Fungal Genome Collection
University of Nebraska Lincoln
School of Biological Sciences and Center for Plant Science Innovation
Home About FGC Use Cases Species List


UniProt_SwissProt BLAST: Single locus
Species:
Saccharomyces cerevisiae S288C
Locus:
YNL214W
Length:
199
Number of sequences:
5887
Description:
YNL214W PEX17 SGDID:S000005158, Chr XIV from 245617-246216, Genome Release 64-1-1, Verified ORF, "Peroxisomal membrane peroxin and subunit of the docking complex that facilitates the import of peroxisomal matrix proteins; required for peroxisome biogenesis"
rec.SubjectHit LengthDescriptionAlign.LenE valueBit score% ident.  % pos.GO associations
1P40155    199   PEX17_YEAST Peroxisomal membrane protein PEX1...1993e-144     407     100     100GO:0005778; C:peroxisomal membrane; IMP:SGD.
GO:0005515; F:protein binding; IPI:IntAct.
GO:0016560; P:protein import into peroxisome matrix, docking; IPI:SGD.
2P80285    184   ATPF_MICLC ATP synthase subunit b OS=3333 / N...480.93     33.1     38     56GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.::GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.::GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
3Q00864    510   CHLB_PINTH Light-independent protochlorophyll...711.5     33.1     30     55GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
GO:0016730; F:oxidoreductase activity, acting on iron-sulfur proteins as donors; IEA:InterPro.
GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.::GO:0019685; P:photosynthesis, dark reaction; IEA:InterPro.
4Q95666    511   CHLB_PINST Light-independent protochlorophyll...712.5     32.3     30     54GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
GO:0016730; F:oxidoreductase activity, acting on iron-sulfur proteins as donors; IEA:InterPro.
GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.::GO:0019685; P:photosynthesis, dark reaction; IEA:InterPro.
5P37846    509   CHLB_EPHAL Light-independent protochlorophyll...792.7     32.3     30     52GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
GO:0016730; F:oxidoreductase activity, acting on iron-sulfur proteins as donors; IEA:InterPro.
GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.::GO:0019685; P:photosynthesis, dark reaction; IEA:InterPro.
6Q85X76    510   CHLB_PINKO Light-independent protochlorophyll...712.8     32.3     30     54GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
GO:0016730; F:oxidoreductase activity, acting on iron-sulfur proteins as donors; IEA:InterPro.
GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.::GO:0019685; P:photosynthesis, dark reaction; IEA:InterPro.
7Q2UN00    914   MANBA_ASPOR Probable beta-mannosidase A OS=As...1003.5     32     25     42GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO:0004567; F:beta-mannosidase activity; IEA:EC.::GO:0043169; F:cation binding; IEA:InterPro.
GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
8B8NP78    914   MANBA_ASPFN Probable beta-mannosidase A OS=12...1005.4     31.6     25     42GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO:0004567; F:beta-mannosidase activity; IEA:EC.::GO:0043169; F:cation binding; IEA:InterPro.
GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
9Q54SP2    1126   FORB_DICDI Formin-B OS=Dictyostelium discoide...1917.7     31.2     23     40
GO:0003779; F:actin binding; IEA:UniProtKB-KW.::GO:0005522; F:profilin binding; ISS:dictyBase.::GO:0017048; F:Rho GTPase binding; IEA:InterPro.
GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
10Q5BCI8    940   MANBA_EMENI Probable beta-mannosidase A OS=19...1008     30.8     24     42GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO:0004567; F:beta-mannosidase activity; IEA:EC.::GO:0043169; F:cation binding; IEA:InterPro.
GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
11Q91ZU6    7389   DYST_MOUSE Dystonin OS=Mus musculus (Mouse). ...709.1     30.8     23     47GO:0015629; C:actin cytoskeleton; IDA:MGI.::GO:0030424; C:axon; IEA:UniProtKB-SubCell.::GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.::GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.::GO:0005925; C:focal adhesion; IDA:UniProtKB.::GO:0031673; C:H zone; IEA:UniProtKB-SubCell.::GO:0030056; C:hemidesmosome; IDA:MGI.::GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.::GO:0014704; C:intercalated disc; IDA:UniProtKB.::GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.::GO:0009898; C:internal side of plasma membrane; IDA:UniProtKB.::GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.::GO:0035371; C:microtubule plus end; ISS:UniProtKB.::GO:0060053; C:neurofilament cytoskeleton; IDA:MGI.::GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.::GO:0005634; C:nucleus; IDA:UniProtKB.::GO:0097038; C:perinuclear endoplasmic reticulum; IDA:UniProtKB.::GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.::GO:0001725; C:stress fiber; IDA:UniProtKB.::GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
GO:0003779; F:actin binding; IEA:UniProtKB-KW.::GO:0005509; F:calcium ion binding; IEA:InterPro.::GO:0051010; F:microtubule plus-end binding; ISS:UniProtKB.::GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO:0007409; P:axonogenesis; IMP:MGI.::GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.::GO:0007050; P:cell cycle arrest; IEA:InterPro.::GO:0031122; P:cytoplasmic microtubule organization; IMP:MGI.::GO:0045104; P:intermediate filament cytoskeleton organization; ISS:UniProtKB.::GO:0046907; P:intracellular transport; IDA:UniProtKB.::GO:0031110; P:regulation of microtubule polymerization or depolymerization; IMP:MGI.::GO:0008090; P:retrograde axon cargo transport; IMP:MGI.
records
Previous ‹‹ ›› Next Total records: 11 1 - 11
Elimate unknown annotation:
Filter for keyword on hit description:
Select upper E value:
Select lower bit score:
Select lower %idenity value:
Select lower %positive value:
Taxonomic division:
Lower limit on hit length:
Lower limit on alignment length::