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Conserved domains on  [gi|1883543185|ref|NP_001372838|]
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antiviral innate immune response receptor RIG-I isoform 3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEXHc_RIG-I_DDX58 cd18073
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ...
 241-442 3.43e-144

DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I is a member 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: 350831 [Multi-domain]  Cd Length: 202  Bit Score: 424.23  E-value: 3.43e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 241 FKPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKGKVVFFANQIPVYEQQKSVFSKYFERHGYR 320
Cdd:cd18073     1 FKPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKGKVVFFATKVPVYEQQKSVFSKYFERHGYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 321 VTGISGATAENVPVEQIVENNDIIILTPQILVNNLKKGTIPSLSIFTLMIFDECHNTSKQHPYNMIMFNYLDQKLGGSSG 400
Cdd:cd18073    81 VTGISGATAENVPVEQIIENNDIIILTPQILVNNLKKGTIPSLSIFTLMIFDECHNTSGNHPYNMIMFRYLDQKLGGSSG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1883543185 401 PLPQVIGLTASVGVGDAKNTDEALDYICKLCASLDASVIATV 442
Cdd:cd18073   161 PLPQIIGLTASVGVGDAKNTDEALDYICKLCASLDASVIATV 202
RIG-I_C cd15805
C-terminal domain of Retinoic acid-inducible gene (RIG)-I protein, a cytoplasmic viral RNA ...
 748-861 1.40e-51

C-terminal domain of Retinoic acid-inducible gene (RIG)-I protein, a cytoplasmic viral RNA receptor; Retinoic acid-inducible gene (RIG)-I protein, also called DEAD box protein 58 (DDX58), is one of three members of the RIG-I-like Receptor (RLR) family. RLRs are cytoplasmic RNA receptors that recognize non-self RNA and act as molecular sensors to detect viral pathogens. RIG-I is activated by blunt-ended double-stranded RNA with or without a 5'-triphosphate (ppp), by single-stranded RNA marked by a 5'-ppp and by polyuridine sequences. It has been found to confer resistance to many negative-sense RNA viruses, including orthomyxoviruses, rhabdoviruses, bunyaviruses, and paramyxoviruses, as well as the positive-strand hepatitis C virus. RLRs are characterized by a central DExD/H-box helicase domain and a C-terminal domain, both of which are responsible for binding viral RNA. The helicase domain catalyzes the unwinding of double stranded RNA in an ATP-dependent manner. RIG-I and MDA5 also contain two N-terminal caspase activation and recruitment domains (CARDs), which initiate downstream signaling upon viral RNA sensing.


:

Pssm-ID: 276943  Cd Length: 112  Bit Score: 175.92  E-value: 1.40e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 748 NKKLLCRKCKALACYTADVRVIEECHYTVLGDAFKECFVSRPHPKPKQFSSFEKRAKIFCArqNCSHDWGIHVKYKTFEI 827
Cdd:cd15805     1 SYKLLCGKCKTFACNSDDIRVIKESHHVVIDPSFKERYTTKPHPKPKTFDGFEKKGKIFCK--KCGHDWGIMASYKIQNL 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1883543185 828 PVIKIESFVVEDIATGVQTLYSKWKDFHFEKIPF 861
Cdd:cd15805    79 PVLKIESFVVENPVTGQQLLFRKWKDVPFAIKEF 112
MDA5_ID cd12090
Insert domain of MDA5; MDA5 (melanoma-differentiation-associated gene 5, also known as IFIH1), ...
 469-604 3.49e-49

Insert domain of MDA5; MDA5 (melanoma-differentiation-associated gene 5, also known as IFIH1), as well as RIG-I (Retinoic acid Inducible Gene I, also known as DDX58) and LPG2 (also known as DHX58), contain two N-terminal CARD domains and a C-terminal SF2 helicase domain. They are cytoplasmic DEAD box RNA helicases acting as key innate immune pattern-recognition receptor (PRRs) that play an important role in host antiviral response by sensing incoming viral RNA. Their SF2 helicase domain is comprised of 3 structural domains, the 2 generally conserved helicase domains and a helical domain inserted between the two domains. The inserted domain is involved in conformational changes upon ligand binding.


:

Pssm-ID: 277189  Cd Length: 120  Bit Score: 169.42  E-value: 3.49e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 469 DKFKYIIAQLMRDTESLAKRICKDlenlsqIQNREFGTQKYEQWIVTVQKACMVFqmpdkdeesrICKALFLYTSHLRKY 548
Cdd:cd12090     1 DPFGDIIKKLMTDIEELLKMTPPD------IQPREFGTQKYEQWVVTLEKKAAKL----------GNRALRTCAEHLRKY 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1883543185 549 NDALIISEHARMKDALDYLKDFFSNVRAAGFDEIEQDLTQRFEEKLQELESVSRDP 604
Cdd:cd12090    65 NDALLINDTARMKDALQYLKEFYTNLKEAKFDETERFLTDLFEENLEELKKLARDP 120
CARD_RIG-I_r2 cd08817
Caspase activation and recruitment domain found in RIG-I, second repeat; Caspase activation ...
 100-189 7.08e-43

Caspase activation and recruitment domain found in RIG-I, second repeat; Caspase activation and recruitment domain (CARD) found in RIG-I (Retinoic acid Inducible Gene I, also known as Ddx58), second repeat. RIG-I is a cytoplasmic RNA helicase that plays an important role in host antiviral response by sensing incoming viral RNA. RIG-I contains two N-terminal CARD domains and a C-terminal RNA helicase. Upon activation, the signal is transferred to downstream pathways via the adaptor molecule IPS-1 (MAVS, VISA, CARDIF), leading to the induction of type I interferons. Although very similar in sequence, RIG-I recognizes different sets of viruses compared to MDA5, a related RNA helicase. RIG-I associates with IPS-1 through a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


:

Pssm-ID: 260076  Cd Length: 91  Bit Score: 150.68  E-value: 7.08e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 100 LEEYRLLLKRLQPEFKTRIIPTDIISDLSECLINQECEEILQICSTKGMMAGAEKLVECLLRSDKENWPKTLKLALEKE- 178
Cdd:cd08817     1 LEEHRQLLKRIEPSFTKRIKPRDLIPYLSDCLIDRECEEILQIEEQKGMIAGAEKLVECLLRSDKENWPKTLKLALEKCg 80

                          90
                  ....*....|.
gi 1883543185 179 RNKFSELWIVE 189
Cdd:cd08817    81 YDAASELWPDE 91
DD super family cl14633
Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) ...
 2-92 2.07e-39

Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) superfamily includes the DD, Pyrin, CARD (Caspase activation and recruitment domain) and DED (Death Effector Domain) families. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. They are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways including those that impact innate immunity, inflammation, differentiation, and cancer.


The actual alignment was detected with superfamily member cd08816:

Pssm-ID: 472698  Cd Length: 90  Bit Score: 140.66  E-value: 2.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185   2 TTEQRRSLQAFQDYIRKTLDPTYILSYMAPWFREEEVQYIQAEKNnKGPMEAATLFLKFLLELQEEGWFRGFLDALDHAG 81
Cdd:cd08816     1 TALEKRNLRCYRDYIEKILRPSYVLGFMTTWLEDELVERILSEEE-KGVTEAAQLFLDAVLQLEEEGWFQGFLDALLAAG 79

                          90
                  ....*....|.
gi 1883543185  82 YSGLYEAIESW 92
Cdd:cd08816    80 YTGLCEAIENW 90
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 609-671 3.16e-15

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd18802:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 142  Bit Score: 73.39  E-value: 3.16e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1883543185 609 PKLEDLCFILQEEYHLNPETITILFVKTRALVDALKNWIEGNPK-LSFLKPGILTGRGKTNQNT 671
Cdd:cd18802     7 PKLQKLIEILREYFPKTPDFRGIIFVERRATAVVLSRLLKEHPStLAFIRCGFLIGRGNSSQRK 70
 
Name Accession Description Interval E-value
DEXHc_RIG-I_DDX58 cd18073
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ...
 241-442 3.43e-144

DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I is a member 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: 350831 [Multi-domain]  Cd Length: 202  Bit Score: 424.23  E-value: 3.43e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 241 FKPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKGKVVFFANQIPVYEQQKSVFSKYFERHGYR 320
Cdd:cd18073     1 FKPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKGKVVFFATKVPVYEQQKSVFSKYFERHGYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 321 VTGISGATAENVPVEQIVENNDIIILTPQILVNNLKKGTIPSLSIFTLMIFDECHNTSKQHPYNMIMFNYLDQKLGGSSG 400
Cdd:cd18073    81 VTGISGATAENVPVEQIIENNDIIILTPQILVNNLKKGTIPSLSIFTLMIFDECHNTSGNHPYNMIMFRYLDQKLGGSSG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1883543185 401 PLPQVIGLTASVGVGDAKNTDEALDYICKLCASLDASVIATV 442
Cdd:cd18073   161 PLPQIIGLTASVGVGDAKNTDEALDYICKLCASLDASVIATV 202
RIG-I_C cd15805
C-terminal domain of Retinoic acid-inducible gene (RIG)-I protein, a cytoplasmic viral RNA ...
 748-861 1.40e-51

C-terminal domain of Retinoic acid-inducible gene (RIG)-I protein, a cytoplasmic viral RNA receptor; Retinoic acid-inducible gene (RIG)-I protein, also called DEAD box protein 58 (DDX58), is one of three members of the RIG-I-like Receptor (RLR) family. RLRs are cytoplasmic RNA receptors that recognize non-self RNA and act as molecular sensors to detect viral pathogens. RIG-I is activated by blunt-ended double-stranded RNA with or without a 5'-triphosphate (ppp), by single-stranded RNA marked by a 5'-ppp and by polyuridine sequences. It has been found to confer resistance to many negative-sense RNA viruses, including orthomyxoviruses, rhabdoviruses, bunyaviruses, and paramyxoviruses, as well as the positive-strand hepatitis C virus. RLRs are characterized by a central DExD/H-box helicase domain and a C-terminal domain, both of which are responsible for binding viral RNA. The helicase domain catalyzes the unwinding of double stranded RNA in an ATP-dependent manner. RIG-I and MDA5 also contain two N-terminal caspase activation and recruitment domains (CARDs), which initiate downstream signaling upon viral RNA sensing.


Pssm-ID: 276943  Cd Length: 112  Bit Score: 175.92  E-value: 1.40e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 748 NKKLLCRKCKALACYTADVRVIEECHYTVLGDAFKECFVSRPHPKPKQFSSFEKRAKIFCArqNCSHDWGIHVKYKTFEI 827
Cdd:cd15805     1 SYKLLCGKCKTFACNSDDIRVIKESHHVVIDPSFKERYTTKPHPKPKTFDGFEKKGKIFCK--KCGHDWGIMASYKIQNL 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1883543185 828 PVIKIESFVVEDIATGVQTLYSKWKDFHFEKIPF 861
Cdd:cd15805    79 PVLKIESFVVENPVTGQQLLFRKWKDVPFAIKEF 112
RIG-I_C-RD pfam11648
C-terminal domain of RIG-I; This family of proteins represents the regulatory domain RD of ...
 749-866 5.18e-51

C-terminal domain of RIG-I; This family of proteins represents the regulatory domain RD of RIG-I, a protein which initiates a signalling cascade that provides essential antiviral protection for the host. The RD domain binds viral RNA, activating the RIG-I ATPase by RNA-dependant dimerization. The structure of RD contains a zinc-binding domain and is thought to confer ligand specificity.


