ID A0A2B4RC39_STYPI Unreviewed; 1992 AA.
AC A0A2B4RC39;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Deleted in malignant brain tumors 1 protein {ECO:0000313|EMBL:PFX14349.1};
GN Name=DMBT1 {ECO:0000313|EMBL:PFX14349.1};
GN ORFNames=AWC38_SpisGene21499 {ECO:0000313|EMBL:PFX14349.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX14349.1, 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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:PFX14349.1}.
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DR EMBL; LSMT01000794; PFX14349.1; -; Genomic_DNA.
DR STRING; 50429.A0A2B4RC39; -.
DR EnsemblMetazoa; XM_022952153.1; XP_022807888.1; LOC111344886.
DR Proteomes; UP000225706; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR Gene3D; 3.10.250.10; SRCR-like domain; 8.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR PANTHER; PTHR19331:SF487; DELETED IN MALIGNANT BRAIN TUMORS 1 PROTEIN-LIKE-RELATED; 1.
DR PANTHER; PTHR19331; SCAVENGER RECEPTOR DOMAIN-CONTAINING; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00530; SRCR; 8.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00202; SR; 8.
DR SUPFAM; SSF54277; CAD & PB1 domains; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR SUPFAM; SSF56487; SRCR-like; 8.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50287; SRCR_2; 8.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1992
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012044136"
FT TRANSMEM 1811..1834
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 504..1015
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 742..842
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 852..949
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 1024..1133
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 1145..1246
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 1259..1362
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 1412..1518
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 1529..1639
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 1651..1761
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT REGION 63..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1867..1888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1900..1992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1869..1886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1939..1953
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1955..1992
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 533
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT DISULFID 780..841
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 810..820
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 917..927
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 1094..1104
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 1184..1245
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 1215..1225
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 1329..1339
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 1486..1496
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 1599..1609
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 1720..1730
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 1992 AA; 219054 MW; EAA5F4E093523EE7 CRC64;
MRLPLNAVIF LTLGLGKLSF TSSSENKTQT QKLTFEKVKK NIGIFLSQPG ASERFGNMTL
SEFAEFQQSK ENQEDARKPS SRKKKQKITA QIPTVMSKST MATPTPETTT RKSTITEPAI
ITKPSTKKST NAKQTTTKST TTESTTTKSM TTKSTTPKST TTASTATIPA TNKPTAKPEV
TKTTKASQLT ISEPTAKLTT TNPTTKAGTK AKAATTKPST KKSTIAEQKT AKETTTNQTT
ATAKNAEATA TKPVITNETN ETEPTTVSSK GADKSNSTLE NSGDAQQQAN TEDLPVGVNK
ISINYNGMKT KNRKCKKNGT NESVFIKGEG SRGVEGIAWE GREEDPRSNM RNCEANSKLK
PTPTKGEAVD WTVHQNIIFR DVLEAISQVM PHATATAFEY EDEEGDRITV RGDEELQAMI
NGHTWMNCER QRRGVSPEPL IVYPKACRTS RRRNFCGLTV NTKAAAVNNA VPTNASLPTE
SSHKPERGDI QIILENGQVS HTDIQYLDIL GHGNGGTVYR ALHTSTSRII AVKVIPLDVT
PDVQKQIISE LEILFQLVNS IATTYVGTHA YMAPERIQGD EYSIRSELWS LXGGSLDQYG
CIPEPVLGRI AVSVVKGLLY LWELKIMHRD VKPSNILVST RGQVKLCDFG VSRQLVNSIA
TTYVGTHAYM APERIQGDEY SIRSELWSLG VSLLEVKKIS KVFYLELSFF IKQIKLDCDK
SLSFISTTDG FGKVSLPNGM LVRLRGSPSS NMGRVEVYYG GIWGSIYASG WDIKDATAVC
RQLGYVTASL AGRQLFCSIT LPPLFSNFRC YGNESALDQC AWDFFVYSWS SAYSNCANVR
CSNSMAGSGM LVRLRGSPSS NMGRVEVYYQ GIWGSIYASG WDIKDATIVC RQLGYTAASL
AGSRLFCSST LFSNFRCYGN ESALDQCAWD FYVYSWSSAY SYCANVMCSN TIRAGSGMLV
RLRGSPSSNM GRVENPPRLP EDKFSPAFVD FVSQCMQKNP ISRLTPEAVL AHPFIASNDD
DFNVRLTGSR FTFAGTIEVM FYGVWGGVLG QGYVDINAGH VVCRQLGYPG ADYIFQYADF
GRLNGPLWIW RIRCNGNESS ISNCAVTTWD KITSVWSHIY YQRPYFAAGV LCRQANFNPS
QNAGIRLTGS NVTFAGRVEV LSYGVWGRID GSSSWDRTEA EVVCRQLGFP GVVTALRYSP
FGEASGPVLM SNVRCIGNEK TLKQCQYNDW LKINVYQNRE AGVICKTPEV STDIRDISIR
LRGSSIPNAG RVEVLYAGIW GAISGTNWDV NDAKVVCRQL GYQAGPEIAS ANGVYGPVSG
PVWITNLQCY GSEANLMSCS HDAIGNKSET QNRWNVAGVI CKNSSHTNSR WCYGNESALD
QCIWDFTPPT WSGSYCANVM CSNGRADSGF DIRLTNSSVR HAGRIELRIH GVWGTLHSHY
YDIHYINVDG VICRQLNFSD SILAVGRAAF GPGTGPQWYD TWDIDCLGYK SNLQNCTHYS
QPRLTIYNRE DDLSVICKPS AAQANDFEVR LTGSRLNFAG KIEVMYYGVW GGVLGIGYID
INVGHVVCRQ LGYPGADEIF QYAAFGQLKG LLWIGMIRCV GNESNISDCV VSTWEDPSIP
YWIRSYYQNP FYAAGVLCRQ ANFNSTQMLN VRLTGAPISN AGRVEVFYAG DWGTVDSWGW
DINAAHVVCR QLGYPASLSS GYNNQFGSST GPRWFRNLRC FGNETNLGEC TKYVYGYPSR
GSSAATALCK LPYQAAVRPC QSHPCTNNSF CHDNETHYSC VINEAENPAS LATSDGSSQK
QNGSTTSKTT FIIILSILAS LVFLLIAAVI YLIFQNRRLS TLKARNQHAN FSNMAFRSDK
EETNNCDEID LGTGANQSSI PTRDNTNPLY EIAPFHETTT SRALPPIPPP HKAARMNPQA
AREKANRRNG GVKTRGAAEG PKRTTRGAEE HYMALSKENN STASRNISAD GGPNPNEYMS
LSQNRHTDIS HS
//
