Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for A1CL59

Entry ID Method Resolution Chain Position Source
AF-A1CL59-F1 Predicted AlphaFoldDB

No variants for A1CL59

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1CL59

No associated diseases with A1CL59

6 regional properties for A1CL59

Type Name Position InterPro Accession
conserved_site ATP-dependent RNA helicase DEAD-box, conserved site 195 - 203 IPR000629
domain Helicase, C-terminal 280 - 437 IPR001650
domain DEAD/DEAH box helicase domain 38 - 237 IPR011545
domain Helicase superfamily 1/2, ATP-binding domain 33 - 262 IPR014001
domain RNA helicase, DEAD-box type, Q motif 14 - 42 IPR014014
domain Domain of unknown function DUF4217 438 - 501 IPR025313

Functions

Description
EC Number 3.6.4.13 Acting on ATP; involved in cellular and subcellular movement
Subcellular Localization
  • Nucleus, nucleolus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
90S preribosome A large ribonucleoprotein complex considered to be the earliest preribosomal complex. In S. cerevisiae, it has a size of 90S and consists of the 35S pre-rRNA, early-associating ribosomal proteins most of which are part of the small ribosomal subunit, the U3 snoRNA and associated 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.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
preribosome, large subunit precursor A preribosomal complex consisting of 27SA, 27SB, and/or 7S pre-rRNA, 5S rRNA, ribosomal proteins including late-associating large subunit proteins, and associated proteins; a precursor of the eukaryotic cytoplasmic large ribosomal subunit.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
RNA binding Binding to an RNA molecule or a portion thereof.
RNA helicase activity Unwinding of an RNA helix, driven by ATP hydrolysis.

3 GO annotations of biological process

Name Definition
assembly of large subunit precursor of preribosome The aggregation, arrangement and bonding together of a set of components to form the large subunit precursor of the preribosome.
maturation of LSU-rRNA Any process involved in the maturation of a precursor Large SubUnit (LSU) ribosomal RNA (rRNA) molecule into a mature LSU-rRNA molecule.
ribosomal large subunit assembly The aggregation, arrangement and bonding together of constituent RNAs and proteins to form the large ribosomal subunit.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAPNPPKGTS SRAWDAVTPP LSEWVLEAMS SMGFARMTPV QASAIPLFMA HKDVVVEAVT
70 80 90 100 110 120
GSGKTLSFLL PIVEKLLRLE EPIKKHHIGA IIISPTRELA SQIHSVMQSL LAFHPPSAAA
130 140 150 160 170 180
MTPLDDDDAP RQKFPSSTLK VVPQLLLGGS TTPAEDLSRF LKLSPNVLVS TPGRLLELLS
190 200 210 220 230 240
SPHVHCPQSS FEMLVLDEAD RLLDLGFKET LQNILRRLPK QRRTGLFSAS VSEAVDQIVR
250 260 270 280 290 300
VGLRNPVKIM VKVKGTSGVD DKRTPASLQM TYLSTPPLHK FAALKNILSS VQPTPQKSIF
310 320 330 340 350 360
FVSTCSGVDY LSAILPLLLG DDFLLIPLHG KHQANVRQKN FNRFLSSHSP AILLTTDVAS
370 380 390 400 410 420
RGLDIPSVDL VVQIDPPSDP KTFIHRCGRA GRAGRRGLSV VMLHPGREED YVSFLDVRKT
430 440 450 460 470 480
PVVPFSPSIS FSDADATSAT ARARKAVLAD RALHDRGQKA FVSWLRSYSK HQASSIFRVA
490 500 510 520 530 540
DLDWEALGKA WGLLKLPKMP ELRSFTGDKT LGVSLDWDNF SYKDKQREKR RKELLQEAAE
550 560 570 580 590 600
SGVSQPSSNK RRASESVAWS QNAENKNKKL QRREYKKLKQ EKTKWENMTE EERQKARETK
610 620 630
EMVEELRAKN LEERRFRQAA AKAETAKAGG EDEEFKGFD