Pssm-ID: 463318  Cd Length: 117  Bit Score: 174.36  E-value: 5.18e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 749 KKLLCRKCKALACYTADVRVIEECHYTVLGDAFKECFVSR-PHPKPKQFSSFEKRAKIFCArqNCSHDWGIHVKYKTFEI 827
Cdd:pfam11648   1 VKLLCRKCKKFVCSGSDIRKIENSHHVVVNPDFKERYIVKePHKKPKSFEDWEPGGKISCK--KCGQDWGIMMKYKGVEL 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1883543185 828 PVIKIESFVVEDIATGVQTLYSKWKDFHFEKIPFDPAEM 866
Cdd:pfam11648  79 PVLKIKSFVVETPATGRRKTKKKWKDVPFEVPEFDYTEY 117
MDA5_ID cd12090
Insert domain of MDA5; MDA5 (melanoma-differentiation-associated gene 5, also known as IFIH1), ...
 469-604 3.49e-49

Insert domain of MDA5; MDA5 (melanoma-differentiation-associated gene 5, also known as IFIH1), as well as RIG-I (Retinoic acid Inducible Gene I, also known as DDX58) and LPG2 (also known as DHX58), contain two N-terminal CARD domains and a C-terminal SF2 helicase domain. They are cytoplasmic DEAD box RNA helicases acting as key innate immune pattern-recognition receptor (PRRs) that play an important role in host antiviral response by sensing incoming viral RNA. Their SF2 helicase domain is comprised of 3 structural domains, the 2 generally conserved helicase domains and a helical domain inserted between the two domains. The inserted domain is involved in conformational changes upon ligand binding.


Pssm-ID: 277189  Cd Length: 120  Bit Score: 169.42  E-value: 3.49e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 469 DKFKYIIAQLMRDTESLAKRICKDlenlsqIQNREFGTQKYEQWIVTVQKACMVFqmpdkdeesrICKALFLYTSHLRKY 548
Cdd:cd12090     1 DPFGDIIKKLMTDIEELLKMTPPD------IQPREFGTQKYEQWVVTLEKKAAKL----------GNRALRTCAEHLRKY 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1883543185 549 NDALIISEHARMKDALDYLKDFFSNVRAAGFDEIEQDLTQRFEEKLQELESVSRDP 604
Cdd:cd12090    65 NDALLINDTARMKDALQYLKEFYTNLKEAKFDETERFLTDLFEENLEELKKLARDP 120
CARD_RIG-I_r2 cd08817
Caspase activation and recruitment domain found in RIG-I, second repeat; Caspase activation ...
 100-189 7.08e-43

Caspase activation and recruitment domain found in RIG-I, second repeat; Caspase activation and recruitment domain (CARD) found in RIG-I (Retinoic acid Inducible Gene I, also known as Ddx58), second repeat. RIG-I is a cytoplasmic RNA helicase that plays an important role in host antiviral response by sensing incoming viral RNA. RIG-I contains two N-terminal CARD domains and a C-terminal RNA helicase. Upon activation, the signal is transferred to downstream pathways via the adaptor molecule IPS-1 (MAVS, VISA, CARDIF), leading to the induction of type I interferons. Although very similar in sequence, RIG-I recognizes different sets of viruses compared to MDA5, a related RNA helicase. RIG-I associates with IPS-1 through a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260076  Cd Length: 91  Bit Score: 150.68  E-value: 7.08e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 100 LEEYRLLLKRLQPEFKTRIIPTDIISDLSECLINQECEEILQICSTKGMMAGAEKLVECLLRSDKENWPKTLKLALEKE- 178
Cdd:cd08817     1 LEEHRQLLKRIEPSFTKRIKPRDLIPYLSDCLIDRECEEILQIEEQKGMIAGAEKLVECLLRSDKENWPKTLKLALEKCg 80

                          90
                  ....*....|.
gi 1883543185 179 RNKFSELWIVE 189
Cdd:cd08817    81 YDAASELWPDE 91
RIG-I_C pfam18119
RIG-I receptor C-terminal domain; This is the C-terminal domain of Innate Immune ...
 458-601 1.84e-41

RIG-I receptor C-terminal domain; This is the C-terminal domain of Innate Immune Pattern-Recognition Receptor RIG-I present in homo sapiens. RIG-I is a key cytosolic pattern-recognition receptors of the vertebrate innate immune system that form the first line of defense against RNA viral infection. RNA binding to RIG-I is mediated both by the C-terminal domain and by the helicase domain. The C-terminal domain specifically binds the 5'triphosphate end with a 10-fold higher affinity compared to 5'OH-dsRNA.


Pssm-ID: 465656  Cd Length: 139  Bit Score: 148.26  E-value: 1.84e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 458 KFFRKVESRISDKFKYIIAQLMRDTESLAKRIcKDLENLSQIQNREFGTQKYEQWIVTVQKACMVfqmpDKDEESRICka 537
Cdd:pfam18119   2 KFVVKVTSRKEDPFGDIIKDIMSKIEDHLNKS-YNLDDLSKLKPSDKGTQKYEQWIVTLQKKGAE----DPEEERRVC-- 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1883543185 538 LFLYTSHLRKYNDALIISEHARMKDALDYLKDFFSNVRAAGFDEIEQDLTQRFEEKLQELESVS 601
Cdd:pfam18119  75 RALCTEHLRKYNDALIINDDARTKDALEYLLKFLKELKETKFDETERKLYRLFEEKREELQRLA 138
CARD_RIG-I_r1 cd08816
Caspase activation and recruitment domain found in RIG-I, first repeat; Caspase activation and ...
 2-92 2.07e-39

Caspase activation and recruitment domain found in RIG-I, first repeat; Caspase activation and recruitment domain (CARD) found in RIG-I (Retinoic acid Inducible Gene I, also known as Ddx58), first repeat. RIG-I is a cytoplasmic RNA helicase that plays an important role in host antiviral response by sensing incoming viral RNA. RIG-I contains two N-terminal CARD domains and a C-terminal RNA helicase. Upon activation, the signal is transferred to downstream pathways via the adaptor molecule IPS-1 (MAVS, VISA, CARDIF), leading to the induction of type I interferons. Although very similar in sequence, RIG-I recognizes different sets of viruses compared to MDA5, a related RNA helicase. RIG-I associates with IPS-1 through a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260075  Cd Length: 90  Bit Score: 140.66  E-value: 2.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185   2 TTEQRRSLQAFQDYIRKTLDPTYILSYMAPWFREEEVQYIQAEKNnKGPMEAATLFLKFLLELQEEGWFRGFLDALDHAG 81
Cdd:cd08816     1 TALEKRNLRCYRDYIEKILRPSYVLGFMTTWLEDELVERILSEEE-KGVTEAAQLFLDAVLQLEEEGWFQGFLDALLAAG 79

                          90
                  ....*....|.
gi 1883543185  82 YSGLYEAIESW 92
Cdd:cd08816    80 YTGLCEAIENW 90
CARD_2 pfam16739
Caspase recruitment domain; In the probable ATP-dependent RNA helicase DDX58 this CARD domain ...
 1-93 2.05e-36

Caspase recruitment domain; In the probable ATP-dependent RNA helicase DDX58 this CARD domain is found near the N-terminus and interacts with the C-terminal domain.


Pssm-ID: 465251  Cd Length: 93  Bit Score: 132.33  E-value: 2.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185   1 MTTEQRRSLQAFQDYIRKTLDPTYILSYMAPWFREEEVQYIQAEKNNKGPMEAATLFLKFLLELQEEGWFRGFLDALDHA 80
Cdd:pfam16739   1 EDDEYRRLLRLFRPRLKDTIKPTEILPHLPECLTEDDKERIRAETNNKGNTAAAELLLDRLVRSDREGWFRAFLDALRKT 80

                          90
                  ....*....|...
gi 1883543185  81 GYSGLYEAIESWD 93
Cdd:pfam16739  81 GHDGLAEELEGEY 93
CARD_2 pfam16739
Caspase recruitment domain; In the probable ATP-dependent RNA helicase DDX58 this CARD domain ...
 99-190 2.47e-28

Caspase recruitment domain; In the probable ATP-dependent RNA helicase DDX58 this CARD domain is found near the N-terminus and interacts with the C-terminal domain.


Pssm-ID: 465251  Cd Length: 93  Bit Score: 109.22  E-value: 2.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185  99 KLEEYRLLLKRLQPEFKTRIIPTDIISDLSECLINQECEEILQICSTKGMMAGAEKLVECLLRSDKENWPKTLKLALEK- 177
Cdd:pfam16739   1 EDDEYRRLLRLFRPRLKDTIKPTEILPHLPECLTEDDKERIRAETNNKGNTAAAELLLDRLVRSDREGWFRAFLDALRKt 80

                          90
                  ....*....|...
gi 1883543185 178 ERNKFSELWIVEK 190
Cdd:pfam16739  81 GHDGLAEELEGEY 93
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
243-672 1.92e-25

ERCC4-related helicase [Replication, recombination and repair];


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 112.90  E-value: 1.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 243 PRNYQLELALPAMKgKNTIICAPTGCGKTFVSLLICEHHLKKfpqgQKGKVVFFANQIPVYEQQKSVFSKYFERHGYRVT 322
Cdd:COG1111     4 RRLYQLNLAASALR-KNTLVVLPTGLGKTAVALLVIAERLHK----KGGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 323 GISGataeNVPVEQ---IVENNDIIILTPQILVNNLKKGTIpSLSIFTLMIFDECHNTSKQHPYNMIMFNYLDQKlggss 399
Cdd:COG1111    79 VFTG----EVSPEKrkeLWEKARIIVATPQVIENDLIAGRI-DLDDVSLLIFDEAHRAVGNYAYVYIAERYHEDA----- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 400 gPLPQVIGLTASVGvgdakNTDEALDYICKlcaSLdasVIATVKHNLEELEQVV-YKPQKFFRKVESRISDKFKYIIAQL 478
Cdd:COG1111   149 -KDPLILGMTASPG-----SDEEKIEEVCE---NL---GIENVEVRTEEDPDVApYVHDTEVEWIRVELPEELKEIRDLL 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 479 mrdTESLAKRIcKDLENLSQIQNREFGTQKYE--QWIVTVQKacmvfQMPDKDEEsrickalflytshlrKYNDALIISE 556
Cdd:COG1111   217 ---NEVLDDRL-KKLKELGVIVSTSPDLSKKDllALQKKLQR-----RIREDDSE---------------GYRAISILAE 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 557 HARMKDALDY--------LKDFFSNVRAAGFDEIEQDLTQRF--EEKLQELESVSRDPSNENPKLEDLCFILQEEYHLNP 626
Cdd:COG1111   273 ALKLRHALELletqgveaLLRYLERLEEEARSSGGSKASKRLvsDPRFRKAMRLAEEADIEHPKLSKLREILKEQLGTNP 352

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1883543185 627 ETITILFVKTR----ALVDALKNwiEGnpklsfLKPGILTGRGKTNQNTG 672
Cdd:COG1111   353 DSRIIVFTQYRdtaeMIVEFLSE--PG------IKAGRFVGQASKEGDKG 394
PRK13766 PRK13766
Hef nuclease; Provisional
 243-674 9.14e-24

