GenomeNet

Database: UniProt
Entry: A0A2B4RV69_STYPI
LinkDB: A0A2B4RV69_STYPI
Original site: A0A2B4RV69_STYPI 
ID   A0A2B4RV69_STYPI        Unreviewed;       713 AA.
AC   A0A2B4RV69;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=ERN1 {ECO:0000313|EMBL:PFX20218.1};
GN   ORFNames=AWC38_SpisGene15361 {ECO:0000313|EMBL:PFX20218.1};
OS   Stylophora pistillata (Smooth cauliflower coral).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC   Astrocoeniina; Pocilloporidae; Stylophora.
OX   NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX20218.1, ECO:0000313|Proteomes:UP000225706};
RN   [1] {ECO:0000313|Proteomes:UP000225706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA   Tambutte S., Allemand D., Aranda M.;
RT   "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT   digitifera provides evidence for extensive differences between species of
RT   corals.";
RL   bioRxiv 0:0-0(2017).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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:PFX20218.1}.
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; LSMT01000326; PFX20218.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B4RV69; -.
DR   STRING; 50429.A0A2B4RV69; -.
DR   Proteomes; UP000225706; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004521; F:RNA endonuclease activity; IEA:InterPro.
DR   GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd09769; Luminal_IRE1; 1.
DR   CDD; cd10422; RNase_Ire1; 1.
DR   Gene3D; 1.20.1440.180; KEN domain; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR045133; IRE1/2-like.
DR   InterPro; IPR010513; KEN_dom.
DR   InterPro; IPR038357; KEN_sf.
DR   InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR13954; IRE1-RELATED; 1.
DR   PANTHER; PTHR13954:SF6; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF06479; Ribonuc_2-5A; 1.
DR   SMART; SM00564; PQQ; 5.
DR   SMART; SM00580; PUG; 1.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR   PROSITE; PS51392; KEN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PFX20218.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..713
FT                   /note="non-specific serine/threonine protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012134554"
FT   TRANSMEM        483..503
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          580..708
FT                   /note="KEN"
FT                   /evidence="ECO:0000259|PROSITE:PS51392"
FT   REGION          367..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          511..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..399
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   713 AA;  80903 MW;  A02C12FD436CADFA CRC64;
     MSRYTIFGLC LGLIFFVSWH SVVASEEART LSVPESLLFI STLDGTMHAV KKQTGDVRWS
     LKEGCVFYYV LSGGLHPFGD QYRRQANIIA GEFNLEKIIN CEMFTEAKDL IRMMLKPSPS
     ESAIFIPDPK DGSLYGFGSA HDGLKKLPFT IPELVRASPC RSSDGILYTG RKTDVWYAID
     LDTGIKQQTL KLDGTETVCP IMSNKKAPVF LGRTEYMITM YDSKTREKRW NATFHDYSSH
     LAQDVDYDLH HMCSSSDGFM VTMDESTGEI LWTKNYGSPV VGIYRMDNEA LLKVKVNHIA
     KETLKHLIGA NTSSSSHQNT FLGDRGEIVL QPTLYIGEHA GGLYALPSLI EEGSPLVEAK
     VLLIEGPRSG LPKTGNPTKS SDAVSAREHS ANTSPPVRRP IQQPKVLEPK AALLLGHHQV
     PLVANPQLHI THIPDKLMPM YMHHHHLHNM KMAPKRIEKT TTKEEDRRQQ QEMFEMMKIH
     QRLLYTIIAT IGIPVVLLVL FFIERSTRQS AVSSRRSSPP SSSSSSSQRV DEQTSEQSPD
     ILTSISFLKE KKGCFRIPFA EGLRKPSAKG ILKHPFFWSR EKQLAFFQDV SDRIEKESED
     AELLVLLQKD SIPVVRGDWK VHLGSELQED LRRFRTYKGS HVRDLLRAMR NKKHHYRELP
     DHVKEALGSV PDGYMRYFSS RFPRLLMHTY NAMATCKSEP VFQTYYFQKV PLT
//
DBGET integrated database retrieval system