ID W2RTL2_9EURO Unreviewed; 1545 AA.
AC W2RTL2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF1541_05305 {ECO:0000313|EMBL:ETN39083.1};
OS Cyphellophora europaea CBS 101466.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN39083.1, ECO:0000313|Proteomes:UP000030752};
RN [1] {ECO:0000313|EMBL:ETN39083.1, ECO:0000313|Proteomes:UP000030752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN39083.1,
RC ECO:0000313|Proteomes:UP000030752};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phialophora europaea CBS 101466.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KB822721; ETN39083.1; -; Genomic_DNA.
DR RefSeq; XP_008717868.1; XM_008719646.1.
DR STRING; 1220924.W2RTL2; -.
DR GeneID; 19972644; -.
DR VEuPathDB; FungiDB:HMPREF1541_05305; -.
DR eggNOG; KOG2068; Eukaryota.
DR HOGENOM; CLU_001793_0_0_1; -.
DR InParanoid; W2RTL2; -.
DR OrthoDB; 1748at2759; -.
DR Proteomes; UP000030752; Unassembled WGS sequence.
DR GO; GO:0030014; C:CCR4-NOT complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR CDD; cd16618; mRING-HC-C4C4_CNOT4; 1.
DR CDD; cd12438; RRM_CNOT4; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR034261; CNOT4_RRM.
DR InterPro; IPR039780; Mot2.
DR InterPro; IPR039515; NOT4_mRING-HC-C4C4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR003954; RRM_dom_euk.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12603; CCR4-NOT TRANSCRIPTION COMPLEX RELATED; 1.
DR PANTHER; PTHR12603:SF0; CCR4-NOT TRANSCRIPTION COMPLEX SUBUNIT 4; 1.
DR Pfam; PF14570; zf-RING_4; 1.
DR SMART; SM00361; RRM_1; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW Reference proteome {ECO:0000313|Proteomes:UP000030752};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00723}.
FT DOMAIN 16..60
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 202..229
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 202..229
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 81..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..1232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1455..1481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1492..1526
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 255..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..990
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1455..1480
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1545 AA; 168263 MW; D945A461BBD9BE9A CRC64;
MSRSQDTVID DEEDTCPLCI EEFDLSDKNF RPCPCGYQIC QFCFNSLKTT YEKSTCPNCR
RPYDEKTIQY KIPTAEEFKA DQANKNKKQI AARRKETEKR EVETSSRRNL AGVRVKQQNL
VYVIGLVPQT KDESALLQTL RGPEYFGQYG DIDKIVVSKA KPGAPNQGVG VYVTYARKED
AALCIQTVDG SMNGDRMLRA QFGTTKYCSA FLRGETCQNK NCSFLHDAGE DGQTSSLQGE
AHAPKPKSAT IMVPPPRPES TTHSISSQPM ARQGSKDSEG HKDSTDASAL PSSASWANAP
SAAKVRRTSQ STSRDTPSPR LAHTAPTSQT QPQNPEAKGK QTAAAQPVSE PSKSIARSSL
PPTRAKSKAP SSDPIQALFD HLLETSSRPF QFVFSDACLS DEEKERLKDF PCLIDPYGGA
KRRAMQDKEE AERARLESDA KTKLEAQAKS AAEDALDDEN MGAGSLALGG EPEDNPRSSS
ARGAIGRPTA GSAFMAEQFA TMNLNPRSLT PQQRQQMALL SGNVQQAPGL QPPSQNTAFE
MSDFDRSAPQ FSQAQYDQIR SHQRHGSRYF NSETKPSGSR FQGQQQSQQQ QQQQQQQQGF
YSSGVQGPPP GLPASGTPPV SGGGMFAHGQ NFTNPGFGAG KDANTDLHMR GRSGTGAGPD
AKRELLLSLQ DNPLRSPPQS SAPAPAPGLF NPLYGQYSGA YQDPGLVKQR KKGKKHRHAN
TSSSGGGVEH LADPSIVQAR IHQGQGSNTG QGQGLYSGGN QVHDKNFPPL PVRTETQPSV
LHSRVSSFQS RSSTPRVPPG FESHVQPPIG SISGSGVATP DRKGTPVDSK IQRIVSTTVI
PAVPDLPIAP RTSTPKPSKD VTRGKEVKAP NDQVITGSGG EMNNSDISLG SPKPRMRQPA
LPDKKDPVGG QNEALTTSPA KTPPSKASAK ASSIGQKKPT KIDIPIAAKS TDVDKPTTPT
QTTALEAQSI VTPSATESPR ASTPATTTSE RERVPGPRPK TLRLTTTNTT KPVTPGVEQV
LPSATIEKST PVSTVTVPTK DPHHFPHLPS RQHSISSAPR LDKDSRPSTP MSEQSHPTST
THSRMLSEVA SRSSTPPPGG SIVGSAPERV KSKNQLKKER REKSKAKEKK PIPDQVPDGS
VAPSPVKGTP TTEEVGPIVS RQKKQKKEKT KKVYDPPSAK TSNDAKKKEE SQEKIQEQVE
NQEATKTKVE VTPEPAIIES ETPTELEPER EPIETSYTVA DFYADLAKAN APSMQALLAK
KTASFDKIFS HLLADGDITK DHPLLNPPSL TSKEYRLPGD SRKGQEYLDA HGYTTTSAFG
YVYVPRSQRR ELLDGSHIKI GEEVAANGKE DLLKNCLITP SGTVMRHLTS KEADRAIELE
DRRAYYREEY GDDVGGMHAL EARLENDDNI NLEGGPEEIV RRGESKGVIW VYEEGDDDDD
VDPGDETEEE ILEAGEYDDE EEVWEGDDDY DDDDDEEDAF DHSTNVARER KVNLHAMTHE
ELQKRIAETQ REVDASRREM ERLDKTMAKG NKDVAKFRDR TLKSL
//