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 107.65  E-value: 9.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 243 PRNYQLELALPAMKgKNTIICAPTGCGKTFVSLLICEHHLKKFPqgqkGKVVFFANQIPVYEQQKSVFSKYFERHGYRVT 322
Cdd:PRK13766   16 ARLYQQLLAATALK-KNTLVVLPTGLGKTAIALLVIAERLHKKG----GKVLILAPTKPLVEQHAEFFRKFLNIPEEKIV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 323 GISGATAenvPVE--QIVENNDIIILTPQILVNNLKKGTIpSLSIFTLMIFDECHNTSKQHPYNMIMFNYLDQklggSSG 400
Cdd:PRK13766   91 VFTGEVS---PEKraELWEKAKVIVATPQVIENDLIAGRI-SLEDVSLLIFDEAHRAVGNYAYVYIAERYHED----AKN 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 401 PLpqVIGLTASVGVGDAKntdealdyicklcasldasvIATVKHNLeeleqvvykpqkFFRKVESRISD----------- 469
Cdd:PRK13766  163 PL--VLGLTASPGSDEEK--------------------IKEVCENL------------GIEHVEVRTEDdpdvkpyvhkv 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 470 KFKYIIAQL---MRDTESLAKRICKD----LENLSQIQNREFGTQKYEqwIVTVQKAcmVFQMPDKDEESriCKALFLYT 542
Cdd:PRK13766  209 KIEWVRVELpeeLKEIRDLLNEALKDrlkkLKELGVIVSISPDVSKKE--LLGLQKK--LQQEIANDDSE--GYEAISIL 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 543 SHLRKYNDALIISEHARMKDALDYLKDFFSNVRAAGFDEIEQDLTQrfEEKLQELESVSRDPSNENPKLEDLCFILQEEY 622
Cdd:PRK13766  283 AEAMKLRHAVELLETQGVEALRRYLERLREEARSSGGSKASKRLVE--DPRFRKAVRKAKELDIEHPKLEKLREIVKEQL 360

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1883543185 623 HLNPETITILFVKTR----ALVDALKnwiegnpklsflKPGILTGR--GKTNQNTGRG 674
Cdd:PRK13766  361 GKNPDSRIIVFTQYRdtaeKIVDLLE------------KEGIKAVRfvGQASKDGDKG 406
DEXDc smart00487
DEAD-like helicases superfamily;
235-410 3.11e-22

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 95.25  E-value: 3.11e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185  235 TNLYSPFKPRNYQLELALPAMKG-KNTIICAPTGCGKTFVSLLICEHHLKKfpqGQKGKVVFFANQIPVYEQQKSVFSKY 313
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKR---GKGGRVLVLVPTRELAEQWAEELKKL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185  314 FERHGYRVTGISGATAENVPVEQIVENN-DIIILTPQILVNNLKKGTIpSLSIFTLMIFDECHNTSKQHPYNMIMfnyld 392
Cdd:smart00487  78 GPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKL-SLSNVDLVILDEAHRLLDGGFGDQLE----- 151

                          170
                   ....*....|....*...
gi 1883543185  393 qKLGGSSGPLPQVIGLTA 410
Cdd:smart00487 152 -KLLKLLPKNVQLLLLSA 168
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
 609-671 3.16e-15

C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains 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: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 73.39  E-value: 3.16e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1883543185 609 PKLEDLCFILQEEYHLNPETITILFVKTRALVDALKNWIEGNPK-LSFLKPGILTGRGKTNQNT 671
Cdd:cd18802     7 PKLQKLIEILREYFPKTPDFRGIIFVERRATAVVLSRLLKEHPStLAFIRCGFLIGRGNSSQRK 70
ResIII pfam04851
Type III restriction enzyme, res subunit;
241-410 5.26e-15

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 73.48  E-value: 5.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 241 FKPRNYQLE-----LALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPqgqKGKVVFFANQIPVYEQQKSVFSKYFE 315
Cdd:pfam04851   2 LELRPYQIEaienlLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGP---IKKVLFLVPRKDLLEQALEEFKKFLP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 316 RHGYRVTGISGATAenvpvEQIVENNDIIILTPQILVNNLKKGTIPSLS-IFTLMIFDECHNTSKQHpYNMImFNYLDQk 394
Cdd:pfam04851  79 NYVEIGEIISGDKK-----DESVDDNKIVVTTIQSLYKALELASLELLPdFFDVIIIDEAHRSGASS-YRNI-LEYFKP- 150

                         170
                  ....*....|....*.
gi 1883543185 395 lggssgplPQVIGLTA 410
Cdd:pfam04851 151 --------AFLLGLTA 158
DEXH_lig_assoc TIGR04121
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ...
 241-272 8.29e-03

DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.


Pssm-ID: 274994 [Multi-domain]  Cd Length: 804  Bit Score: 39.84  E-value: 8.29e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1883543185 241 FKPRNYQLELALPAMKGKNTIICAPTGCGKTF 272
Cdd:TIGR04121  12 WTPRPFQLEMWAAALEGRSGLLIAPTGSGKTL 43
 
Name Accession Description Interval E-value
DEXHc_RIG-I_DDX58 cd18073
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ...
 241-442 3.43e-144

DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I is a member 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: 350831 [Multi-domain]  Cd Length: 202  Bit Score: 424.23  E-value: 3.43e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 241 FKPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKGKVVFFANQIPVYEQQKSVFSKYFERHGYR 320
Cdd:cd18073     1 FKPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKGKVVFFATKVPVYEQQKSVFSKYFERHGYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 321 VTGISGATAENVPVEQIVENNDIIILTPQILVNNLKKGTIPSLSIFTLMIFDECHNTSKQHPYNMIMFNYLDQKLGGSSG 400
Cdd:cd18073    81 VTGISGATAENVPVEQIIENNDIIILTPQILVNNLKKGTIPSLSIFTLMIFDECHNTSGNHPYNMIMFRYLDQKLGGSSG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1883543185 401 PLPQVIGLTASVGVGDAKNTDEALDYICKLCASLDASVIATV 442
Cdd:cd18073   161 PLPQIIGLTASVGVGDAKNTDEALDYICKLCASLDASVIATV 202
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
 241-442 3.58e-118

DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members 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: 350794 [Multi-domain]  Cd Length: 204  Bit Score: 357.17  E-value: 3.58e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 241 FKPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKKFP-QGQKGKVVFFANQIPVYEQQKSVFSKYFERhGY 319
Cdd:cd18036     1 LELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRsAGEKGRVVVLVNKVPLVEQQLEKFFKYFRK-GY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 320 RVTGISGATAENVPVEQIVENNDIIILTPQILVNNLKKGTI---PSLSIFTLMIFDECHNTSKQHPYNMIMFNYLDQKLg 396
Cdd:cd18036    80 KVTGLSGDSSHKVSFGQIVKASDVIICTPQILINNLLSGREeerVYLSDFSLLIFDECHHTQKEHPYNKIMRMYLDKKL- 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1883543185 397 GSSGPLPQVIGLTASVGVGDAKNTDEALDYICKLCASLDASVIATV 442
Cdd:cd18036   159 SSQGPLPQILGLTASPGVGGARSFEEALEHILKLCANLDASVIATV 204
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
 241-442 1.64e-115

DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family 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: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 349.81  E-value: 1.64e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 241 FKPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKGKVVFFANQIPVYEQQKSVFSKYFERHGYR 320
Cdd:cd17927     1 FKPRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKGKVVFLANKVPLVEQQKEVFRKHFERPGYK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 321 VTGISGATAENVPVEQIVENNDIIILTPQILVNNLKKGTIPSLSIFTLMIFDECHNTSKQHPYNMIMFNYLDQKLgGSSG 400
Cdd:cd17927    81 VTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGTIVSLSDFSLLVFDECHNTTKNHPYNEIMFRYLDQKL-GSSG 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1883543185 401 PLPQVIGLTASVGVGDAKNTDEALDYICKLCASLDASVIATV 442
Cdd:cd17927   160 PLPQILGLTASPGVGGAKNTEEALEHICKLCANLDISVIATV 201
DEXHc_RLR-2 cd18074
DEXH-box helicase domain of RLR-2; RIG-I-like receptor 2 (RLR-2, also known as melanoma ...
 244-442 9.01e-52

DEXH-box helicase domain of RLR-2; RIG-I-like receptor 2 (RLR-2, also known as melanoma differentiation-associated protein 5 or Mda5 and IFIH1) is a viral double-stranded RNA (dsRNA) receptor that shares sequence similarity and signaling pathways with RIG-I, yet plays essential functions in antiviral immunity through distinct specificity for viral RNA. RLR-2 recognizes the internal duplex structure, whereas RIG-I recognizes the terminus of dsRNA. RLR-2 uses direct protein-protein contacts to stack along dsRNA in a head-to-tail arrangement. The signaling domain (tandem CARD), which decorates the outside of the core RLR-2 filament, also has an intrinsic propensity to oligomerize into an elongated structure that activates the signaling adaptor, MAVS. RLR-2 uses long dsRNA as a signaling platform to cooperatively assemble the core filament, which in turn promotes stochastic assembly of the tandem CARD oligomers for signaling. LGP2 appears to positively and negatively regulate RLR-2 and RIG-I signaling, respectively. RLR-2 is a member 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: 350832 [Multi-domain]  Cd Length: 216  Bit Score: 180.44  E-value: 9.01e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 244 RNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHL-KKFPQGQKGKVVFFANQIPVYEQQKSVFSKYFERHGYRVT 322
Cdd:cd18074     4 RDYQMEVAKPALEGKNIIICLPTGSGKTRVAVYITKDHLdKKRKASEPGKVIVLVNKVPLVEQHYRKEFNPFLKHWYQVI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 323 GISGATAENVPVEQIVENNDIIILTPQILVNNLKKGTIPS-----LSIFTLMIFDECHNTSKQHPYNMIMFNYLDQKLGG 397
Cdd:cd18074    84 GLSGDSQLKISFPEVVKRYDVIICTAQILENSLLNATEEEdegvqLSDFSLIIIDECHHTQKEAVYNNIMRRYLKQKIKN 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1883543185 398 SSG--------PLPQVIGLTASVGVGDAKNTDEALDYICKLCASLDASVIATV 442
Cdd:cd18074   164 RKQkkenkpliPLPQILGLTASPGVGGAKNNKKAEEHILKICANLDAFRIMTV 216
RIG-I_C cd15805
C-terminal domain of Retinoic acid-inducible gene (RIG)-I protein, a cytoplasmic viral RNA ...
 748-861 1.40e-51

C-terminal domain of Retinoic acid-inducible gene (RIG)-I protein, a cytoplasmic viral RNA receptor; Retinoic acid-inducible gene (RIG)-I protein, also called DEAD box protein 58 (DDX58), is one of three members of the RIG-I-like Receptor (RLR) family. RLRs are cytoplasmic RNA receptors that recognize non-self RNA and act as molecular sensors to detect viral pathogens. RIG-I is activated by blunt-ended double-stranded RNA with or without a 5'-triphosphate (ppp), by single-stranded RNA marked by a 5'-ppp and by polyuridine sequences. It has been found to confer resistance to many negative-sense RNA viruses, including orthomyxoviruses, rhabdoviruses, bunyaviruses, and paramyxoviruses, as well as the positive-strand hepatitis C virus. RLRs are characterized by a central DExD/H-box helicase domain and a C-terminal domain, both of which are responsible for binding viral RNA. The helicase domain catalyzes the unwinding of double stranded RNA in an ATP-dependent manner. RIG-I and MDA5 also contain two N-terminal caspase activation and recruitment domains (CARDs), which initiate downstream signaling upon viral RNA sensing.


