ID A0A401L0K5_ASPAW Unreviewed; 649 AA.
AC A0A401L0K5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Cruciform DNA-recognizing protein 1 {ECO:0000313|EMBL:GCB25159.1};
GN ORFNames=AAWM_08044 {ECO:0000313|EMBL:GCB25159.1};
OS Aspergillus awamori (Black koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=105351 {ECO:0000313|EMBL:GCB25159.1, ECO:0000313|Proteomes:UP000286921};
RN [1] {ECO:0000313|EMBL:GCB25159.1, ECO:0000313|Proteomes:UP000286921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 58123 {ECO:0000313|EMBL:GCB25159.1,
RC ECO:0000313|Proteomes:UP000286921};
RA Kusuya Y., Shimizu M., Takahashi H., Yaguchi T.;
RT "Aspergillus awamori IFM 58123T.";
RL Submitted (SEP-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:GCB25159.1}.
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DR EMBL; BDHI01000021; GCB25159.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401L0K5; -.
DR STRING; 105351.A0A401L0K5; -.
DR Proteomes; UP000286921; Unassembled WGS sequence.
DR CDD; cd02859; E_set_AMPKbeta_like_N; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR032640; AMPK1_CBM.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR10343; 5'-AMP-ACTIVATED PROTEIN KINASE , BETA SUBUNIT; 1.
DR PANTHER; PTHR10343:SF81; AMP-ACTIVATED PROTEIN KINASE GLYCOGEN-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF16561; AMPK1_CBM; 1.
DR SUPFAM; SSF81296; E set domains; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000286921}.
FT DOMAIN 4..80
FT /note="AMP-activated protein kinase glycogen-binding"
FT /evidence="ECO:0000259|Pfam:PF16561"
FT REGION 118..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..649
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 649 AA; 65710 MW; 5BFF7F1764AAD18E CRC64;
MGSYTFTWPY NANEVFVTGT FDDWGKTVKL DRVGDVFEKE VPLPVTDEKV HYKFVVDGIW
TTDNRAPEED DGSSNINNVL YPDQILKDST TPLLNGTAAM AGVTPGSTTA ALAAGVPKES
SSKHGQNGYY PTISSAAPGS TTAALGQDVP LEQRANVPGS FPVTPASEAD KFSVNPIPAS
SGAGNPIKLN PGEKVPDPST FNTNTISSTA RTDRAGYEQG ISGGFPGSPA YDASAFAIPP
VSKNMIPESS LPMGESQGAT EPTYTIQSAA PTSTTAGLAA AVPLESQRQT SSGAPTRDVP
DVVRQSMSEA HRDPEAATNK EAVDEKKEME EELRRKVPVD NSTGAPAPTT VAGLGTSSGL
GFTAGAAPST NLGPSTGLDV ATGMGTTTGL DSVSGPTAAQ SFQKETTSGL PAHDVPDVVK
QSISEAHKDP EAAGVEEAVG EKREVEEELQ QKVPVSNQSG TPAPVITAAT SETAPGSGAE
PASERAPRAT GGGPASAQIS PRATTPTDGP TVTTGVATSK APEESGPGVS GREETTEIPT
KPAAGATGAS ATKTVDSGVE SGIAPEDTTS APTAGATGAS ATKTADPTET SGAPTSGATK
PAESAPTNNA AATSKPATNN GAGAATNGKE EKKKKKGFFS RLKEKLKSV
//
