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Database: UniProt
Entry: A0A183S831_SCHSO
LinkDB: A0A183S831_SCHSO
Original site: A0A183S831_SCHSO 
ID   A0A183S831_SCHSO        Unreviewed;       643 AA.
AC   A0A183S831;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Lariat debranching enzyme A {ECO:0000313|WBParaSite:SSLN_0000039701-mRNA-1};
GN   ORFNames=SSLN_LOCUS379 {ECO:0000313|EMBL:VDL85500.1};
OS   Schistocephalus solidus (Tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Diphyllobothriidea; Diphyllobothriidae; Schistocephalus.
OX   NCBI_TaxID=70667 {ECO:0000313|Proteomes:UP000050788, ECO:0000313|WBParaSite:SSLN_0000039701-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SSLN_0000039701-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDL85500.1, ECO:0000313|Proteomes:UP000275846}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NST_G2 {ECO:0000313|EMBL:VDL85500.1,
RC   ECO:0000313|Proteomes:UP000275846};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the lariat debranching enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006045}.
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DR   EMBL; UYSU01000250; VDL85500.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A183S831; -.
DR   STRING; 70667.A0A183S831; -.
DR   WBParaSite; SSLN_0000039701-mRNA-1; SSLN_0000039701-mRNA-1; SSLN_0000039701.
DR   Proteomes; UP000050788; Unplaced.
DR   Proteomes; UP000275846; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008419; F:RNA lariat debranching enzyme activity; IEA:UniProt.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd00844; MPP_Dbr1_N; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR007708; DBR1_C.
DR   InterPro; IPR041816; Dbr1_N.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   PANTHER; PTHR12849:SF0; LARIAT DEBRANCHING ENZYME; 1.
DR   PANTHER; PTHR12849; RNA LARIAT DEBRANCHING ENZYME; 1.
DR   Pfam; PF05011; DBR1; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   SMART; SM01124; DBR1; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   Reference proteome {ECO:0000313|Proteomes:UP000275846};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          236..437
FT                   /note="Lariat debranching enzyme C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01124"
FT   REGION          456..556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          588..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        492..506
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..528
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..556
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   643 AA;  71191 MW;  043E4C39D6A556B0 CRC64;
     MVRVCVVGCL HGELDKVYED IANMDRELST RTELVLCCGD FQSLRNPADL HSMSVPAKFY
     RMGDFYRYYS EEVTAPIPTV FVGGNHEASC YLQELPYGGW VAPNIWYMGY AGVVQFAGLR
     IAGLSGIYKQ HDYPMGHFER PPYSEATKRS VYHLRSIEVF RLGQLARRVD IVLSHDWPRG
     IYNYGETKEL LQRKRHFYEE VNSNTLGSPP GEQLLCRLRP RYWFSAHLHC KFAAVVAHSD
     PQRDTTKFLA LDKCLPSRDY LQFLDIDPSP SFATYSADGL VCSPNEEAPL IVSLPPSASE
     DSAESPTLCL DPEWLCVLRA TNDLMSLTQI PSILPGQDGK PTRSYVASTD DLQQLWEPFA
     GTFSIPENFE RTAPAYKPTD VNLLTTSANK MNSKNHQSGG VGPNLAHLAE EGARKQQIFS
     NPQTELICAM LELINPNALH LGRDSYNLAD LATRMHPGDD EEEEGDDACE RELGRPPANP
     TPSPPAAADE DVSDGAAEDS GEDQEGSEVE APTFVTTPNT SLFFSMVSDE TTEEYDPTDP
     SPNKRSRPSD SIDVHAEYEN PEEINLNDLV EGDEEEKTED GQVVVDTGDA GDLQHVTTGV
     SPSKADKSGA VEVTYQPRPL SQPAEAVITV DALNTESEYA YQP
//
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