ID A0A0D2IFB5_9EURO Unreviewed; 1675 AA.
AC A0A0D2IFB5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=B30.2/SPRY domain-containing protein {ECO:0000259|PROSITE:PS50188};
GN ORFNames=Z520_08514 {ECO:0000313|EMBL:KIX95806.1};
OS Fonsecaea multimorphosa CBS 102226.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIX95806.1, ECO:0000313|Proteomes:UP000053411};
RN [1] {ECO:0000313|EMBL:KIX95806.1, ECO:0000313|Proteomes:UP000053411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 102226 {ECO:0000313|EMBL:KIX95806.1,
RC ECO:0000313|Proteomes:UP000053411};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN848080; KIX95806.1; -; Genomic_DNA.
DR RefSeq; XP_016629929.1; XM_016779010.1.
DR STRING; 1442371.A0A0D2IFB5; -.
DR GeneID; 27714260; -.
DR VEuPathDB; FungiDB:Z520_08514; -.
DR OrthoDB; 1949153at2759; -.
DR Proteomes; UP000053411; Unassembled WGS sequence.
DR CDD; cd12885; SPRY_RanBP_like; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR044736; Vid30/RanBPM/SPLA_SPRY.
DR PANTHER; PTHR24126:SF14; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 10-RELATED; 1.
DR PANTHER; PTHR24126; ANKYRIN REPEAT, PH AND SEC7 DOMAIN CONTAINING PROTEIN SECG-RELATED; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00248; ANK; 11.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 4.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS50188; B302_SPRY; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000053411};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 1146..1180
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1181..1213
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1214..1246
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1322..1354
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1436..1645
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT REGION 743..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 244..287
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 743..763
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..879
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..906
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1675 AA; 186697 MW; A6D531E654D03F13 CRC64;
MSNYDQKKDE TFEKEAWNAA RAVFSGNHDP VNFQPFLKDY TTPESARSSV VQAQKEANSE
YNGKLGAILD KVDQFMKVGD LAIKSAPESI GLAWTGIRLC LHSVQDDFAT FSLFSGACSD
ILGILISCRV YGGLYASQDH PPEFTDLHEK VLSYIKETYV NIIEFSYQMW KYARSNAGVR
VIKGLFRSAQ GKFQPKIKAI KDNEAQMNKY ASQANQQVSQ YYQKKGLDND QKMMKGLSDQ
MEMLQAWHEE AAKQNQLLEE LMKRDELQRK DQRLTAAEIT HENWERQKKE LPSLDDNQQA
LESKMTDRKP GTCGWILENS KFQDFVKAEG GNVTWLVGTG GTGKSFLMSA VIEDLKNKAH
RHDSLVHYFF ISKASQATTQ ADEIERHLLA QLYQDAAQSL DTLDKCNKIM SEYIEHHNKK
NNTKTTSKKS GDGSAGFEQT YTALAKVINK RTYLMIDALD ECADRETQEF IQTIKKLAST
QGLKLNVFCS SRDEPDISAI LENCPRINVE ENNSKDIAEH VQAEMARLPG FTPAEREEAC
REITQKAGCY FRYVELAMDF MRRPWRRPLS SHLESLPSGV ENIYAQRLNQ TNPAYYDLLT
HCLTWTILAG EELGVQELID GYKGNFTDEE STPVVGEDQE NVNLELYEDQ IRQAGSGFLR
VNPDHTVSLV HNTVRDFFLQ SGSVANGSAK SASEPECQCA RCQRELKSSK KFVVSEREGH
MQIITTILHH LLSPLFQRKY YAKPPDKSDD KENDEKEVNG GDTTDVVKSE NVAAPAEATP
AEATPVAPPG APPAEAQDED IQNNGVQAQD QSPDDPADKL GSAQQISEHQ NEEAGTNSPP
EINGEPSEHV ASDDLDSKSD MPNGGSNQAQ ENNNPPNGEE TRDTNKDGAA DEETDDHSVV
DSDENVDLTD QDRARLWDLQ SASDLFQARY EITRLTWHLT QLEDVYPANE RSGEQWNKLR
ELLERFLDPE SEAWRGWIRT MCAAGRAIDT MEMYIDIEEL PPLVFAACCG LTSLAHILLA
RPNASDFVNL KMPEGMSVLS FVVTYQMTTE KNQDSFLLAM LEAGADPNAN NHWDDQYIGS
SFHFLLLCQT VSRAQLEMFL AHGADINNLD DSGGNALHFF AAGAADLEIG IALVEAGADM
HIRNSRGESI MHMLARRDNC RVDMMQYFID KGAEVDAEDD ASERPLLEAS LAGNCEAVRL
LLDHGADIED VNENDQTALF VAALAGNTEV VKVLLERGAD PLKRNSMGAT PFGMACRHGD
AESALLLGRA MVEKGEIEHL NWQNSSGKTP IMRAASRGIS KVIDFLLDHV DTEAALKTMS
KKGWTALHYA ALRARPEATI TLLNRGADSR CKDPQGKTPL QLCYAKIWTK PDEDREKTIS
ALIDHDRQAA IAEIELLHTL AINDSPDLVA KLLEFGANPY ATDEHGWNVL QLAEQYDRPD
VVEVIKASKL KAGSRPSRLV GSFSDVLICS PSGLEIELRE RGKPVAEPLE GFLCYATDQS
LITEHPIPAS AERYYFEMAI ADQENKPEDP MFVIGITQKP TGSTKLWFPG WSKPGTSSWG
YHSDDGKIWC VADPPKIKDL GSARKYGYGD TAGCGIDVKK RTVFWTLNGK RLMEAGFQNV
RGQIYPVIAV SHIGKVKVNL GLNLKDEPFL WLPGITCDFE SDVPPPSLRR LKSEH
//