Pssm-ID: 276943  Cd Length: 112  Bit Score: 175.92  E-value: 1.40e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 748 NKKLLCRKCKALACYTADVRVIEECHYTVLGDAFKECFVSRPHPKPKQFSSFEKRAKIFCArqNCSHDWGIHVKYKTFEI 827
Cdd:cd15805     1 SYKLLCGKCKTFACNSDDIRVIKESHHVVIDPSFKERYTTKPHPKPKTFDGFEKKGKIFCK--KCGHDWGIMASYKIQNL 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1883543185 828 PVIKIESFVVEDIATGVQTLYSKWKDFHFEKIPF 861
Cdd:cd15805    79 PVLKIESFVVENPVTGQQLLFRKWKDVPFAIKEF 112
RIG-I_C-RD pfam11648
C-terminal domain of RIG-I; This family of proteins represents the regulatory domain RD of ...
 749-866 5.18e-51

C-terminal domain of RIG-I; This family of proteins represents the regulatory domain RD of RIG-I, a protein which initiates a signalling cascade that provides essential antiviral protection for the host. The RD domain binds viral RNA, activating the RIG-I ATPase by RNA-dependant dimerization. The structure of RD contains a zinc-binding domain and is thought to confer ligand specificity.


Pssm-ID: 463318  Cd Length: 117  Bit Score: 174.36  E-value: 5.18e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 749 KKLLCRKCKALACYTADVRVIEECHYTVLGDAFKECFVSR-PHPKPKQFSSFEKRAKIFCArqNCSHDWGIHVKYKTFEI 827
Cdd:pfam11648   1 VKLLCRKCKKFVCSGSDIRKIENSHHVVVNPDFKERYIVKePHKKPKSFEDWEPGGKISCK--KCGQDWGIMMKYKGVEL 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1883543185 828 PVIKIESFVVEDIATGVQTLYSKWKDFHFEKIPFDPAEM 866
Cdd:pfam11648  79 PVLKIKSFVVETPATGRRKTKKKWKDVPFEVPEFDYTEY 117
MDA5_ID cd12090
Insert domain of MDA5; MDA5 (melanoma-differentiation-associated gene 5, also known as IFIH1), ...
 469-604 3.49e-49

Insert domain of MDA5; MDA5 (melanoma-differentiation-associated gene 5, also known as IFIH1), as well as RIG-I (Retinoic acid Inducible Gene I, also known as DDX58) and LPG2 (also known as DHX58), contain two N-terminal CARD domains and a C-terminal SF2 helicase domain. They are cytoplasmic DEAD box RNA helicases acting as key innate immune pattern-recognition receptor (PRRs) that play an important role in host antiviral response by sensing incoming viral RNA. Their SF2 helicase domain is comprised of 3 structural domains, the 2 generally conserved helicase domains and a helical domain inserted between the two domains. The inserted domain is involved in conformational changes upon ligand binding.


Pssm-ID: 277189  Cd Length: 120  Bit Score: 169.42  E-value: 3.49e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 469 DKFKYIIAQLMRDTESLAKRICKDlenlsqIQNREFGTQKYEQWIVTVQKACMVFqmpdkdeesrICKALFLYTSHLRKY 548
Cdd:cd12090     1 DPFGDIIKKLMTDIEELLKMTPPD------IQPREFGTQKYEQWVVTLEKKAAKL----------GNRALRTCAEHLRKY 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1883543185 549 NDALIISEHARMKDALDYLKDFFSNVRAAGFDEIEQDLTQRFEEKLQELESVSRDP 604
Cdd:cd12090    65 NDALLINDTARMKDALQYLKEFYTNLKEAKFDETERFLTDLFEENLEELKKLARDP 120
DEXHc_RLR-3 cd18075
DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of ...
 244-441 8.27e-46

DEXH-box helicase domain of RLR-3; RIG-I-like receptor 3 (RLR-3, also known as laboratory of genetics and physiology 2 or LGP2 and DHX58) appears to positively and negatively regulate MDA5 and RIG-I signaling, respectively. RLR-3 resembles a chimera combining a MDA5-like helicase domain and RIG-I like CTD supporting both stem and end binding. RNA binding is required for RLR-3-mediated enhancement of MDA5 activation. RLR-3 end-binding may promote nucleation of MDA5 oligomerization on dsRNA. RLR-3 is a member 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: 350833 [Multi-domain]  Cd Length: 200  Bit Score: 163.10  E-value: 8.27e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 244 RNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKkfpQGQKGKVVFFANQIPVYEQQksvFSKYFERH--GYRV 321
Cdd:cd18075     4 HGYQWEVVAPALRGKNSIIWLPTGAGKTRAAVYVARRHLE---TKRGAKVAVLVNKVHLVDQH---LEKEFHVLldKYTV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 322 TGISGATAENVPVEQIVENNDIIILTPQILVNNLKKGTIPS---LSIFTLMIFDECHNTSKQHPYNMIMFNYLDQKLGGS 398
Cdd:cd18075    78 TAISGDSSHKCFFGQLARGSDVVICTAQILQNALLSGEEEAhveLTDFSLLVIDECHHTHKEAVYNKIMLSYLEKKLSRQ 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1883543185 399 sGPLPQVIGLTASVGVGDAKNTDEALDYICKLCASLDASVIAT 441
Cdd:cd18075   158 -GDLPQILGLTASPGTGGATSFDGAVEHILQICANLDTWVIMS 199
CARD_RIG-I_r2 cd08817
Caspase activation and recruitment domain found in RIG-I, second repeat; Caspase activation ...
 100-189 7.08e-43

Caspase activation and recruitment domain found in RIG-I, second repeat; Caspase activation and recruitment domain (CARD) found in RIG-I (Retinoic acid Inducible Gene I, also known as Ddx58), second repeat. RIG-I is a cytoplasmic RNA helicase that plays an important role in host antiviral response by sensing incoming viral RNA. RIG-I contains two N-terminal CARD domains and a C-terminal RNA helicase. Upon activation, the signal is transferred to downstream pathways via the adaptor molecule IPS-1 (MAVS, VISA, CARDIF), leading to the induction of type I interferons. Although very similar in sequence, RIG-I recognizes different sets of viruses compared to MDA5, a related RNA helicase. RIG-I associates with IPS-1 through a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260076  Cd Length: 91  Bit Score: 150.68  E-value: 7.08e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 100 LEEYRLLLKRLQPEFKTRIIPTDIISDLSECLINQECEEILQICSTKGMMAGAEKLVECLLRSDKENWPKTLKLALEKE- 178
Cdd:cd08817     1 LEEHRQLLKRIEPSFTKRIKPRDLIPYLSDCLIDRECEEILQIEEQKGMIAGAEKLVECLLRSDKENWPKTLKLALEKCg 80

                          90
                  ....*....|.
gi 1883543185 179 RNKFSELWIVE 189
Cdd:cd08817    81 YDAASELWPDE 91
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
 241-444 2.71e-42

DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member 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: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 152.81  E-value: 2.71e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 241 FKPRNYQLELALPAMKgKNTIICAPTGCGKTFVS-LLICEHHLKKFPQGQKGKVVFF-ANQIPVYEQQKSVFSKYFerhG 318
Cdd:cd18034     1 FTPRSYQLELFEAALK-RNTIVVLPTGSGKTLIAvMLIKEMGELNRKEKNPKKRAVFlVPTVPLVAQQAEAIRSHT---D 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 319 YRVTGISGATAENVPVEQI----VENNDIIILTPQILVNNLKKGTIpSLSIFTLMIFDECHNTSKQHPYNMIMFNYLDQK 394
Cdd:cd18034    77 LKVGEYSGEMGVDKWTKERwkeeLEKYDVLVMTAQILLDALRHGFL-SLSDINLLIFDECHHATGDHPYARIMKEFYHLE 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1883543185 395 lggSSGPLPQVIGLTASVgVGDAKNTDEALDYICKLCASLDaSVIATVKH 444
Cdd:cd18034   156 ---GRTSRPRILGLTASP-VNGKGDPKSVEKKIQQLEELLN-STIKTVSD 200
RIG-I_C pfam18119
RIG-I receptor C-terminal domain; This is the C-terminal domain of Innate Immune ...
 458-601 1.84e-41

RIG-I receptor C-terminal domain; This is the C-terminal domain of Innate Immune Pattern-Recognition Receptor RIG-I present in homo sapiens. RIG-I is a key cytosolic pattern-recognition receptors of the vertebrate innate immune system that form the first line of defense against RNA viral infection. RNA binding to RIG-I is mediated both by the C-terminal domain and by the helicase domain. The C-terminal domain specifically binds the 5'triphosphate end with a 10-fold higher affinity compared to 5'OH-dsRNA.


Pssm-ID: 465656  Cd Length: 139  Bit Score: 148.26  E-value: 1.84e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 458 KFFRKVESRISDKFKYIIAQLMRDTESLAKRIcKDLENLSQIQNREFGTQKYEQWIVTVQKACMVfqmpDKDEESRICka 537
Cdd:pfam18119   2 KFVVKVTSRKEDPFGDIIKDIMSKIEDHLNKS-YNLDDLSKLKPSDKGTQKYEQWIVTLQKKGAE----DPEEERRVC-- 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1883543185 538 LFLYTSHLRKYNDALIISEHARMKDALDYLKDFFSNVRAAGFDEIEQDLTQRFEEKLQELESVS 601
Cdd:pfam18119  75 RALCTEHLRKYNDALIINDDARTKDALEYLLKFLKELKETKFDETERKLYRLFEEKREELQRLA 138
CARD_RIG-I_r1 cd08816
Caspase activation and recruitment domain found in RIG-I, first repeat; Caspase activation and ...
 2-92 2.07e-39

Caspase activation and recruitment domain found in RIG-I, first repeat; Caspase activation and recruitment domain (CARD) found in RIG-I (Retinoic acid Inducible Gene I, also known as Ddx58), first repeat. RIG-I is a cytoplasmic RNA helicase that plays an important role in host antiviral response by sensing incoming viral RNA. RIG-I contains two N-terminal CARD domains and a C-terminal RNA helicase. Upon activation, the signal is transferred to downstream pathways via the adaptor molecule IPS-1 (MAVS, VISA, CARDIF), leading to the induction of type I interferons. Although very similar in sequence, RIG-I recognizes different sets of viruses compared to MDA5, a related RNA helicase. RIG-I associates with IPS-1 through a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260075  Cd Length: 90  Bit Score: 140.66  E-value: 2.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185   2 TTEQRRSLQAFQDYIRKTLDPTYILSYMAPWFREEEVQYIQAEKNnKGPMEAATLFLKFLLELQEEGWFRGFLDALDHAG 81
Cdd:cd08816     1 TALEKRNLRCYRDYIEKILRPSYVLGFMTTWLEDELVERILSEEE-KGVTEAAQLFLDAVLQLEEEGWFQGFLDALLAAG 79

                          90
                  ....*....|.
gi 1883543185  82 YSGLYEAIESW 92
Cdd:cd08816    80 YTGLCEAIENW 90
RLR_C cd15804
C-terminal domain of Retinoic acid-inducible gene (RIG)-I-like Receptors; Retinoic ...
 750-861 1.99e-36

C-terminal domain of Retinoic acid-inducible gene (RIG)-I-like Receptors; Retinoic acid-inducible gene (RIG)-I-like Receptors (RLRs) are cytoplasmic RNA receptors that recognize non-self RNA and act as molecular sensors to detect viral pathogens. They play crucial roles in innate antiviral responses, including the production of proinflammatory cytokines and type I interferon. There are three RLRs in vertebrates, RIG-I, LGP2, and MDA5. They are characterized by a central DExD/H-box helicase domain and a C-terminal domain, both of which are responsible for binding viral RNA. The helicase domain catalyzes the unwinding of double stranded RNA in an ATP-dependent manner. RIG-I and MDA5 also contain two N-terminal caspase activation and recruitment domains (CARDs), which initiate downstream signaling upon viral RNA sensing. They may detect partially overlapping viral substrates, including dengue virus, West Nile virus (WNV), reoviruses, and several paramyxoviruses (such as measles virus and Sendai virus). LGP2 lacks CARD and may play a regulatory role in RLR signaling. It may cooperate with either RIG-I or MDA5 to sense viral RNA.


