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Database: UniProt
Entry: A0A1Q9CWR0_SYMMI
LinkDB: A0A1Q9CWR0_SYMMI
Original site: A0A1Q9CWR0_SYMMI 
ID   A0A1Q9CWR0_SYMMI        Unreviewed;      2455 AA.
AC   A0A1Q9CWR0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Pullulanase 1, chloroplastic {ECO:0000313|EMBL:OLP87329.1};
GN   Name=PU1 {ECO:0000313|EMBL:OLP87329.1};
GN   ORFNames=AK812_SmicGene31456 {ECO:0000313|EMBL:OLP87329.1};
OS   Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS   microadriatica).
OC   Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC   Symbiodinium.
OX   NCBI_TaxID=2951 {ECO:0000313|EMBL:OLP87329.1, ECO:0000313|Proteomes:UP000186817};
RN   [1] {ECO:0000313|EMBL:OLP87329.1, ECO:0000313|Proteomes:UP000186817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP2467 {ECO:0000313|EMBL:OLP87329.1,
RC   ECO:0000313|Proteomes:UP000186817};
RA   Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA   Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA   Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT   "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT   adaptations to a symbiotic lifestyle.";
RL   Submitted (FEB-2016) 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:OLP87329.1}.
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DR   EMBL; LSRX01000866; OLP87329.1; -; Genomic_DNA.
DR   OrthoDB; 1326984at2759; -.
DR   Proteomes; UP000186817; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd02854; E_set_GBE_euk_N; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 3.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR008615; FNIP.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR004193; Glyco_hydro_13_N.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR024561; Pullul_strch_C.
DR   PANTHER; PTHR43651; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR   PANTHER; PTHR43651:SF2; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME, CHLOROPLASTIC_AMYLOPLASTIC; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02922; CBM_48; 1.
DR   Pfam; PF05725; FNIP; 1.
DR   Pfam; PF11852; Pullul_strch_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000186817}.
FT   DOMAIN          791..946
FT                   /note="Alpha-1,6-glucosidases pullulanase-type C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11852"
FT   DOMAIN          1023..1104
FT                   /note="Glycoside hydrolase family 13 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02922"
FT   DOMAIN          2309..2397
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00128"
FT   REGION          12..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1224..1256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1526..1778
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1228..1256
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1545..1560
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1569..1583
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1601..1778
