ID A0A093JXU1_STRCA Unreviewed; 1257 AA.
AC A0A093JXU1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1 {ECO:0000313|EMBL:KFV83274.1};
DE Flags: Fragment;
GN ORFNames=N308_01281 {ECO:0000313|EMBL:KFV83274.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV83274.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV83274.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV83274.1};
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}.
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DR EMBL; KL206550; KFV83274.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093JXU1; -.
DR STRING; 441894.ENSSCUP00000014657; -.
DR Proteomes; UP000053584; 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:SF12; MEMBRANE-ASSOCIATED GUANYLATE KINASE, WW AND PDZ DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF16663; MAGI_u1; 1.
DR Pfam; PF16666; MAGI_u5; 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 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KFV83274.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000053584};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:KFV83274.1}.
FT DOMAIN 1..45
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 159..192
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 219..252
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 337..406
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 508..586
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 713..795
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 870..966
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1025..1107
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 41..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..854
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV83274.1"
FT NON_TER 1257
FT /evidence="ECO:0000313|EMBL:KFV83274.1"
SQ SEQUENCE 1257 AA; 137605 MW; 611546B7E56183F4 CRC64;
TTRPPREGEV PGVDYNFLTV QEFLELERSG TLLEVGTYEG NYYGTPKPPS QPVSGKVTST
DALQNLQSGS KQSTPKRTKS YNDMQNAGIV HTENEEEDDV PEMSSSFTAE SGDQGEHNTH
ITRERAPPSV IDSHTNVPTT EPSQNLPQYL PPSAEDNLGP LPENWEMAYT ENGEVYFIDH
NTKTTSWLDP RCLNKQQKPL EECEDDEEGV HTEELDSELE LPAGWEKIED PVYGVYYVDH
INRKTQYENP VLEAKRKKQL EQQQQPPEGW HQGGAVVKQV TFPSLPSLEW TEECPSLPPP
AAPNHVSNNQ EAVREAPVQG KPFFTRNPSE LKGKFIHTKL RKSSRGFGFT VVGGDEPDEF
LQIKSLVLDG PAALDGKMET GDVIVSVNDT CVLGHTHAQV VKIFQSIPIG ASVDLELCRG
YPLPFDPDDP NTSLVTSVAI LDKEPIIVNG QENYDSPASH SSKTGKVNGT KEARPSSPAE
VSSNGSHGYP NDTVSLASSI ATQPELITVH IVKGPMGFGF TIADSPGGGG QRVKQIVDSP
RCRGLKEGDL IVEVNKKNVQ SLTHNQVVDM LIECPKGSEV TLLVQRGGLP VPKKSPKSQP
LERKDSQNSS QHSVSSHRSG HTASPVHSTQ VLPDYAASEA PAADQPDSSG QKKPDPFKIW
AQSRSMYESR PMSPSPAAGL SKGEREREIN STSFGECKTV PRMYLFPDYQ EQDIFLWRKE
TGFGFRILGG NEPGEPIYIG HIVPLGAADA DGRLRSGDEL ICVDGTPVVG KSHQLVVQLM
QQAAKQGHVN LTVRRKVVYT VPKAENEVPS PASSHHSSNQ PASLTEEKRT PQGSQNSLNT
VSSGSGSTSG IGSGGGGGSG VVSTVVQPYD VEIRRGENEG FGFVIVSSVS RPEAGTTFAG
NACVAMPHKI GRIIEGSPAD RCGKLKVGDR ILAVNGCSIT NKSHSDIVNL IKEAGNTVTL
RIIPGDESSN ATLLTNAEKI ATITTTHTPQ QIPQESSRNN AKPKQESQFD FKPPQAAQQD
QDFYTVELER GAKGFGFSLR GGREYNMDLY VLRLAEDGPA ERCGKMRIGD EILEINGETT
KNMKHARAIE LIKNGGRRVR LFLKRGDGSV PEYDPSSDRN SPATGSQNVP EMRAAPSDRR
QHPSSESSYP PDLHKSSPHG DKRTYVRDLK GSREASRHPN EHHTWNGTSK TTGSVPGRRT
ERSPERRRDG QPERLVVVNG QKRRPPEKRR EGTRSADTTL ERRERPERRR DPSPERR
//
