O13799

PR
Gene name
SPAC17H9.02
Protein name
Uncharacterized helicase C17H9.02
Names
Species
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
KEGG Pathway
spo:SPAC17H9.02
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-120 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for O13799

Entry ID Method Resolution Chain Position Source
AF-O13799-F1 Predicted AlphaFoldDB

10 variants for O13799

Variant ID(s) Position Change Description Diseaes Association Provenance
I_2005532_T_C 232 I>T No Jeffares_SNPs
I_2005926_T_G 363 N>K No Jeffares_SNPs
I_2006416_A_G 527 I>V No Jeffares_SNPs
I_2006728_C_T 631 P>S No Jeffares_SNPs
I_2006959_C_T 708 P>S No Jeffares_SNPs
I_2007266_G_A 810 R>K No Jeffares_SNPs
I_2007367_G_A 844 V>I No Jeffares_SNPs
I_2007593_T_C 919 M>T No Jeffares_SNPs
I_2007609_T_G 924 I>M No Jeffares_SNPs
I_2007869_G_T 1011 S>I No Jeffares_SNPs

No associated diseases with O13799

4 regional properties for O13799

Type Name Position InterPro Accession
domain PKD domain 832 - 904 IPR000601
domain VPS10 219 - 821 IPR006581
domain Sortilin, C-terminal 664 - 816 IPR031777
domain Sortilin, N-terminal 229 - 656 IPR031778

Functions

Description
EC Number
Subcellular Localization
  • Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
heterochromatin island A region of facultative heterochromatin formed dynamically at specific loci in response to environmental signals, independently of RNAi.
MTREC complex Protein complex formed by an RNA binding protein Red1, an RNA helicase Mtl1, Red5, Rmn1, Iss10/Pir1, and Ars2/Pir2. This complex is required for the recruitment of the nuclear exosome to Mmi1 nuclear focus. It is likely related to the human CBCN complex. This complex is also known as RNA silencing (NURS) complex.
nuclear body Extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins.
nucleolus A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
hydrolase activity Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
RNA binding Binding to an RNA molecule or a portion thereof.
RNA helicase activity Unwinding of an RNA helix, driven by ATP hydrolysis.

9 GO annotations of biological process

Name Definition
maturation of 5.8S rRNA Any process involved in the maturation of a precursor 5.8S ribosomal RNA (rRNA) molecule into a mature 5.8S rRNA molecule.
ncRNA polyadenylation involved in polyadenylation-dependent ncRNA catabolic process The enzymatic addition of a sequence of adenylyl residues (polyadenylation) at the 3' end of a non-coding RNA, occurring as part of the process of polyadenylation-dependent non-coding RNA catabolism.
nuclear-transcribed mRNA catabolic process, meiosis-specific transcripts The chemical reactions and pathways resulting in the selective degradation of meiosis-specific transcripts during vegetative growth, by a mechanism that requires determinant of selective removal (DSR) sequences in the targeted mRNAs and involves a YTH family protein.
regulation of siRNA-dependent facultative heterochromatin assembly Any process that modulates the frequency, rate or extent of siRNA-dependent facultative heterochromatin formation.
regulation of siRNA-independent facultative heterochromatin assembly Any process that modulates the frequency, rate or extent of siRNA-independent facultative heterochromatin assembly.
regulation of telomere maintenance via telomerase Any process that modulates the frequency, rate or extent of the addition of telomeric repeats by telomerase.
RNA catabolic process The chemical reactions and pathways resulting in the breakdown of RNA, ribonucleic acid, one of the two main type of nucleic acid, consisting of a long, unbranched macromolecule formed from ribonucleotides joined in 3',5'-phosphodiester linkage.
sno(s)RNA processing Any process involved in the conversion of a primary snoRNA family RNA transcript into a mature snoRNA (eukaryota) or sRNA (archaea).
tRNA catabolic process The chemical reactions and pathways resulting in the breakdown of tRNA, transfer RNA, a class of relatively small RNA molecules responsible for mediating the insertion of amino acids into the sequence of nascent polypeptide chains during protein synthesis.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSENSTDSKN FQFSEGSRES SNDELKVLLR DTETKEDEKS SFSNSEEESI IENLSDSSVN
70 80 90 100 110 120
KEYAKNSLKL SDAVSESKYL NPLLKDKRHD RSFALHKVVV PDDYDYIPLN KHIPSDPPAK
130 140 150 160 170 180
TYPFELDPFQ STAIKCVERM ESVLVSAHTS AGKTVIAEYA IAQALKNRQR VIYTSPIKSL
190 200 210 220 230 240
SNQKYRELLS EFGDVGLMTG DVSINPSASC LIMTTEILRA MLYKNSEIMH EIAWVIFDEV
250 260 270 280 290 300
HYMRDKDRGV VWEETLILLP DAIRFIFLSA TLPNALQFAR WISEIHKQPC HVVYTDYRPT
310 320 330 340 350 360
PLQHFIYPQG ADGIYMLVDE KNKFKTENFK KVLEVLDHST RQENYSKSSK KVKKSSSLER
370 380 390 400 410 420
IINMVLSNRY DPIIVFCFSK KECEINAHQF GKLDLNDTEN KELVTEIFDS AINQLSEEDR
430 440 450 460 470 480
GLRQFEEMRS LLLRGIGIHH SGLLPILKEL VEILFQEGLV RILFATETFS IGLNMPARTV
490 500 510 520 530 540
LFTKAQKFSG NNFRWLTSGE YMQMSGRAGR RGIDTKGLSI VILDQSIDEQ AARCLMNGQA
550 560 570 580 590 600
DVLNSAFHLS YGMILNLMRI EEISPEDILK KSFYQFQNME SLPLIKEELM QLKNEETSIN
610 620 630 640 650 660
IPNETAVKEF HDLKLQLEKY GEEIQKVMTH PDNCLPYLQS GRLIQIKLGG IIFPWGVLVN
670 680 690 700 710 720
VIKREFDPNT REQVAPHETY VLDVLLPISS NSMSNHKVNP SILVPPRPNE TPLYEIVSVL
730 740 750 760 770 780
LTAVCNISSI RIYMPRELNS NESKLRAYRR VNEVIEEFKE IPYLDPLEHM HIESSTLSLS
790 800 810 820 830 840
LRKLEILEPK LFDSPYYKDS KHRAEYHEFR KKLNLRAQIK DISTKITNTE AIIQLRELKI
850 860 870 880 890 900
RQRVLRRLGF CTLENVIDIK GRVACEITSG DELLLVELIF QGFFNQMPPE EIAAALSCFV
910 920 930 940 950 960
YEDKSEVSTL NLKEPFKKMY LTIIEAAKRI ATVSLESKLQ FNESDYLHQF KPDIMEPVSL
970 980 990 1000 1010 1020
WINGASFQEI CIVSKLYEGS IVRTFRRLDE LLKQLEHAAI VLGNNELKEK SVLTEQKLHR
DIIFSASLYL