KLDC1_ARTBC
ID KLDC1_ARTBC Reviewed; 668 AA.
AC D4AYG1;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Kelch repeat-containing protein ARB_01230;
DE Flags: Precursor;
GN ORFNames=ARB_01230;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(2011).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}. Secreted {ECO:0000269|PubMed:21919205}.
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DR EMBL; ABSU01000018; EFE31977.1; -; Genomic_DNA.
DR RefSeq; XP_003012617.1; XM_003012571.1.
DR AlphaFoldDB; D4AYG1; -.
DR SMR; D4AYG1; -.
DR STRING; 63400.XP_003012617.1; -.
DR EnsemblFungi; EFE31977; EFE31977; ARB_01230.
DR GeneID; 9522694; -.
DR KEGG; abe:ARB_01230; -.
DR eggNOG; KOG0379; Eukaryota.
DR HOGENOM; CLU_012508_0_0_1; -.
DR OMA; QMNVIDV; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR Gene3D; 2.120.10.80; -; 2.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR SUPFAM; SSF50965; SSF50965; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Kelch repeat; Membrane; Reference proteome; Repeat; Secreted;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..668
FT /note="Kelch repeat-containing protein ARB_01230"
FT /id="PRO_0000434930"
FT TOPO_DOM 33..522
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 523..543
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 544..668
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 62..108
FT /note="Kelch 1"
FT /evidence="ECO:0000255"
FT REPEAT 125..176
FT /note="Kelch 2"
FT /evidence="ECO:0000255"
FT REPEAT 283..331
FT /note="Kelch 3"
FT /evidence="ECO:0000255"
FT REPEAT 340..395
FT /note="Kelch 4"
FT /evidence="ECO:0000255"
FT REPEAT 396..445
FT /note="Kelch 5"
FT /evidence="ECO:0000255"
FT REPEAT 463..509
FT /note="Kelch 6"
FT /evidence="ECO:0000255"
FT REGION 611..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 668 AA; 71480 MW; 9AFF97A28BDB8A97 CRC64;
MEVGRFASKS ASMTYLLLVL LVGFILPQQG QHAHARTLAR RDNSPTDICK RWSQQTAIVN
GTLYIYGGRS TTDASQKDNT WNDNFLTLDL KSSWGISAPK LTGLPRGDNG PPPVSNGYLW
NSFSSLFLYG GEFSDNPATE PVDFSLWEYS IPSSSWIEHK SPKTSSGENS AEANIPVQRS
AEGAGINVPD LGRGWYFGGH LDGYTTKGWS QSIPRVYLKS MIEYTFPGHT NNGVKINTDD
KRAGPEGVWR NITEGGLQDS AGFTERADGV LVYIPGFGKE GIILGLAGGT NATFTQMNVI
DVFDIASSKW YKQATSGKTP KIRVNPCAVA ASAADGSSTQ VYLFGGQNLI PYGEQIQYND
MWILSIPSFT WIEAKTDGQS VPPARAGHTC NIWNSQIVVT GGYVGQDLSC DSPGIYVFDA
SELTWKNQYT ALEGGNDLNQ QASQTRDSSG LGGSYGYRVP KVVQSVIGGD ETGKATQTVP
AVAPTDGPLA TGQPLTYTVL PTAGSGPHAG SPGSGSDGPN IAAIVAGVIA GCLGVLAIYL
GFVTWLYRRR LAIYKSHLAA TQRSSIGSYG DKISSFPPRY SDHMSSSGLG TTGSTGNLTV
TTARMSWISG DNQRHNHTRS SSGGNFDHLA QPERPSTSSS VEDLLAGQEP TFLGVMLNPR
QTLRVINQ