Pssm-ID: 276942  Cd Length: 111  Bit Score: 132.82  E-value: 1.99e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 750 KLLCRKCKALACYTADVRVIEECHYTVLGDAFKECFVSRPHPKPKQFS-SFEKRAKIFCArqNCSHDWGIHVKYKTFEIP 828
Cdd:cd15804     2 TLLCKKCSAFACNSDDIRKIEGSHHVVIDPDFLERVKIEEDPKKKKKFeDTQILGKIKCK--KCGHDWGTMMKYKGVELP 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1883543185 829 VIKIESFVVEDIaTGVQTLYSKWKDFHFEKIPF 861
Cdd:cd15804    80 VLKIKNFVFVDE-DEERATKKKWKDVPFAIPEI 111
CARD_2 pfam16739
Caspase recruitment domain; In the probable ATP-dependent RNA helicase DDX58 this CARD domain ...
 1-93 2.05e-36

Caspase recruitment domain; In the probable ATP-dependent RNA helicase DDX58 this CARD domain is found near the N-terminus and interacts with the C-terminal domain.


Pssm-ID: 465251  Cd Length: 93  Bit Score: 132.33  E-value: 2.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185   1 MTTEQRRSLQAFQDYIRKTLDPTYILSYMAPWFREEEVQYIQAEKNNKGPMEAATLFLKFLLELQEEGWFRGFLDALDHA 80
Cdd:pfam16739   1 EDDEYRRLLRLFRPRLKDTIKPTEILPHLPECLTEDDKERIRAETNNKGNTAAAELLLDRLVRSDREGWFRAFLDALRKT 80

                          90
                  ....*....|...
gi 1883543185  81 GYSGLYEAIESWD 93
Cdd:pfam16739  81 GHDGLAEELEGEY 93
RLR_C_like cd15803
C-terminal domain of Retinoic acid-inducible gene (RIG)-I-like Receptors, Cereblon (CRBN), and ...
 751-835 1.71e-34

C-terminal domain of Retinoic acid-inducible gene (RIG)-I-like Receptors, Cereblon (CRBN), and similar protein domains; Retinoic acid-inducible gene (RIG)-I-like Receptors (RLRs) are cytoplasmic RNA receptors that recognize non-self RNA and act as molecular sensors to detect viral pathogens. They play crucial roles in innate antiviral responses, including the production of proinflammatory cytokines and type I interferon. There are three RLRs in vertebrates, RIG-I, LGP2, and MDA5. They are characterized by a central DExD/H-box helicase domain and a C-terminal domain, both of which are responsible for binding viral RNA. Cereblon is part of an E3 ubiquitin ligase complex, together with damaged DNA binding protein 1 (DDB1), CUL4A and ROC1. Cereblon interacts directly with DDB1, although the C-terminal domain characterized here does not contribute to that interaction. The C-terminal domain of Cereblon was shown to contain the binding site for thalidomide and its analogs, a class of teratogenic drugs that exhibit an antiproliferative effect on myelomas. Mutations in CRBN, some of which map onto the C-terminal domain, were associated with autosomal recessive mental retardation, which may have to do with interactions between CRBN and ion channels in the brain. RLRs and Cereblon contain a common conserved zinc binding site in their C-terminal domains.


Pssm-ID: 276941  Cd Length: 84  Bit Score: 126.48  E-value: 1.71e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 751 LLCRKCKALACYTADVRVIEECHYTVLGDAFKECFVSRPHPKPKQ-FSSFEKRAKIFCArqNCSHDWGIHVKYKTFEIPV 829
Cdd:cd15803     1 LLCKNCSALACTGEDIRVIELCHHVVYKPAFKNNYNVIGRPSTVHkWFDGYAWGIISCK--ICSSHWGWHFTYKPQKLPV 78


                  ....*.
gi 1883543185 830 IKIESF 835
Cdd:cd15803    79 LKRESF 84
CARD_2 pfam16739
Caspase recruitment domain; In the probable ATP-dependent RNA helicase DDX58 this CARD domain ...
 99-190 2.47e-28

Caspase recruitment domain; In the probable ATP-dependent RNA helicase DDX58 this CARD domain is found near the N-terminus and interacts with the C-terminal domain.


Pssm-ID: 465251  Cd Length: 93  Bit Score: 109.22  E-value: 2.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185  99 KLEEYRLLLKRLQPEFKTRIIPTDIISDLSECLINQECEEILQICSTKGMMAGAEKLVECLLRSDKENWPKTLKLALEK- 177
Cdd:pfam16739   1 EDDEYRRLLRLFRPRLKDTIKPTEILPHLPECLTEDDKERIRAETNNKGNTAAAELLLDRLVRSDREGWFRAFLDALRKt 80

                          90
                  ....*....|...
gi 1883543185 178 ERNKFSELWIVEK 190
Cdd:pfam16739  81 GHDGLAEELEGEY 93
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
243-672 1.92e-25

ERCC4-related helicase [Replication, recombination and repair];


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 112.90  E-value: 1.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 243 PRNYQLELALPAMKgKNTIICAPTGCGKTFVSLLICEHHLKKfpqgQKGKVVFFANQIPVYEQQKSVFSKYFERHGYRVT 322
Cdd:COG1111     4 RRLYQLNLAASALR-KNTLVVLPTGLGKTAVALLVIAERLHK----KGGKVLFLAPTKPLVEQHAEFFKEALNIPEDEIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 323 GISGataeNVPVEQ---IVENNDIIILTPQILVNNLKKGTIpSLSIFTLMIFDECHNTSKQHPYNMIMFNYLDQKlggss 399
Cdd:COG1111    79 VFTG----EVSPEKrkeLWEKARIIVATPQVIENDLIAGRI-DLDDVSLLIFDEAHRAVGNYAYVYIAERYHEDA----- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 400 gPLPQVIGLTASVGvgdakNTDEALDYICKlcaSLdasVIATVKHNLEELEQVV-YKPQKFFRKVESRISDKFKYIIAQL 478
Cdd:COG1111   149 -KDPLILGMTASPG-----SDEEKIEEVCE---NL---GIENVEVRTEEDPDVApYVHDTEVEWIRVELPEELKEIRDLL 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 479 mrdTESLAKRIcKDLENLSQIQNREFGTQKYE--QWIVTVQKacmvfQMPDKDEEsrickalflytshlrKYNDALIISE 556
Cdd:COG1111   217 ---NEVLDDRL-KKLKELGVIVSTSPDLSKKDllALQKKLQR-----RIREDDSE---------------GYRAISILAE 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 557 HARMKDALDY--------LKDFFSNVRAAGFDEIEQDLTQRF--EEKLQELESVSRDPSNENPKLEDLCFILQEEYHLNP 626
Cdd:COG1111   273 ALKLRHALELletqgveaLLRYLERLEEEARSSGGSKASKRLvsDPRFRKAMRLAEEADIEHPKLSKLREILKEQLGTNP 352

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1883543185 627 ETITILFVKTR----ALVDALKNwiEGnpklsfLKPGILTGRGKTNQNTG 672
Cdd:COG1111   353 DSRIIVFTQYRdtaeMIVEFLSE--PG------IKAGRFVGQASKEGDKG 394
PRK13766 PRK13766
Hef nuclease; Provisional
 243-674 9.14e-24

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 107.65  E-value: 9.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 243 PRNYQLELALPAMKgKNTIICAPTGCGKTFVSLLICEHHLKKFPqgqkGKVVFFANQIPVYEQQKSVFSKYFERHGYRVT 322
Cdd:PRK13766   16 ARLYQQLLAATALK-KNTLVVLPTGLGKTAIALLVIAERLHKKG----GKVLILAPTKPLVEQHAEFFRKFLNIPEEKIV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 323 GISGATAenvPVE--QIVENNDIIILTPQILVNNLKKGTIpSLSIFTLMIFDECHNTSKQHPYNMIMFNYLDQklggSSG 400
Cdd:PRK13766   91 VFTGEVS---PEKraELWEKAKVIVATPQVIENDLIAGRI-SLEDVSLLIFDEAHRAVGNYAYVYIAERYHED----AKN 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 401 PLpqVIGLTASVGVGDAKntdealdyicklcasldasvIATVKHNLeeleqvvykpqkFFRKVESRISD----------- 469
Cdd:PRK13766  163 PL--VLGLTASPGSDEEK--------------------IKEVCENL------------GIEHVEVRTEDdpdvkpyvhkv 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 470 KFKYIIAQL---MRDTESLAKRICKD----LENLSQIQNREFGTQKYEqwIVTVQKAcmVFQMPDKDEESriCKALFLYT 542
Cdd:PRK13766  209 KIEWVRVELpeeLKEIRDLLNEALKDrlkkLKELGVIVSISPDVSKKE--LLGLQKK--LQQEIANDDSE--GYEAISIL 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 543 SHLRKYNDALIISEHARMKDALDYLKDFFSNVRAAGFDEIEQDLTQrfEEKLQELESVSRDPSNENPKLEDLCFILQEEY 622
Cdd:PRK13766  283 AEAMKLRHAVELLETQGVEALRRYLERLREEARSSGGSKASKRLVE--DPRFRKAVRKAKELDIEHPKLEKLREIVKEQL 360

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1883543185 623 HLNPETITILFVKTR----ALVDALKnwiegnpklsflKPGILTGR--GKTNQNTGRG 674
Cdd:PRK13766  361 GKNPDSRIIVFTQYRdtaeKIVDLLE------------KEGIKAVRfvGQASKDGDKG 406
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 257-410 8.62e-23

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: 95.16  E-value: 8.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 257 GKNTIICAPTGCGKTFVSLLICEHHLKKfpqgQKGKVVFFANQIPVYEQQKSVFSKYFeRHGYRVTGISGATAENVPVEQ 336
Cdd:cd00046     1 GENVLITAPTGSGKTLAALLAALLLLLK----KGKKVLVLVPTKALALQTAERLRELF-GPGIRVAVLVGGSSAEEREKN 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1883543185 337 IVENNDIIILTPQILVNNLKKGTIPSLSIFTLMIFDECHNTSKQHPYnMIMFNYLDQKLGgssGPLPQVIGLTA 410
Cdd:cd00046    76 KLGDADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLIDSRG-ALILDLAVRKAG---LKNAQVILLSA 145
DEXDc smart00487
DEAD-like helicases superfamily;
235-410 3.11e-22

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 95.25  E-value: 3.11e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185  235 TNLYSPFKPRNYQLELALPAMKG-KNTIICAPTGCGKTFVSLLICEHHLKKfpqGQKGKVVFFANQIPVYEQQKSVFSKY 313
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKR---GKGGRVLVLVPTRELAEQWAEELKKL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185  314 FERHGYRVTGISGATAENVPVEQIVENN-DIIILTPQILVNNLKKGTIpSLSIFTLMIFDECHNTSKQHPYNMIMfnyld 392
Cdd:smart00487  78 GPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKL-SLSNVDLVILDEAHRLLDGGFGDQLE----- 151

                          170
                   ....*....|....*...
gi 1883543185  393 qKLGGSSGPLPQVIGLTA 410
Cdd:smart00487 152 -KLLKLLPKNVQLLLLSA 168
helicase_insert_domain cd12088
helicase_insert_domain; helicase_insert_domain; This helical domain can be found inserted in a ...
 537-604 1.37e-21

helicase_insert_domain; helicase_insert_domain; This helical domain can be found inserted in a subset of SF2-type DEAD-box related helicases, like archaeal Hef helicase, MDA5-like helicases and FancM-like helicases. The exact function of this domain is unknown, but seems to play a role in interaction with nucleotides and/or the stabilization of the nucleotide complex.


