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Conserved domains on  [gi|24641139|ref|NP_572663|]
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uncharacterized protein Dmel_CG1582, isoform A [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HrpA super family cl34328
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
452-1075 3.73e-119

HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member COG1643:

Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 390.98  E-value: 3.73e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  452 QLPAFAEIERILALIESSPVVVISGETGCGKSTQVPQFILD-NWFFRALqlpakenlphveIICTQPRRLSAIGVAERVA 530
Cdd:COG1643    9 DLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLElGWGAGGR------------IGMLEPRRLAARAAAERMA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  531 AERLDRIGQLVGYQIRLENKVSQSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSEESDFlllil-knllRERKD 609
Cdd:COG1643   77 EELGEPVGETVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLllallldlqpALRPD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  610 LKVILMSATLNAALFSDYFGGAPVLDIPGRTFPVqqlfledilemsdfvmeyDTKYcrklkkQEQEILERELEYADVQAS 689
Cdd:COG1643  157 LKLLVMSATLDAERFARLLGDAPVIESSGRTYPV------------------EVRY------RPLPADERDLEDAVADAV 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  690 GEApgkkikdekltLAETyqryaeyskptcksiylmepmtinpeliesvlkyivegshdwprEGTILIFLPGFGEIQSVH 769
Cdd:COG1643  213 REA-----------LAEE--------------------------------------------PGDILVFLPGEREIRRTA 237
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  770 DSLldnalfSPRAGKFILV-PLHSALSGEDQALVFKKAPPGKRKIVLSTNIAETSVTIDDCVFVVDCGLMKEKCFDSNRN 848
Cdd:COG1643  238 EAL------RGRLPPDTEIlPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSG 311
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  849 MESLDLVWVSRANAKQRKGRAGRVMPGVCIHLYTsyRYQYHIL-AQPVPEIQRVPLEQIVLRIKTL-----QTFAsrntl 922
Cdd:COG1643  312 VTRLPTERISQASANQRAGRAGRLAPGICYRLWS--EEDFARRpAFTDPEILRADLASLILELAAWglgdpEDLP----- 384
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  923 svlleTLEAPTEDSVLGALTRLRDVGALDAEDQLTPLGHHLAALPVDVRIGKLMLYGAIFQCLDSVLTIAACLSNKSPFv 1002
Cdd:COG1643  385 -----FLDPPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPR- 458
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24641139 1003 splnkRTEADkckrmfalgnSDHLTVLNAYRKWLDvarrgnyaasrnyASEHFLSLNTLETIADLKYQYLELL 1075
Cdd:COG1643  459 -----RGAAG----------SDLLARLNLWRRLRE-------------QQREFLSYLRLREWRDLARQLRRLL 503
RWD_DHX57 cd23825
RWD domain of DEAH box protein 57 (DHX57) and related proteins; DHX57 (EC 3.6.4.13) is a ...
175-367 2.97e-42

RWD domain of DEAH box protein 57 (DHX57) and related proteins; DHX57 (EC 3.6.4.13) is a putative ATP-dependent RNA helicase. A genome-wide association study (GWAS) of cerebellar epigenetic age acceleration identified significant SNPs (single nucleotide polymorphisms) in a loci 2p22.1 inside the DHX57 gene, suggesting that variants in DHX57 are associated with epigenetic age in the cerebellum.


:

Pssm-ID: 467661  Cd Length: 115  Bit Score: 150.04  E-value: 2.97e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  175 QEILDMRADEKEALESIFDKAYEEREANRVWNLKFRIDHLLahspsevrkareavlaaaaaaaqaaldkkkkpplrcrnf 254
Cdd:cd23825    1 DELLEQRQEEAMALESIYGEAFSERIPNKVWTIKLDLPYLP--------------------------------------- 41
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  255 drdgtckygpkcrfahlpqqptesdttkkdsvdendnelWFHVEVRFPPGSRYPYEAPFIYLKTTCHDIPHELRLRYARH 334
Cdd:cd23825   42 ---------------------------------------WFELEIRFPKGNKYPYEPPIVAFSSTNENFPKAVCLNITER 82
                        170       180       190
                 ....*....|....*....|....*....|...
gi 24641139  335 LYKEAKEICRDGIPCVYSICDLLQSNEQLAGRL 367
Cdd:cd23825   83 LMEEALELAEDGEPVVFSLVSLLEDEEEILELL 115
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
1114-1212 6.96e-18

Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus of the DEAD-box helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. There do seem to be a couple of instances where it occurs by itself -. The structure PDB:3i4u adopts an OB-fold. helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. This C-terminal domain of the yeast helicase contains an oligonucleotide/oligosaccharide-binding (OB)-fold which seems to be placed at the entrance of the putative nucleic acid cavity. It also constitutes the binding site for the G-patch-containing domain of Pfa1p. When found on DEAH/RHA helicases, this domain is central to the regulation of the helicase activity through its binding of both RNA and G-patch domain proteins.


:

Pssm-ID: 400182 [Multi-domain]  Cd Length: 82  Bit Score: 79.60  E-value: 6.96e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   1114 LTSLLCAALYPNIVKiMTPDRVYIQTAggavprepshhdlrfktRGDGYVKIHPSSVNSQVSVFQAPFLVFQEKVRTSAI 1193
Cdd:pfam07717    1 LRAALAAGLYPNVAR-RDPKGKGYTTL-----------------SDNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKV 62
                           90
                   ....*....|....*....
gi 24641139   1194 YIRDCSMLPLIAMVLFAGS 1212
Cdd:pfam07717   63 YIRTVTAISPEWLLLFAPH 81
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
245-272 1.02e-06

Zinc finger C-x8-C-x5-C-x3-H type (and similar);


:

Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 46.03  E-value: 1.02e-06
                           10        20
                   ....*....|....*....|....*...
gi 24641139    245 KKPPLrCRNFDRDGTCKYGPKCRFAHLP 272
Cdd:pfam00642    1 YKTEL-CRFFLRTGYCKYGDRCKFAHGQ 27
UBA_like_SF super family cl21463
UBA domain-like superfamily; The ubiquitin-associated (UBA) domain-like superfamily contains ...
123-154 2.03e-03

UBA domain-like superfamily; The ubiquitin-associated (UBA) domain-like superfamily contains alpha-helical structural homology ubiquitin-binding domains, including UBA domains and coupling of ubiquitin conjugation to endoplasmic reticulum degradation (CUE) domains which share a common three-helical bundle architecture. UBA domains are commonly occurring sequence motifs found in proteins involved in ubiquitin-mediated proteolysis. They contribute to ubiquitin (Ub) binding or ubiquitin-like (UbL) domain binding. However, some kinds of UBA domains can only bind the UbL domain, but not the Ub domain. UBA domains are normally comprised of compact three-helix bundles which contain a conserved GF/Y-loop. They can bind polyubiquitin with high affinity. They also bind monoubiquitin and other proteins. Most UBA domain-containing proteins have one UBA domain, but some harbor two or three UBA domains. CUE domain containing proteins are characterized by an FP and a di-leucine-like sequence and bind to monoubiquitin with varying affinities. Some higher eukaryotic CUE domain proteins do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains. This superfamily also includes many UBA-like domains found in AMP-activated protein kinase (AMPK) related kinases, the NXF family of mRNA nuclear export factors, elongation factor Ts (EF-Ts), nascent polypeptide-associated complex subunit alpha (NACA) and similar proteins. Although many UBA-like domains may have a conserved TG but not GF/Y-loop, they still show a high level of structural and sequence similarity with three-helical ubiquitin binding domains.


The actual alignment was detected with superfamily member cd14306:

Pssm-ID: 473871  Cd Length: 36  Bit Score: 37.04  E-value: 2.03e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 24641139  123 LAKLENYGFQAVHCLEAYEHCSGDTEAALLLL 154
Cdd:cd14306    1 VAKLMELGFPEEDCIRALRACGGNVEEAANWL 32
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
452-1075 3.73e-119

HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 390.98  E-value: 3.73e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  452 QLPAFAEIERILALIESSPVVVISGETGCGKSTQVPQFILD-NWFFRALqlpakenlphveIICTQPRRLSAIGVAERVA 530
Cdd:COG1643    9 DLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLElGWGAGGR------------IGMLEPRRLAARAAAERMA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  531 AERLDRIGQLVGYQIRLENKVSQSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSEESDFlllil-knllRERKD 609
Cdd:COG1643   77 EELGEPVGETVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLllallldlqpALRPD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  610 LKVILMSATLNAALFSDYFGGAPVLDIPGRTFPVqqlfledilemsdfvmeyDTKYcrklkkQEQEILERELEYADVQAS 689
Cdd:COG1643  157 LKLLVMSATLDAERFARLLGDAPVIESSGRTYPV------------------EVRY------RPLPADERDLEDAVADAV 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  690 GEApgkkikdekltLAETyqryaeyskptcksiylmepmtinpeliesvlkyivegshdwprEGTILIFLPGFGEIQSVH 769
Cdd:COG1643  213 REA-----------LAEE--------------------------------------------PGDILVFLPGEREIRRTA 237
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  770 DSLldnalfSPRAGKFILV-PLHSALSGEDQALVFKKAPPGKRKIVLSTNIAETSVTIDDCVFVVDCGLMKEKCFDSNRN 848
Cdd:COG1643  238 EAL------RGRLPPDTEIlPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSG 311
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  849 MESLDLVWVSRANAKQRKGRAGRVMPGVCIHLYTsyRYQYHIL-AQPVPEIQRVPLEQIVLRIKTL-----QTFAsrntl 922
Cdd:COG1643  312 VTRLPTERISQASANQRAGRAGRLAPGICYRLWS--EEDFARRpAFTDPEILRADLASLILELAAWglgdpEDLP----- 384
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  923 svlleTLEAPTEDSVLGALTRLRDVGALDAEDQLTPLGHHLAALPVDVRIGKLMLYGAIFQCLDSVLTIAACLSNKSPFv 1002
Cdd:COG1643  385 -----FLDPPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPR- 458
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24641139 1003 splnkRTEADkckrmfalgnSDHLTVLNAYRKWLDvarrgnyaasrnyASEHFLSLNTLETIADLKYQYLELL 1075
Cdd:COG1643  459 -----RGAAG----------SDLLARLNLWRRLRE-------------QQREFLSYLRLREWRDLARQLRRLL 503
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
453-636 1.57e-95

DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350743 [Multi-domain]  Cd Length: 177  Bit Score: 303.30  E-value: 1.57e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  453 LPAFAEIERILALIESSPVVVISGETGCGKSTQVPQFILDNWFFRALqlpakenLPHVEIICTQPRRLSAIGVAERVAAE 532
Cdd:cd17985    1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPP-------LPVANIICTQPRRISAISVAERVAQE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  533 RLDRIGQLVGYQIRLENKVSQSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSEESDFLLLILKNLLRERKDLKV 612
Cdd:cd17985   74 RAERVGQSVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKV 153
                        170       180
                 ....*....|....*....|....
gi 24641139  613 ILMSATLNAALFSDYFGGAPVLDI 636
Cdd:cd17985  154 ILMSATLNAELFSDYFNSCPVIHI 177
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
453-1000 4.03e-79

ATP-dependent helicase HrpB; This model represents HrpB, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria, but also in a few species of other lineages. The member from Rhizobium meliloti has been designated HelO. HrpB is typically about 800 residues in length, while its paralog HrpA (TIGR01967), also uncharacterized, is about 1300 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273901 [Multi-domain]  Cd Length: 819  Bit Score: 278.96  E-value: 4.03e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139    453 LPAFAEIERILALIESSPVVVISGETGCGKSTQVPQFILDnwffralqlpakENLPHVEIICTQPRRLSAIGVAERVAAE 532
Cdd:TIGR01970    1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLD------------APGIGGKIIMLEPRRLAARSAAQRLASQ 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139    533 RLDRIGQLVGYQIRLENKVSQSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSEESDFLLLILKNLLRE-RKDLK 611
Cdd:TIGR01970   69 LGEAVGQTVGYRVRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSSlREDLK 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139    612 VILMSATLNAALFSDYFGGAPVLDIPGRTFPVqqlfledilemsdfvmeyDTKYcrkLKKQEQEILEreleyadvqasge 691
Cdd:TIGR01970  149 ILAMSATLDGERLSSLLPDAPVVESEGRSFPV------------------EIRY---LPLRGDQRLE------------- 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139    692 apgkkikdekltlaetyqryaeyskptcksiylmepmtinPELIESVLKYIVEGShdwpreGTILIFLPGFGEIQSVHDS 771
Cdd:TIGR01970  195 ----------------------------------------DAVSRAVEHALASET------GSILVFLPGQAEIRRVQEQ 228
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139    772 LLDnALFSpragKFILVPLHSALSGEDQALVFKKAPPGKRKIVLSTNIAETSVTIDDCVFVVDCGLMKEKCFDSNRNMES 851
Cdd:TIGR01970  229 LAE-RLDS----DVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITR 303
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139    852 LDLVWVSRANAKQRKGRAGRVMPGVCIHLYTSYRYQyHILAQPVPEIQRVPLEQIVLRiktLQTFASRNTLSVLLetLEA 931
Cdd:TIGR01970  304 LETVRISQASATQRAGRAGRLEPGVCYRLWSEEQHQ-RLPAQDEPEILQADLSGLALE---LAQWGAKDPSDLRW--LDA 377
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24641139    932 PTEDSVLGALTRLRDVGALDAEDQLTPLGHHLAALPVDVRIGKLMLYGAIFQCLDSVLTIAACLSNKSP 1000
Cdd:TIGR01970  378 PPSVALAAARQLLQRLGALDAQGRLTAHGKAMAALGCHPRLAAMLLSAHSTGLAALACDLAALLEERGL 446
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
432-1030 6.19e-71

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 260.76  E-value: 6.19e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   432 QQFVERRKEERyqKIIDGRKQLPAFAEIERILALIESSPVVVISGETGCGKSTQVPQFILDnwffraLQLPAKENLPHve 511
Cdd:PRK11131   54 AQRVLLREAAR--PEITYPENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLE------LGRGVKGLIGH-- 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   512 iicTQPRRLSAIGVAERVAAERLDRIGQLVGYQIRLENKVSQSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSE 591
Cdd:PRK11131  124 ---TQPRRLAARTVANRIAEELETELGGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSL 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   592 ESDFLLLILKNLLRERKDLKVILMSATLNAALFSDYFGGAPVLDIPGRTFPVqqlfledilemsdfvmeyDTKYcRKLKK 671
Cdd:PRK11131  201 NIDFILGYLKELLPRRPDLKVIITSATIDPERFSRHFNNAPIIEVSGRTYPV------------------EVRY-RPIVE 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   672 QEQEILERELEyadvqasgeapgkkikdekltlaetyqryaeyskptcksiylmepmtinpELIESVLKYIVEGShdwpr 751
Cdd:PRK11131  262 EADDTERDQLQ--------------------------------------------------AIFDAVDELGREGP----- 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   752 eGTILIFLPGFGEIQSVHDSLLDNALFSPRagkfiLVPLHSALSGEDQALVFKkaPPGKRKIVLSTNIAETSVTIDDCVF 831
Cdd:PRK11131  287 -GDILIFMSGEREIRDTADALNKLNLRHTE-----ILPLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKY 358
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   832 VVDCGLMKEKCFDSNRNMESLDLVWVSRANAKQRKGRAGRVMPGVCIHLYTSYRYqyhiLAQPV---PEIQRVPLEQIVL 908
Cdd:PRK11131  359 VIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDF----LSRPEftdPEILRTNLASVIL 434
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   909 RIKTL-----QTFAsrntlsvlleTLEAPTEDSVLGALTRLRDVGALDAED-----QLTPLGHHLAALPVDVRIGKLMLY 978
Cdd:PRK11131  435 QMTALglgdiAAFP----------FVEAPDKRNIQDGVRLLEELGAITTDEqasayKLTPLGRQLAQLPVDPRLARMVLE 504
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|..
gi 24641139   979 GAIFQCLDSVLTIAACLSNKSPFVSPLNKRTEADKCKRMFALGNSDHLTVLN 1030
Cdd:PRK11131  505 AQKHGCVREVMIITSALSIQDPRERPMDKQQASDEKHRRFADKESDFLAFVN 556
RWD_DHX57 cd23825
RWD domain of DEAH box protein 57 (DHX57) and related proteins; DHX57 (EC 3.6.4.13) is a ...
175-367 2.97e-42

RWD domain of DEAH box protein 57 (DHX57) and related proteins; DHX57 (EC 3.6.4.13) is a putative ATP-dependent RNA helicase. A genome-wide association study (GWAS) of cerebellar epigenetic age acceleration identified significant SNPs (single nucleotide polymorphisms) in a loci 2p22.1 inside the DHX57 gene, suggesting that variants in DHX57 are associated with epigenetic age in the cerebellum.