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2455 AA;  271250 MW;  455D99DA5A5F1200 CRC64;
     MGIALNCKFD FGTVPERPED RAEPMMPKKA GPDSEGQQLA VMEVADKDAC MSTPCRRPQE
     AAARKNGSLP AGDLCRDFGR TATGGFVLLG APLLVTAASK EGDVQIAALD KAAGALVAAD
     PDNPSFVEQS DVEEDTDIPR FHLERPRSRA RDFRDTVIGD ATSPKTDVQF RWIKRDGEAY
     RMQMRVPKSD GGGMKEGGTF SRREDAVDAA KGPNFLISEA GGRPSSHGTS ETGQLLLPAS
     KPARRGSLAW FVLLLWKRLL DENTLSDADV AALDEMMWYS GRELSQNIRL PGSLQSLTFG
     YVFNQSLEDI QLPSSLQRLT FGYAFDQRLR ASNYRARFDV WLCVQPAFNW GYDPVLYGVP
     EGSYSSDPDG MARVLEHRRM VAGLHKKGLR VIADVVFNHV FGSGPKGNHS VLDKHLGDPC
     ELFRTLRVHH VDLWSKSILI QSNLERLVVD MIRHWAIEHR MDGFRFDLMG HITLECIQKC
     RAALDELSVE EHGIDGPRLL LYGEGWEFGE IEGGARGATA CQRQLAGTGI GSFNDNLRGA
     VLGGNAFEDP RLQGFATGLG LREPSDVALK TTTSELELLV AFGRDIWRED PHTPGIYEYK
     DTKDYRGPQR VVDKSSWERV REEEVEDEKA VSKGLGRTSP LGRRRRRPVA PALLGGDDFF
     RKFTTGATGE LSLNGDPMAN SESAQRASVH GGKAAYVSSP EEVVNFICVH DNETLYDSTI
     WKMSPETTDP EERMRANWLC SATLALGHGV PLFHAGDEVL RSKSLDRDSY NSGDWFNLLD
     YSGETSAFGA GNHTKWELMK PLLRDDRLRP NKEMVAATTA KFCELLGIRK STALLGLREA
     ADIVDKVHFP GCGLGQIPGV VVMEVRNGTS SASGTPLCDK YSRVVVVFSA RPDEVRIPAP
     TSRSGGMLML HPLQVASADT RTREARYDEA TDELVVPALT AAVFVEPQPN QPSFKASERR
     AQFRPALRER PIVGDGMGLV AADPACVPFK GHFEYRWKVY TDLRKHISET SGSLTEFASG
     FRKLGFTKDE ASGAITYREW LPPAKAVSLV GDFNNWDEGA TPLARDAFGT WEVTLPAKSI
     AHRTKVKFCA TTPDGSKVYR VPAWIRWSCP DLGKFGSTYD GYYWDPSEDV LSPDELAIVV
     QNYRDGGLNA QPETPEKEEA PRKKGSLLEW EHPSKVGLIN RRSLMLNWKV TRFFEEIEDH
     RLKAIFDEVA KSWPPKIRSR KTLVVAEEDG EIEDEQEEEE EEEQQLTEDD EEDGQPAEVD
     GYLAQSLGIV PGSPAPPASA YVATVAYELS DEGPPVPYAA ALPNGDDDTD LVRQLAELEQ
     QIAHRRAALS GRQAIERWHS LQHMDSQRTI AWPETLQEFV AEQPAPLSSA TEGGYFRQGA
     SSNLSLGHVE AKDVAPCNVP VATPARAASV APAVSEDLAD PTDVAVAPGV SEDLADPTKA
     AVAPGVSEDL ADKAAVAPGV SEDLADKAPV APGVSEDLAE PAVAPGVSQD LADPAQLAVA
     PGVLKDLADR AVAPGVLKDL ADPVAPRVSD DLGEATPATP RPESVSLEIA SSSQPPSPEL
     LALKVQTRRA EQMRGREGGT QEDVPVFKRP AAKGWPKGKA KARPAKGELL DDEPTKRAKK
     GQQGDDEPKK RATKGEQGDD EPKPKRATKG EQQGDEPKPK RAKKGEQGDE PKPKRAKKGE
     QQGEEEPKPK RAKKGKQGDD EPKRAKKGEQ QGDDEPKRAK KGKQGDEPKR AQKGKQGDEP
     KRAQKGKQGD EEPKPKPAKK GKQGDEPKPL KKTFAKRWEP EVEGRSKCLW TSIRDAFNDL
     IRPQLRFPTK FEDPFWMHCR PKLIELEEAT AKDTKRCINQ MQTPTQPEEK RRNDSLEFQL
     EAYWMAYRQT HSTHPVFGRG LDLGTTIPLA FYSDEGKGPK RGNFVVVAIE SPIGLMDVAD
     DFTCTCQEDV KKAPQQFVPG QQAAGPYTPM EEAALKQNTT CKGHSYLTRH VLFGLPDWIY
     KHHPEVLEKM TQQVADELTT LFSSGLEING KVYTACLVGI KGDLKQIAEK IAYLNRYYAR
     LGPVSYNDIC GSLVLLARLG YYDDPNGGDE TNLRARLIRC FQHFRLWRLA AGKSAAVRYF
     SASLFNLKRL SDFAWSNTKG SDTMLLLEYL SFYLTILLRR PNLPAAHAVM FRVLKKTIGE
     SQKAFNLMYK HGLWLRRTCA QNLYLRLMSV LSGYQHLAQH ALTMGMTFFA LKPKYHAIHH
     VAYELRVALL TEAKLIPNPI TWNCEMGEDL IGRICALSLK AGKEEYCFEG FQAARPSLPS
     TLRIYEAHVG MSSTEPKCNS YLEFAKDVLP RIKEAGYNCV QLMAIMEHSY YGSFGYHVTS
     PFAVSSRSGT PDEFKALVEE AHRLGMLVLI DLVHSHVSNN ADDGLNGMDF GQAESESYFM
     TGERGYHKLW DSRVVLPMSA TAKQDTGGRE RQTAGCTPHT ADIQTQLCLQ HSHVQ
//
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