ID A0A0L0CE53_LUCCU Unreviewed; 2028 AA.
AC A0A0L0CE53;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 03-MAY-2023, entry version 25.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=FF38_02289 {ECO:0000313|EMBL:KNC30530.1};
OS Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Luciliinae; Lucilia.
OX NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC30530.1, ECO:0000313|Proteomes:UP000037069};
RN [1] {ECO:0000313|EMBL:KNC30530.1, ECO:0000313|Proteomes:UP000037069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS {ECO:0000313|EMBL:KNC30530.1,
RC ECO:0000313|Proteomes:UP000037069};
RC TISSUE=Full body {ECO:0000313|EMBL:KNC30530.1};
RX PubMed=26108605; DOI=10.1038/ncomms8344;
RA Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT interventions.";
RL Nat. Commun. 6:7344-7344(2015).
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:KNC30530.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JRES01000505; KNC30530.1; -; Genomic_DNA.
DR STRING; 7375.A0A0L0CE53; -.
DR EnsemblMetazoa; KNC30530; KNC30530; FF38_02289.
DR OMA; DDCAKHG; -.
DR Proteomes; UP000037069; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd02961; PDI_a_family; 4.
DR Gene3D; 3.40.50.11390; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 14.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR19991; L 2 01289; 1.
DR PANTHER; PTHR19991:SF3; LETHAL (2) 01289, ISOFORM F; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 13.
DR PROSITE; PS51352; THIOREDOXIN_2; 3.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000037069};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..2028
FT /note="Thioredoxin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005536245"
FT TRANSMEM 1991..2011
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..152
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 676..823
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 1748..1896
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 1058..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1476..1531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1143
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2028 AA; 232361 MW; 48E6941A47A5B84D CRC64;
MHFPRLKSLL TLVICSLFVL SFPENVNCAN KKGSTNSNPA PAAPLEPEAV IEEVNAKQLE
KLLADKDYVA VFWYARSCVT CDKVLAELEK IDDDTDSFGV DFVKINDKRL AKQYGIKNFP
ALTYFREKEP IIYDGDLMDE EGVLDFLTSL EAMDLPDRIE EVNAKILLKI IEDTDFVAVL
FCPDHATCPP RIMDKPQCRK CSKALQELEN IDDEADQLGI GFVKIHDEAL AEEYNLGNLP
ALVYYRHQTP IIYEGELSRE EDVLEWLVQN KSTGDEDDVI EDVTPKTLAT LISNIDNLVV
LFYDHGNDDS MTVLEELEQI DDDCDKHGIQ FVKIDDARTA EEFGIDSIPA IVYFEKEIPN
IYDGDLMDEE QILHWLVSQL EHDEIEDVTD EMLDKMVKEG RVLAVLFYDN NDEKSEKVLE
ELENIDDECD QLGITFVKID NPEEALEYGI NKVPKLIYFE KGIPTIYEGN LEDEQKLLKW
LEEQTSSDQI EDITDEMLDL IIEKMAHVAV LFYDKDQKKS QKVLAELENI DDECDQNDIA
FVKIDDDNEA KEWGIDEIPS IVLFERGIPH VYEGDLMKED ELLGWLVHQK RYSEIPEVTD
EMKDKLVENT EHLAVIFYDK DDKQDIRILN ELENIDDELE KEGIVIVRID NAAEAKEYGL
DHLPALIYFE NKIPALYEGD LMNEDEVLEW LILQKKTATI EEVTDEILTN LVNDHEYVVV
FFSGPCEPGE KCDKTLNALE TIDDELDETG IIFVTTEDTG IAKKLNIKSY PQLVFFRNRD
PLHFTGDLED EDEVLSWITD EDTLEIPGKI EDVNVKMLDK ILAENEHVVV FFYDEDDKKS
LKILNELENI DDECEEKNID FVKTSDDDVE KEYDLPGLPA LAFYRNKFRT IYTGDLMKEE
EILEWVIELY ESTADVIESV DRKTLQVLIN DVEHLAVFFY DDKCVSCPGI LEELENIDDD
TDKHGIQFVK SNDVKLAHEI GIFAFPALVY YETGVPIMYD GNLKNENRVL QWLINQKNDE
CFYVGLGQEG RSAKRGNNNA PDNYKPFQCC PTKLEKSTKV PKMTAQRIGH TAASEGGKRQ
QGNFQFGTPD STPVSNTKTS TANKNKSQKS KKPAPKAAKK PVVVDSDEDD DDEDDDDDDD
STEEPLVKVS YAKHKTSNKP APKAEKLPTI KPASKSATAS KKTLAKNDDK LNVKTGNMED
ENEVFKWILE QKADESIELI DRETLFEYIG SKDFLAVVFY KEDDPDSPRV LRHIELIDDE
ASEYGIQIVK CHDKLMAKKY GFRNPPGITY FRKGKYINYD GDIDDEEEVL DWLTSPANME
MTDHIEQVNR KMFEKIRKSS DYLAVIFYSE DCKQCPRVLA EVEHIDDEAD KAGIDFVKID
DKQMAKEMGV FALPAIVFFK PTSKEPVIYA GDLYEEEQIL TWLLTQKDPS GDVIEDLEGE
KLINLIEESG SIAVYFWNKT QCDICNSKAA RKARLKKEKE QQAQDPGAGA AAAAFAAAGT
EGEGGEAGAE GTAANEPSTP TSSKQHEEDT DGCETCTKVL EELENIDDDC DKHGIKFVKT
KDFSVADGYG VHDYPALVYF ESGIPNVFEG ELQEEEEVLQ WLITQKTEDR IELITRQMLE
TMVEETQYLA VYFLPPERKG HKQPAYCRTY CVPMSNNEVN FNNSSSNTHK SKQFLKNYIS
RKRKRIESQD KINCNICDQI LEGLELIDDE CDVFGIHMVK IQDPQLAKRY SIKTFPALVY
FRNGNPLLFE GDLQNEQSVL EWLIDDDNRE LADEIEEVNE RMLERLMAES TLLVVFFYDE
DCAECEEILE ELEEIDGEAD MFGIDFVKIA SVEAAKKYDV VNIPSLVYFR KQVPVLYDGD
LHQHDKIITW LTSQDVFEIK NEIEEVNRKM LDKLLEENEF ITVFFYEHNQ QESIAALEKL
ENIDSETDNL DITFVKMADS RYAKKWGVTK LPAMVYFRRR FPSIYRGDLL SEDEVLEWLR
KNRFRQPELN IFMYALIALS VAFVLYTAFL LQCFKPAPPP PPQHPKQS
//