLFE
     FLRLEPFSSR YWWNCIILHK YLALGEQSFL DWFHCIVHSV MIRNSKAMIR NELQLPNQYD
     NDTKLLRFSM VEAHYYQKKA NECSQEARLL FQKYFRGGRS IQDISISHLN SILAPLLVLR
     QTCQHFQVGG HAVKPLTMST MTMEQLLDRL IENATIEAKN HQKSVIHSLN CLAAARIIRN
     EFSIASQLYL DAINMFKSNE NHFKVDWFQE LHTFYNLNFL FKQFKNQINL IEKQIEKLSN
     KENNNNNNPN NSNNQTIEEK LKDIEKIKEI ISNITDGGKI NLDDKCEKLR NSYLQGKNHQ
     MLQNQKEFEE YHQKVNEALD EYDKNTNKSE KMPWFERALQ LIEEEENAKP GVVPNPFLKR
     VETRLFIPRN LPQFQFSIVN KFTNFFGLSL IISKHITDLL KYRVNFIKTL TPLLHSFTEK
     DVEISINCRE CCDKTQRTQN LESPVCPHCI AMDNLTLFRE KLFSKVGNQN KSRGGGGGSG
     NTSMMTIDNN GLTDEQRKDI DSIRLNIGAS ESVTDSEVEI VLKLMIPLLK QIDIDIAKEG
     EDFLKLLKIM KLELSSASES WASSKNYLNS FDEVDSSTTR ITLKYQGEII QPYQQQFKLN
     NLVEVDQFIQ RFELEKKKSI EQFKTSNGQL LYLYNLKKSN LSTKSNTNTN NNNNNSTVTD
     EKSICAICQE VFGKNVVMLL CGHSFCYDCV MFMIEKVPNC RTIQCPICRA RSNIEEISYL
     STDKENGELV DNSNVKGSYG TKIESLVQSV INIQKKSIKT IQPNIIPTTT STTTTTTTTT
     TNTNTNTTNS NINIKKDESI QKIIIFSQWA DVLEIISRAL KENEIQFAKA VHRGSSFEMA
     INQFRKDPNV NVLLLPLIKG GNGLNLIEAT HVFLVEPILN PALEKQAINR VHRFGQNKET
     NIHRFIIKNT IEEKVVQMNQ LKEQKRKNTN ENTIDLDNEQ LQKQQLLLMS GKKSKENDNI
     LSKDDIEFLI LD
//
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