Pssm-ID: 277187  Cd Length: 82  Bit Score: 89.45  E-value: 1.37e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1883543185 537 ALFLYTSHLRKYNDALIISEHARMKDALDYLKDFFSNVRAAGFDEIEQDLTQRFEEKLQELESVSRDP 604
Cdd:cd12088    15 LKLLYTAHLRKLNDALELLEDAGIWDALKYIKMFFTEVREGIFDELERKLTLRFDEKLQKLIALSRDP 82
CARD_IPS-1_RIG-I cd08789
Caspase activation and recruitment domains (CARDs) found in IPS-1 and RIG-I-like RNA helicases; ...
 2-92 1.12e-19

Caspase activation and recruitment domains (CARDs) found in IPS-1 and RIG-I-like RNA helicases; Caspase activation and recruitment domains (CARDs) found in IPS-1 (Interferon beta promoter stimulator protein 1) and Retinoic acid Inducible Gene I (RIG-I)-like DEAD box helicases. RIG-I-like helicases and IPS-1 play important roles in the induction of interferons in response to viral infection. They are crucial in triggering innate immunity and in developing adaptive immunity against viral pathogens. RIG-I-like helicases, including MDA5 and RIG-I, contain two N-terminal CARD domains and a C-terminal DEAD box RNA helicase domain. They are cytoplasmic RNA helicases that play an important role in host antiviral response by sensing incoming viral RNA. Upon activation, the signal is transferred to downstream pathways via the adaptor molecule IPS-1 (MAVS, VISA, CARDIF), leading to the induction of type I interferons. MDA5 and RIG-I associate with IPS-1 through a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260057  Cd Length: 91  Bit Score: 84.43  E-value: 1.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185   2 TTEQRRSLQAFQDYIRKTLDPTYILSYMAPWFREEEVQYIQAEKNNKGPMEAATLFLKFLLELQEEGWFRGFLDALDHAG 81
Cdd:cd08789     1 TDDEKQLLQCYRATVERSLDVVYVLPYLTDCLPDEDRERIRAAEENRGNSGAAALLLNTLLQLEKEGWFRGFLDALRATG 80

                          90
                  ....*....|.
gi 1883543185  82 YSGLYEAIESW 92
Cdd:cd08789    81 YTGARELIDNW 91
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
 242-413 1.93e-19

DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member 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: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 86.80  E-value: 1.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 242 KPRNYQLELALPAMKGkNTIICAPTGCGKTFVSLLICEHHLKKfpqgQKGKVVFFANQIPVYEQQKSVFSKYFERHGyRV 321
Cdd:cd18035     2 ERRLYQVLIAAVALNG-NTLIVLPTGLGKTIIAILVAADRLTK----KGGKVLILAPSRPLVEQHAENLKRVLNIPD-KI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 322 TGISGATAENvPVEQIVENNDIIILTPQILVNNLKKGTIpSLSIFTLMIFDECHNTSKQHPYNMIMFNYLDQklggSSGP 401
Cdd:cd18035    76 TSLTGEVKPE-ERAERWDASKIIVATPQVIENDLLAGRI-TLDDVSLLIFDEAHHAVGNYAYVYIAHRYKRE----ANNP 149

                         170
                  ....*....|..
gi 1883543185 402 LpqVIGLTASVG 413
Cdd:cd18035   150 L--ILGLTASPG 159
DEXDc_FANCM cd18033
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ...
 244-439 4.51e-19

DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM is a member 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: 350791 [Multi-domain]  Cd Length: 182  Bit Score: 85.84  E-value: 4.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 244 RNYQLELALPAMKgKNTIICAPTGCGKTFVSLLICEHHLKKFPqgqKGKVVFFANQIPVYEQQKSVFskyferhgYRVTG 323
Cdd:cd18033     4 RDYQFTIVQKALF-QNTLVALPTGLGKTFIAAVVMLNYYRWFP---KGKIVFMAPTKPLVSQQIEAC--------YKITG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 324 I-SGATAE---NVPVE---QIVENNDIIILTPQILVNNLKKGTIPSLSIfTLMIFDECHNTSKQHPYNMIMfnyldQKLG 396
Cdd:cd18033    72 IpSSQTAEltgSVPPTkraELWASKRVFFLTPQTLENDLKEGDCDPKSI-VCLVIDEAHRATGNYAYCQVV-----RELM 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1883543185 397 GSSGPLpQVIGLTASVGVGdakntdeaLDYICKLCASLDASVI 439
Cdd:cd18033   146 RYNSHF-RILALTATPGSK--------LEAVQQVIDNLLISHI 179
CARD_IPS-1_RIG-I cd08789
Caspase activation and recruitment domains (CARDs) found in IPS-1 and RIG-I-like RNA helicases; ...
 100-186 3.33e-17

Caspase activation and recruitment domains (CARDs) found in IPS-1 and RIG-I-like RNA helicases; Caspase activation and recruitment domains (CARDs) found in IPS-1 (Interferon beta promoter stimulator protein 1) and Retinoic acid Inducible Gene I (RIG-I)-like DEAD box helicases. RIG-I-like helicases and IPS-1 play important roles in the induction of interferons in response to viral infection. They are crucial in triggering innate immunity and in developing adaptive immunity against viral pathogens. RIG-I-like helicases, including MDA5 and RIG-I, contain two N-terminal CARD domains and a C-terminal DEAD box RNA helicase domain. They are cytoplasmic RNA helicases that play an important role in host antiviral response by sensing incoming viral RNA. Upon activation, the signal is transferred to downstream pathways via the adaptor molecule IPS-1 (MAVS, VISA, CARDIF), leading to the induction of type I interferons. MDA5 and RIG-I associate with IPS-1 through a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260057  Cd Length: 91  Bit Score: 77.50  E-value: 3.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 100 LEEYRLLLKRLQPEFKTRIIPTDIISDLSECLINQECEEILQICSTKGMMAGAEKLVECLLRSDKENWPKTLKLAL-EKE 178
Cdd:cd08789     1 TDDEKQLLQCYRATVERSLDVVYVLPYLTDCLPDEDRERIRAAEENRGNSGAAALLLNTLLQLEKEGWFRGFLDALrATG 80


                  ....*...
gi 1883543185 179 RNKFSELW 186
Cdd:cd08789    81 YTGARELI 88
LGP2_C cd15806
C-terminal domain of Laboratory of Genetics and Physiology 2 (LGP2), a cytoplasmic viral RNA ...
 750-862 5.71e-16

C-terminal domain of Laboratory of Genetics and Physiology 2 (LGP2), a cytoplasmic viral RNA receptor; Laboratory of Genetics and Physiology 2 (LGP2) is one of three members of the RIG-I-like Receptor (RLR) family. RLRs are cytoplasmic RNA receptors that recognize non-self RNA and act as molecular sensors to detect viral pathogens. They are characterized by a central DExD/H-box helicase domain and a C-terminal domain, both of which are responsible for binding viral RNA. LGP2 lacks the caspase activation and recruitment domains (CARDs) that are present in other RLRs, which initiate downstream signaling upon viral RNA sensing. LGP2 may play a regulatory role in RLR signaling, and may cooperate with either RIG-I or MDA5 to sense viral RNA.


Pssm-ID: 276944  Cd Length: 112  Bit Score: 74.38  E-value: 5.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 750 KLLCRKCKALACYTADVRVIEECHYTVLGDAFKECF-VSRPHPKPKQFSSFEKRAKIFCArqNCSHDWGIHVKYKTFEIP 828
Cdd:cd15806     2 QLLCRNCFVAVAHGSDLRKVEGTHHVNINPNFSRYYkVGGKPILIRTFEDWEPGGTISCS--NCGQVWGMEMIYKSVLLP 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1883543185 829 VIKIESFVVEDIATGVQtlYSKWKDFHFEKIPFD 862
Cdd:cd15806    80 VLSIKNFVLETPEGRRQ--AKKWKDVPFSVEEFD 111
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 245-376 1.10e-15

DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 75.76  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 245 NYQLELALPAM-KGKNTIICAPTGCGKTFVSLLICEHHLKKfpqgQKGKVVFFANQIPVYEQQKSVFSKYFERHGYRVTG 323
Cdd:cd17921     4 PIQREALRALYlSGDSVLVSAPTSSGKTLIAELAILRALAT----SGGKAVYIAPTRALVNQKEADLRERFGPLGKNVGL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1883543185 324 ISGATAENvpvEQIVENNDIIILTPQILVNNLKKGTIPSLSIFTLMIFDECHN 376
Cdd:cd17921    80 LTGDPSVN---KLLLAEADILVATPEKLDLLLRNGGERLIQDVRLVVVDEAHL 129
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
 609-671 3.16e-15

C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains 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: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 73.39  E-value: 3.16e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1883543185 609 PKLEDLCFILQEEYHLNPETITILFVKTRALVDALKNWIEGNPK-LSFLKPGILTGRGKTNQNT 671
Cdd:cd18802     7 PKLQKLIEILREYFPKTPDFRGIIFVERRATAVVLSRLLKEHPStLAFIRCGFLIGRGNSSQRK 70
ResIII pfam04851
Type III restriction enzyme, res subunit;
241-410 5.26e-15

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 73.48  E-value: 5.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 241 FKPRNYQLE-----LALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPqgqKGKVVFFANQIPVYEQQKSVFSKYFE 315
Cdd:pfam04851   2 LELRPYQIEaienlLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGP---IKKVLFLVPRKDLLEQALEEFKKFLP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 316 RHGYRVTGISGATAenvpvEQIVENNDIIILTPQILVNNLKKGTIPSLS-IFTLMIFDECHNTSKQHpYNMImFNYLDQk 394
Cdd:pfam04851  79 NYVEIGEIISGDKK-----DESVDDNKIVVTTIQSLYKALELASLELLPdFFDVIIIDEAHRSGASS-YRNI-LEYFKP- 150

