ID A0A060W9J5_ONCMY Unreviewed; 2051 AA.
AC A0A060W9J5;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CDQ63988.1};
GN ORFNames=GSONMT00070190001 {ECO:0000313|EMBL:CDQ63988.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ63988.1, ECO:0000313|Proteomes:UP000193380};
RN [1] {ECO:0000313|EMBL:CDQ63988.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24755649; DOI=10.1038/ncomms4657;
RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA Guiguen Y.;
RT "The rainbow trout genome provides novel insights into evolution after
RT whole-genome duplication in vertebrates.";
RL Nat. Commun. 5:3657-3657(2014).
RN [2] {ECO:0000313|EMBL:CDQ63988.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FR904456; CDQ63988.1; -; Genomic_DNA.
DR STRING; 8022.A0A060W9J5; -.
DR PaxDb; 8022-A0A060W9J5; -.
DR Proteomes; UP000193380; Unassembled WGS sequence.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR CDD; cd01671; CARD; 1.
DR CDD; cd00992; PDZ_signaling; 4.
DR CDD; cd11860; SH3_DLG5; 1.
DR Gene3D; 2.30.42.10; -; 4.
DR Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR006907; DLG5_N.
DR InterPro; IPR035537; DLG5_SH3.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR46360; DISKS LARGE HOMOLOG 5; 1.
DR PANTHER; PTHR46360:SF1; DISKS LARGE HOMOLOG 5; 1.
DR Pfam; PF16610; dbPDZ_assoc; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 4.
DR Pfam; PF04822; Takusan; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 4.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF47986; DEATH domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 4.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50209; CARD; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 4.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000193380};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443}.
FT DOMAIN 1..92
FT /note="CARD"
FT /evidence="ECO:0000259|PROSITE:PS50209"
FT DOMAIN 703..793
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 788..884
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1474..1553
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1634..1715
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1871..2037
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 102..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1095..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1291..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1558..1616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 149..484
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 515..675
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 102..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..945
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1171..1196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1222..1236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1325..1365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1382..1403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2051 AA; 230732 MW; 70DED530DABB1656 CRC64;
MEPKHKELLE QFHQNLLDSI TDADRLIELL ILSGTLSQLD RFELDQNCSS SAEKVDQLLK
MLVNKESDHF LELCVALEKA YPDLYSALFT NGGGPVDHSS GSTYSVLSTM PSDSESSSSL
SSVGSPPGNG SASSPPPVVN DNRPAGDNLD TILFQLRQVT RERDELRKRL ALASPGTTFD
DCRPNSKASH DYERLKSQCM RAMADLQSLQ NQHTKTLKRC EEAVKEADFY HMLHSRVLGD
QSQLKEELDV LRRDNTQLVR EHNHLKQSCE ELRRLHSEDQ KEVADMRRQQ QEVMRENGSS
EVLNKLYDTA MDKLEGVRKE YDSLSKRYSE KVANHNTDLS RLEQVEEENR RLQKQMDTLL
RQRDTAIHYQ QQCSTSMRRF DSVQQELNKS SGQNKELQRE MERLQSEVTR CKNFQLKAVK
DCEKYKEERD SVFNEYRLIM SERDQVIKEL DKLQTELEAA EARLKNTSSE RMVASEEMEA
LRQVQELNSS LVDRDRAICE RNELLEKYCH EVKDKAEAQK ELSQACKDIE TVREERDVAR
KERTEAIIQR DQLLREYYQA RQKQDSATLD IERANKEIEV LRKQYEAMSQ ELKEATQEAE
VAKCRRDWAF QERDKIVAER ESIRTLCDNL RRERDRAVSD LADALRNLDD MRKQKNDASR
ELKELKEKME SQLDKEARFC QLMAHSSHDS AIDTDSLEWE TEVVEFEKDR DDMDLKALGF
DIAEGVNDPY LPGDCGIFVT RVDKGSIADG RLRVNDWLLK INDMDLTNKD RKQVVKAVLN
RGGLINMVVR RRKSLGGRLV TPVHINLIGH KVTAIKNSGG GGGNGVFVTA LVQGSPASRE
GSLTVGDRLI AINGIALDNK SVTECETLLR NCRDSLSLSL MKFFPHSSSG QNIFDSLRES
SSNSRLSEVH SRNSRNLKHN SSTQTDIFCP DTGGRERRKS RGGEAEEGMG PYGDVRKPFS
TGSLHATSLR PSSDLGLGPR SRYGPSAFQE CCSGSPYAKP PPPPMTYDPS NPPDCITMET
TLEKKHSGGT WPKMIVGGMS VAVDTTTATT PTQLSIFKSP KQRKSIFDTD AFKPRPEMAP
PSSKIEYLLP SQLVAHSPQT SKTESLSSSS TATPTPPLPP TRSDSFKFKH KQQSNSASDC
TLTSDGNGGK GEARERDRNG NHYFLDGKVL TSRKSCDEDI GRTRGEEPDV KRPRPKSAPA
LRRRMTPQSI TLPSFQSYSN DDHSPEPREM LRSSPNRSHR HSVGFVSTVY NSTLPANSAH
RGLAPCPAVT AVMRNPVYTV RSHRVHTNNC PSVSSQICQH QHNNQHPSPQ HQGRLSLDLS
QKRPAADYSE SSSRSSRTSH GTNSLPSSAR LGLDSSSNVQ YRTERIKIPS TPRYPRSMLG
SDRGSLSHSE CSSPSLITPP QSPLNLETSS FASSQSQSSI STLPRISVSP VPIGERRKDR
SLHRNRSFLR IPLAARPRFS SLRSLRPYLE EPRNVIVHKG AEPLGISIVS GENGGIFVSK
VTGGSIAHQA GLEYGDQLLE YNGINLRNAT EQQARLIIGQ QCDTITIMAQ YNPHMYQLGN
HSRSSSRLEP VSSQSTPHGS GATTPDNHST IDTLSEQDEG TLTPSSKQTT PTTSPHSFIR
MLSEGSRKVC EPRVVTVRRA QGAELGLGLC GGNLRGVYVE SLEEDSPARG TEGLQPGDLI
LEYGSVNMKN KTVEEVYVEM LKPAETVTLK VQQRQEDFNI VKDTPGDGFY IRALYERTVE
AELDLSFKKD DILYVDDTLP KGSFGTWMAW QLDENAQQIQ RGQIPSKYMM DQELYRRHSM
TELKDDKDSK SLSAAARRSF FRRKHKHKRS GSKDGKELVA LDAISTDSIP FLEDCVSMAY
QRVQKVECVS PRPVLILGPL SDPVKDMLVK ESPGKFCRCV LEVMKASQQA IERGVKDCLF
IDYKRRSGHF DVTTVASIKE ITEKDCHCLL DIAPHAIERL HSVHIYPIVI FIRYKNSKQI
KEQKDPVYLR DKVSQKHSKE QFEVAQKIEQ EYSKFFTGIV QGGTLPYICT QIMTIVDQEQ
SKVLWTPLGC S
//
