ID A0A3M2SY21_9EURO Unreviewed; 1393 AA.
AC A0A3M2SY21;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Ankyrin repeat protein {ECO:0000313|EMBL:RMJ22423.1};
GN ORFNames=PHISP_06709 {ECO:0000313|EMBL:RMJ22423.1};
OS Aspergillus sp. HF37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1960876 {ECO:0000313|EMBL:RMJ22423.1, ECO:0000313|Proteomes:UP000272442};
RN [1] {ECO:0000313|EMBL:RMJ22423.1, ECO:0000313|Proteomes:UP000272442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HF37 {ECO:0000313|EMBL:RMJ22423.1,
RC ECO:0000313|Proteomes:UP000272442};
RA Tafer H., Lopandic K.;
RL Submitted (APR-2017) 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:RMJ22423.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RAQS01000338; RMJ22423.1; -; Genomic_DNA.
DR STRING; 1960876.A0A3M2SY21; -.
DR Proteomes; UP000272442; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd00102; IPT; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR PANTHER; PTHR24173; ANKYRIN REPEAT CONTAINING; 1.
DR PANTHER; PTHR24173:SF71; SOCS BOX DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01833; TIG; 1.
DR SMART; SM00248; ANK; 2.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000272442};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1346..1366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 792..860
FT /note="IPT/TIG"
FT /evidence="ECO:0000259|Pfam:PF01833"
FT REPEAT 982..1014
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1015..1047
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 60..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1393 AA; 150764 MW; B8BCEE7335BF6C3C CRC64;
MESANVASSP SFPVLDPIIV DDDMENTYRD TDMDFLDPAR LSMSSADAGR DFDDLFAHAA
SPRATPASES SRLSPSELSG KHQYKEHDKL KQPHMLTSGS PAESPDNSSR SSSSESPRNH
IRNPSVTSSS SAAHSENTAA PFRFSSEDWM NPELESVKEE PLFGLDNAMP ADGGLAMGPD
MESSNKAMDA AFDFESAASS PSYLNSDSTS QAKYKARVKS KLRSSPNSTR RSVDKHLPTS
GLPFFHGFNN DPSSFSASKP SGQARSPSSH WEGQSPSSVL EESFGGISMS GGSPLNPALS
SNVNYAPNLP FGMDFASPGS QRNLKSENPQ RHILTVHPTS VKSRVETQIP IRLTLYPLPA
GVTKLRLPGH TISKFKFLAP PSTEPSSDTL ELHTSLVCTS AMQDEDKLKR AFARARGDRT
SPGSASNLAD GSLEDDKPSY GGEVKICGGC IQRERKRASR KKQRKPEEDE LFQKYEEQRV
IVFNTNEIKQ WSEPSKHAVP GYGDIPGPAV PAGAMQVELP MRVACYCRHQ NEKLGFQVIF
TIKDHLRNVV SQAITNSIMI TDDHKTHSAP APPAAGPGPS PVLPDGTQLP GVGVFRSGAV
DPKGQQPGSY ALPQNSANGA SNSQAPRSLS RQASPNEFQG PMSKRRKRSS SGRLPPELVM
TRAGSQPTGT SYVSGTNSGT QSPTPRGYAS PTERPFVTAS AMSNQFTNGP PTPNSNDNIP
FFNPTAQHSS LDSIVQQQLV SAPNPSHPSR PGTPGGSTRN GLQDQNLNVT AGPNATQQMW
PLTSAGNRLP SVIHKLVPAE GSIAGGTEVT LLGSGFYPGM EVVFGDTLAT TTTFWGDKCL
NCLTPPALQP GLVAVVFKHE HPTFGQLQPT PPMIPKQQLF FRYVDDRELQ MYRLALGILG
HKLGNQADAF QTAQQIMGSD PKAVINAQKD IHSGSSGNQR QVPGLDAQGK MSDLDSKMLT
YLEFVDLDDS PRPPRYNSRC ITGQTLLHFA SSMGLTRFVA GLLARGANPD VQDNTGNTPM
HLAALSGHAH IVHKLRLAGA NPNARSIRGF TPADLGISLA AHQAALLPSH NYRSRSVGSL
ASSRRRQSSS TSLNSLWEST SASESLGRTV DDSDDVDEDR ADAESDSDVQ ESSLNYTMSR
RSSAHQNADA GPVQTPGEQA EVPEDGRGFS PPAALIAWRN QLAAQINQFQ QGVANAFPNL
PALPPMPALP DYQAYPMMRR ITNLVPNRPA ATRAAGDGWW DMLKGNSAQS SNEPPPYEEL
YPRKEDDDGE ASNLKKTSLL RAATDTVVDQ HFEAQASAPE SSRANEQQEE IQDVKIGRKV
ISREEQKQLR EHQARRMKGL ASDRRLYLIW IPLLLLVICA WLRSFVPDIW EGVSGVYEFV
KSRYAQRALE VGN
//