Pssm-ID: 467661  Cd Length: 115  Bit Score: 150.04  E-value: 2.97e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  175 QEILDMRADEKEALESIFDKAYEEREANRVWNLKFRIDHLLahspsevrkareavlaaaaaaaqaaldkkkkpplrcrnf 254
Cdd:cd23825    1 DELLEQRQEEAMALESIYGEAFSERIPNKVWTIKLDLPYLP--------------------------------------- 41
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  255 drdgtckygpkcrfahlpqqptesdttkkdsvdendnelWFHVEVRFPPGSRYPYEAPFIYLKTTCHDIPHELRLRYARH 334
Cdd:cd23825   42 ---------------------------------------WFELEIRFPKGNKYPYEPPIVAFSSTNENFPKAVCLNITER 82
                        170       180       190
                 ....*....|....*....|....*....|...
gi 24641139  335 LYKEAKEICRDGIPCVYSICDLLQSNEQLAGRL 367
Cdd:cd23825   83 LMEEALELAEDGEPVVFSLVSLLEDEEEILELL 115
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
940-1028 6.92e-26

Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 461295 [Multi-domain]  Cd Length: 104  Bit Score: 103.09  E-value: 6.92e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139    940 ALTRLRDVGALDAEDQLTPLGHHLAALPVDVRIGKLMLYGAIFQCLDSVLTIAACLSNKSPFVSPLN------------- 1006
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFldprsaakaarrr 80
                           90       100
                   ....*....|....*....|....
gi 24641139   1007 KRTEADKCKRMFA--LGNSDHLTV 1028
Cdd:pfam04408   81 RRAADEKARAKFArlDLEGDHLTL 104
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
948-1029 4.67e-25

Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 214852 [Multi-domain]  Cd Length: 82  Bit Score: 100.04  E-value: 4.67e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139     948 GALDAEDQLTPLGHHLAALPVDVRIGKLMLYGAIFQCLDSVLTIAACLSNKSPFvsPLNKRTEADKCKRMFALGNSDHLT 1027
Cdd:smart00847    3 GALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR--PKEKREDADAARRRFADPESDHLT 80

                    ..
gi 24641139    1028 VL 1029
Cdd:smart00847   81 LL 82
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
1114-1212 6.96e-18

Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus of the DEAD-box helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. There do seem to be a couple of instances where it occurs by itself -. The structure PDB:3i4u adopts an OB-fold. helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. This C-terminal domain of the yeast helicase contains an oligonucleotide/oligosaccharide-binding (OB)-fold which seems to be placed at the entrance of the putative nucleic acid cavity. It also constitutes the binding site for the G-patch-containing domain of Pfa1p. When found on DEAH/RHA helicases, this domain is central to the regulation of the helicase activity through its binding of both RNA and G-patch domain proteins.


Pssm-ID: 400182 [Multi-domain]  Cd Length: 82  Bit Score: 79.60  E-value: 6.96e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   1114 LTSLLCAALYPNIVKiMTPDRVYIQTAggavprepshhdlrfktRGDGYVKIHPSSVNSQVSVFQAPFLVFQEKVRTSAI 1193
Cdd:pfam07717    1 LRAALAAGLYPNVAR-RDPKGKGYTTL-----------------SDNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKV 62
                           90
                   ....*....|....*....
gi 24641139   1194 YIRDCSMLPLIAMVLFAGS 1212
Cdd:pfam07717   63 YIRTVTAISPEWLLLFAPH 81
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
283-360 9.96e-09

RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. The function of this domain is unknown. GCN2 is the alpha-subunit of the only translation initiation factor (eIF2 alpha) kinase that appears in all eukaryotes. Its function requires an interaction with GCN1 via the domain at its N-terminus, which is termed the RWD domain after three major RWD-containing proteins: RING finger-containing proteins, WD-repeat-containing proteins, and yeast DEAD (DEXD)-like helicases. The structure forms an alpha + beta sandwich fold consisting of two layers: a four-stranded antiparallel beta-sheet, and three side-by-side alpha-helices.


Pssm-ID: 399058  Cd Length: 111  Bit Score: 54.25  E-value: 9.96e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24641139    283 KDSVDENDNELWFHVEVRFPPGsrYPYEAPFIYLKTTcHDIPHELRLRYARHLYKEAKEICrdGIPCVYSICDLLQSN 360
Cdd:pfam05773   38 DSDESDSSHLPPLVLKFTLPED--YPDEPPKISLSSP-WNLSDEQVLSLLEELEELAEENL--GEVMIFELIEWLQEN 110
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
245-272 1.02e-06

Zinc finger C-x8-C-x5-C-x3-H type (and similar);


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 46.03  E-value: 1.02e-06
                           10        20
                   ....*....|....*....|....*...
gi 24641139    245 KKPPLrCRNFDRDGTCKYGPKCRFAHLP 272
Cdd:pfam00642    1 YKTEL-CRFFLRTGYCKYGDRCKFAHGQ 27
ZnF_C3H1 smart00356
zinc finger;
246-270 1.09e-04

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 40.31  E-value: 1.09e-04
                            10        20
                    ....*....|....*....|....*
gi 24641139     246 KPPLrCRNFDRdGTCKYGPKCRFAH 270
Cdd:smart00356    3 KTEL-CKFFKR-GYCPRGDRCKFAH 25
UBA_VP13D cd14306
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ...
123-154 2.03e-03

UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar proteins; VP13D is a chorea-acanthocytosis (CHAC)-similar protein encoded by gene VPS13D. it contains two putative domains, ubiquitin-associated (UBA) domain and lectin domain of ricin B chain profile (ricin-B-lectin), suggesting it may interact with, and be involved in the trafficking of, proteins modified with ubiquitin and/or carbohydrate molecules. Further investigation is required.


Pssm-ID: 270491  Cd Length: 36  Bit Score: 37.04  E-value: 2.03e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 24641139  123 LAKLENYGFQAVHCLEAYEHCSGDTEAALLLL 154
Cdd:cd14306    1 VAKLMELGFPEEDCIRALRACGGNVEEAANWL 32
 
Name Accession Description Interval E-value
HrpA COG1643
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
452-1075 3.73e-119

HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441249 [Multi-domain]  Cd Length: 836  Bit Score: 390.98  E-value: 3.73e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  452 QLPAFAEIERILALIESSPVVVISGETGCGKSTQVPQFILD-NWFFRALqlpakenlphveIICTQPRRLSAIGVAERVA 530
Cdd:COG1643    9 DLPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLElGWGAGGR------------IGMLEPRRLAARAAAERMA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  531 AERLDRIGQLVGYQIRLENKVSQSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSEESDFlllil-knllRERKD 609
Cdd:COG1643   77 EELGEPVGETVGYRVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLllallldlqpALRPD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  610 LKVILMSATLNAALFSDYFGGAPVLDIPGRTFPVqqlfledilemsdfvmeyDTKYcrklkkQEQEILERELEYADVQAS 689
Cdd:COG1643  157 LKLLVMSATLDAERFARLLGDAPVIESSGRTYPV------------------EVRY------RPLPADERDLEDAVADAV 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  690 GEApgkkikdekltLAETyqryaeyskptcksiylmepmtinpeliesvlkyivegshdwprEGTILIFLPGFGEIQSVH 769
Cdd:COG1643  213 REA-----------LAEE--------------------------------------------PGDILVFLPGEREIRRTA 237
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  770 DSLldnalfSPRAGKFILV-PLHSALSGEDQALVFKKAPPGKRKIVLSTNIAETSVTIDDCVFVVDCGLMKEKCFDSNRN 848
Cdd:COG1643  238 EAL------RGRLPPDTEIlPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSG 311
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  849 MESLDLVWVSRANAKQRKGRAGRVMPGVCIHLYTsyRYQYHIL-AQPVPEIQRVPLEQIVLRIKTL-----QTFAsrntl 922
Cdd:COG1643  312 VTRLPTERISQASANQRAGRAGRLAPGICYRLWS--EEDFARRpAFTDPEILRADLASLILELAAWglgdpEDLP----- 384
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  923 svlleTLEAPTEDSVLGALTRLRDVGALDAEDQLTPLGHHLAALPVDVRIGKLMLYGAIFQCLDSVLTIAACLSNKSPFv 1002
Cdd:COG1643  385 -----FLDPPPARAIADARALLQELGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSERDPR- 458
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24641139 1003 splnkRTEADkckrmfalgnSDHLTVLNAYRKWLDvarrgnyaasrnyASEHFLSLNTLETIADLKYQYLELL 1075
Cdd:COG1643  459 -----RGAAG----------SDLLARLNLWRRLRE-------------QQREFLSYLRLREWRDLARQLRRLL 503
DEXHc_DHX57 cd17985
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ...
453-636 1.57e-95

DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350743 [Multi-domain]  Cd Length: 177  Bit Score: 303.30  E-value: 1.57e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  453 LPAFAEIERILALIESSPVVVISGETGCGKSTQVPQFILDNWFFRALqlpakenLPHVEIICTQPRRLSAIGVAERVAAE 532
Cdd:cd17985    1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNSLQGPP-------LPVANIICTQPRRISAISVAERVAQE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  533 RLDRIGQLVGYQIRLENKVSQSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSEESDFLLLILKNLLRERKDLKV 612
Cdd:cd17985   74 RAERVGQSVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKV 153
                        170       180
                 ....*....|....*....|....
gi 24641139  613 ILMSATLNAALFSDYFGGAPVLDI 636
Cdd:cd17985  154 ILMSATLNAELFSDYFNSCPVIHI 177
DEAH_box_HrpB TIGR01970
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ...
453-1000 4.03e-79

