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Database: UniProt
Entry: U3JQ86_FICAL
LinkDB: U3JQ86_FICAL
Original site: U3JQ86_FICAL 
ID   U3JQ86_FICAL            Unreviewed;       782 AA.
AC   U3JQ86;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 2.
DT   24-JAN-2024, entry version 52.
DE   SubName: Full=Phosphoglucomutase 2 like 1 {ECO:0000313|Ensembl:ENSFALP00000004940.2};
GN   Name=PGM2L1 {ECO:0000313|Ensembl:ENSFALP00000004940.2};
OS   Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX   NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000004940.2, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000004940.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231}.
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DR   AlphaFoldDB; U3JQ86; -.
DR   STRING; 59894.ENSFALP00000004940; -.
DR   Ensembl; ENSFALT00000004964.2; ENSFALP00000004940.2; ENSFALG00000004747.2.
DR   eggNOG; KOG1220; Eukaryota.
DR   GeneTree; ENSGT00940000158353; -.
DR   HOGENOM; CLU_016950_0_1_1; -.
DR   OrthoDB; 1482at2759; -.
DR   Proteomes; UP000016665; Unplaced.
DR   GO; GO:0047933; F:glucose-1,6-bisphosphate synthase activity; IEA:Ensembl.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd05799; PGM2; 1.
DR   Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR   InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR   InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR   InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR   InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR   InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR   PANTHER; PTHR45745:SF2; GLUCOSE 1,6-BISPHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 1.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 1.
DR   SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000016665}.
FT   DOMAIN          225..368
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          398..504
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          514..629
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          57..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..123
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   782 AA;  86610 MW;  FC6DB1DC3883C127 CRC64;
     MLSPGSAWQQ GGHTRRTARS DPIPVGSCRS APSCSCSCSC SCSSQLGLIL GACGGHGRQQ
     PDGGLAAKPA GSADRPEPEP AGGRALPRPA PARRPRRPRP QRQRLHVHPV RHDALRRHRG
     QPHPGLHPLP QGGQAQRPLP RLHQEQGLHD PALPRSLPAA MGDCGAPGDV NSNVLVARST
     GDAQLDKAVW QWLSWDKNQK TKAQIERLLQ DGKHRELRER LCCRLSFGTA GLRSAMGAGF
     CYINDLTVIQ STQGIYKYLE RNFSDFKQRG FVVGYDTRGQ VTSNCSSKKL AKLTAAVLLA
     KDVPVYFFST YVPTPFVPYA VQQLGAVAGV MITASHNRKE DNGYKVYWEN GAQITSPHDK
     EIIKCIEECV EPWSGSWNEN LVDTSPLRQD PLKKICDSYM EDLTKICYHR ELNVQSSLKF
     VHTSFHGVGH DYVQLAFQAF GFQPPIPVPE QKDPDPDFST VKCPNPEEGE SVLELSLRLA
     EKEGAKVVVA TDPDADRLAV AEQQENGSWK VFTGNELAAL FGWWMFSCWK ENCSPDADVR
     NVYMLATTVS SKILRAIALK EGFHFEETLP GFKWIGSRVK NLLDNGKEVL FAFEESIGFM
     CGTSVLDKDG VSAAVVIAEM ATYLQGQSLT LAQKLLGIYE TYGYHISKTS YFLCYDPATI
     KRIFERLRNW DGPQCYPQCC GVYSILHVRD VTTGYDSSQP DQQSVLPVSR SSQMITFTFQ
     NGCVATLRTS GTEPKIKYYA EMCALPGHSD RAVLEEELQR LVEALVENFL EPAKNGLTWR
     SA
//
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