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Conserved domains on  [gi|193909766|gb|EDW08633|]
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uncharacterized protein Dmoj_GI19460, isoform A [Drosophila mojavensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AKAP7_NLS pfam10469
AKAP7 2'5' RNA ligase-like domain; AKAP7_NLS is the N-terminal domain of the cyclic ...
 148-352 1.60e-90

AKAP7 2'5' RNA ligase-like domain; AKAP7_NLS is the N-terminal domain of the cyclic AMP-dependent protein kinase A, PKA, anchor protein AKAP7. This protein anchors PKA for its role in regulating PKA-mediated gene transcription in both somatic cells and oocytes. AKAP7_NLS carries the nuclear localization signal (NLS) KKRKK, that indicates the cellular destiny of this anchor protein. Binding to the regulatory subunits RI and RII of PKA is mediated via the family AKAP7_RIRII_bdg. at the C-terminus. This family represents a region that contains two 2'5' RNA ligase like domains pfam02834. Presumably this domain carried out some as yet unknown enzymatic function.


:

Pssm-ID: 402204 [Multi-domain]  Cd Length: 207  Bit Score: 269.91  E-value: 1.60e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193909766  148 PTHFLAAPLNSGEVQKRFNELKQSILDaQLPGIDEDLFISERCIHITLGVYVLLDDAERQKAITELNACRQWLTDLR--T 225
Cdd:pfam10469   1 PTHFLSIPLNSPELRKRLEEFQESVLK-QLPGLDESLFIPPEKLHITLLVLVLLDDEEVARAKEALRECREEIKDILngN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193909766  226 PFEIKIKGLEIMNDDPSATKVLYAHVE----SPNLQVFADKCLNYFQSTGLCATDNieRDSIKLHMTVLNARYRKEKvNN 301
Cdd:pfam10469  80 PLSLRFKGLETFNDDPSAVRVLYAKVEeddhSPKLQELADRIIRRFQEAGLLVKEN--NSRVKLHMTLMNTRYRKKK-YA 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 193909766  302 NDRNCFDAREILKRFGDFDFGTAQCNEVHMCVLKSSRDVDDFYKITGTLKF 352
Cdd:pfam10469 157 KSKESFDAREILDEFKDFDFGTQKVSELHLCSMGSSDESDGFYHVEASVKL 207
KH-I_ASCC1 cd22419
type I K homology (KH) RNA-binding domain found in activating signal cointegrator 1 complex ...
 73-139 4.97e-16

type I K homology (KH) RNA-binding domain found in activating signal cointegrator 1 complex subunit 1 (ASCC1) and similar proteins; ASCC1, also called ASC-1 complex subunit p50, or Trip4 complex subunit p50, plays a role in DNA damage repair as component of the ASCC complex. It is part of the ASC-1 complex that enhances NF-kappa-B, SRF and AP1 transactivation. In cells responding to gastrin-activated paracrine signals, it is involved in the induction of SERPINB2 expression by gastrin. ASCC1 may also play a role in the development of neuromuscular junction.


:

Pssm-ID: 411847 [Multi-domain]  Cd Length: 66  Bit Score: 71.84  E-value: 4.97e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193909766  73 YKLALHVPKSFYGGLIGFKGSTKRRIETESQTEIHVPRQNDsSNDLIIQSNDRKNVCAALRKIRLLV 139
Cdd:cd22419    1 FRLSLDVPSALFKFIIGKKGETKKRLESETKTQIRIPRQGK-EGDIVITGKDRSGVDSARTRIEVLV 66
 
Name Accession Description Interval E-value
AKAP7_NLS pfam10469
AKAP7 2'5' RNA ligase-like domain; AKAP7_NLS is the N-terminal domain of the cyclic ...
 148-352 1.60e-90

AKAP7 2'5' RNA ligase-like domain; AKAP7_NLS is the N-terminal domain of the cyclic AMP-dependent protein kinase A, PKA, anchor protein AKAP7. This protein anchors PKA for its role in regulating PKA-mediated gene transcription in both somatic cells and oocytes. AKAP7_NLS carries the nuclear localization signal (NLS) KKRKK, that indicates the cellular destiny of this anchor protein. Binding to the regulatory subunits RI and RII of PKA is mediated via the family AKAP7_RIRII_bdg. at the C-terminus. This family represents a region that contains two 2'5' RNA ligase like domains pfam02834. Presumably this domain carried out some as yet unknown enzymatic function.