ATP-dependent helicase HrpB; This model represents HrpB, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria, but also in a few species of other lineages. The member from Rhizobium meliloti has been designated HelO. HrpB is typically about 800 residues in length, while its paralog HrpA (TIGR01967), also uncharacterized, is about 1300 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273901 [Multi-domain]  Cd Length: 819  Bit Score: 278.96  E-value: 4.03e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139    453 LPAFAEIERILALIESSPVVVISGETGCGKSTQVPQFILDnwffralqlpakENLPHVEIICTQPRRLSAIGVAERVAAE 532
Cdd:TIGR01970    1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPLALLD------------APGIGGKIIMLEPRRLAARSAAQRLASQ 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139    533 RLDRIGQLVGYQIRLENKVSQSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSEESDFLLLILKNLLRE-RKDLK 611
Cdd:TIGR01970   69 LGEAVGQTVGYRVRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVQSSlREDLK 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139    612 VILMSATLNAALFSDYFGGAPVLDIPGRTFPVqqlfledilemsdfvmeyDTKYcrkLKKQEQEILEreleyadvqasge 691
Cdd:TIGR01970  149 ILAMSATLDGERLSSLLPDAPVVESEGRSFPV------------------EIRY---LPLRGDQRLE------------- 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139    692 apgkkikdekltlaetyqryaeyskptcksiylmepmtinPELIESVLKYIVEGShdwpreGTILIFLPGFGEIQSVHDS 771
Cdd:TIGR01970  195 ----------------------------------------DAVSRAVEHALASET------GSILVFLPGQAEIRRVQEQ 228
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139    772 LLDnALFSpragKFILVPLHSALSGEDQALVFKKAPPGKRKIVLSTNIAETSVTIDDCVFVVDCGLMKEKCFDSNRNMES 851
Cdd:TIGR01970  229 LAE-RLDS----DVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITR 303
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139    852 LDLVWVSRANAKQRKGRAGRVMPGVCIHLYTSYRYQyHILAQPVPEIQRVPLEQIVLRiktLQTFASRNTLSVLLetLEA 931
Cdd:TIGR01970  304 LETVRISQASATQRAGRAGRLEPGVCYRLWSEEQHQ-RLPAQDEPEILQADLSGLALE---LAQWGAKDPSDLRW--LDA 377
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24641139    932 PTEDSVLGALTRLRDVGALDAEDQLTPLGHHLAALPVDVRIGKLMLYGAIFQCLDSVLTIAACLSNKSP 1000
Cdd:TIGR01970  378 PPSVALAAARQLLQRLGALDAQGRLTAHGKAMAALGCHPRLAAMLLSAHSTGLAALACDLAALLEERGL 446
DEXHc_RHA-like cd17917
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
471-636 4.56e-78

DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438707 [Multi-domain]  Cd Length: 159  Bit Score: 253.92  E-value: 4.56e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  471 VVVISGETGCGKSTQVPQFILDNWFfralqlpakENLPHVEIICTQPRRLSAIGVAERVAAERLDRIGQLVGYQIRLENK 550
Cdd:cd17917    3 VVVIVGETGSGKTTQVPQFLLEDGL---------AKGGKGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  551 VSQSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSEESDFLLLILKNLLRERKDLKVILMSATLNAALFSDYFGG 630
Cdd:cd17917   74 TSSKTRIKFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGG 153

                 ....*.
gi 24641139  631 APVLDI 636
Cdd:cd17917  154 APVIHI 159
PRK11131 PRK11131
ATP-dependent RNA helicase HrpA; Provisional
432-1030 6.19e-71

ATP-dependent RNA helicase HrpA; Provisional


Pssm-ID: 182986 [Multi-domain]  Cd Length: 1294  Bit Score: 260.76  E-value: 6.19e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   432 QQFVERRKEERyqKIIDGRKQLPAFAEIERILALIESSPVVVISGETGCGKSTQVPQFILDnwffraLQLPAKENLPHve 511
Cdd:PRK11131   54 AQRVLLREAAR--PEITYPENLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLE------LGRGVKGLIGH-- 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   512 iicTQPRRLSAIGVAERVAAERLDRIGQLVGYQIRLENKVSQSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSE 591
Cdd:PRK11131  124 ---TQPRRLAARTVANRIAEELETELGGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSL 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   592 ESDFLLLILKNLLRERKDLKVILMSATLNAALFSDYFGGAPVLDIPGRTFPVqqlfledilemsdfvmeyDTKYcRKLKK 671
Cdd:PRK11131  201 NIDFILGYLKELLPRRPDLKVIITSATIDPERFSRHFNNAPIIEVSGRTYPV------------------EVRY-RPIVE 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   672 QEQEILERELEyadvqasgeapgkkikdekltlaetyqryaeyskptcksiylmepmtinpELIESVLKYIVEGShdwpr 751
Cdd:PRK11131  262 EADDTERDQLQ--------------------------------------------------AIFDAVDELGREGP----- 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   752 eGTILIFLPGFGEIQSVHDSLLDNALFSPRagkfiLVPLHSALSGEDQALVFKkaPPGKRKIVLSTNIAETSVTIDDCVF 831
Cdd:PRK11131  287 -GDILIFMSGEREIRDTADALNKLNLRHTE-----ILPLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPGIKY 358
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   832 VVDCGLMKEKCFDSNRNMESLDLVWVSRANAKQRKGRAGRVMPGVCIHLYTSYRYqyhiLAQPV---PEIQRVPLEQIVL 908
Cdd:PRK11131  359 VIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDF----LSRPEftdPEILRTNLASVIL 434
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   909 RIKTL-----QTFAsrntlsvlleTLEAPTEDSVLGALTRLRDVGALDAED-----QLTPLGHHLAALPVDVRIGKLMLY 978
Cdd:PRK11131  435 QMTALglgdiAAFP----------FVEAPDKRNIQDGVRLLEELGAITTDEqasayKLTPLGRQLAQLPVDPRLARMVLE 504
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|..
gi 24641139   979 GAIFQCLDSVLTIAACLSNKSPFVSPLNKRTEADKCKRMFALGNSDHLTVLN 1030
Cdd:PRK11131  505 AQKHGCVREVMIITSALSIQDPRERPMDKQQASDEKHRRFADKESDFLAFVN 556
SF2_C_RHA cd18791
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ...
725-881 3.15e-70

C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350178 [Multi-domain]  Cd Length: 171  Bit Score: 232.42  E-value: 3.15e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  725 MEPMTINPELIESVLKYIVEGSHDWPrEGTILIFLPGFGEIQSVHDSLLDNALFsPRAGKFILVPLHSALSGEDQALVFK 804
Cdd:cd18791   17 ISSEKEDPDYVDAAVRLILQIHRTEE-PGDILVFLPGQEEIERLCELLREELLS-PDLGKLLVLPLHSSLPPEEQQRVFE 94
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24641139  805 KAPPGKRKIVLSTNIAETSVTIDDCVFVVDCGLMKEKCFDSNRNMESLDLVWVSRANAKQRKGRAGRVMPGVCIHLY 881
Cdd:cd18791   95 PPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRAGRTRPGKCYRLY 171
PRK11664 PRK11664
ATP-dependent RNA helicase HrpB; Provisional
452-995 1.44e-69

ATP-dependent RNA helicase HrpB; Provisional


Pssm-ID: 236950 [Multi-domain]  Cd Length: 812  Bit Score: 250.61  E-value: 1.44e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   452 QLPAFAEIERILALIESSPVVVISGETGCGKSTQVPqfildnwffraLQLPAKENLPHvEIICTQPRRLSAIGVAERVAA 531
Cdd:PRK11664    3 SLPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLP-----------LQLLQHGGING-KIIMLEPRRLAARNVAQRLAE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   532 ERLDRIGQLVGYQIRLENKVSQSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSEESDFLLLILKNLLRE-RKDL 610
Cdd:PRK11664   71 QLGEKPGETVGYRMRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALLLDVQQGlRDDL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   611 KVILMSATLNAALFSDYFGGAPVLDIPGRTFPVqqlfledilemsdfvmeydtkycrklkkqeqeilEReleyadvqasg 690
Cdd:PRK11664  151 KLLIMSATLDNDRLQQLLPDAPVIVSEGRSFPV----------------------------------ER----------- 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   691 eapgkkikdekltlaetyqRYAeyskptcksiylmePMTINPELIESVLKYIvegSHDWPRE-GTILIFLPGFGEIQSVH 769
Cdd:PRK11664  186 -------------------RYQ--------------PLPAHQRFDEAVARAT---AELLRQEsGSLLLFLPGVGEIQRVQ 229
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   770 DsLLDNALfsprAGKFILVPLHSALSGEDQALVFKKAPPGKRKIVLSTNIAETSVTIDDCVFVVDCGLMKEKCFDSNRNM 849
Cdd:PRK11664  230 E-QLASRV----ASDVLLCPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGL 304
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   850 ESLDLVWVSRANAKQRKGRAGRVMPGVCIHLYTSYRYQyHILAQPVPEIQRVPLEQIVLRIktLQTFASRntlSVLLETL 929
Cdd:PRK11664  305 TRLVTQRISQASMTQRAGRAGRLEPGICLHLYSKEQAE-RAAAQSEPEILHSDLSGLLLEL--LQWGCHD---PAQLSWL 378
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24641139   930 EAPTEDSVLGALTRLRDVGALDAEDQLTPLGHHLAALPVDVRIGKLMLYGAifQCLDSVLTIAACL 995
Cdd:PRK11664  379 DQPPAAALAAAKRLLQQLGALDGQGRLTARGRKMAALGNDPRLAAMLVAAK--EDDEAALATAAKL 442
DEXHc_YTHDC2 cd17987
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ...
453-636 3.95e-62

DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) regulates mRNA translation and stability via binding to N6-methyladenosine, a modified RNA nucleotide enriched in the stop codons and 3' UTRs of eukaryotic messenger RNAs. YTHDC2 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350745 [Multi-domain]  Cd Length: 176  Bit Score: 209.69  E-value: 3.95e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  453 LPAFAEIERILALIESSPVVVISGETGCGKSTQVPQFILDNWFfralqlpaKENLPhVEIICTQPRRLSAIGVAERVAAE 532
Cdd:cd17987    1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCY--------ANGIP-CRIFCTQPRRLAAIAVAERVAAE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  533 RLDRIGQLVGYQIRLENKVSQSTRLSFCTTGILLRRL-ASDPLLGSVTHVIVDEVHERSEESDFLLLILKNLLRERKDLK 611
Cdd:cd17987   72 RGEKIGQTVGYQIRLESRVSPKTLLTFCTNGVLLRTLmAGDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLK 151
                        170       180
                 ....*....|....*....|....*
gi 24641139  612 VILMSATLNAALFSDYFGGAPVLDI 636
Cdd:cd17987  152 LILSSAALDVNLFIRYFGSCPVIYI 176
DEXHc_DHX36 cd17981
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ...
453-636 1.29e-59

DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as G4-resolvase 1 or G4R1, MLE-like protein 1 and RNA helicase associated with AU-rich element or RHAU) unwinds a G4-quadruplex in human telomerase RNA. DHX36 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350739 [Multi-domain]  Cd Length: 180  Bit Score: 202.38  E-value: 1.29e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  453 LPAFAEIERILALIESSPVVVISGETGCGKSTQVPQFILDNWFFRALQLPAKenlphveIICTQPRRLSAIGVAERVAAE 532
Cdd:cd17981    1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDAIERGKGSSCR-------IVCTQPRRISAISVAERVAAE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  533 RLD--RIGQLVGYQIRLENKVSQS-TRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSEESDFLLLILKNLLRERKD 609
Cdd:cd17981   74 RAEscGLGNSTGYQIRLESRKPRKqGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSD 153
                        170       180
                 ....*....|....*....|....*..
gi 24641139  610 LKVILMSATLNAALFSDYFGGAPVLDI 636
Cdd:cd17981  154 LKVILMSATLNAEKFSDYFNNCPMIHI 180
DEXHc_DHX34 cd17979
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ...
453-636 4.47e-54

DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in the nonsense-mediated decay (NMD), a surveillance mechanism that degrades aberrant mRNAs. DHX34 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350737 [Multi-domain]  Cd Length: 170  Bit Score: 186.11  E-value: 4.47e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  453 LPAFAEIERILALIESSPVVVISGETGCGKSTQVPQFILDNWFFRalqlpakenlphveIICTQPRRLSAIGVAERVAAE 532
Cdd:cd17979    1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRH--------------IACTQPRRIACISLAKRVAFE 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  533 RLDRIGQLVGYQIRLENKVSQSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSEESDFLLLILKNLLRERKDLKV 612
Cdd:cd17979   67 SLNQYGSKVAYQIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKL 146
                        170       180
                 ....*....|....*....|....
gi 24641139  613 ILMSATLNAALFSDYFGGAPVLDI 636
Cdd:cd17979  147 ILMSATINIELFSGYFEGAPVVQV 170
DEXHc_DHX29 cd17975
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ...
453-636 3.29e-53

DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of the 43S pre-initiation complex involved in translation initiation of mRNAs with structured 5'-UTRs. DHX29 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350733 [Multi-domain]  Cd Length: 183  Bit Score: 184.35  E-value: 3.29e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  453 LPAFAEIERILALIESSPVVVISGETGCGKSTQVPQFILDNWFFRALQlPAKENlphveIICTQPRRLSAIGVAERVAAE 532
Cdd:cd17975    1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEDLLLNGGT-AQKCN-----IVCTQPRRISAMSLATRVCEE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  533 RLDRIG-----QLVGYQIRLENKVSQSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSEESDFLLLILKNLLRER 607
Cdd:cd17975   75 LGCESGpggknSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKR 154
                        170       180
                 ....*....|....*....|....*....
gi 24641139  608 KDLKVILMSATLNAALFSDYFGGAPVLDI 636
Cdd:cd17975  155 SDLHLILMSATVDCEKFSSYFTHCPILRI 183
DEXHc_DHX33 cd17978
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ...
453-636 6.09e-53

DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA polymerase I transcription of the 47S precursor rRNA. DHX33 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438710 [Multi-domain]  Cd Length: 178  Bit Score: 183.32  E-value: 6.09e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  453 LPAFAEIERILALIESSPVVVISGETGCGKSTQVPQFILDNWFFRALQlpakenlphveIICTQPRRLSAIGVAERVAAE 532
Cdd:cd17978    1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARGGM-----------IGITQPRRVAAVSVAKRVAEE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  533 RLDRIGQLVGYQIRLENKVSQSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSEESDFLLLILKNLLRERKD--- 609
Cdd:cd17978   70 MGVELGQLVGYSVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRKEqkl 149
                        170       180
                 ....*....|....*....|....*....
gi 24641139  610 --LKVILMSATLNAALFSDYFGGAPVLDI 636
Cdd:cd17978  150 spLKVIIMSATLDADLFSEYFNGAPVLYI 178
DEXHc_DHX30 cd17976
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ...
453-636 2.10e-51

DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an important role in the assembly of the mitochondrial large ribosomal subunit. DHX30 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350734 [Multi-domain]  Cd Length: 178  Bit Score: 178.83  E-value: 2.10e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  453 LPAFAEIERILALIESSPVVVISGETGCGKSTQVPQFILDNWFFRAlqlpakeNLPHVEIICTQPRRLSAIGVAERVAAE 532
Cdd:cd17976    1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLRG-------RGARCNVVITQPRRISAVSVAQRVAHE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  533 RLDRIGQLVGYQIRLENKV-SQSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSEESDFLLLILKNLLRERKDLK 611
Cdd:cd17976   74 LGPNLRRNVGYQVRLESRPpPRGGALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELR 153
                        170       180
                 ....*....|....*....|....*
gi 24641139  612 VILMSATLNAALFSDYFGGAPVLDI 636
Cdd:cd17976  154 VVLMSATGDNQRLSRYFGGCPVVRV 178
DEXHc_DHX15 cd17973
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ...
441-636 2.64e-51

DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA. DHX15 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438709 [Multi-domain]  Cd Length: 187  Bit Score: 179.15  E-value: 2.64e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  441 ERYQKIIDGRKQLPAFAEIERILALIESSPVVVISGETGCGKSTQVPQFILDnwfFRALQLPAKEnlphveIICTQPRRL 520
Cdd:cd17973    1 QRYFEILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLD---DELPHQPKKL------VACTQPRRV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  521 SAIGVAERVAAERLDRIGQLVGYQIRLENKVSQSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSEESDFLLLIL 600
Cdd:cd17973   72 AAMSVAQRVAEEMDVKLGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLL 151
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 24641139  601 KNLLRERKDLKVILMSATLNAALFSDYFGGAPVLDI 636
Cdd:cd17973  152 KEVVRRRPDLKLIVMSATLDAGKFQKYFDNAPLLKV 187
DEXHc_DHX9 cd17972
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ...
436-636 1.34e-50

DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ATP-dependent RNA helicase A or RHA and leukophysin or LKP) plays an important role in many cellular processes, including regulation of DNA replication, transcription, translation, microRNA biogenesis, RNA processing and transport, and maintenance of genomic stability. DHX9 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350730 [Multi-domain]  Cd Length: 234  Bit Score: 178.87  E-value: 1.34e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  436 ERRKEERYQKIIDGRKQLPAFAEIERILALIESSPVVVISGETGCGKSTQVPQFILDNWFfralqlpAKENLPHVEIICT 515
Cdd:cd17972   42 QREQDHNLQQILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDDFI-------QNDRAAECNIVVT 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  516 QPRRLSAIGVAERVAAERLDRIGQLVGYQIRLENKVSQS-TRLSFCTTGILLRRLASDplLGSVTHVIVDEVHERSEESD 594
Cdd:cd17972  115 QPRRISAVSVAERVAFERGEEVGKSCGYSVRFESVLPRPhASILFCTVGVLLRKLEAG--IRGISHVIVDEIHERDINTD 192
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 24641139  595 FLLLILKNLLRERKDLKVILMSATLNAALFSDYFGGAPVLDI 636
Cdd:cd17972  193 FLLVVLRDVVQAYPDLRVILMSATIDTSMFCEYFFNCPVIEV 234
DEXHc_TDRD9 cd17988
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ...
453-629 2.25e-50

DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also known as HIG-1or NET54 or C14orf75) is a part of the nuclear PIWI-interacting RNA (piRNA) pathway essential for transposon silencing and male fertility TDRD9 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350746 [Multi-domain]  Cd Length: 180  Bit Score: 176.15  E-value: 2.25e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  453 LPAFAEIERILALIESSPVVVISGETGCGKSTQVPQFILDNWffralqlpAKENLPhVEIICTQPRRLSAIGVAERVAAE 532
Cdd:cd17988    1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHY--------YKRGKY-CNIVVTQPRRIAAISIARRVSQE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  533 RLDRIGQLVGYQIRLENKVSQSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSEESDFLLLILKNLLR-ERKDLK 611
Cdd:cd17988   72 REWTLGSLVGYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRtNSRHVK 151
                        170
                 ....*....|....*...
gi 24641139  612 VILMSATLNAALFSDYFG 629
Cdd:cd17988  152 IILMSATISCKEFADYFT 169
DEXHc_DHX35 cd17980
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ...
453-628 2.05e-44

DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and seems to be associated with risk to thyroid cancers. It also has been shown to positively regulate poxviruses, such as Myxoma virus. DEAH-box helicase 35 (DHX35) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350738 [Multi-domain]  Cd Length: 185  Bit Score: 159.17  E-value: 2.05e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  453 LPAFAEIERILALIESSPVVVISGETGCGKSTQVPQFILD-NWF--FRAlqlpakenlphveIICTQPRRLSAIGVAERV 529
Cdd:cd17980    1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEaGWTagGRV-------------VGCTQPRRVAAVTVAGRV 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  530 AAERLDRIGQLVGYQIRLENKVS-QSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSEESDFLLLILKNLLRERK 608
Cdd:cd17980   68 AEEMGAVLGHEVGYCIRFDDCTDpQATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRG 147
                        170       180
                 ....*....|....*....|
gi 24641139  609 DLKVILMSATLNAALFSDYF 628
Cdd:cd17980  148 DLRLIVASATLDAEKFRDFF 167
DEXHc_DHX16 cd17974
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ...
453-636 3.63e-44

DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably involved in pre-mRNA splicing. DHX16 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350732 [Multi-domain]  Cd Length: 174  Bit Score: 158.05  E-value: 3.63e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  453 LPAFAEIERILALIESSPVVVISGETGCGKSTQVPQFILDNWFFRALQlpakenlphvEIICTQPRRLSAIGVAERVAAE 532
Cdd:cd17974    1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTKGGG----------KIGCTQPRRVAAMSVAARVAEE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  533 RLDRIGQLVGYQIRLENKVSQSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSEESDFLLLILKNLLRERKDLKV 612
Cdd:cd17974   71 MGVKLGNEVGYSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKL 150
                        170       180
                 ....*....|....*....|....
gi 24641139  613 ILMSATLNAALFSDYFGGAPVLDI 636
Cdd:cd17974  151 LISSATMDAEKFSAFFDDAPIFRI 174
DEXHc_HrpB cd17990
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
453-634 1.68e-42

DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438711 [Multi-domain]  Cd Length: 174  Bit Score: 153.26  E-value: 1.68e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  453 LPAFAEIERILALIESSPVVVISGETGCGKSTQVPqfildnwffraLQLPAKENLPHVEIICTQPRRLSAIGVAERVAAE 532
Cdd:cd17990    1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVP-----------LALLAELWIAGGKIIVLEPRRVAARAAARRLATL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  533 RLDRIGQLVGYQIRLENKVSQSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSEESDFLLLILKNLLRE-RKDLK 611
Cdd:cd17990   70 LGEAPGETVGYRVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQQLlRDDLR 149
                        170       180
                 ....*....|....*....|...
gi 24641139  612 VILMSATLNAALFSDYFGGAPVL 634
Cdd:cd17990  150 LLAMSATLDGDGLAALLPEAPVV 172
RWD_DHX57 cd23825
RWD domain of DEAH box protein 57 (DHX57) and related proteins; DHX57 (EC 3.6.4.13) is a ...
175-367 2.97e-42

RWD domain of DEAH box protein 57 (DHX57) and related proteins; DHX57 (EC 3.6.4.13) is a putative ATP-dependent RNA helicase. A genome-wide association study (GWAS) of cerebellar epigenetic age acceleration identified significant SNPs (single nucleotide polymorphisms) in a loci 2p22.1 inside the DHX57 gene, suggesting that variants in DHX57 are associated with epigenetic age in the cerebellum.


Pssm-ID: 467661  Cd Length: 115  Bit Score: 150.04  E-value: 2.97e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  175 QEILDMRADEKEALESIFDKAYEEREANRVWNLKFRIDHLLahspsevrkareavlaaaaaaaqaaldkkkkpplrcrnf 254
Cdd:cd23825    1 DELLEQRQEEAMALESIYGEAFSERIPNKVWTIKLDLPYLP--------------------------------------- 41
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  255 drdgtckygpkcrfahlpqqptesdttkkdsvdendnelWFHVEVRFPPGSRYPYEAPFIYLKTTCHDIPHELRLRYARH 334
Cdd:cd23825   42 ---------------------------------------WFELEIRFPKGNKYPYEPPIVAFSSTNENFPKAVCLNITER 82
                        170       180       190
                 ....*....|....*....|....*....|...
gi 24641139  335 LYKEAKEICRDGIPCVYSICDLLQSNEQLAGRL 367
Cdd:cd23825   83 LMEEALELAEDGEPVVFSLVSLLEDEEEILELL 115
DEXHc_DHX37 cd17982
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ...
453-626 1.33e-41

DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the human nervous system and has been linked to schizophrenia. It also negatively regulates poxviruses such as Myxoma virus. DEAH-box helicase 37 (DHX37) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350740 [Multi-domain]  Cd Length: 191  Bit Score: 151.35  E-value: 1.33e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  453 LPAFAEIERILALIESSPVVVISGETGCGKSTQVPQFILDNWFfralqlpAKENLPHVEII-CTQPRRLSAIGVAERVAA 531
Cdd:cd17982    1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGF-------GSPESDNPGMIgITQPRRVAAVSMAKRVAE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  532 ErLDRIGQLVGYQIRLENKVSQSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSEESDFLLLILKNLLRERKD-- 609
Cdd:cd17982   74 E-LNVFGKEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKly 152
                        170       180
                 ....*....|....*....|....*
gi 24641139  610 --------LKVILMSATLNAALFSD 626
Cdd:cd17982  153 lqdqtvkpLKLVIMSATLRVEDFTE 177
DEXHc_DHX38 cd17983
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ...
453-636 1.20e-40

DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as PRP16) is involved in pre-mRNA splicing. DHX38 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350741 [Multi-domain]  Cd Length: 173  Bit Score: 147.99  E-value: 1.20e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  453 LPAFAEIERILALIESSPVVVISGETGCGKSTQVPQFILDNWFFRalqlpakenlpHVEIICTQPRRLSAIGVAERVAAE 532
Cdd:cd17983    1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYTD-----------YGMIGCTQPRRVAAMSVAKRVSEE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  533 RLDRIGQLVGYQIRLENKVSQSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSEESDFLLLILKNLLRERKDLKV 612
Cdd:cd17983   70 MGVELGEEVGYAIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKL 149
                        170       180
                 ....*....|....*....|....
gi 24641139  613 ILMSATLNAALFSDYFGGAPVLDI 636
Cdd:cd17983  150 IVTSATMDADKFADFFGNVPIFTI 173
DEXHc_DHX8 cd17971
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ...
448-637 8.27e-40

DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as pre-mRNA-splicing factor ATP-dependent RNA helicase PRP22) acts late in the splicing of pre-mRNA and mediates the release of the spliced mRNA from spliceosomes. DHX8 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350729 [Multi-domain]  Cd Length: 179  Bit Score: 145.70  E-value: 8.27e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  448 DGRKQLPAFAEIERILALIESSPVVVISGETGCGKSTQVPQFIldnwffralqlpAKENLPHVEII-CTQPRRLSAIGVA 526
Cdd:cd17971    1 EQRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYL------------AEAGYTSRGKIgCTQPRRVAAMSVA 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  527 ERVAAERLDRIGQLVGYQIRLENKVSQSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSEESDFLLLILKNLLRE 606
Cdd:cd17971   69 KRVAEEFGCCLGQEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQK 148
                        170       180       190
                 ....*....|....*....|....*....|.
gi 24641139  607 RKDLKVILMSATLNAALFSDYFGGAPVLDIP 637
Cdd:cd17971  149 RPDLKLIVTSATLDAVKFSQYFYEAPIFTIP 179
DEXHc_HrpA cd17989
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ...
453-636 3.56e-39

DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpA belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350747 [Multi-domain]  Cd Length: 173  Bit Score: 143.75  E-value: 3.56e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  453 LPAFAEIERILALIESSPVVVISGETGCGKSTQVPQFILDnwffraLQLPAKENLPHveiicTQPRRLSAIGVAERVAAE 532
Cdd:cd17989    1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLE------LGRGIRGLIGH-----TQPRRLAARSVAERIAEE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  533 RLDRIGQLVGYQIRLENKVSQSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSEESDFLLLILKNLLRERKDLKV 612
Cdd:cd17989   70 LKTELGGAVGYKVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKV 149
                        170       180
                 ....*....|....*....|....
gi 24641139  613 ILMSATLNAALFSDYFGGAPVLDI 636
Cdd:cd17989  150 IITSATIDAERFSRHFNNAPIIEV 173
DEXHc_DHX40 cd17984
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ...
453-636 3.61e-34

DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350742 [Multi-domain]  Cd Length: 178  Bit Score: 129.59  E-value: 3.61e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  453 LPAFAEIERILALIESSPVVVISGETGCGKSTQVPQFILDNWFFRalqlpakenlpHVEIICTQPRRLSAIGVAERVAAE 532
Cdd:cd17984    1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQ-----------HGMIGVTQPRRVAAISVAQRVAEE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  533 RLDRIGQLVGYQIRLENKVSQSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSEESD-----FLLLILKNLLRER 607
Cdd:cd17984   70 MKCTLGSKVGYQVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDilfglLKKLFQEKSPNRK 149
                        170       180
                 ....*....|....*....|....*....
gi 24641139  608 KDLKVILMSATLNAALFSDYFGGAPVLDI 636
Cdd:cd17984  150 EHLKVVVMSATLELAKLSAFFGNCPVFDI 178
DEXHc_DHX32 cd17977
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ...
453-636 5.74e-26

DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350735 [Multi-domain]  Cd Length: 176  Bit Score: 106.06  E-value: 5.74e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  453 LPAFAEIERILALIESSPVVVISGETGCGKSTQVPQFILDnwFFRALQLPakenlpHVEIICTQPRRLSAIGVAERVAAE 532
Cdd:cd17977    1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAE--YCLSAHYQ------HGVVVCTQVHKQTAVWLALRVADE 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  533 RLDRIGQLVGYQIRLENKVSQSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSEESDFLLLILKNLLRERKDLKV 612
Cdd:cd17977   73 MDVNIGHEVGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKL 152
                        170       180
                 ....*....|....*....|....
gi 24641139  613 ILMSATLNAALFSDYFGGAPVLDI 636
Cdd:cd17977  153 VIITCPHLSSKLLSYYGNVPLIEV 176
HA2 pfam04408
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ...
940-1028 6.92e-26

Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 461295 [Multi-domain]  Cd Length: 104  Bit Score: 103.09  E-value: 6.92e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139    940 ALTRLRDVGALDAEDQLTPLGHHLAALPVDVRIGKLMLYGAIFQCLDSVLTIAACLSNKSPFVSPLN------------- 1006
Cdd:pfam04408    1 ALELLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPNFldprsaakaarrr 80
                           90       100
                   ....*....|....*....|....
gi 24641139   1007 KRTEADKCKRMFA--LGNSDHLTV 1028
Cdd:pfam04408   81 RRAADEKARAKFArlDLEGDHLTL 104
DEXQc_DQX1 cd17986
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ...
453-636 2.48e-25

DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 (DQX1) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350744 [Multi-domain]  Cd Length: 177  Bit Score: 104.21  E-value: 2.48e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  453 LPAFAEIERILALIES-SPVVVISGETGCGKSTQVPQFILDNWFFRALQlpakenlpHVEIICTQPRRLSAIGVAERVAA 531
Cdd:cd17986    1 LPIWAAKFTFLEQLESpSGIVLVSGEPGSGKSTQVPQWCAEFALSRGFQ--------KGQVTVTQPHPLAARSLALRVAD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  532 ERLDRIGQLVGYQIRLENKVSQSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHERSEESDFLLLILKNLLRERKDLK 611
Cdd:cd17986   73 EMDLNLGHEVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELR 152
                        170       180
                 ....*....|....*....|....*.
gi 24641139  612 VILM-SATLNAALFSdYFGGAPVLDI 636
Cdd:cd17986  153 VVVVtSPALEPKLRA-FWGNPPVVHV 177
HA2 smart00847
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ...
948-1029 4.67e-25

Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.


Pssm-ID: 214852 [Multi-domain]  Cd Length: 82  Bit Score: 100.04  E-value: 4.67e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139     948 GALDAEDQLTPLGHHLAALPVDVRIGKLMLYGAIFQCLDSVLTIAACLSNKSPFvsPLNKRTEADKCKRMFALGNSDHLT 1027
Cdd:smart00847    3 GALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGDPR--PKEKREDADAARRRFADPESDHLT 80

                    ..
gi 24641139    1028 VL 1029
Cdd:smart00847   81 LL 82
DEXDc smart00487
DEAD-like helicases superfamily;
462-642 4.07e-19

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 87.16  E-value: 4.07e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139     462 ILALIESSPVVVISGETGCGKSTQVPQFILDnwffralqlpAKENLPHVEIICTQPRRLSAIGVAERVAAE----RLDRI 537
Cdd:smart00487   17 IEALLSGLRDVILAAPTGSGKTLAALLPALE----------ALKRGKGGRVLVLVPTRELAEQWAEELKKLgpslGLKVV 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139     538 GQLVGYQIR--LENKVSQSTRLSFCTTGILLRRLASDPL-LGSVTHVIVDEVHERSeESDFLLLILKNLLRERKDLKVIL 614
Cdd:smart00487   87 GLYGGDSKReqLRKLESGKTDILVTTPGRLLDLLENDKLsLSNVDLVILDEAHRLL-DGGFGDQLEKLLKLLPKNVQLLL 165
                           170       180       190
                    ....*....|....*....|....*....|
gi 24641139     615 MSATLNAAL--FSDYFGGAPVLDIPGRTFP 642
Cdd:smart00487  166 LSATPPEEIenLLELFLNDPVFIDVGFTPL 195
OB_NTP_bind pfam07717
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ...
1114-1212 6.96e-18

Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus of the DEAD-box helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. There do seem to be a couple of instances where it occurs by itself -. The structure PDB:3i4u adopts an OB-fold. helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. This C-terminal domain of the yeast helicase contains an oligonucleotide/oligosaccharide-binding (OB)-fold which seems to be placed at the entrance of the putative nucleic acid cavity. It also constitutes the binding site for the G-patch-containing domain of Pfa1p. When found on DEAH/RHA helicases, this domain is central to the regulation of the helicase activity through its binding of both RNA and G-patch domain proteins.


Pssm-ID: 400182 [Multi-domain]  Cd Length: 82  Bit Score: 79.60  E-value: 6.96e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   1114 LTSLLCAALYPNIVKiMTPDRVYIQTAggavprepshhdlrfktRGDGYVKIHPSSVNSQVSVFQAPFLVFQEKVRTSAI 1193
Cdd:pfam07717    1 LRAALAAGLYPNVAR-RDPKGKGYTTL-----------------SDNQRVFIHPSSVLFNEKTFPPEWVVYQELVETTKV 62
                           90
                   ....*....|....*....
gi 24641139   1194 YIRDCSMLPLIAMVLFAGS 1212
Cdd:pfam07717   63 YIRTVTAISPEWLLLFAPH 81
HELICc smart00490
helicase superfamily c-terminal domain;
781-871 2.82e-11

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 60.69  E-value: 2.82e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139     781 RAGKFILVPLHSALSGEDQALVFKKAPPGKRKIVLSTNIAETSVTIDDCVFVVDCGLmkekcfdsnrnmesldlvWVSRA 860
Cdd:smart00490    8 KELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDL------------------PWSPA 69
                            90
                    ....*....|.
gi 24641139     861 NAKQRKGRAGR 871
Cdd:smart00490   70 SYIQRIGRAGR 80
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
751-872 6.54e-10

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 57.61  E-value: 6.54e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139    751 REGTILIFLPGFgeiqsvhdSLLDNALFSPRAGkFILVPLHSALSGEDQALVFKKAPPGKRKIVLSTNIAETSVTIDDCV 830
Cdd:pfam00271   14 RGGKVLIFSQTK--------KTLEAELLLEKEG-IKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVD 84
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 24641139    831 FVVDcglmkekcfdsnrnmesLDLVWvSRANAKQRKGRAGRV 872
Cdd:pfam00271   85 LVIN-----------------YDLPW-NPASYIQRIGRAGRA 108
PHA02653 PHA02653
RNA helicase NPH-II; Provisional
461-882 3.20e-09

