ID A0A093LJX1_FULGA Unreviewed; 1037 AA.
AC A0A093LJX1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=A-kinase anchor protein 13 {ECO:0000313|EMBL:KFW09231.1};
DE Flags: Fragment;
GN ORFNames=N327_07701 {ECO:0000313|EMBL:KFW09231.1};
OS Fulmarus glacialis (Northern fulmar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Procellariiformes; Procellariidae;
OC Fulmarus.
OX NCBI_TaxID=30455 {ECO:0000313|EMBL:KFW09231.1, ECO:0000313|Proteomes:UP000053806};
RN [1] {ECO:0000313|EMBL:KFW09231.1, ECO:0000313|Proteomes:UP000053806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N327 {ECO:0000313|EMBL:KFW09231.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; KK606126; KFW09231.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093LJX1; -.
DR Proteomes; UP000053806; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20878; C1_AKAP13; 1.
DR CDD; cd13392; PH_AKAP13; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR13944:SF18; A-KINASE ANCHOR PROTEIN 13; 1.
DR PANTHER; PTHR13944; AGAP007712-PA; 1.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Kinase {ECO:0000313|EMBL:KFW09231.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053806};
KW Transferase {ECO:0000313|EMBL:KFW09231.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 29..75
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 229..426
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 466..568
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 802..836
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 862..913
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 927..945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..990
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW09231.1"
FT NON_TER 1037
FT /evidence="ECO:0000313|EMBL:KFW09231.1"
SQ SEQUENCE 1037 AA; 118970 MW; CE9E34AAFEC40596 CRC64;
QEKEKDKEKT KEKDKDSKEK ERDKKLLNGH LFTATSVVAQ ATCYHCMKPF NKDSYYCANC
NAIVHKGCKE SFASCAKVKM KPQRGMLQAH DTSSLPTVTM RNKSSQPKER PRSAILAPDE
NTVTSIFNNR RSQQTTALSK SVSIQNIAGV GNDDSLIHTW KFLSQSTDSL HKISRVNESM
ESLVDEGADM NEGQLMGDLE LDSKQLEAES WSQVVDSKFL QQQNKDVVKR QDVIYELMQT
EMHHVRTLKI MNDVYSAGML KELQYDQQVV DKIFPCLENL LHIHSHFFQR ILERKKESLA
DKSEKNFVIK RIGDILVNQF SGESAERMKK TYGKFCGHHN EAVNNFKDLY SKDKRFQAFV
KKKMSSSLVR RLGISECILL VTQRITKYPV LLQRILQYTK ENEVEHEDLT QSLNLVKDVI
AAVNSKVSNY EKKMRLGEIY NRTDSKSIMR MKSGQMFARE DLRHRKLIRD GPVSLKNAAG
RLKEVQAVLL SDMLVFLQEK DQKYVFASLD QKSTVISLKK LIVREVAHEE KGLFLISMGV
KDPEMVEVHA SSKEERNGWI QIIQDTMNTM DKDEDEGVPC ESEFEKKVSD AKVRGLKEQL
QKKDKQILLL LEEKAKIFRD MADSSVQEDM PGSRLLFRAN TEEAPKGEAI MKTAINEVEL
LQDLVNRSLG TALGQQVSSS AMEQEGGVGP ISLPRRAETF GGFDSHQMNA SKCGAKDEGD
DAQDLRRTES DSILKKGGNA NLMFMLKRNN EQVLQTITSL HKLLSALQGV VLQQDTYIED
QKLALSERAL TRSFFRPTSL LEQEKQRNLE KQRQELANLK KQQTQHQEER RRREKEWEVR
EKELAEQEAH LAQREEQVQR GWQDLEREQE ELQVKKASYQ LDLERLRTAQ KQLEREKAQF
KQDVERLAQM RQEPDHNQVS NLHEKLARVA SQSSIDDSSK KSPSLPKQGH FDAELSVSPK
RNSLSRTHKE KSTFHLLSTT NQTNKAAEEQ PQMPTRLFSL AKPKEKKEKK KKGRGHRSQQ
SDSHSSEAPP EGEEIFC
//