Pssm-ID: 402204 [Multi-domain]  Cd Length: 207  Bit Score: 269.91  E-value: 1.60e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193909766  148 PTHFLAAPLNSGEVQKRFNELKQSILDaQLPGIDEDLFISERCIHITLGVYVLLDDAERQKAITELNACRQWLTDLR--T 225
Cdd:pfam10469   1 PTHFLSIPLNSPELRKRLEEFQESVLK-QLPGLDESLFIPPEKLHITLLVLVLLDDEEVARAKEALRECREEIKDILngN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193909766  226 PFEIKIKGLEIMNDDPSATKVLYAHVE----SPNLQVFADKCLNYFQSTGLCATDNieRDSIKLHMTVLNARYRKEKvNN 301
Cdd:pfam10469  80 PLSLRFKGLETFNDDPSAVRVLYAKVEeddhSPKLQELADRIIRRFQEAGLLVKEN--NSRVKLHMTLMNTRYRKKK-YA 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 193909766  302 NDRNCFDAREILKRFGDFDFGTAQCNEVHMCVLKSSRDVDDFYKITGTLKF 352
Cdd:pfam10469 157 KSKESFDAREILDEFKDFDFGTQKVSELHLCSMGSSDESDGFYHVEASVKL 207
KH-I_ASCC1 cd22419
type I K homology (KH) RNA-binding domain found in activating signal cointegrator 1 complex ...
 73-139 4.97e-16

type I K homology (KH) RNA-binding domain found in activating signal cointegrator 1 complex subunit 1 (ASCC1) and similar proteins; ASCC1, also called ASC-1 complex subunit p50, or Trip4 complex subunit p50, plays a role in DNA damage repair as component of the ASCC complex. It is part of the ASC-1 complex that enhances NF-kappa-B, SRF and AP1 transactivation. In cells responding to gastrin-activated paracrine signals, it is involved in the induction of SERPINB2 expression by gastrin. ASCC1 may also play a role in the development of neuromuscular junction.


Pssm-ID: 411847 [Multi-domain]  Cd Length: 66  Bit Score: 71.84  E-value: 4.97e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193909766  73 YKLALHVPKSFYGGLIGFKGSTKRRIETESQTEIHVPRQNDsSNDLIIQSNDRKNVCAALRKIRLLV 139
Cdd:cd22419    1 FRLSLDVPSALFKFIIGKKGETKKRLESETKTQIRIPRQGK-EGDIVITGKDRSGVDSARTRIEVLV 66
PLN00108 PLN00108
unknown protein; Provisional
 149-352 1.22e-15

unknown protein; Provisional


Pssm-ID: 177724  Cd Length: 257  Bit Score: 75.88  E-value: 1.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193909766 149 THFLAAPLN-SGEVQKRFNELKQSIL--DAQLP----------GIDEDLFISERCIHITLGVYVLLDDAERQKAITELNA 215
Cdd:PLN00108  37 THFVSLPLAiYPDLKKNIEAFQNSVLgnNDKDPlkfqstlaemGIEKSIFVSPKTFHLTVVMLKLENNESVVKAQNILKS 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193909766 216 ----CRQWLTDlrTPFEIKIKGLEIMNDDPSATKVLYAHVESPNLQ-VFADKC---LNYFQSTGLCATDNIERdsIKLHM 287
Cdd:PLN00108 117 icsnVRQALKD--RPVFIRLRGLDCMNGSLDKTRVLYAPVEEVGHEgRLLNAChviIDAFENAGFAGKDAKSR--LKLHA 192

