ID A0A498P2Z4_LABRO Unreviewed; 2038 AA.
AC A0A498P2Z4;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=A-kinase anchor 13-like protein {ECO:0000313|EMBL:RXN38571.1};
GN ORFNames=ROHU_035909 {ECO:0000313|EMBL:RXN38571.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN38571.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN38571.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN38571.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN38571.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXN38571.1}.
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DR EMBL; QBIY01004728; RXN38571.1; -; Genomic_DNA.
DR STRING; 84645.A0A498P2Z4; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd13392; PH_AKAP13; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 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; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
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; SSF48403; Ankyrin repeat; 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.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:RXN38571.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW Transferase {ECO:0000313|EMBL:RXN38571.1}.
FT DOMAIN 1385..1578
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1619..1721
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 329..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1201..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1879..1911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..997
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1018
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1883..1902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2038 AA; 227599 MW; D080CC9DC6358D0C CRC64;
MQSMDTAFSN RWKLESGKCV LTVQLCDEAL GEGEQGEVQF FLLFTGSAQR HLTSTLKVNH
ATLQAVCPAH NCCESVLVTL CSSGPDGSIH TLATRHLDFV QDLAFDMAQF LVSTVGQTNL
LEEALLLDEH QIPLQECEKL DQSLSLALKH ITLPSGWSLL GNNTRLEPQE TLLHFAARRG
LLRVASFLLK QPGAQEALSL CNKQGATPVV IAQSRGYTAL LELFNREDLD TDVEVEALRQ
LSSSGGRVVQ HHPSLNTYTL SVGTEPGGAP PNLQADVLEL RRLILSCYQG KGGVAFQPSS
ESPHIAQECD DGLETRECCC EEAPHDSLDT REKGFTPFST EENKGEPNDR LDPSQIREGD
GGPSLSCETA PALLHNGNSE DQRACACENT ETDCREQEER SDVVSTGDVG DSSDGLQSVV
NRTASCGQQK EEADKADDLI CEALGRVEGP EGENQEKEHK FVEELKLCEC SPTVEAEDMG
ITQSLDTPES SDVESCSQGA ETDDEEEDGC EDLIDLKEVR EENKEPLDVN PDGDTPLDCS
QLNLFENEMR ACQDVCDKTD YVGTQLEGDI CENFMCNVED SRDLDSSGRV DQEEADEEFH
ETLEMPYLET DGNQQMEELS DTTSKTSFAE DESIFHLHDE KQELFAVEKT ILSIEDSVGF
DGPESSSNAL QTELAPEHGS SKDTLEDLEV LLGSGCEGTE DVQGNQENEP VCEAQASAEE
VLESAIPTDT EKVNLPDDSS LDPRQDMTSN DEVMQGTAAV DLSEEVAGVV FVNKDETGDQ
HVLVDLSDII ATSNESEIAE ESLADNAKDL LGVSVHSDHV DGALHVSNAL DEDSVILPSG
CPEKTQASLD LVSQETEALG QEAVQPMGKE DLLKDSDAGL EDQMDFQKTL LPDITDKKDA
VIHRDKDALC SSVSQKRHSL STESSQYPEF HTCNSEAVAF RDSGSDTDGF LSPDTGEDNI
FRKGQEAVGG GDSTSEVSVS CSSTDDTASV GHPSSSAESS EEVRHGGEAE EEAKDRLTEV
PLPASLFRST VRSLSPFRRH SWGPGKNQGG EEEMNQRSYS LEGLAAGIED GKRWLPQSGG
PSKDQRGIQR QESEERSSLT SLTEEGPEFN LGECTSPGGQ KSRKYHQFRH SGPSVALPLT
KSISMLSISQ RDIDGMTSFT STTSSMGYSI TEEEPGPLRG DFEKSTTKVS RTFSYLKNKM
YKKAREKEKE KNREKDREAK EREKKTVNGH VFSTSNSLHP ALCQQCNKTL NTKDTVSCTT
STLRERPWSA IFSPEEHSVI VPSRRPTSIM PFHSSNLSKS MSINNIAMFD DMPLRGRRYL
SQSTDSLHKP NKVTASTESL DEGTEMVDSR LMGEFEADVK ELEADSWSLT VDKKYLKQLK
KDVIKRQDVI YELIQTEMHH LRTLRIMADV YSKGLLTDLQ LEVQMVEKMF PMLEELLELH
SLFFSALIER KKEGKLQGTD GFIINRIGDV LFSDSNAESM KKIYGKFCSR HNEAVNFYKE
LHARDKHFQA FIRKKMSSSV VRRLGIPECI LLVTQRITKY PVLLQRVLQH TKESEKDFED
LTQALQLVKD IIASVDSKVN EHEKKRRLKE IYGRTDSKSI TRMKSGQMFA REDLQRNRKL
LHDGPLQLKN AAGRLKDVHA LLLSDVFVFL QEKDQKYVFA SLDQRATVIS LQKLIVREVA
HEERGLFLIT AGIANPEMVE VHASSREERN TWMQLIQDAM HSMKDEQIVS LLLEKMKLFR
EMCGSSDDAA SAVKMLFRAN NEDVPKGEPI MMDALKEVEM LQALVNSSLG GAVGQQVACA
QGNVGPVCLP RRAETFGGFD SHQMNICKHG DKEESEDLRR TESDSVLKKG GNANLLLLLK
RNSEAVVLQQ DTFIEDQRQA LTERTPSRPS SRPSSRPPSL VEQEKQRSLE RHRQEAAALQ
RQQAAHAEEK RRKEKEWDVK ERELTDREVL LHVKEEEMRR RHKELEEAQQ VLLGRKEDYQ
RDLERLRDAQ RRLEREKEQM QREVEKVEHL REVEVRLELH IQARFVPPYC LYVTHSQY
//
