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Database: UniProt
Entry: A0A3Q3EWZ5_9LABR
LinkDB: A0A3Q3EWZ5_9LABR
Original site: A0A3Q3EWZ5_9LABR 
ID   A0A3Q3EWZ5_9LABR        Unreviewed;       256 AA.
AC   A0A3Q3EWZ5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=ADP-ribose glycohydrolase MACROD2-like {ECO:0000313|Ensembl:ENSLBEP00000011986.1};
OS   Labrus bergylta (ballan wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000011986.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000011986.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3Q3EWZ5; -.
DR   Ensembl; ENSLBET00000012608.1; ENSLBEP00000011986.1; ENSLBEG00000009217.1.
DR   GeneTree; ENSGT00940000157404; -.
DR   Proteomes; UP000261660; Unplaced.
DR   Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR   InterPro; IPR002589; Macro_dom.
DR   InterPro; IPR043472; Macro_dom-like.
DR   PANTHER; PTHR11106:SF27; ADP-RIBOSE GLYCOHYDROLASE MACROD2; 1.
DR   PANTHER; PTHR11106; GANGLIOSIDE INDUCED DIFFERENTIATION ASSOCIATED PROTEIN 2-RELATED; 1.
DR   Pfam; PF01661; Macro; 1.
DR   SUPFAM; SSF52949; Macro domain-like; 1.
DR   PROSITE; PS51154; MACRO; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000261660}.
FT   DOMAIN          1..69
FT                   /note="Macro"
FT                   /evidence="ECO:0000259|PROSITE:PS51154"
FT   REGION          77..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..130
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..177
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..209
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..225
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   256 AA;  28625 MW;  D4939469EFCB30F8 CRC64;
     MKEHGLSTVA FPCISTGIYG FPNEPAAEIA LSTVKSWIED NPDKITRVIF CVFLETDFAI
     YKKKIPEIFQ DNDMEVTEEQ LQGDNNPPSA KSKEDSEESG RGKEEAGDEE EDDNDAAGNE
     DVEMESQNPD DITETPDPTQ GKDNDDTENQ DKEEDAGADS DNKKDEKDKK DEEKDTDNPK
     EKDEEEDKED KPPAEKTDDD DDNTVKSTVE MEDVSEVNNT GTSNGEEIKE RVESPEEPDS
     ILTDSNQSKD TVEKKE
//
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