RNA helicase NPH-II; Provisional


Pssm-ID: 177443 [Multi-domain]  Cd Length: 675  Bit Score: 61.15  E-value: 3.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   461 RILALIESSPVVVISGETGCGKSTQVPQFILdnWF---------FRALQLPAKEN-----LPHVEIIctqprRLSAIGVA 526
Cdd:PHA02653  171 KIFEAWISRKPVVLTGGTGVGKTSQVPKLLL--WFnylfggfdnLDKIDPNFIERpivlsLPRVALV-----RLHSITLL 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   527 ERVAAERLD------RIGqlvGYQIRLENKVSQSTRLSFCTTGILLRRLasdpllGSVTHVIVDEVHERSEESDFLLLIL 600
Cdd:PHA02653  244 KSLGFDEIDgspislKYG---SIPDELINTNPKPYGLVFSTHKLTLNKL------FDYGTVIIDEVHEHDQIGDIIIAVA 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   601 KNLLRERKDLkvILMSATL--NAALFSDYFGGAPVLDIPGRT-FPVQQLFLEDilemsdfvmEYDTKYCRKLKKQE-QEI 676
Cdd:PHA02653  315 RKHIDKIRSL--FLMTATLedDRDRIKEFFPNPAFVHIPGGTlFPISEVYVKN---------KYNPKNKRAYIEEEkKNI 383
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   677 LERELEYA-DVQASGeapgkKIKDEKLTLAETYQRYAEYSKPtcksIYLMepmtinpeliesvlkYIVegsHdwpregti 755
Cdd:PHA02653  384 VTALKKYTpPKGSSG-----IVFVASVSQCEEYKKYLEKRLP----IYDF---------------YII---H-------- 428
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139   756 liflpgfGEIQSVHDSLLDnalfspragkfilvplhsalsgedqalVFKKAPPgkrKIVLSTNIAETSVTIDDCVFVVDC 835
Cdd:PHA02653  429 -------GKVPNIDEILEK---------------------------VYSSKNP---SIIISTPYLESSVTIRNATHVYDT 471
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 24641139   836 GLMKEKCFDSNRNMesldlvWVSRANAKQRKGRAGRVMPGVCIHLYT 882
Cdd:PHA02653  472 GRVYVPEPFGGKEM------FISKSMRTQRKGRVGRVSPGTYVYFYD 512
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
472-618 3.83e-09

N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 56.64  E-value: 3.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139  472 VVISGETGCGKSTQVPQFILDnwffRALQLPAKenlphVEIICtqPRRLSAIGVAERVAAERL--DRIGQLVGYQ--IRL 547
Cdd:cd00046    4 VLITAPTGSGKTLAALLAALL----LLLKKGKK-----VLVLV--PTKALALQTAERLRELFGpgIRVAVLVGGSsaEER 72
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24641139  548 ENKVSQSTRLSFCTTGILLRRLASDPLLGS--VTHVIVDEVHERSEESDFLLLILKNLLR-ERKDLKVILMSAT 618
Cdd:cd00046   73 EKNKLGDADIIIATPDMLLNLLLREDRLFLkdLKLIIVDEAHALLIDSRGALILDLAVRKaGLKNAQVILLSAT 146
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
283-360 9.96e-09

RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. The function of this domain is unknown. GCN2 is the alpha-subunit of the only translation initiation factor (eIF2 alpha) kinase that appears in all eukaryotes. Its function requires an interaction with GCN1 via the domain at its N-terminus, which is termed the RWD domain after three major RWD-containing proteins: RING finger-containing proteins, WD-repeat-containing proteins, and yeast DEAD (DEXD)-like helicases. The structure forms an alpha + beta sandwich fold consisting of two layers: a four-stranded antiparallel beta-sheet, and three side-by-side alpha-helices.


Pssm-ID: 399058  Cd Length: 111  Bit Score: 54.25  E-value: 9.96e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24641139    283 KDSVDENDNELWFHVEVRFPPGsrYPYEAPFIYLKTTcHDIPHELRLRYARHLYKEAKEICrdGIPCVYSICDLLQSN 360
Cdd:pfam05773   38 DSDESDSSHLPPLVLKFTLPED--YPDEPPKISLSSP-WNLSDEQVLSLLEELEELAEENL--GEVMIFELIEWLQEN 110
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
460-623 1.83e-07

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 52.24  E-value: 1.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139    460 ERILALIESSPVVVISGETGCGKSTqvpqfildnwffrALQLPA----KENLPHVEIICTQPRRLSAIGVAERvAAERLD 535
Cdd:pfam00270    5 AEAIPAILEGRDVLVQAPTGSGKTL-------------AFLLPAlealDKLDNGPQALVLAPTRELAEQIYEE-LKKLGK 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641139    536 RIGQLV-----GYQIRLENKVSQSTRLSFCTTGILLRRLASDPLLGSVTHVIVDEVHeRSEESDFLLLILKNLLRERKDL 610
Cdd:pfam00270   71 GLGLKVasllgGDSRKEQLEKLKGPDILVGTPGRLLDLLQERKLLKNLKLLVLDEAH-RLLDMGFGPDLEEILRRLPKKR 149
                          170
                   ....*....|...
gi 24641139    611 KVILMSATLNAAL 623
Cdd:pfam00270  150 QILLLSATLPRNL 162
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
245-272 1.02e-06

Zinc finger C-x8-C-x5-C-x3-H type (and similar);


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 46.03  E-value: 1.02e-06
                           10        20
                   ....*....|....*....|....*...
gi 24641139    245 KKPPLrCRNFDRDGTCKYGPKCRFAHLP 272
Cdd:pfam00642    1 YKTEL-CRFFLRTGYCKYGDRCKFAHGQ 27
ZnF_C3H1 smart00356
zinc finger;
246-270 1.09e-04

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 40.31  E-value: 1.09e-04
                            10        20
                    ....*....|....*....|....*
gi 24641139     246 KPPLrCRNFDRdGTCKYGPKCRFAH 270
Cdd:smart00356    3 KTEL-CKFFKR-GYCPRGDRCKFAH 25
zf_CCCH_4 pfam18345
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch ...
251-270 6.06e-04

Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch domain-containing proteins such as ZIP. Functional studies indicate that ZIP specifically targets EGFR and represses its transcription, and that the zinc finger and the coiled-coil domains are central to that process.


Pssm-ID: 465719 [Multi-domain]  Cd Length: 19  Bit Score: 38.17  E-value: 6.06e-04
                           10        20
                   ....*....|....*....|
gi 24641139    251 CRNFdRDGTCKYGPKCRFAH 270
Cdd:pfam18345    1 CKFF-LKGRCRYGDKCRFAH 19
UBA_VP13D cd14306
UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar ...
123-154 2.03e-03

UBA domain found in vacuolar protein sorting-associated protein 13D (VP13D) and similar proteins; VP13D is a chorea-acanthocytosis (CHAC)-similar protein encoded by gene VPS13D. it contains two putative domains, ubiquitin-associated (UBA) domain and lectin domain of ricin B chain profile (ricin-B-lectin), suggesting it may interact with, and be involved in the trafficking of, proteins modified with ubiquitin and/or carbohydrate molecules. Further investigation is required.


Pssm-ID: 270491  Cd Length: 36  Bit Score: 37.04  E-value: 2.03e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 24641139  123 LAKLENYGFQAVHCLEAYEHCSGDTEAALLLL 154
Cdd:cd14306    1 VAKLMELGFPEEDCIRALRACGGNVEEAANWL 32
RWD_GCN2 cd23823
RWD domain of eIF-2-alpha kinase GCN2 and related proteins; GCN2 (EC 2.7.11.1), also called ...
284-359 3.52e-03

RWD domain of eIF-2-alpha kinase GCN2 and related proteins; GCN2 (EC 2.7.11.1), also called eukaryotic translation initiation factor 2-alpha kinase 4 (EIF2AK4), acts as a metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to low amino acid availability. It also plays a role in modulating the adaptive immune response to yellow fever virus infection and promotes dendritic cells to initiate autophagy and antigene presentation to both CD4(+) and CD8(+) T-cells under amino acid starvation.


Pssm-ID: 467659  Cd Length: 117  Bit Score: 38.74  E-value: 3.52e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24641139  284 DSVDENDNELWFHVEVRFPPgsRYPYEAPFIYLKtTCHDIPHELRLRYARHLYKEAKEicRDGIPCVYSICDLLQS 359
Cdd:cd23823   41 QEGESEENHVSVDLHVKFPP--TYPDVPPEIELE-NVKGLSDEQLEELLKELEELAKE--LLGEEMIFELAEAVQE 111
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
812-882 7.46e-03

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 36.53  E-value: 7.46e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24641139  812 KIVLSTNIAETSVTIDDCVFVVDCGlmkekcfdsnrnmesldlVWVSRANAKQRKGRAGRVMPGVC-IHLYT 882
Cdd:cd18785   24 EILVATNVLGEGIDVPSLDTVIFFD------------------PPSSAASYIQRVGRAGRGGKDEGeVILFV 77
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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