ID A0A167E4J9_9PEZI Unreviewed; 1304 AA.
AC A0A167E4J9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Ankyrin repeat protein {ECO:0000313|EMBL:KZL84696.1};
GN ORFNames=CI238_07888 {ECO:0000313|EMBL:KZL84696.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL84696.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL84696.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL84696.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) 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:KZL84696.1}.
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DR EMBL; LFIW01000814; KZL84696.1; -; Genomic_DNA.
DR STRING; 1573173.A0A167E4J9; -.
DR Proteomes; UP000076584; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
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; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR PANTHER; PTHR23206:SF7; ANKYRIN REPEAT AND KH DOMAIN-CONTAINING PROTEIN 1 ISOFORM X1; 1.
DR PANTHER; PTHR23206; MASK PROTEIN; 1.
DR Pfam; PF12796; Ank_2; 4.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 13.
DR SUPFAM; SSF48403; Ankyrin repeat; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 9.
DR PROSITE; PS50088; ANK_REPEAT; 11.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Reference proteome {ECO:0000313|Proteomes:UP000076584};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 881..913
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 914..946
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 970..1002
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1003..1028
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1035..1067
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1052..1093
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT REPEAT 1067..1108
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1109..1141
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1142..1174
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1175..1207
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1208..1240
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1241..1275
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
SQ SEQUENCE 1304 AA; 143789 MW; F5D1F9A0C9553150 CRC64;
MAMLDDTHPD LPKAPNDHNA YTLGSVGEHN IVIACLPKGQ YGTASAATVA TRMIMTFPAI
KFGLMIGIGG GIPVKVRLGD VVVGTPTGQF PGVVQWDLGK ATDGGGFQRT GALNNPPAVL
VSALQKLESR HELHGSKVNE YLEEMVRRYP RLKSKYARSA ALEDVLFKSE YAHVDRTPTG
SLGTAFEDVE EDEEEEEDER EGGCLHCDRT KTRKRKPRTH MKVHYGLIAS GNQVIKDAVR
RDKLNKDLGG NVLCVEMEAA GLVNNFPCLV IRGICDYADS HKNKAWQEHA AAVAAAFARE
LLGYVQPRDV DEECSVLEQI PELQRKVQEI HSATSAIGDD VRHLGTLAQS AADQEILDWL
TPIDYGSQQS DTLRRRQKGT CEWFLASEEY RLWLETPGQT LFCPGMPRAG KTVLTSAVVD
NLTTRYSADL SIGVAYVYFN FRQQSTQQLE DMLSSLLKQL AWAQCILPKS IRDLHTNHNR
SRTRPSETEI SQALSEVSKS FSRVFFVVDA VDECQADGCR PKFLSTLFNL IRSHSVRANV
FATSRFMSDI ERKFEGSIRR EIKAVDQDVC RYIQQYLPEI FTRITPLPGL EVEITNGIVS
AVSGMFLLAQ LYLASLKDTT SVAEVRTVLK GFKIQQSVRN GVENAMERAY DQAYDEAMIR
LNGQTPKLRD LGRRMEDPYF DCDNIREVNV ILSVCAGLVT VDQDSNIIRL VHYTAQEFFQ
RKNAQGNLDD HCHMTETCIE YLRFALDRCS LPASPSQFAS SELAQTYPLT SYAHYNWGYH
ASKATTLSQR VIDFLLNYEK PTELHKSLRF GNITTPTTPL EWAAYHGILK AIDWFHKGEL
ITNVGVSFSI SKALHWAIRQ GQVESVECLL GLGTTLTQNE TKETPLHLAA YRGNIAVIAM
LLAHGADINA TNSSGWSPLD IASKQGDLDV IKFLLEKGAS VSVDTTYNSS PAVMAMLIEY
GVDIDAVNSS GKRPLEIALE RGDLGRVKTL LQKGASIDAA DTYGRTPIEI AARKHDLASA
DLLLEKGAVC TLGLSEFPPL NEVVSDGCFK LMKYLIDNGA DVNLRTNAKT PLHYETERHV
NRRADLSGLG AVVSFLIEKG ADIEAKDEDG RTPLAVACKF GHDTTVRLLI ERGADIETKD
NNGMTPLANA CFLGHDAAVS LLIEKGADIE VKDEDGRTPL VIACKFRRDT AVSLLVEKGA
DIEAKDEDGR TPLVIACFLE YDAAARLLIE KGADIEAKDE DGRTPLAIAC MSGYGEVAVV
SLLVEKGADI EAKDEDGRTP LTIARKCGQD DLAKILREAV VDRT
//
