ID A0A093GV55_TYTAL Unreviewed; 822 AA.
AC A0A093GV55;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Obscurin {ECO:0000313|EMBL:KFV46418.1};
DE Flags: Fragment;
GN ORFNames=N341_04754 {ECO:0000313|EMBL:KFV46418.1};
OS Tyto alba (Barn owl).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto.
OX NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV46418.1, ECO:0000313|Proteomes:UP000054190};
RN [1] {ECO:0000313|EMBL:KFV46418.1, ECO:0000313|Proteomes:UP000054190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV46418.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KK376978; KFV46418.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093GV55; -.
DR Proteomes; UP000054190; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20971; IgI_1_Titin-A168_like; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR35971:SF4; OBSCURIN; 1.
DR PANTHER; PTHR35971; SI:DKEY-31G6.6; 1.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000054190};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 1..75
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 93..202
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 212..302
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 306..396
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT REGION 440..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV46418.1"
FT NON_TER 822
FT /evidence="ECO:0000313|EMBL:KFV46418.1"
SQ SEQUENCE 822 AA; 91851 MW; 81C1C45DB256074A CRC64;
IFQRYTDEIL TNEDPSQPLI PPLQHYLEKP INKIQQYQTI IKELIRNKAR NSQNCTLLEQ
AYAIVSALTR RAENNLHVSL IENYPGTLES LGEPIRQGHF IVWEGAPGAR MAWKGHKRHV
FLFKNYIVIC KPKRDTKTDT YSYIFKNIMK LNNIDVNDLV EGDDRAFEIW HEREDLVRKY
LLQARTVIIK NSWVKEICGI QQRISEPVWI PPDFEEELAD CTAELGETVK LACKVTGAPK
PSVSWYKDGK PVEVDPHHII IEDPDGSCTL ILDNLMGLDS GQYMCFASSP AGNASTLGKI
LVQVPPRFVN KVRNAYFVEG EDAQFTCTIE GAPRPQIRWY KDGVLLKDTS KYQTFSEPRS
GIIVLVVKNP SNEDMGHYEC ELVNRLGSAK SGAELYHHSA AALTQERRGD QAITIEVTEQ
ETKVPKKTII IEETITTVVK SPRQRGRVSP ARSSSGHSPS RSPRADPTPE PVFVSKIRQP
VHRHEQEATP KSAVPMLFVT EPEDRQGAAA RDVVIETKVE EKKPKWVEVE EIIEFKVKKS
PKPARKRGSS PVKQEKDDSG VLTFTFPSSR PRRSPEDDPN TNNSNNKLVE QSKSLPNDSL
SEADIQPVVY ATEQEEPQVS SEDRSSPCGS DIASPLLACG EEDNVIIVDE PEELQTDDIS
TRDRKILTHN GKVLTLEDLE DYVPEEGETY GCDDQNHTAE KPCEISVLQT EINEPTIGQR
FFSQFEEHVP GGMFMSTSRV TGVQSVGPSN ISFHVSDTCL SMTPGVHAAT AVASPLPSIT
VKPSFCTEVQ LSADNGQSSF KTEVSTRTLS YGTVGEPVTL HI
//
