ID A0A452I1J3_9SAUR Unreviewed; 879 AA.
AC A0A452I1J3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000021372.1};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000021372.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000021372.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the MAGUK family.
CC {ECO:0000256|ARBA:ARBA00007014}.
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DR AlphaFoldDB; A0A452I1J3; -.
DR Ensembl; ENSGAGT00000024344.1; ENSGAGP00000021372.1; ENSGAGG00000015673.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd00071; GMPK; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd12081; SH3_CASK; 1.
DR CDD; cd14094; STKc_CASK; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 6.10.140.620; -; 1.
DR Gene3D; 1.10.287.650; L27 domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR035473; CASK_SH3.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR014775; L27_C.
DR InterPro; IPR004172; L27_dom.
DR InterPro; IPR036892; L27_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23122; MEMBRANE-ASSOCIATED GUANYLATE KINASE MAGUK; 1.
DR PANTHER; PTHR23122:SF40; PERIPHERAL PLASMA MEMBRANE PROTEIN CASK; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF02828; L27; 2.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00569; L27; 2.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF101288; L27 domain; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS51022; L27; 2.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..264
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 331..386
FT /note="L27"
FT /evidence="ECO:0000259|PROSITE:PS51022"
FT DOMAIN 390..443
FT /note="L27"
FT /evidence="ECO:0000259|PROSITE:PS51022"
FT DOMAIN 478..559
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 565..635
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 692..864
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
SQ SEQUENCE 879 AA; 100186 MW; E442030CC44C36D3 CRC64;
MPVILRLRGP FSVVRRCINR ETGQQFAVKI VDVAKFTSSP GLSTEDLKRE ASICHMLKHP
HIVELLETYS SDGMLYMVFE FMDGADLCFE IVKRADAGFV YSEAVASHYM RQILEALRYC
HDNNIIHRDV KPHCVLLASK ENSAPVKLGG FGVAIQLGES GLVAGGRVGT PHFMAPEVVK
REPYGKPVDV WGCGVILFIL LSGCLPFYGT KERLFEGIIK GKYKMNPRQW SHISESAKDL
VRRMLMLDPA ERITVYEALN HPWLKERDRY AYKIHLPETV EQLRKFNARR KLKGAVLAAV
SSHKFNSFYG DPPEELPDFS EDPTSSGLLA AERAVSQVLD SLEEIHALTD CSEKDLDFLH
SVFQDQHLHT LLDLYDKINT KSSPQIRNPP SDAVQRAKEV LEEISCYPEN NDAKELKRIL
TQPHFMALLQ THDVVAHEVY SDEALRVTPP PTSPYLNGDS PESANGDMDM ENVTRVRLVQ
FQKNTDEPMG ITLKMNELNH CIVARIMHGG MIHRQGTLHV GDEIREINGI SVANQTVEQL
QKMLREMRGS ITFKIVPSYR TQSSSCEIYV RAQFEYDPAK DDLIPCKEAG IRFRVGDIIQ
IISKDDHNWW QGKLENSKNG TAGLIPSPEL QEWRVACIAM EKTKQEQQAS CTWFGKKKKQ
YKDKYLAKHN AVFDQLDLVT YEEVVKLPAF KRKTLVLLGA HGVGRRHIKN TLITKHPDRF
AYPIPHTTRP PKKDEENGKN YYFVSHDQMM QDISNNEYLE YGSHEDAMYG TKLETIRKIH
EQGLIAILDV EPQALKVLRT AEFAPFVVFI AAPTITLGIN EDESLQRLQK ESEILQRTYA
HYFDLTIINN EIDETIRHLE EAIELVCTAS QWVPVSWVY
//
