Q1DKI1

PR
Gene name
DCL1 (CIMG_13589)
Protein name
Dicer-like protein 1
Names
Species
Coccidioides immitis (strain RS) (Valley fever fungus)
KEGG Pathway
cim:CIMG_13589
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-111 (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 Q1DKI1

Entry ID Method Resolution Chain Position Source
AF-Q1DKI1-F1 Predicted AlphaFoldDB

No variants for Q1DKI1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q1DKI1

No associated diseases with Q1DKI1

6 regional properties for Q1DKI1

Type Name Position InterPro Accession
domain Ribonuclease III domain 1029 - 1189 IPR000999-1
domain Ribonuclease III domain 1223 - 1397 IPR000999-2
domain Helicase, C-terminal 426 - 597 IPR001650
domain Dicer dimerisation domain 623 - 713 IPR005034
domain Helicase/UvrB, N-terminal 101 - 269 IPR006935
domain Helicase superfamily 1/2, ATP-binding domain 95 - 303 IPR014001

Functions

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

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

6 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
helicase activity Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive the unwinding of a DNA or RNA helix.
metal ion binding Binding to a metal ion.
ribonuclease III activity Catalysis of the endonucleolytic cleavage of RNA with 5'-phosphomonoesters and 3'-OH termini; makes two staggered cuts in both strands of dsRNA, leaving a 3' overhang of 2 nt.
RNA binding Binding to an RNA molecule or a portion thereof.

4 GO annotations of biological process

Name Definition
defense response to virus Reactions triggered in response to the presence of a virus that act to protect the cell or organism.
gene silencing by RNA A process in which an RNA molecule reduces expression of target genes. This can occur pre-transcriptionally by assembly of heterochromatin and prevention of transcription or co- or post-transcriptionally by targeting RNAs for degradation or by interfering with splicing or translation. This process starts once the inhibitory RNA molecule has been transcribed, and includes processing of the RNA such as cleavage, modifications, transport from the nucleus to the cytoplasm, loading onto the RISC complex, and the effect on transcription or translation.
regulation of defense response to virus Any process that modulates the frequency, rate or extent of the antiviral response of a cell or organism.
RNA processing Any process involved in the conversion of one or more primary RNA transcripts into one or more mature RNA molecules.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MEEPQRINDE PNDSVVPDPA GPSEPAESDS EDEHTHPNNA DEPSIRRKQN LRFKELLSAR
70 80 90 100 110 120
AEEITAEDIK EVIKATKDDE LSMSNLLAKQ DFASVIHDPR EYQVELFEKA KKDNIIAVLD
130 140 150 160 170 180
TGSGKTLIAV LLLKHIIEQE LIDRSAEKPH RVSFFLVDSV TLVFQQAAVL QNNINQRVDK
190 200 210 220 230 240
FCGAMETDLW NGETWERHLA KNMVIVCTAE VLYQCLLHAF VKMENINLLI FDEAHNAKKD
250 260 270 280 290 300
HPYARIVKDF YLKDGNAKRP KIFGMTASPV DAKMDVVKAA RNLETLLNSQ IATASNLSLL
310 320 330 340 350 360
RQSVPRPNEE VWSYDRLDQP FETRLYKELR SRFGDLRALE KLFTFSLKAS SNLGAWCADW
370 380 390 400 410 420
VWSYALTEES LPKLEGRAAR TAMGNLPIAK IVRPEAEIQR IREASEIIRS HKFGDPAVRP
430 440 450 460 470 480
ELLSPKVRRL HHELLKYFER HTDTKCIVFT EQRHTARILC DLFSRIGTKH LRPGVLIGVR
490 500 510 520 530 540
SDASGGMNIS FRQQVLAVVS FRKGEVNCLF ATSVAEEGLD IPDCNLIVRF DLASTLTQYI
550 560 570 580 590 600
QSRGRARHMN STFAHLVERD NFVHRESVNH LQSSEEIMKR FCISLPKDRI LNSDDVDALY
610 620 630 640 650 660
ESDRNRKSYT VQTTGAKLTY SSSLVVLAHF ANSLQYEKET STVVSYYHRF TKNAFVCEVV
670 680 690 700 710 720
LPEKSPIRGI VGKPASKKLI AKQSAAFETC LLLRKHGLLD DHFVSTYHKR LPAMRNARLA
730 740 750 760 770 780
ISSKKSNQYD MKVKPKLWET SRGIIPTSLN IVVLGFRPRR LLHREYHPLV LLTREKLPHF
790 800 810 820 830 840
PEFPLYLEDD IECDVICSSI SSGFQVSSHD LEVLTTFTLR IFQDIFHKVY DRDVGMMTYW
850 860 870 880 890 900
LAPLNLSCDI SSSASRDLLD WGILQFVFDN PEIPWSSSNS AAFFANRFVY DRWDGRYRYF
910 920 930 940 950 960
THGIDPSLRP SDPPPSSMAR RRHMGNIMDY CLSLFKNARK KFLENCDWTQ PVIKAEIIQL
970 980 990 1000 1010 1020
RRNLLDKRTN KEKIKEGDYY ICLEPLTISA IPASVAAFAF AFPAIISRIE SYLIALEACQ
1030 1040 1050 1060 1070 1080
ELDLPISPEL ALEALTKDSD NTDEHRAQQI HFQRGMGKNY ERLEFLGDCF LKMATSISLF
1090 1100 1110 1120 1130 1140
AMNPDNDEYD FHVKRMCLVC NQNLFKTAVR FKLYAFIRSQ SFSRRGWYPG GLTLLQGKGQ
1150 1160 1170 1180 1190 1200
SKGATENKHA LADKTIADVC EALIGACCLL ASKNHRFDIA VKAVTALVSS DDHNVLNWEQ
1210 1220 1230 1240 1250 1260
YSRLYSIPKY QTAVVDAAEL DLAAQVKKKL GYDFKYPKLL RSAFTHPSYP SAWARVPCYQ
1270 1280 1290 1300 1310 1320
RLEFLGDALL DMACVEHIYH KHPDKDPQWL TEHKMAMVSN KFLGSVAVRL GLHSHLNHFS
1330 1340 1350 1360 1370 1380
TSLQSQITNY VEEIEAAELE SGDPPDAWTL TSDPPKCLPD MVEAYIGAIF IDSGFSFEVV
1390 1400 1410 1420 1430 1440
EEFFQKFLKK HFEDMTIYDT YANKHPTTYL HNRLAIDFGC SNYCLKAGEV PYVDGPGTRV
1450 1460 1470 1480 1490
LAAVIVHDEV VAEGVASSSR YAKLKASEAA LSKLEGLPPF RFREIYGCNC QAGQSEAGNE