ID A0A369S9N2_9METZ Unreviewed; 1325 AA.
AC A0A369S9N2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Inhibitor of Bruton tyrosine kinase {ECO:0000313|EMBL:RDD43616.1};
GN ORFNames=TrispH2_004299 {ECO:0000313|EMBL:RDD43616.1};
OS Trichoplax sp. H2.
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=287889 {ECO:0000313|EMBL:RDD43616.1, ECO:0000313|Proteomes:UP000253843};
RN [1] {ECO:0000313|EMBL:RDD43616.1, ECO:0000313|Proteomes:UP000253843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Panama {ECO:0000313|EMBL:RDD43616.1,
RC ECO:0000313|Proteomes:UP000253843};
RC TISSUE=Whole clonal animals {ECO:0000313|EMBL:RDD43616.1};
RX PubMed=30042472; DOI=10.1038/s41598-018-29400-y;
RA Kamm K., Osigus H.J., Stadler P.F., DeSalle R., Schierwater B.;
RT "Trichoplax genomes reveal profound admixture and suggest stable wild
RT populations without bisexual reproduction.";
RL Sci. Rep. 8:11168-11168(2018).
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:RDD43616.1}.
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DR EMBL; NOWV01000036; RDD43616.1; -; Genomic_DNA.
DR STRING; 287889.A0A369S9N2; -.
DR Proteomes; UP000253843; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0003908; F:methylated-DNA-[protein]-cysteine S-methyltransferase activity; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd18500; BACK_IBtk; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR001497; MethylDNA_cys_MeTrfase_AS.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR22872:SF2; BTB_POZ DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR22872; BTK-BINDING PROTEIN-RELATED; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF00651; BTB; 2.
DR Pfam; PF00415; RCC1; 2.
DR PRINTS; PR01415; ANKYRIN.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00225; BTB; 2.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF54695; POZ domain; 2.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50097; BTB; 2.
DR PROSITE; PS00374; MGMT; 1.
DR PROSITE; PS50012; RCC1_3; 3.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Kinase {ECO:0000313|EMBL:RDD43616.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000253843};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:RDD43616.1}.
FT REPEAT 55..88
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 90..122
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 148..204
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 205..256
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 257..311
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT DOMAIN 557..625
FT /note="BTB"
FT /evidence="ECO:0000259|PROSITE:PS50097"
FT DOMAIN 731..800
FT /note="BTB"
FT /evidence="ECO:0000259|PROSITE:PS50097"
FT REGION 957..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1154..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1210..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1049
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1325 AA; 148837 MW; 93937BA5DD412337 CRC64;
MATKSNKVST WQCTSKCKLI EHGRKINEAI ATKSLISIQS SWHSCANADH QHDALGRTPL
HMAASYGRYD LVRWLIKDRK LDVNARDDES GWTPLHRCLF YGHLDVAALL VKLGADLFAE
DREGLTPLDM VLIDRKQTFP SLHLSPPAHV FTWGLNDNFT LGHAESNCRL PGRVKFITAS
QAAKTISIKQ IVMCQFHSVF LSHDGRVFTC GHGQGGRLGI ADEETTLRAS EISSITGIKI
AQIAAARDHT VLLTDKGAVY TFGMNNYHQL GQVPSPKRCL KPKQISSKHL HNKVMIGIAA
GTYHTVMHTN EELYTCGTNY GQIGHAAMER QVTLPKLVSS LSLESSTELV KRKIQIVATS
EYATACTTDV GEIYIMSDFN IRKIRIPRGQ QSIERLRLKS FAIPSNNSNS NEHRIMLFVI
CKPNFQLLSW TNEYRKLYIC KWAQKPDMHI MDIAFTEDNK KAFKESTKLS STMPSSLSLT
EICIRLNSEV IHYLDLKRVP LVHHAKQVAM DDKGSNFAVL QWDAYQGMNN RASKSESKLN
ADMAKLLQTA SLNDHIHDII IKVDGLVIPC HRFVLCSRSI AFAEILGKGA VDEATMGIYQ
IDDMSYDVAI NLLQFIYTRD CILLQRNTAY SRQEMQDLET SNSKLPLTDI ELSRKKMEHE
QASTTANYEK TKYGYIPVNV KELRRAAKHY KIPGLRESID ALYYREQFSD DLNTANIGKL
CFNHDTIQES SDFTLESNDG ETFCCHKCMF IHRSEYFFSM LSCSWKESKA GLVRLKLMIP
SDLLKCIVEY IYNDNTEVFT ESNDAEFLSN IVVAADYVRF IFRYLRVPLL LSDLKQICEW
RLSKLITLKT VITFTDFSLT YNAKLLNDAC IEFICINLGY LLEGRIFDNV TLSVLENVSD
MYKTKITGIL SRTVSFQSSH IDYTSASNDG ASFVTLESNS NVEPLKDDLP KSTVAAKSLH
TSTPTKDIHK TLPSSSGACS KIDDNTHSSA SVEDSIMSDI LAYDLSDILD TSDTLLLPAI
NQQTTNEEAS FTTTISKNNE NTNSNSVSQS NKRKKKRSQK MRKAELLKVG TAATVTAEPP
KNTPPLSKSQ PTVNTNASSR VKKWNSSQSA NSNSLLSIMA EEEEDSLHPT KPNSYQSANN
TTYNEAIKWG VAQDVKKKSN RQRNISTSSN ISLSSNETEM LASSSSKCPW GNVKQSASFS
LGDVMKQEEV ARLDGRGSNN RRVQSSSSSS KTMPSKGTSR FLDIVSSQAE ENYISFRRGK
KSLSSIQLEE KAMSELLHEY GGRYNPEEYI IVEYERPEGL FFTESPCRYK SFLFEVVFLF
IVKTS
//