                         170
                  ....*....|....*.
gi 1883543185 395 lggssgplPQVIGLTA 410
Cdd:pfam04851 151 --------AFLLGLTA 158
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 246-375 1.13e-14

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: 72.66  E-value: 1.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 246 YQLELALPAMKGKNTIICAPTGCGKTFVSLL-ICEHHLKKFPqgqKGKVVFFANQIPVYEQQKSVFSKYFERHGYRVTGI 324
Cdd:pfam00270   3 IQAEAIPAILEGRDVLVQAPTGSGKTLAFLLpALEALDKLDN---GPQALVLAPTRELAEQIYEELKKLGKGLGLKVASL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1883543185 325 SGATAENvPVEQIVENNDIIILTPQILVNNLKKgtIPSLSIFTLMIFDECH 375
Cdd:pfam00270  80 LGGDSRK-EQLEKLKGPDILVGTPGRLLDLLQE--RKLLKNLKLLVLDEAH 127
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
247-503 1.27e-14

Replicative superfamily II helicase [Replication, recombination and repair];


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 77.63  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 247 QLElALPA--MKGKNTIICAPTGCGKTFV-SLLICEHHLKkfpqgqKGKVVF------FANQipVYEQqksvFSKYFERH 317
Cdd:COG1204    27 QAE-ALEAglLEGKNLVVSAPTASGKTLIaELAILKALLN------GGKALYivplraLASE--KYRE----FKRDFEEL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 318 GYRVTGISGataENVPVEQIVENNDIIILTPQILVNNLKKGTIPsLSIFTLMIFDECHntskqhpynmimfnYLDQklgG 397
Cdd:COG1204    94 GIKVGVSTG---DYDSDDEWLGRYDILVATPEKLDSLLRNGPSW-LRDVDLVVVDEAH--------------LIDD---E 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 398 SSGPL--------------PQVIGLTASVGvgdakNTDEALDYicklcasLDASVIAT----VkhnleELEQVVYKPQKF 459
Cdd:COG1204   153 SRGPTlevllarlrrlnpeAQIVALSATIG-----NAEEIAEW-------LDAELVKSdwrpV-----PLNEGVLYDGVL 215

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1883543185 460 -FRKVESRISDKFKYIIAQLM-------------RDTESLAKRICKDLENLSQIQNRE 503
Cdd:COG1204   216 rFDDGSRRSKDPTLALALDLLeeggqvlvfvssrRDAESLAKKLADELKRRLTPEERE 273
MDA5_C cd15807
C-terminal domain of Melanoma differentiation-associated protein 5, a cytoplasmic viral RNA ...
 751-853 4.87e-13

C-terminal domain of Melanoma differentiation-associated protein 5, a cytoplasmic viral RNA receptor; Melanoma differentiation-associated protein 5 (MDA5) is also called Interferon-induced helicase C domain-containing protein 1 (IFIH1) or RIG-I-like receptor 2 (RLR-2). It is one of three members of the RLR family. RLRs are cytoplasmic RNA receptors that recognize non-self RNA and act as molecular sensors to detect viral pathogens. It has been shown to detect viruses from the Picornaviridae and Caliciviridae families. RLRs are characterized by a central DExD/H-box helicase domain and a C-terminal domain, both of which are responsible for binding viral RNA. The helicase domain catalyzes the unwinding of double stranded RNA in an ATP-dependent manner. RIG-I and MDA5 also contain two N-terminal caspase activation and recruitment domains (CARDs), which initiate downstream signaling upon viral RNA sensing.


Pssm-ID: 276945  Cd Length: 117  Bit Score: 66.36  E-value: 4.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 751 LLCRKCKALACYTADVRVIEECHYTVLGDAFKECFVSRPHPK-PKQFSSFEKRAKIFCarQNCSHDWGIHVKYKTFEIPV 829
Cdd:cd15807     6 FLCKNCSVLVCSGEDIQVIEKMHHVNVTPEFKELYIKRENKAlQEKLADYQTNGEIIC--KTCGQAWGTMMVHKGLELPC 83

                          90       100
                  ....*....|....*....|....
gi 1883543185 830 IKIESFVVEDIATGVQTLYSKWKD 853
Cdd:cd15807    84 LKIRNFVVTFKNNSTKKTYKKWVE 107
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 243-378 6.63e-13

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are 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: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 66.95  E-value: 6.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 243 PRNYQLElALPAMKGKNT----IICAPTGCGKTFVSL-LICEHHlkkfpqgqKGKVVFFANQIPVYEQQKSVFSKYFERH 317
Cdd:cd17926     1 LRPYQEE-ALEAWLAHKNnrrgILVLPTGSGKTLTALaLIAYLK--------ELRTLIVVPTDALLDQWKERFEDFLGDS 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1883543185 318 G-YRVTGISgataenvpvEQIVENNDIIILTPQILVNNLKKGTIPSLSiFTLMIFDECHNTS 378
Cdd:cd17926    72 SiGLIGGGK---------KKDFDDANVVVATYQSLSNLAEEEKDLFDQ-FGLLIVDEAHHLP 123
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
234-378 1.70e-11

Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 67.74  E-value: 1.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 234 DTNLYSPFKPRNYQLE-----LALPAMKGKNTIICAPTGCGKTFVSLLICEHHLkkfpqgQKGKVVFFANQIPVYEQQKS 308
Cdd:COG1061    72 DEASGTSFELRPYQQEalealLAALERGGGRGLVVAPTGTGKTVLALALAAELL------RGKRVLVLVPRRELLEQWAE 145

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 309 VFSKYFerhgyRVTGISGATAEnvpveqivENNDIIILTPQILVNNLKKGTIPSLsiFTLMIFDECHNTS 378
Cdd:COG1061   146 ELRRFL-----GDPLAGGGKKD--------SDAPITVATYQSLARRAHLDELGDR--FGLVIIDEAHHAG 200
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
 243-420 7.06e-09

DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members 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: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 55.65  E-value: 7.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 243 PRNYQLElALPAM-----KGKNTI-ICAPTGCGKTFVSLLICEHHLKkfpQGQKGKVVFFANQIPVYEQQKSVFSKYFer 316
Cdd:cd18032     1 PRYYQQE-AIEALeeareKGQRRAlLVMATGTGKTYTAAFLIKRLLE---ANRKKRILFLAHREELLEQAERSFKEVL-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 317 HGYRVTGISGATAEnvpveqiVENNDIIILTPQILVNNlKKGTIPSLSIFTLMIFDECH-NTSKQhpYNMImFNYLDQKL 395
Cdd:cd18032    75 PDGSFGNLKGGKKK-------PDDARVVFATVQTLNKR-KRLEKFPPDYFDLIIIDEAHhAIASS--YRKI-LEYFEPAF 143

                         170       180
                  ....*....|....*....|....*
gi 1883543185 396 ggssgplpqVIGLTASVGVGDAKNT 420
Cdd:cd18032   144 ---------LLGLTATPERTDGLDT 159
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
 251-373 5.38e-08

DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350715 [Multi-domain]  Cd Length: 198  Bit Score: 53.75  E-value: 5.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 251 ALPAM-KGKNTIICAPTGCGKTFVSLLICEHHLKKfPQGQKG--KVVF-----FANQIpvYEQqksvFSKYFERHGYRVT 322
Cdd:cd17957    20 AIPILlHGRDLLACAPTGSGKTLAFLIPILQKLGK-PRKKKGlrALILaptreLASQI--YRE----LLKLSKGTGLRIV 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1883543185 323 GISGATAENVP-VEQIVENNDIIILTPQILVNNLKKGTIpSLSIFTLMIFDE 373
Cdd:cd17957    93 LLSKSLEAKAKdGPKSITKYDILVSTPLRLVFLLKQGPI-DLSSVEYLVLDE 143
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
 249-374 5.63e-07

DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350669 [Multi-domain]  Cd Length: 196  Bit Score: 50.90  E-value: 5.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 249 ELALP-AMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKGKVVFF--------ANQIpvyeqqKSVFSKYFERHGY 319
Cdd:cd00268    18 AQAIPlILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRGPQALvlaptrelAMQI------AEVARKLGKGTGL 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1883543185 320 RVTGISGATAENVPVEQIVENNDIIILTPQILVNNLKKGTIpSLSIFTLMIFDEC 374
Cdd:cd00268    92 KVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKL-DLSNVKYLVLDEA 145
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
 245-349 1.15e-05

DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 47.35  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 245 NYQLELALPAM--KGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKG--KVVFFAnqiP----VYEQQKSVFSKyFER 316
Cdd:cd18023     3 NRIQSEVFPDLlySDKNFVVSAPTGSGKTVLFELAILRLLKERNPLPWGnrKVVYIA---PikalCSEKYDDWKEK-FGP 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1883543185 317 HGYRVTGISGATaENVPVEQIvENNDIIILTPQ 349
Cdd:cd18023    79 LGLSCAELTGDT-EMDDTFEI-QDADIILTTPE 109
CARD_IPS1 cd08811
Caspase activation and recruitment domain (CARD) found in IPS-1; Caspase activation and ...
 101-177 1.19e-05

Caspase activation and recruitment domain (CARD) found in IPS-1; Caspase activation and recruitment domain (CARD) found in IPS-1 (Interferon beta promoter stimulator protein 1), also known as CARDIF, VISA or MAVS. IPS-1 is an adaptor protein that plays an important role in interferon induction in response to viral infection. It is crucial in triggering innate immunity and in developing adaptive immunity against viral pathogens. The CARD of IPS-1 associates with the CARDs of two RNA helicases, RIG-I and MDA5, which bind viral DNA in the cytoplasm during the initial stage of intracellular antiviral response, leading to the induction of type I interferons. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260073  Cd Length: 92  Bit Score: 44.66  E-value: 1.19e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1883543185 101 EEYRLLLKRLQPEFKTRIIPTDIISDLSeCLINQECEEILQICSTKGMMAGAEKLVECLLRsdKENWPKTLKLALEK 177
Cdd:cd08811     4 DKEYKYLRRNMGVFCHDIKVSEIIPYLP-CLTRSDRDEILAKKDMSGNRDTAWTLLDHLQR--RPGWVEDFIKALRN 77
DEXHc_Brr2_2 cd18021
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ...
 259-406 3.39e-05

C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350779 [Multi-domain]  Cd Length: 191  Bit Score: 45.71  E-value: 3.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 259 NTIICAPTGCGKTFVSLLICEHHLKkfpQGQKGKVVFFAnqiPVYEQQKSVF----SKYFERHGYRVTGISGATAENVpv 334
Cdd:cd18021    21 NVFVGAPTGSGKTVCAELALLRHWR---QNPKGRAVYIA---PMQELVDARYkdwrAKFGPLLGKKVVKLTGETSTDL-- 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1883543185 335 eQIVENNDIIILTPQ---ILVNNLK-KGTIPSLSiftLMIFDECHntskqhpynMImfnyldqklGGSSGPLPQVI 406
Cdd:cd18021    93 -KLLAKSDVILATPEqwdVLSRRWKqRKNVQSVE---LFIADELH---------LI---------GGENGPVYEVV 146
DEXHc_ASCC3_2 cd18022
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
 258-406 6.62e-05

