ID A0A2T7NQ34_POMCA Unreviewed; 658 AA.
AC A0A2T7NQ34;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=UBX domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=C0Q70_16526 {ECO:0000313|EMBL:PVD23262.1};
OS Pomacea canaliculata (Golden apple snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD23262.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD23262.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD23262.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD23262.1};
RA Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA Zhang G., Qian W., Fan W.;
RT "The genome of golden apple snail Pomacea canaliculata provides insight
RT into stress tolerance and invasive adaptation.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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:PVD23262.1}.
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DR EMBL; PZQS01000010; PVD23262.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7NQ34; -.
DR STRING; 400727.A0A2T7NQ34; -.
DR EnsemblMetazoa; XM_025253289.1; XP_025109074.1; LOC112573169.
DR OrthoDB; 8912at2759; -.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg10.
DR CDD; cd17129; Ubl1_FAF1; 1.
DR CDD; cd01771; UBX_UBXN3A; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR033043; FAF1-like_UBX.
DR InterPro; IPR049483; FAF1_2-like_UAS.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR006577; UAS.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR PANTHER; PTHR23322:SF56; FAS-ASSOCIATED FACTOR 1; 1.
DR PANTHER; PTHR23322; FAS-ASSOCIATED PROTEIN; 1.
DR Pfam; PF21021; FAF1; 1.
DR Pfam; PF14555; UBA_4; 1.
DR Pfam; PF00789; UBX; 1.
DR SMART; SM00594; UAS; 1.
DR SMART; SM00166; UBX; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 3.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
DR PROSITE; PS50033; UBX; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000245119}.
FT DOMAIN 103..172
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 577..654
FT /note="UBX"
FT /evidence="ECO:0000259|PROSITE:PS50033"
FT REGION 50..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 513..563
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 83..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 658 AA; 74527 MW; 9C4B454CD313822B CRC64;
MADTRDQMLV DFQQITGIED VDTCMAILTQ QDWNLELAVN TIMHDEPVTE VDASPGRMSD
IDISHSSSAP EHISPVVIDD DASASGPSSS HSFSSTRNAS RMIHFNVEYR LRNIPIVLPD
SETVGKIKEM IQAELGIPVD KQQLKGLVKR HVDDSVVLQD LHLPKDNVLY LLTPDLCSPT
DNTSNVDNGQ VSHRNDEYRL KVVYRNGSSY RIYNLNLKGS KTIKEVKQDV YSLTDVPVRY
QEWKGWPLGA SEDESLCSCG ISFPTHELEV ERKVSTTLEQ HPVPNNEASM ESESDEENMD
IANDEDLFEV PSSRRIAPLI SPNAQTEAEA LEQFTHEFSE RYGEIHPVFY IGSLDDAIRD
ALQVKATDRK LLALYLHHDG SIQANVFCSQ LLCSESVVNV LSANFLTWAW DLTHPENMVR
FLTLATKHFG SIAASQIRSY RTEQLPALLI ISRSKATNEV IDAIQGHVTL VELMTRLLHA
VDVFTEQKEL DIAEERERMD RERIKAEQDL AYLESLETDR KKAEAARVEE ERIRQEKAKE
QELRKEEERK RLKEEAIKEA FQASVAKSVP EEPAEDAEGA VSRLRFRVPG GGVITRSFWS
ENTLQDVLNF LTAQGFHTED YKVITTYPRR DITQLDSTQT LQSAKLFPQE TLTLEEKS
//
