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Database: UniProt
Entry: A0A1R1PM34_ZANCU
LinkDB: A0A1R1PM34_ZANCU
Original site: A0A1R1PM34_ZANCU 
ID   A0A1R1PM34_ZANCU        Unreviewed;       961 AA.
AC   A0A1R1PM34;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Leucine-rich repeat-containing protein 40 {ECO:0000313|EMBL:OMH82007.1};
GN   ORFNames=AX774_g4532 {ECO:0000313|EMBL:OMH82007.1};
OS   Zancudomyces culisetae (Gut fungus) (Smittium culisetae).
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Harpellomycetes; Harpellales; Legeriomycetaceae; Zancudomyces.
OX   NCBI_TaxID=1213189 {ECO:0000313|EMBL:OMH82007.1, ECO:0000313|Proteomes:UP000188320};
RN   [1] {ECO:0000313|Proteomes:UP000188320}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL-18-3 {ECO:0000313|Proteomes:UP000188320};
RA   Wang Y., White M., Kvist S., Moncalvo J.-M.;
RL   Submitted (JAN-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:OMH82007.1}.
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DR   EMBL; LSSK01000762; OMH82007.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R1PM34; -.
DR   Proteomes; UP000188320; Unassembled WGS sequence.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR48051; -; 1.
DR   PANTHER; PTHR48051:SF1; ZGC:77287; 1.
DR   Pfam; PF00560; LRR_1; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   SMART; SM00365; LRR_SD22; 5.
DR   SMART; SM00369; LRR_TYP; 9.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF52047; RNI-like; 1.
DR   PROSITE; PS51450; LRR; 4.
PE   4: Predicted;
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188320};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..961
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012955172"
FT   REGION          132..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..161
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..226
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   961 AA;  107085 MW;  2377A69A240AD954 CRC64;
     MRISAAAFMT AGLVTGVLSM PAAPINVQDN SGLPRDTPVT GNSNMVPVIM VGNEEAASDR
     AIMTKLKEEM QSPDTGKSEK AAEVVQYLDQ MFSEEQAHLQ KRLGSTYKLA PRLNVSIVQM
     DGVKRTNKYQ HVKSSGYGVR SPTTYTNSRK GTATKDSDES IPPQKLSLIG VGPKNPEKND
     GGNNQTKKTG IPTTNIASIK KIPTIRRDGD ASYTKPSDDL KAKGASGTER KTFQPSVRKT
     AVTNTFTSSM RTDTGKVDRS VFSTRANVTR VGSRQINAQG TTVGRDLVSK DTNLSLSKIS
     PEFKKNPVLN TNKVSSQQGL AVERRYTRNN TINTLNKNVS GTATRSVQSK NNFRAGAASL
     HTSTTDKGKT EVVKPWRVKQ RKMDESEIFQ QMIQRARKEG RLNLSNRGLK EIPKAVYDMY
     EAQRSAIDMD LGTDSTEKWW ENEAMTYMNF SGNEIEMVEE KINVFNSLEH FDLSYNLIKQ
     LPTSFGEFNY LTVVSLAGNK FTEFPSVLTE LEGIEEVYLQ RNEISILPSD MGGLKKSLKI
     LDLSNNKIEK VKSQLEGMQV LKKVELSNNT ITEMPRGVDW LRGVEELGLS NNKLEYLFEF
     GDSVDGEIGL DNIVYLDASG NELRSLFKDE ANQDKIRFPN LSTLMLSKNN MTKMPCVINP
     LQMPRLTILS IAENGIEDIS GIFSRHGDGK LKLRRIDISN NRIKRLPREL IKQCDDLIGV
     DFEGNPLSAR PQGTTRSHLE AHFKRFEGMS GAGDERRSDI DVEWMDIDKN EQRIGGGGGV
     HEMVQETMKD KCDKKLKALV ESVGGKTMDL SEKLDVLKLD EANGSDISIK TLLDAVKNQN
     IGVDVRKLVL KNNRLEKIPL EVVELICIMN TGELEEIDLS NNQLLNVDEL YEVLSNENMS
     LVGQKLAKTK VLDLSNNKIS HFGGLNHYGN KERVLKLGQV FPELRELDLS NNRLTDIGTR
     Y
//
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