C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350780 [Multi-domain]  Cd Length: 189  Bit Score: 44.67  E-value: 6.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 258 KNTIICAPTGCGKTFVSLLICEHHLKKFPqgqKGKVVFFAnqiP----VYEQQKSVFSKYFERHGYRVTGISGataENVP 333
Cdd:cd18022    18 NNVLLGAPTGSGKTIAAELAMFRAFNKYP---GSKVVYIA---PlkalVRERVDDWKKRFEEKLGKKVVELTG---DVTP 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1883543185 334 VEQIVENNDIIILTPQ----ILVNNLKKGTIPSLSiftLMIFDECHntskqhpynmimfnyldqKLGGSSGPLPQVI 406
Cdd:cd18022    89 DMKALADADIIITTPEkwdgISRSWQTREYVQQVS---LIIIDEIH------------------LLGSDRGPVLEVI 144
DEXHc_Brr2_1 cd18019
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ...
 259-375 8.49e-05

N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350777 [Multi-domain]  Cd Length: 214  Bit Score: 44.67  E-value: 8.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 259 NTIICAPTGCGKTFVSLLICEHHLKKF--PQG----QKGKVVFFANQIPVYEQQKSVFSKYFERHGYRVTGISGatAENV 332
Cdd:cd18019    35 NLLLCAPTGAGKTNVALLTILREIGKHrnPDGtinlDAFKIVYIAPMKALVQEMVGNFSKRLAPYGITVAELTG--DQQL 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1883543185 333 PVEQIVENNdIIILTPQIL-VNNLKKGTIPSLSIFTLMIFDECH 375
Cdd:cd18019   113 TKEQISETQ-IIVTTPEKWdIITRKSGDRTYTQLVRLIIIDEIH 155
DEXHc_POLQ-like cd18026
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ...
 245-422 9.65e-05

DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.


Pssm-ID: 350784 [Multi-domain]  Cd Length: 202  Bit Score: 44.51  E-value: 9.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 245 NYQLE-LALPAMK-GKNTIICAPTGCGKTFVS-LLIcehhLKKFPQGQKgKVVFFANQIPVYEQQKSVFSKYFERHGYRV 321
Cdd:cd18026    19 DWQKEcLSLPGLLeGRNLVYSLPTSGGKTLVAeILM----LKRLLERRK-KALFVLPYVSIVQEKVDALSPLFEELGFRV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 322 TGISGATAENVPVEqiVENNDIIILTP---QILVNNL-KKGTIPSLSiftLMIFDECHntskqhpynMIMFNY----LDQ 393
Cdd:cd18026    94 EGYAGNKGRSPPKR--RKSLSVAVCTIekaNSLVNSLiEEGRLDELG---LVVVDELH---------MLGDGHrgalLEL 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1883543185 394 ---KLGGSSGPLPQVIGLTASVGvgdakNTDE 422
Cdd:cd18026   160 lltKLLYAAQKNIQIVGMSATLP-----NLEE 186
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
 256-441 2.16e-04

DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 43.09  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 256 KGKNTIICAPTGCGKTFVSLLICEHHLkkfpqgQKGKVVFFANQIPVYEQQKSVFSKYFERHGYRVtGISgaTAENVPVE 335
Cdd:cd18028    16 KGENLLISIPTASGKTLIAEMAMVNTL------LEGGKALYLVPLRALASEKYEEFKKLEEIGLKV-GIS--TGDYDEDD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 336 QIVENNDIIILTPQILvNNLKKGTIPSLSIFTLMIFDECHNTSkqhpynmimfnylDQKLGG----------SSGPLPQV 405
Cdd:cd18028    87 EWLGDYDIIVATYEKF-DSLLRHSPSWLRDVGVVVVDEIHLIS-------------DEERGPtlesivarlrRLNPNTQI 152

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1883543185 406 IGLTASVGvgdakNTDEaldyickLCASLDASVIAT 441
Cdd:cd18028   153 IGLSATIG-----NPDE-------LAEWLNAELVES 176
PRK00254 PRK00254
ski2-like helicase; Provisional
 254-413 3.00e-04

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 44.42  E-value: 3.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 254 AMKGKNTIICAPTGCGKTFVSLLICEHHLKKfpqgQKGKVVFFANQIPVYEQQKSVFsKYFERHGYRVtgiSGATAENVP 333
Cdd:PRK00254   36 VLEGKNLVLAIPTASGKTLVAEIVMVNKLLR----EGGKAVYLVPLKALAEEKYREF-KDWEKLGLRV---AMTTGDYDS 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 334 VEQIVENNDIIILTPQILVNNLKKGTiPSLSIFTLMIFDECH---NTSKQHPYNMIMFNYLDQKlggssgplpQVIGLTA 410
Cdd:PRK00254  108 TDEWLGKYDIIIATAEKFDSLLRHGS-SWIKDVKLVVADEIHligSYDRGATLEMILTHMLGRA---------QILGLSA 177


                  ...
gi 1883543185 411 SVG 413
Cdd:PRK00254  178 TVG 180
DEXHc_DDX60 cd18025
DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an ...
 242-375 4.04e-04

DEXH-box helicase domain of DEAD box protein 60; DEAD box protein 60 (DDX60) is an IFN-inducible cytoplasmic helicase that plays a role in RIG-I-mediated type I interferon (IFN) nuclease-mediated viral RNA degradation. DDX60 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350783 [Multi-domain]  Cd Length: 192  Bit Score: 42.36  E-value: 4.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 242 KPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKkfpQGQKGKVVFFA------NQIpVYEQQKSVFSKYFE 315
Cdd:cd18025     1 NPDAWQRELLDIVDRRESALIVAPTSSGKTFISYYCMEKVLR---ESDDGVVVYVAptkalvNQV-VAEVYARFSKKYPP 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1883543185 316 RHGYRVTGISGATAENVPveqivENNDIIILTPQILVNNLkkgTIPSLSIFT----LMIFDECH 375
Cdd:cd18025    77 SGKSLWGVFTRDYRHNNP-----MNCQVLITVPECLEILL---LSPHNASWVprikYVIFDEIH 132
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
 243-411 5.16e-04

DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350696 [Multi-domain]  Cd Length: 204  Bit Score: 42.31  E-value: 5.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 243 PRNYQLElALP-AMKGKNTIICAPTGCGKTF---------VSLLICEhhlkkfPQGQkgkvvfFANQipVYEQQKSvFSK 312
Cdd:cd17938    22 PTDIQAE-AIPlILGGGDVLMAAETGSGKTGafclpvlqiVVALILE------PSRE------LAEQ--TYNCIEN-FKK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 313 YFERHGYRVTGISGATAENVPVEQIVENNDIIILTPQILVNNLKKGTIpSLSIFTLMIFDECHNTSKQHPYNMIMFNYLD 392
Cdd:cd17938    86 YLDNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKL-DLSSVRFFVLDEADRLLSQGNLETINRIYNR 164

                         170
                  ....*....|....*....
gi 1883543185 393 QKLGGSSGPLPQVIGLTAS 411
Cdd:cd17938   165 IPKITSDGKRLQVIVCSAT 183
CARD_MDA5_r2 cd08819
Caspase activation and recruitment domain found in MDA5, second repeat; Caspase activation and ...
 33-87 7.11e-04

Caspase activation and recruitment domain found in MDA5, second repeat; Caspase activation and recruitment domain (CARD) found in MDA5 (melanoma-differentiation-associated gene 5), second repeat. MDA5, also known as IFIH1, contains two N-terminal CARD domains and a C-terminal RNA helicase domain. MDA5 is a cytoplasmic DEAD box RNA helicase that plays an important role in host antiviral response by sensing incoming viral RNA. Upon activation, the signal is transferred to downstream pathways via the adaptor molecule IPS-1 (MAVS, VISA, CARDIF), leading to the induction of type I interferons. Although very similar in sequence, MDA5 recognizes different sets of viruses compared to RIG-I, a related RNA helicase. MDA5 associates with IPS-1 through a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260078  Cd Length: 92  Bit Score: 39.62  E-value: 7.11e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1883543185  33 FREEEVQYIQAEKNNKGPMEAATLFLKFLLElQEEGWFRGFLDALDHAGYSGLYE 87
Cdd:cd08819    33 LTAEDRERILAATENHGNRSGARELLSRIVR-QKEGWFSKFLQALRETEHNNLAE 86
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
 242-373 8.76e-04

DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 41.97  E-value: 8.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 242 KPRNYQLeLALPA-MKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKGK-----VVFFANQIPVYEQQKSVFSKYFE 315
Cdd:cd17948    12 KPTTVQK-QGIPSiLRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPfnaprGLVITPSRELAEQIGSVAQSLTE 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1883543185 316 RHGYRVTGISGATAENVPVEQIVENNDIIILTPQILVNNLKKGtIPSLSIFTLMIFDE 373
Cdd:cd17948    91 GLGLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSR-IYSLEQLRHLVLDE 147
uvsW PHA02558
UvsW helicase; Provisional
 232-396 2.90e-03

UvsW helicase; Provisional


Pssm-ID: 222875 [Multi-domain]  Cd Length: 501  Bit Score: 41.15  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 232 VSDTNLYS---PFKPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKKFpqgqKGKVVFFANQIPVYEQQKS 308
Cdd:PHA02558  101 VSSLEIYSgnkKIEPHWYQYDAVYEGLKNNRRLLNLPTSAGKSLIQYLLSRYYLENY----EGKVLIIVPTTSLVTQMID 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 309 VFSKY--FERHGyrVTGISGATAENVpveqiveNNDIIILTPQILVNNLKKgtipSLSIFTLMIFDECH-NTSKQHPYNM 385
Cdd:PHA02558  177 DFVDYrlFPREA--MHKIYSGTAKDT-------DAPIVVSTWQSAVKQPKE----WFDQFGMVIVDECHlFTGKSLTSII 243

                         170
                  ....*....|.
gi 1883543185 386 IMFNYLDQKLG 396
Cdd:PHA02558  244 TKLDNCKFKFG 254
Dob10 COG4581
Superfamily II RNA helicase [Replication, recombination and repair];
240-375 2.95e-03

Superfamily II RNA helicase [Replication, recombination and repair];


Pssm-ID: 443638 [Multi-domain]  Cd Length: 751  Bit Score: 41.46  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883543185 240 PFKPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLkkfpqgQKGKVVFF-------ANQipvyeqqksvfsK 312
Cdd:COG4581    23 GFELDPFQEEAILALEAGRSVLVAAPTGSGKTLVAEFAIFLAL------ARGRRSFYtapikalSNQ------------K 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1883543185 313 YF---ERHGYR----VTGisgataenvpveQIVENND--IIILTPQILvNNLKKGTIPSLSIFTLMIFDECH 375
Cdd:COG4581    85 FFdlvERFGAEnvglLTG------------DASVNPDapIVVMTTEIL-RNMLYREGADLEDVGVVVMDEFH 143
DEXH_lig_assoc TIGR04121
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ...
 241-272 8.29e-03

DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.


Pssm-ID: 274994 [Multi-domain]  Cd Length: 804  Bit Score: 39.84  E-value: 8.29e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1883543185 241 FKPRNYQLELALPAMKGKNTIICAPTGCGKTF 272
Cdd:TIGR04121  12 WTPRPFQLEMWAAALEGRSGLLIAPTGSGKTL 43
 
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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