ID U4LAZ8_PYROM Unreviewed; 2405 AA.
AC U4LAZ8;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Similar to Ankyrin-1 acc. no. P16157 {ECO:0000313|EMBL:CCX11112.1};
GN ORFNames=PCON_10706 {ECO:0000313|EMBL:CCX11112.1};
OS Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Pyronema.
OX NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX11112.1};
RN [1] {ECO:0000313|EMBL:CCX11112.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX11112.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX11112.1};
RX PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT "The genome and development-dependent transcriptomes of Pyronema confluens:
RT a window into fungal evolution.";
RL PLoS Genet. 9:E1003820-E1003820(2013).
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DR EMBL; HF935594; CCX11112.1; -; Genomic_DNA.
DR STRING; 1076935.U4LAZ8; -.
DR eggNOG; KOG1477; Eukaryota.
DR eggNOG; KOG4177; Eukaryota.
DR OrthoDB; 33889at2759; -.
DR Proteomes; UP000018144; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd12885; SPRY_RanBP_like; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 4.
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; IPR003877; SPRY_dom.
DR InterPro; IPR044736; Vid30/RanBPM/SPLA_SPRY.
DR PANTHER; PTHR24118:SF99; CHARON; 1.
DR PANTHER; PTHR24118; POTE ANKYRIN DOMAIN; 1.
DR Pfam; PF00023; Ank; 3.
DR Pfam; PF12796; Ank_2; 4.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF00622; SPRY; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 20.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 8.
DR PROSITE; PS50088; ANK_REPEAT; 10.
DR PROSITE; PS50188; B302_SPRY; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 329..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 372..391
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 460..481
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 1190..1226
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1261..1293
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1330..1354
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1362..1394
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1395..1427
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1642..1666
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1676..1708
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1712..1744
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1843..1864
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1879..1911
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 2122..2323
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT REGION 235..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2344..2405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2344..2369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2405 AA; 268400 MW; 3BA6A2148E676EA9 CRC64;
