ID A0A091MNP7_9PASS Unreviewed; 1069 AA.
AC A0A091MNP7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3 {ECO:0000256|ARBA:ARBA00016171};
DE AltName: Full=Membrane-associated guanylate kinase inverted 3 {ECO:0000256|ARBA:ARBA00033438};
DE Flags: Fragment;
GN ORFNames=N310_08744 {ECO:0000313|EMBL:KFP78248.1};
OS Acanthisitta chloris (rifleman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC Acanthisitta.
OX NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP78248.1, ECO:0000313|Proteomes:UP000053537};
RN [1] {ECO:0000313|EMBL:KFP78248.1, ECO:0000313|Proteomes:UP000053537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP78248.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the MAGUK family.
CC {ECO:0000256|ARBA:ARBA00007014}.
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DR EMBL; KK833426; KFP78248.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091MNP7; -.
DR Proteomes; UP000053537; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00992; PDZ_signaling; 5.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.20.70.10; -; 2.
DR Gene3D; 2.30.42.10; -; 5.
DR Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR10316; MEMBRANE ASSOCIATED GUANYLATE KINASE-RELATED; 1.
DR PANTHER; PTHR10316:SF10; MEMBRANE-ASSOCIATED GUANYLATE KINASE, WW AND PDZ DOMAIN-CONTAINING PROTEIN 3; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 5.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 5.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 5.
DR SUPFAM; SSF51045; WW domain; 2.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 5.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:KFP78248.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000053537};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:KFP78248.1}.
FT DOMAIN 9..85
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 188..221
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 234..267
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 305..373
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 474..537
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 621..703
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 745..832
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 912..994
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 77..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP78248.1"
FT NON_TER 1069
FT /evidence="ECO:0000313|EMBL:KFP78248.1"
SQ SEQUENCE 1069 AA; 116394 MW; DB6989F1ABEC63A0 CRC64;
GKVINKDLRH YLSLQFQKGS IDHKLQQVIR DNLYLRTIPC TTRAPRDGEV PGVDYNFIPV
EQFKALEESG ALLESGTYDG NFYGTPKPPA EPSPFQPDPV DQVLFDNDFD TESQRKRTTS
VSKMQRMESS LPEEEEEEEK EAVNGSGGIE NKEKHSDSPD WMKPVPSYNQ TSSNMDFRNY
LSRDETLEPL PKNWEMAYTD TGMIYFIDHN TKTTTWLDPR LCKKAKAPED CEDGELPYGW
EKIEDPQYGT YYVDHINQKT QFENPVLEAK RKKQLGQTDA GTSKPGPGKS VFTRDPSQLT
GALIRTSLKK STMGFGFTII GGDRPDEFLQ VKNVLKDGPA AQDGRIAPGD VIVDINGSCV
LGHTHADVVQ MFQLVPVNQY VNMTLCRGYP LPDDTEDNVV DIVTATPIIN GPPVAKGDVS
VPSQELIAGT VVLDQNGKMG PMLVNGRLNG PSLDTAEQRI SLASSGGSQP ELVTIPLVKG
PKGFGFAIAD SPTGQKVKMI LDSQWCQGLQ KGDVIKEICH QNVQSLTHLQ VVEVLKQFPV
GAEVPLLILR GGPPSPTKSA KGKDKQDSSG SLEAVSDPIP QPMPFPPSAV RSGSPKLDPS
EVYLKSKTLY EDKPPNTRDL DVFLRKQESG FGFRVLGGDG PDQPIYIGAI IPLGAAEKDG
RLRAADELMC IDGVPVKGKS HKQVLDLMTS AARNGQVLLT VRRKIFFGGE KQAEEEEAQP
GLAQNGSPRP NRVEFTNQPC PEVYDVRLQR KENEGFGFVI LTSKNKPPPG VIPHKIGRVI
EGSPADQCGK LKVGDRISAV NGQSIVELSH DSIVQLIKDA GNVVTLTVVA EEEHRGPPSG
TNSARQSPAP QHRALGPAQL STDRGATEGE AGKEVSGAYR LSWPEHKHVV QSDAGAAAVV
GSRHSQSPGC FPVELERGPR GFGFSLRGGK EYNMGLFILR LAEDGPAVKD GRVHVGDQIV
EINGEPTQGI THTRAIELIQ AGGNKVLLLL RPGTGLIPDH SDWDSYNPSS SNVIYEEQSP
LPPSSHSASP SEVCYFPVPG ETLSRVQLSE ELEQAENTVP DKISTLTEN
//
