ID A0A2U9C2S4_SCOMX Unreviewed; 2516 AA.
AC A0A2U9C2S4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=DnaJ homolog subfamily C member 16 {ECO:0008006|Google:ProtNLM};
GN ORFNames=SMAX5B_002698 {ECO:0000313|EMBL:AWP09332.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP09332.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP09332.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP026253; AWP09332.1; -; Genomic_DNA.
DR STRING; 52904.ENSSMAP00000014938; -.
DR Proteomes; UP000246464; Chromosome 11.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd02963; TRX_DnaJ; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR043361; DNAJC16_TRX.
DR InterPro; IPR027882; DUF4482.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR027881; SOGA.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR15742:SF1; PROTEIN SOGA1; 1.
DR PANTHER; PTHR15742; UNCHARACTERIZED; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF14818; DUF4482; 1.
DR Pfam; PF11365; SOGA; 2.
DR Pfam; PF00085; Thioredoxin; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464}.
FT DOMAIN 2..66
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 96..215
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 532..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1296..1319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1466..1562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2047..2067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2175..2194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2211..2240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2259..2293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2312..2342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2485..2516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 847..917
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1083..1110
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1149..1190
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 988..1016
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1474..1495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1497..1517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2225..2240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2270..2293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2502..2516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2516 AA; 279211 MW; 5DDF4598EF2E1EDF CRC64;
MDPYKILGVT RSASQAEIKK VYKRLAKEWH PDKNKDPGAE DMFIKITKSY EILSSEDKRA
NYDRYGQTDD TQPYGGGRYG PRHDSFHFDE SFFNFPFNGK NHRDFADSKY TLHFNQYVND
VVPDSYKRPY LIKITSDWCF SCIHIEPVWK EVVQEMETLG VGIGVVDVGY ERRLANHLGA
HRTPSILGVI NGKVTFFHYA VAKEHLRQFV EDLLPQRLVE RVTDKNDLQF LNSWHDLNKP
HVLLFDQVSV VPLLYQLTAF AYKDYLQFGY VDQGLSETVA LQKQFNINTY APTMLVFKEN
TDKPADIIQA KGMKKQIIDE FMSNNKFLLA PRLVNQKLFN ELCPVKQFHR RRKYCVLLIT
RDEETLSFGN QAFLSFASTN SKEVLRYAYV YQQLQQPLCD ILMQNKDSAQ SPPQVVILER
RNAAGKALFK PVTAWNGSEE DKQCLVDELE RLQKDPSILV HDAVLPELNN EFASMFVIRW
IYASYDYLAE VIDDILHNNW REMMPLLSLI FSALFILFGT VVIQAFSDSS EDKQTKPKAK
DGTKAENGSP GTAASSRPPK KSFVEVTELT DITYISNLVK LRPGHMNIVL VLTDASKNIL
LSKFAKEVYS FTGSLTLHFS FLNIDKHGEW MNTLLGYAHD AMQIDGDEGD GGSRKMDYTG
HVLALNGHKK YLCLFKPVYT GEDLDSKSSE DEGVTSGGRS RSSSRDDHLP RKSKRSRSMS
TLQIHHKLDR LGLWMERLME GTLPRYYVPA WPGLDKITPC RDAEGKSGQE VSVLSSTGDN
DRVGQHAAAK TAWSSAEKDR LSLGAETGEG SISPGEERSV TSFDSRVPAS TSLAFSDLTE
EFVDGMHEEF VREIEELRSE NDYLKDEMEE LRSEMLEMRD MYMEDDVYQL QELRQQLEQA
NKTCRILQYR LRKAERRSLR VAQTGQVDGE LIRTLEQDVK VAKDVSIRLH NQLDSVEKKR
SRLEKENEEL RGRLQDLEVA KQVLQQEIDK NSQKKRGARP NNKPDKKPGP QEDSSDLKCQ
LHFAKEESAL MCKKLTKLVK DSEAMKEELA KFRSLYGDVD ASLTVEEVAD SPHTREAEIR
VHLKLVEEEA NLLSRRIVEL EVENRGLRAE MDDMKGPQDG PQELTGVGLG LGLTGGAMVL
GGGAASENVM ELQRHLQFVE EEAELLRRSL IEMEEQNKLL MNEINRYKSE LPPLMSTLSS
NSLTSLGDGL LNDSPVHTIQ EGAVLISTDT PVQEEELRLA RLQIGELGGK VKKLQYENRV
LLSNLQRCDL AAYNTPSSSS SSSSLRLALE TDAEAGDSAE CLPSSPPHRK EPVGGENDAL
EINERKKKIE DIAEATASLP ACLGQKDHDA LLAMRDQARL VSTAIQLLTS PDSNCLSSSP
SIYHKVCSNE AAEPCDLDKP PPHSQISELS DLADRPLVGA LTSRLQALHT QLQAFVERVD
CLGKPPAGGR DPWVEGVSPL ASPCTSLICS GDDQDGLHTE EEKQPDYRDQ SETEGEGPTE
ENSQSESNES QVQETNQLEQ QEEDKDDALP YESPDLQTRL SEAEESAQET QEELENERPT
QKETALKLTQ LQEGHQKALL RRDFQLQSLG LQARLQQKLW GQERTLLVQE SQHLKQALLL
LSLKLRCFLK QWRLGCKKDT ECKDILEMNS LKDLYLLLEE ENLTSPAHQS DKRSGADEQP
LCPTIKSSAV SSTLADLRVS LQDLSGELRQ ERQGSQELTQ QFAKAKASWE VERTELQSLI
TQFEAKAGKS AAALSSTDTM EPPDLKVALK REREEHQHLL AESYGAVMDL TKQLQIGERN
WGREKLELLE RFSQERAQWE QRVREATAQQ GKVRLCVRAC VRACTQTLPA PAAVVVFFES
QGTFVDAHKL LITHCCLVTA ALLQHVREGC SGIASVFKVV ITSGCFHKHT HTHTHTQRNE
DPHTQLSFQS EGVCCPFLVS LSFPIIPLFP LLIHLFSVIP CLTPSNTGSG CVLHWEPGKR
RSCQWNSVAK TPDVGDTCKT WDGPSGSCSS LVGSEPDLEL VQRSYTAPDR TGIRIYYSPP
AVRRIEQRRR NQESQQAQNG SSSLGPCGWD AGVPAVETLE VQQQQQPSSS SSCSSSYEQW
LSSLSKQHRE LLESRSSCIA SSIPSVVNSG VGSSANSVVD GITSSSAFHG LEISVNLSDD
MKEMTNCVRQ AIRSSSLERK SKEPGSQVVG GMSTRSTQTA AQYVSIGLQT DNLPGSRGTG
LHSKAWSPRP SSTATSSLVS ARARQISTSL DKVHSRIERP CCSPKYGSPK LQRRVSSGST
SRLEVSSSSR DRSMWSLQQR PFGGGGVGVV GGGGGGGGGG GGGGGGRSAW ARSTTTRDSP
VLSGLTDGLS SLFSVVEHSG STESLWRGDG VCGPEPSSQR YGGLVQEFFR NVCSSRGPAG
VTLPGEKVPR DSPGSLRALA GMSACTDSVT RIVNKRFMRQ TAGEEMVNIM GGGKEATSIA
GAAGTGPEDT PCDCAAQSSC SARPSRAAGR HSLGQCKHRP QESTAAAEDK RDACSE
//