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193909766 288 TVLNARYRKEKVNNNDrnCFDAREILKRFGDFDFGTAQCNEVHMCvLKSSRDVDDFYKITGTLKF 352
Cdd:PLN00108 193 TLMNASYRKDKSKKMD--TFDAREIHKEFENKDWGTYLIREAHIS-QRYKYDPNGYFHCCASLPF 254
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 77-136 1.34e-10

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 56.52  E-value: 1.34e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193909766   77 LHVPKSFYGGLIGFKGSTKRRIETESQTEIHVPRQNDSSNDLIIQ-SNDRKNVCAALRKIR 136
Cdd:pfam00013   4 ILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNERIVTiTGTPEAVEAAKALIE 64
KH smart00322
K homology RNA-binding domain;
77-139 7.14e-09

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 51.53  E-value: 7.14e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193909766    77 LHVPKSFYGGLIGFKGSTKRRIETESQTEIHVPRQNDSSNDLIIqSNDRKNVCAALRKIRLLV 139
Cdd:smart00322   7 VLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERVVEI-TGPPENVEKAAELILEIL 68
ThpR COG1514
RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA ligase) [Translation, ribosomal structure and ...
 151-338 5.97e-07

RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA ligase) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441123 [Multi-domain]  Cd Length: 181  Bit Score: 49.26  E-value: 5.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193909766 151 FLAAPLnSGEVQKRFNELKQSILDAqlpgiDEDLFISERCIHITLGVYVLLDDAERQKAITEL-NACRQWltdlrTPFEI 229
Cdd:COG1514    4 FIALPP-PEELREALAALRARLKAA-----PGGRWVRPENLHLTLAFLGEVDEERLEALAEALaRAAAGA-----PPFEL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193909766 230 KIKGLEIMNDDPSatKVLYAHVE-SPNLQVFADKCLNYFQSTGLcatdNIERDSIKLHMTVlnARYRKEKVnnndrncfD 308
Cdd:COG1514   73 RLDGLGAFPRPRP--RVLWLGVEpSPELLALHRRLRAALARAGL----PPERRPFVPHVTL--ARGKRPAP--------P 136

                        170       180       190
                 ....*....|....*....|....*....|
gi 193909766 309 AREILKRFGDFDFGTAQCNEVHmcvLKSSR 338
Cdd:COG1514  137 LAPALAELRDFEFPEFTVDEFV---LYESE 163
 
Name Accession Description Interval E-value
AKAP7_NLS pfam10469
AKAP7 2'5' RNA ligase-like domain; AKAP7_NLS is the N-terminal domain of the cyclic ...
 148-352 1.60e-90

AKAP7 2'5' RNA ligase-like domain; AKAP7_NLS is the N-terminal domain of the cyclic AMP-dependent protein kinase A, PKA, anchor protein AKAP7. This protein anchors PKA for its role in regulating PKA-mediated gene transcription in both somatic cells and oocytes. AKAP7_NLS carries the nuclear localization signal (NLS) KKRKK, that indicates the cellular destiny of this anchor protein. Binding to the regulatory subunits RI and RII of PKA is mediated via the family AKAP7_RIRII_bdg. at the C-terminus. This family represents a region that contains two 2'5' RNA ligase like domains pfam02834. Presumably this domain carried out some as yet unknown enzymatic function.


