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Database: UniProt
Entry: M2SQA7_COCSN
LinkDB: M2SQA7_COCSN
Original site: M2SQA7_COCSN 
ID   M2SQA7_COCSN            Unreviewed;       675 AA.
AC   M2SQA7;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   03-MAY-2023, entry version 43.
DE   RecName: Full=Endoplasmic reticulum chaperone BiP {ECO:0000256|ARBA:ARBA00019933};
DE            EC=3.6.4.10 {ECO:0000256|ARBA:ARBA00012554};
DE   AltName: Full=Immunoglobulin heavy chain-binding protein homolog {ECO:0000256|ARBA:ARBA00031728};
GN   ORFNames=COCSADRAFT_325751 {ECO:0000313|EMBL:EMD64480.1};
OS   Cochliobolus sativus (strain ND90Pr / ATCC 201652) (Common root rot and
OS   spot blotch fungus) (Bipolaris sorokiniana).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=665912 {ECO:0000313|EMBL:EMD64480.1, ECO:0000313|Proteomes:UP000016934};
RN   [1] {ECO:0000313|EMBL:EMD64480.1, ECO:0000313|Proteomes:UP000016934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [2] {ECO:0000313|Proteomes:UP000016934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
CC   -!- FUNCTION: Probably plays a role in facilitating the assembly of
CC       multimeric protein complexes inside the ER. Is required for secretory
CC       polypeptide translocation. May physically associate with SEC63 protein
CC       in the endoplasmic reticulum and this interaction may be regulated by
CC       ATP hydrolysis. {ECO:0000256|ARBA:ARBA00002226}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10;
CC         Evidence={ECO:0000256|ARBA:ARBA00001629};
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
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DR   EMBL; KB445643; EMD64480.1; -; Genomic_DNA.
DR   RefSeq; XP_007700252.1; XM_007702062.1.
DR   AlphaFoldDB; M2SQA7; -.
DR   STRING; 665912.M2SQA7; -.
DR   GeneID; 19136829; -.
DR   KEGG; bsc:COCSADRAFT_325751; -.
DR   eggNOG; KOG0100; Eukaryota.
DR   HOGENOM; CLU_005965_3_0_1; -.
DR   OMA; IDEKIKW; -.
DR   OrthoDB; 143at2759; -.
DR   Proteomes; UP000016934; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   CDD; cd10241; HSPA5-like_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 3.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR042050; BIP_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375:SF144; ENDOPLASMIC RETICULUM CHAPERONE BIP; 1.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003322};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016934};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           37..675
FT                   /note="Endoplasmic reticulum chaperone BiP"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004025861"
FT   REGION          655..675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   675 AA;  73869 MW;  1FCB881D6FB17DA9 CRC64;
     MARSSRNASR RSTWSIAFYL LLVLVGGLML AKTAHAKDNE SAKDDGNAVS GPVIGIDLGT
     TYSCVGVMKN GQVEIIANDQ GNRITPSWVA FTDEERLVGD AAKNQFASNP HRTIFDIKRL
     IGQKFTDKSV QNDIKHFPFK VINKNGQPRV GVEVHGEEKT FTPEEVSAMV LGKMKEVAES
     YLGEPVKNAV VTVPAYFNDA QRAATKDAGT IAGLNVLRVV NEPTAAALAY GLDKTDQGER
     QVLVYDLGGG TFDVSILTIE EGVFEVQATA GDTHLGGEDF DNRVISYFAK KYNKENNVDI
     TKDAKTMGKL KREVEKAKRT LSSQKSTKIE IESFFKGKDF SETLTRAKFE ELNNDLFKKT
     LKPVEQVLKD AKMKKSDIDD IVLVGGSTRI PKVQAMLEEF FGKKARKDVN PDEAVAYGAA
     VQGGVLSGED RTSGVILMDV NPLTLGIETT GGVMTTLIKR GTTIPTKKSQ IFSTAADNQP
     VVLIQVFEGE RSMTKDNNQL GKFELTNIPP APRGVPQIEV TFELDSNGIL KVGAVDKGTG
     KGESITITND KGRLSKEEID RMVEEAEKYA EEDKATRERI EARNKLENYA YSLKNQVNDE
     EGLGGKIEDD DKESLLEAVK ETQDWLESNA GEAAAEDFDE QFQKLSDVAY PITSKLYGSS
     GSAGDDDVPN DHDEL
//
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