MIFTALFTTM LALKTITSGF GTSRFTLILL FFAQTMADPA ISVPPTVAPG VSSFQDTSQS
SQRDGEEFSN NLVSDLAPLL ALFGERFAQQ YMSISTNWID SFIFAMAPLG RARETRAAAE
VELMSSTSHE VCEIWNGDSI VRVMGAPEIE QFIYFDSLPD EFVNLDNSSF KEGEAEETRS
GRNRGIYTLE AAKKANLLVR KEQDKINRLS GKLGEFFSKI QRNISTFTEQ NFLTDNHHGD
DFDPPDTQQK DSASFYGIRA RGLRRPTNRD PMDEEQGPDQ KKSSSKQDDH VSLDAESPTN
DSAESTEEND NSAPNISLNL GNTRKPWEIY TAAAFGLLIQ LGVLVVVGVV TYHPRWRFRK
GGLTVRNYAY PLCAVGLFLQ SIGMFICASV IEQSTLEETW IKNHNAKNSR MVCLWLQRRR
VINDQEFDSF AIFAKKPVES VMTSRRRQPR GENMSYPSSI TNIATACGLA LSVFGFILNF
MGLRGLHWSA TMAQLAATGI MTILRAIIRR GISSRPYAVK LSEHFELDWL ARAILKQSPG
FLEGENVIAG GDPVTSQEKP ERATSLVKTR KHLGRLSKWK SPVSGPAVAA ASAIEMVMNT
LFTNGRENGN NAMDPFTWDM DVRFHNPKAA RKDNQHTKTN APRKIAQDEI SLRVNVSHEE
HDMPQEGIAL PECSPPAEVT TPNRRPCEKI RLSVKKANGS KSWVADATEI EALLSLWLQQ
AADFESEQNK LHKSSTNTDK DWLRQKEQKK NLRFLGPDTV ALRRDLQWWV PDGALGLLKI
QKEKEKNVNS SSIDLNNHVI DYHRITGFYA PKHLKDLFSA PEKPLVEVSF ECTPITPDSL
EYVPKDTPHK NQSSYRSSQD KSLSDQALSP QRPQSLILSK APWETDAYAG PTALGMITGI
DREVLFAQHI FTAFMSAVAS KMDRIQGKSE AFQGAMTNRP TSWQHFRLQN TIVSRLALSV
KNTSLGSLEK AFFCIIPPLS MAHRLPLGVA VDSVLRSMAE DENILNWKRS VDVYSELLRF
SHEFHSPSCL FTVRAAAASI EYLNRMSNAE ELYAEKPSNT DLELLRKTKD TLLEALNNPV
SDNVNMLLRV LYKRQNRAKE YQWFMGEMTE SPELPKDPQK LRASETVVPG SSSTNSYPQS
PASPPADPLS TGDGYAMILG YSPLHNYVVS GLRVPPDPRW CEYVTESDIV GWTPLHYAVM
HTTNNNSCNY IEEILRIKAD PNERDIFGFT PLHYAASKND FQLEQWDLLL SIGQVNARAL
DGTTALHIAA KHGHFDAVKK LLQHKAQVDV QDSTKRTALH WAVYRRNPQI VDCMLAGGTL
GVAAQSRDFQ QNTALHLAAG HGDIDCVKRL IEHSHREARD RNGNTALHIS AKNGHHAVLK
LLLNYNACVD ATNNRGSTPL HLSIKHGRKE NVETLLEHQA NTEVLDVAGN TALHIATLKS
CCFVVNLLLK PEYKVDKMAR DREGRLALEI SAEKGNHGVF QLLYKITAKR ATIDKDEYQA
LYCAEECLRK CVEIATKEGN RDVFELPHDN TAKRATIDKD DYQEKLIAGY KEIIQELVQR
EIDRGVDREV DREMDREADR RVREVLEGPD VESTVMQTPL NETDCVQPGD ISASLIWNLS
KNSEIAKILL EQDDLADFLD TDGNTVLHLA AKYDKTDIAK SLLNNGKADI NAINTEGQTP
IATAVIAGHL KITEFLLSSR FKADLTTKDS RSGDTFLHLA VSKRRQNVID PLIQAGVLLD
VRNANGKTPL HLALHDFAAE KYTDIRRYQL GQWLRSKNEP RDTSKEPSLS IAKQLVNAGA
DINAVDKDGN TTLHICAERG QRDSVGLLLD TKYNTTVSLA NSTGRLALHM ASKEGYLEIV
EMLLAHDREG SVLKIKDFDG HTALDLAIKN GKGDVVECLL ENGGARNATH VEWCAYLLLA
MKHDTSGQER TCCCLLERVK KNTAGLELTI RHHFDRVLHW AYEMNYYSVA KMLFDFDFSM
DQRGVGGSTP LLLTILHFED EMVESDDNIT QGLSEKHASL DLVKLLLTKD ASIGLQDDYG
RSPLILATIR GQISILRIMC EMRPNETEDY HTALQIAILR NDIAITTELI NLGADLWKQD
EHGWTAHLCS LESQPNLRIS ELIAPNIPEG SQQYAPDYTF KPTAFSHQKK DPRIQVSEDG
LTVSYKNEDC GGMRARQAQI QANHPLLPIS QCSHRLSDSG CTDMYFEIDV LETDPESIVG
IGLSNGLVAR FDRFPGWENG SWGYHGDGGQ IFKNSGYGQR YCNEKYGKGD TVGCGVDLKR
RIFFTKNGRH LGDAWYGAYG KLFPLVGLIS NCRIRANFSG PFKYDFRAQN DTRTIKEATE
VDWSNSFEGS SNSGEPASKE RTNFAATTEM NDAPDAHDEH DSGSNSGDVG SDVAESSGPN
GPRGS
//