Pssm-ID: 402204 [Multi-domain]  Cd Length: 207  Bit Score: 269.91  E-value: 1.60e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193909766  148 PTHFLAAPLNSGEVQKRFNELKQSILDaQLPGIDEDLFISERCIHITLGVYVLLDDAERQKAITELNACRQWLTDLR--T 225
Cdd:pfam10469   1 PTHFLSIPLNSPELRKRLEEFQESVLK-QLPGLDESLFIPPEKLHITLLVLVLLDDEEVARAKEALRECREEIKDILngN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193909766  226 PFEIKIKGLEIMNDDPSATKVLYAHVE----SPNLQVFADKCLNYFQSTGLCATDNieRDSIKLHMTVLNARYRKEKvNN 301
Cdd:pfam10469  80 PLSLRFKGLETFNDDPSAVRVLYAKVEeddhSPKLQELADRIIRRFQEAGLLVKEN--NSRVKLHMTLMNTRYRKKK-YA 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 193909766  302 NDRNCFDAREILKRFGDFDFGTAQCNEVHMCVLKSSRDVDDFYKITGTLKF 352
Cdd:pfam10469 157 KSKESFDAREILDEFKDFDFGTQKVSELHLCSMGSSDESDGFYHVEASVKL 207
KH-I_ASCC1 cd22419
type I K homology (KH) RNA-binding domain found in activating signal cointegrator 1 complex ...
 73-139 4.97e-16

type I K homology (KH) RNA-binding domain found in activating signal cointegrator 1 complex subunit 1 (ASCC1) and similar proteins; ASCC1, also called ASC-1 complex subunit p50, or Trip4 complex subunit p50, plays a role in DNA damage repair as component of the ASCC complex. It is part of the ASC-1 complex that enhances NF-kappa-B, SRF and AP1 transactivation. In cells responding to gastrin-activated paracrine signals, it is involved in the induction of SERPINB2 expression by gastrin. ASCC1 may also play a role in the development of neuromuscular junction.


Pssm-ID: 411847 [Multi-domain]  Cd Length: 66  Bit Score: 71.84  E-value: 4.97e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193909766  73 YKLALHVPKSFYGGLIGFKGSTKRRIETESQTEIHVPRQNDsSNDLIIQSNDRKNVCAALRKIRLLV 139
Cdd:cd22419    1 FRLSLDVPSALFKFIIGKKGETKKRLESETKTQIRIPRQGK-EGDIVITGKDRSGVDSARTRIEVLV 66
PLN00108 PLN00108
unknown protein; Provisional
 149-352 1.22e-15

unknown protein; Provisional


Pssm-ID: 177724  Cd Length: 257  Bit Score: 75.88  E-value: 1.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193909766 149 THFLAAPLN-SGEVQKRFNELKQSIL--DAQLP----------GIDEDLFISERCIHITLGVYVLLDDAERQKAITELNA 215
Cdd:PLN00108  37 THFVSLPLAiYPDLKKNIEAFQNSVLgnNDKDPlkfqstlaemGIEKSIFVSPKTFHLTVVMLKLENNESVVKAQNILKS 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193909766 216 ----CRQWLTDlrTPFEIKIKGLEIMNDDPSATKVLYAHVESPNLQ-VFADKC---LNYFQSTGLCATDNIERdsIKLHM 287
Cdd:PLN00108 117 icsnVRQALKD--RPVFIRLRGLDCMNGSLDKTRVLYAPVEEVGHEgRLLNAChviIDAFENAGFAGKDAKSR--LKLHA 192

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193909766 288 TVLNARYRKEKVNNNDrnCFDAREILKRFGDFDFGTAQCNEVHMCvLKSSRDVDDFYKITGTLKF 352
Cdd:PLN00108 193 TLMNASYRKDKSKKMD--TFDAREIHKEFENKDWGTYLIREAHIS-QRYKYDPNGYFHCCASLPF 254
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 77-136 1.34e-10

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 56.52  E-value: 1.34e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193909766   77 LHVPKSFYGGLIGFKGSTKRRIETESQTEIHVPRQNDSSNDLIIQ-SNDRKNVCAALRKIR 136
Cdd:pfam00013   4 ILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNERIVTiTGTPEAVEAAKALIE 64
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 77-136 4.25e-09

K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found in a wide variety of proteins including ribosomal proteins, transcription factors and post-transcriptional modifiers of mRNA. There are two different KH domains that belong to different protein folds, but they share a single KH motif. The KH motif is folded into a beta alpha alpha beta unit. In addition to the core, type II KH domains (e.g. ribosomal protein S3) include an N-terminal extension and type I KH domains (e.g. hnRNP K) contain a C-terminal extension. Some KH-I superfamily members contain a divergent KH domain that lacks the RNA-binding GXXG motif. Some others have a mutated GXXG motif which may or may not have nucleic acid binding ability.


