ID A0A1R2D524_9CILI Unreviewed; 952 AA.
AC A0A1R2D524;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=ARID domain-containing protein {ECO:0000259|PROSITE:PS51011};
GN ORFNames=SteCoe_10 {ECO:0000313|EMBL:OMJ96286.1};
OS Stentor coeruleus.
OC Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC Heterotrichea; Heterotrichida; Stentoridae; Stentor.
OX NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ96286.1, ECO:0000313|Proteomes:UP000187209};
RN [1] {ECO:0000313|EMBL:OMJ96286.1, ECO:0000313|Proteomes:UP000187209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM001 {ECO:0000313|EMBL:OMJ96286.1};
RA Slabodnick M., Ruby J.G., Reiff S.B., Swart E.C., Gosai S., Prabakaran S.,
RA Witkowska E., Larue G.E., Fisher S., Freeman R.M., Gunawardena J., Chu W.,
RA Stover N.A., Gregory B.D., Nowacki M., Derisi J., Roy S.W., Marshall W.F.,
RA Sood P.;
RT "The macronuclear genome of Stentor coeruleus: a giant cell with tiny
RT introns.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the alkB family.
CC {ECO:0000256|ARBA:ARBA00007879}.
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:OMJ96286.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MPUH01000001; OMJ96286.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R2D524; -.
DR OrthoDB; 179931at2759; -.
DR Proteomes; UP000187209; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035515; F:oxidative RNA demethylase activity; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0035553; P:oxidative single-stranded RNA demethylation; IEA:InterPro.
DR CDD; cd16100; ARID; 1.
DR Gene3D; 2.60.120.590; Alpha-ketoglutarate-dependent dioxygenase AlkB-like; 1.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR InterPro; IPR037151; AlkB-like_sf.
DR InterPro; IPR032860; ALKBH5.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR PANTHER; PTHR32074; RNA DEMETHYLASE ALKBH5; 1.
DR PANTHER; PTHR32074:SF2; RNA DEMETHYLASE ALKBH5; 1.
DR Pfam; PF01388; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51011; ARID; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000187209}.
FT DOMAIN 52..145
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
SQ SEQUENCE 952 AA; 109998 MW; DC7B27536EEBEF7D CRC64;
MGTEIRTESV RQQEKAILDK ENPKSAIEMP LNKIPVNKCI CGCNAPMLYA KRDCKIPYSN
ARENFTVILN TFFKHNPIPA LVSEEQPIDL YDFFHIIQKV KKECGRVSWR RVSKSLGVFK
SSSEFRRPLR KYYKRFLRNF EDWLKDKGPV SIGCIDTSLV IIILKEFLPN FINQKPAHES
VSTEQTSPVS QENSNSEIAD LIDYLISEIE AGKVIMKKRK IEEDPPETKK PISKDPIFII
YRKNKEEKKP TIQKVKKVKP PKEKKVEKVP KDLPKLDIVN PMTDEYRSKD PALMGYRTDF
RKGYLPIEMQ EEHEKMEKVQ AERDSKAHFI RKKQSAVNIK RSCGVTYVKP TESKQLGVRH
EFPPLPPLAF QVGTVDRIIP QDEKTQYFNL AKDIIKEIFE SNKLIRTTIQ LGFSEEDLKK
YIIGEKPDGE EVFIKGPKEL WRMLGKDNFV VLHFNADERT LFTPLGPGQF GNCKIGFLVK
KGLCGTRSVK RCLCLPEKDD DPLNMYATQI RLELYITKSL WKNALSTTRK LLCAFIAEFE
GYIQKLLPEW NDLRENIFKT KIIPEGETIY KALDQCSCPK DMTPTPPKSF WEYKSNIRPG
NLDKCPSCLK TLYEQVKTYS KGIEGIFESK SSPNWFYLIN TRDSFSYDLK VKKSYIQYKD
RRITKKVYMF HKDDLPSNYK DWDKFLEGDY VRTGVVAFKN CFTHEELKDL EQEALNTEAN
FLKGQFINST AQPSFGAGGK IKRTKFFFGT RYMWTSHQLA EKQSKIAAGV RIDVSETPAW
MRTKIENPLV EAGIIEKGFI NSIAMNIYHD GKEGLAQHFD DAVRFKQPIY TVKLDSDARL
SFGSQFYGYL NGAFCIPCPR GAVCMMEEFS YAANSAKHCV RPCDLAGRSI TIIMRQIHPF
IMEEARRYDE EIDLPTWFST LSLDDNSVPY SKQKEMQAKI MMKEDGAPKS SY
//
