ID Q6MYM9_ASPFM Unreviewed; 1407 AA.
AC Q6MYM9; Q4WSJ5;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Suppressor protein spt23-related, with ankyrin repeats {ECO:0000313|EMBL:CAF31974.1};
GN ORFNames=AfA5C5.015c {ECO:0000313|EMBL:CAF31974.1};
OS Aspergillus fumigatus (Neosartorya fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=746128 {ECO:0000313|EMBL:CAF31974.1};
RN [1] {ECO:0000313|EMBL:CAF31974.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=14998527; DOI=10.1016/j.fgb.2003.12.003;
RA Pain A., Woodward J., Quail M.A., Anderson M.J., Clark R., Collins M.,
RA Fosker N., Fraser A., Harris D., Larke N., Murphy L., Humphray S.,
RA O'Neil S., Pertea M., Price C., Rabbinowitsch E., Rajandream M-A.,
RA Salzberg S., Saunders D., Seegar K., Sharp S., Warren T., Denning D.W.,
RA Barrell B., Hall N.;
RT "Insight into the genome of Aspergillus fumigatus: analysis of a 922 kb
RT region encompassing the nitrate assimilation gene cluster.";
RL Fungal Genet. Biol. 41:443-453(2004).
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DR EMBL; BX649606; CAF31974.1; -; Genomic_DNA.
DR OMA; HPMMRRI; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; 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; PTHR24171; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 39-RELATED; 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|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1359..1376
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 817..884
FT /note="IPT/TIG"
FT /evidence="ECO:0000259|Pfam:PF01833"
FT REPEAT 1007..1039
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1040..1072
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 91..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1257..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..574
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..751
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1407 AA; 153066 MW; 337D0243974482FF CRC64;
MMGAVEVASS PVFPSLDPIV VDDEMENPYQ DTDLNFLDST RLQMNEAAGQ DFDDLFARSH
SSHTVTDSES VCLSPSELSI KRHFQEHDAL RQPKIVASDS PAESLDNSSP SSSSDSPRNH
GRNTSVASTT SVTNSDQANI MPFGYATEDW INSELGSMKE ETSMFGFDPS LPAMESVFPV
ETDLESSNKA MDAAFDFESA ASSPSALKTD PTAQPKIQKR PKSQMRGTSH SIPRQSASPQ
SRHSVSPFTA GKMPSQSRSS SSHWAGQSPS SLLEESFGGI NMNGGSPLNG NFNFASNGFP
FGINFAPSPP QNNMKAEATQ RHVLTVHPTS LKSRVETQIP IRLTLYPMPS GVKKLRLPTH
TISKPKFLAP PSADRSADTL QLHTSLVCTS AMQDQTKLRK AFARARGETR YRASSSSPNA
TEELPEDDKP LDGGEVKICA GCIQRERKRA FRKKQRKPEE DELFQKDEEK RVIVFNTNEI
KDWAEPSKHA MPGYTDAPAP VIPAGAMQVE LPMRIACYCR HQNEKLGFQV IFTVKDHMDN
VIAQAITNSI MITDDHKTHA PPAPPAPGPS PSLPDGTQLP GVGVFPSGLP VETAKSPVQS
FRSSSTTDLQ GLQQRFNSQY QMSTGSFTTS AQNGQNGQKN ATASSQTPRS LSRQTSPNDF
PGPMTKRRKH SNSGRLPSDL TMTKLENGQS SVGGSNSGVL GNDTSFNAAR GFASPAERPF
VTPSAMSGQF ANRPPTPNSG DNNPFFNPSA TQTSLDTFIQ QQLMSAPNSA QPSRPGTPGN
SARHGFQDQS INISLGSSTS TPAWPPLTNA GNRLPSVIHK VVPAEGSITG GTEVTLLGSG
FYPGMEVVFG DTLATTTTFW GDKCLNCLTP PALQPGMVAV VFKHEHPTFG QMQPAQPLMP
KQQQFFRYVD DRELQMYRLA LGILGQKLGN QADAFQTAQQ IMGSDPKAVF NLQKDFSAGS
GGHQRQVPGL ESQGELSDLD SKMLTYLEFI DLDDNPRPPK YNSRCATGQT LLHFASSLGL
TRFVAGLLAR GANPEVQDNI GNTPMHLAAL HGHAHIVNKL RLAGADVNAR SIRGFTPADL
ATTLPAHQAA LIPARHNRSR SVGSVTSSRR RHSSSASLHS LWESSSVSGS IDPAVYDSHD
EEDDSDDQVD FTISRRSSVH QDVPGPLPSP EQATAAQEAR PFSPPAALVA WRNQLQAQIN
QFQQSVANAF PNLPALPPMP ALPDYQAHPM MRRITNLVPH RPTTSWSSKD GWWDLLTGNS
APSATEPPSY EELYPGQDRQ DEEEASQLKK ATLLRAAAEA AVDQHFESQA NTSVAESSKQ
DNDDIKDIRI GSKLISREQQ KHLREQQARR MKGLGSDRNL YFIWLPLLLL VICAWMRSYV
PGIWQGALDV YGFVKTRYMR GTLDVGS
//
