ID A0A093QT63_PHACA Unreviewed; 960 AA.
AC A0A093QT63;
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=N336_03489 {ECO:0000313|EMBL:KFW91741.1};
OS Phalacrocorax carbo (Great cormorant) (Pelecanus carbo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Suliformes; Phalacrocoracidae;
OC Phalacrocorax.
OX NCBI_TaxID=9209 {ECO:0000313|EMBL:KFW91741.1, ECO:0000313|Proteomes:UP000053238};
RN [1] {ECO:0000313|EMBL:KFW91741.1, ECO:0000313|Proteomes:UP000053238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N336 {ECO:0000313|EMBL:KFW91741.1};
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; KL431401; KFW91741.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093QT63; -.
DR Proteomes; UP000053238; 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; 4.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 4.
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:KFW91741.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000053238};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:KFW91741.1}.
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 917..960
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 272..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..879
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 278..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..593
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW91741.1"
FT NON_TER 960
FT /evidence="ECO:0000313|EMBL:KFW91741.1"
SQ SEQUENCE 960 AA; 104786 MW; E5ABB209D6A0BE20 CRC64;
GKVINKDLRH YLSLQFQKGS IDHKLQQVIR DNLYLRTIPC TTRAPRDGEV PGVDYNFIPV
EQFKALEESG ALLESGTYDG NFYGTPKPPA EPSPFQPDPV DQVLFDNDFD TESQRKRTTS
VSKMQRMDSS LPEEEEEEEK EAVNGSGGIE NKEKHSDSPD WMKPVPSYNQ TSSSMDFRNY
LSRDETLEPL PKNWEMAYTD TGMIYFIDHN TKTTTWLDPR LCKKAKAPED CEDGELPYGW
EKIEDPQYGT YYVDHINQKT QFENPVLEAK RKKQLGQTDV GPSKSGPEKS VFTRDPSQLT
GALIRTSLKK STMGFGFTII GGDRPDEFLQ VKNVLKDGPA AQDGRIAPGD VIVDINGSCV
LGHTHADVVQ MFQLVPVNQY VNMTLCRGYP LPDDNEDPVV DIVTATPIIN GPPVTKGDVC
VTSQDLVAGT VVLDQNGKMG PMLVNGRLNG PSMDTAEQRI SLASSGGSQP ELVTIPLVKG
PKGFGFAIAD SPTGQKVKMI LDSQWCQGLQ KGDVIKEICH QNVQSLTHLQ VVEVLKQFPV
GAEVPLLILR GGPPSPTKTT KGKDKQDSSG SLEAVGDPIP QPMPFPPTAV RPGSPKLDPS
EVYLKSKTIY EDKPPNTRDL DVFLRKQESG FGFRVLGGDG PDQPIYIGAI IPLGAAEKDG
RLRAADELMC IDGVPVKGKS HKQVLDLMTS AARNGQVLLT VRRKIFFGGE KQPEEEESQP
VLTQNGSPRL NRVEFANQQS PEGYDVRLQR KENEGFGFVI LTSKNKPPPG VIPHKIGRVI
DGSPADQCGK LKVGDRISAV NGQSIVELSH DSIVQLIKDA GNVVSLTVVA EEEHRGPPSG
TNSARQSPAP QHRPLAPAPI SPASADRGAT EGEAGKEVSN SYRLSWPEHK HLAQSDAGVA
SAIGSRHSQA QNPGCFPVEL ERGPRGFGFS LRGGKEYNMG LFILRLAEDG PAVKDGRVHV
//
