ID   CRP1_YEASV              Reviewed;         465 AA.
AC   E7LVH4;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 2.
DT   02-JUN-2021, entry version 29.
DE   RecName: Full=Cruciform DNA-recognizing protein 1;
DE   Contains:
DE     RecName: Full=CRP1 short N-terminal subpeptide;
DE   Contains:
DE     RecName: Full=CRP1 short C-terminal subpeptide;
GN   Name=CRP1; ORFNames=VIN13_2191;
OS   Saccharomyces cerevisiae (strain VIN 13) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=764099;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VIN 13;
RX   PubMed=21304888; DOI=10.1371/journal.pgen.1001287;
RA   Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA   Pretorius I.S., Egholm M., Chambers P.J.;
RT   "Whole-genome comparison reveals novel genetic elements that characterize
RT   the genome of industrial strains of Saccharomyces cerevisiae.";
RL   PLoS Genet. 7:E1001287-E1001287(2011).
CC   -!- FUNCTION: Cruciform DNA-binding protein which exerts an enhancing
CC       effect on the cleavage of cruciform DNA (X-DNA) by endonuclease VII
CC       from bacteriophage T4. {ECO:0000250}.
CC   -!- PTM: Cleaved in the vicinity of position 160 to give an X-DNA-binding
CC       N-terminal subpeptide and a non-DNA-binding C-terminal subpeptide.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CRP1/MDG1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EGA78598.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; ADXC01000042; EGA78598.1; ALT_INIT; Genomic_DNA.
DR   EnsemblFungi; EGA78598; EGA78598; VIN13_2191.
DR   HOGENOM; CLU_594765_0_0_1; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR032640; AMPK1_CBM.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   Pfam; PF16561; AMPK1_CBM; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Phosphoprotein.
FT   CHAIN           1..465
FT                   /note="Cruciform DNA-recognizing protein 1"
FT                   /id="PRO_0000409620"
FT   CHAIN           1..160
FT                   /note="CRP1 short N-terminal subpeptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000409621"
FT   CHAIN           161..465
FT                   /note="CRP1 short C-terminal subpeptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000409622"
FT   REGION          107..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          160..161
FT                   /note="X-DNA-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          247..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          298..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..148
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..367
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..432
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         153
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38845"
FT   MOD_RES         156
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38845"
FT   MOD_RES         182
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P38845"
FT   MOD_RES         271
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38845"
FT   MOD_RES         295
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P38845"
FT   MOD_RES         319
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38845"
FT   MOD_RES         343
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38845"
FT   MOD_RES         366
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P38845"
FT   MOD_RES         394
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38845"
FT   MOD_RES         440
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38845"
SQ   SEQUENCE   465 AA;  51089 MW;  1DA7D005F37993A9 CRC64;
     MSSELMFNYT FSWPAGPKDV ILTGTFDDWR GTLPLVKTAK GNFEITMPVK LANKDDTFQF
     KFIVDGVWCV SDSYKKEHVS EGIENNFLQI TDLVETQEVA GASRIPEAGG LLCGKPPRSA
     GPPSTSNRKK NKRNNKKRRS KLKKKSTKNN KKSNESLDDN EEEDGVTGTT TEDVTGTSRE
     ETPLAEPTNV SKEAPGNFHI LPIDQSADTT XSNGIIGGPG PVLVPNPGEI KEFTEIRDVD
     ARELNERLNK KEEVPEPVAG PIVESSVTEK SPALPQADDP IVETKEVAHN VQELTPQVEA
     VTPLINEPEP LPTPEAQISI PESSKVEPVE GSLQSKLVEK RESTEGVLDG SKKVENKAKK
     DEEVFTLDPI VNKAPKLPLT DEQTAEGRKS PAVSEEKEKK KKQEKGSKEV KRSETSKEKK
     PSAKEVKKQT VKASKKQTAS PLSSSTEEPK KKKTGFFGKL KKLFK