ID E3N3V4_CAERE Unreviewed; 1658 AA.
AC E3N3V4;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CRE_24695 {ECO:0000313|EMBL:EFO85262.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DS268522; EFO85262.1; -; Genomic_DNA.
DR RefSeq; XP_003096895.1; XM_003096847.1.
DR STRING; 31234.E3N3V4; -.
DR EnsemblMetazoa; CRE24695.1; CRE24695.1; WBGene00067096.
DR eggNOG; KOG0298; Eukaryota.
DR HOGENOM; CLU_240009_0_0_1; -.
DR InParanoid; E3N3V4; -.
DR OMA; YLQPCEM; -.
DR OrthoDB; 8175at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
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); 1.
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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
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; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1397..1448
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1499..1650
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 191..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..888
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..932
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1658 AA; 192410 MW; 00B4A8A420C7C16B CRC64;
MKNKKKPQEK NWEDLPKSRV IKVLEKSVYQ PSSAQNDYIL LNSLERKFRP DYEQLLGQKA
ILFHKNASKN ALSLYLEAEP QNQSPWKGTR MYIPGTFVED MSLELEAESR FLWLLIRLCK
DTKSLTSAGI FLLYECYPPD NMRVNFYLQS NKIFNSILDY LPKMASIFKQ KIQIILKTII
QCDQIVRKKQ NRENKNESTA EADLLNEETS DSSKQRRQED LNFERFFDLC KVYKKKYSGI
IPKYKIDVDS LNFNLMPYQT ETVRWMMHRE AEGTVDENLS WMFKCEQLPN NPSFFYYPCI
GAITRNQLSQ DEYCDLAKRY TLKGGILSDE MGLGKTVQVL SLISSHRRGD TLDTENNTKK
KTKSTLSDYK IADQVRIAES SFAEMNSAKN NSTLITYNAS DYKEGETIAC SGCAENCSVS
ICGWDFEKFK DEEFYCPDCR NYMPRKPVKT TLVIVPESLI FQWFTEIAKH CSDNFRVMFY
FGVKKHGYLQ ALEMENYDVI LTTYDTLRKE LIFTKDKEQR RSLRNGFKPL HLTSSFMHVS
FWRVIVDESQ VMPQSINSNL LQMILKIEGD NWWCVTGTPL VRTVADMSPL FSFLGLFPFN
NADFFSHYVH PQYLSFALEL QSREQQLDEQ NLPHILLLEI LARIMSRKTK KDVDLQINLP
ELTEIEKKIR FSEVEERQYK EEKERLRFVV EKAIGKAIDS AHLADLSCRD KVLQELRTLR
ETVLTGQNNS SDLGSAGFVY APETVIFRLV RNKKIGIENH VRTYMNHALG LAGAQHLMLD
PVNALSVYEH CLSKFAEVVS STCMEDQIGP EVMLQLKAIT SFSDSPRTNL FDGDDEVDEA
NLIDEKDSDN KDELDRIRKI AGIVRNVKQT LHKYTKKVSN PSTSTGNVEN FEEKHEELTN
DSDDLPGPSE AKRARFDNET ENSDEKDVEM SQEALEPSTM EQSAEEANDE YEEHQRRKHA
NKMALTALKP IRMDATQEFH MFVNMRKIQN SLGVPEENRI PLSRVEMAAN RCIKLEVFCT
LFFINNLLFQ KQAAETISNV LNELTDIWAN DDKNMIHQIR EFFEMMRAHC AIRKDTEALY
ERGTEVREEI KKDHFPNLPY VALYDTNKLK PNKIKHHTKR CMGRCSKFYL ECEMFIGQPC
LKLSDIINKT MNQIVKIDDR RKTEDVKLKS CIQIVMEMSD PNLLLDLIEK KEETKTAKEK
RMLEILSCEH KLIKGTREQQ GHVQQYYHTD HPCEICDTWC KLSLFFFDSG FSSYHGEIRP
KSGVYEFATL LVNNYSPGRK EAQMFSKHYL RPFFERIHDM LKTLQNTTGI FIELVDRYKE
LSQAQTLLTD NQICAWLGDQ DEMEIPMEMK REQYAASHLA NRNDSLQAIQ KDVKELRYLT
NLVKKQFSDE NEEFEECPIC QSLINSFMVF TCGHRICPEC FDRLKVISRH EPHGYGWTTD
SIQCPSCRIR NRSQQIMLAR SGYAERDSII PGVVLSVKVT LNRINFKMFL NFQLSAAIQI
MREILDTDSS NKIIVFTSVE PSSTTVWNYL QKIFKLAKLP FSATSRYNCG KKIVDFEVSE
DVKILLCSLS LCANGLNMTG ANHIIFLDPP HLQSVLNQAI GRINRFGQKR AMRVIHLVVE
GSLDSELREI AKNTYRQEDE KKGWTIGDIR AMFNIDRD
//
