ID A0A401KYF0_ASPAW Unreviewed; 716 AA.
AC A0A401KYF0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Ankyrin-1 {ECO:0000313|EMBL:GCB24399.1};
GN ORFNames=AAWM_07284 {ECO:0000313|EMBL:GCB24399.1};
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:GCB24399.1, ECO:0000313|Proteomes:UP000286921};
RN [1] {ECO:0000313|EMBL:GCB24399.1, ECO:0000313|Proteomes:UP000286921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 58123 {ECO:0000313|EMBL:GCB24399.1,
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:GCB24399.1}.
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DR EMBL; BDHI01000017; GCB24399.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401KYF0; -.
DR STRING; 105351.A0A401KYF0; -.
DR Proteomes; UP000286921; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 6.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR PANTHER; PTHR24178:SF9; ANK_REP_REGION DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24178; MOLTING PROTEIN MLT-4; 1.
DR Pfam; PF00023; Ank; 3.
DR Pfam; PF12796; Ank_2; 5.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 18.
DR SUPFAM; SSF48403; Ankyrin repeat; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Reference proteome {ECO:0000313|Proteomes:UP000286921}.
FT REPEAT 82..103
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 151..184
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 257..289
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 274..287
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT REPEAT 361..394
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 605..638
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
SQ SEQUENCE 716 AA; 79894 MW; 160D54418A8FB389 CRC64;
MLLDLPNEIL LCIAESFDRS RDILSFARVA RRTSHLLLPF LYKFNIGKQH SSALCWATQH
NVSRLAERLV REYHGNVNAV HNGNTPLLYA ASNGSIKVVD ALLASQQTQI NWRNAEGQSA
LWCAAWYGYI DIVKRLLQQH HIQVNIADRT RGTTPLAVAV IRGHAETVES LLTIRRVNVN
IRDRRGWTPV FHALSRAISY GDRSILEMIL TRPNADLLHQ DEEGRTPLIY AVQHNEASLT
AMLLRHPTSR TEPRDFHGRT ALWYAVQQGN TDIIQLLLDS GADIAVLDDY GETPLHKSIK
DGNLSTTSLL LRDPTVWAPV FALHAVNNVL PPLCMAADRG SIEMVRLLVE CGWYVNEVDV
EGRTPLHCAA ENGHDPVVQV LLTNEQLDVN ARDHRKSTAL HEAAWKGHLA VANLLLTKPN
IDINVEDRYG CTPLWYATRH GHHNVALRLL EESNVIVNAV CRFQTMPEKS TSLHHAVNCN
ATLTVQRLLV RTALNPNITD DCGRTPLCCA SHAGNLPMVE LLLGRPDVRV NAAEKSEQPP
LWSAASQGHI QVVERLLQCG DVDINQGWGP YSSPLLAAIT RGHSDVAMRL LNCVPRPDVN
ARTYLGDSAL SLAAREGHVD VVARLLEDWQ TDRNGADRQG RTALWWAARA GQARIVQRLL
EDDRVLVNVL DNDGVDAVDA ARTHYHFEVV GLIRSHYSRR YNNWTGGGPH NLRTRS
//