Pssm-ID: 411802 [Multi-domain]  Cd Length: 63  Bit Score: 52.30  E-value: 4.25e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193909766  77 LHVPKSFYGGLIGFKGSTKRRIETESQTEIHVPRQNDSSND--LIIQSnDRKNVCAALRKIR 136
Cdd:cd00105    3 IEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSGErvVTITG-TPEAVEKAKELIE 63
KH smart00322
K homology RNA-binding domain;
77-139 7.14e-09

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 51.53  E-value: 7.14e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193909766    77 LHVPKSFYGGLIGFKGSTKRRIETESQTEIHVPRQNDSSNDLIIqSNDRKNVCAALRKIRLLV 139
Cdd:smart00322   7 VLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERVVEI-TGPPENVEKAAELILEIL 68
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 73-144 2.78e-08

fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fourteenth one.


Pssm-ID: 411845 [Multi-domain]  Cd Length: 72  Bit Score: 50.28  E-value: 2.78e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193909766  73 YKLALHVPKSFYGGLIGFKGSTKRRIETESQTEIHVPRQNDSSNDLIIQSNDRKNVCAALRKIRLLVDSLRK 144
Cdd:cd22417    1 FTLTVEVDPKYHPKIIGRKGAVITKLRDDHDVNIQFPDKGDENDDEITITGYEKNAEAAKDAILKIVQELES 72
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 77-140 4.29e-08

sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the sixth one.


Pssm-ID: 411804 [Multi-domain]  Cd Length: 68  Bit Score: 49.49  E-value: 4.29e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193909766  77 LHVPKSFYGGLIGFKGSTKRRIETESQTEIHVPRQNDSSNDLIIqSNDRKNVCAALRKIRLLVD 140
Cdd:cd02394    6 IEIDPKFHGHIIGKGGANIKRIREESGVSIRIPDDEANSDEIRI-EGSPEGVKKAKAEILELVD 68
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 77-135 8.09e-08

eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the eighth one.


Pssm-ID: 411839 [Multi-domain]  Cd Length: 62  Bit Score: 48.35  E-value: 8.09e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 193909766  77 LHVPKSFYGGLIGFKGSTKRRIETESQTEIHVPRQNDSSNDLIIQSnDRKNVCAALRKI 135
Cdd:cd22411    4 VPIFKQFHKNIIGKGGATIKKIREETNTRIDLPEENSDSDVITITG-KKEDVEKARERI 61
KH-I_Vigilin_rpt2 cd22406
second type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 73-144 1.25e-07

second type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the second one.


Pssm-ID: 411834 [Multi-domain]  Cd Length: 75  Bit Score: 48.46  E-value: 1.25e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193909766  73 YKLALHVPKSFYGGLIGFKGSTKRRIETESQTEIHVPRQNDSSNDLIIqSNDRKNVCAALRKIRLLVDSLRK 144
Cdd:cd22406    5 ASVTVNIPKEHHRFILGKKGKKLQELELKTATKIVIPRQEDNSDEIKI-TGTKEGIEKARHEIQLISDEQAK 75
ThpR COG1514
RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA ligase) [Translation, ribosomal structure and ...
 151-338 5.97e-07

RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA ligase) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441123 [Multi-domain]  Cd Length: 181  Bit Score: 49.26  E-value: 5.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193909766 151 FLAAPLnSGEVQKRFNELKQSILDAqlpgiDEDLFISERCIHITLGVYVLLDDAERQKAITEL-NACRQWltdlrTPFEI 229
Cdd:COG1514    4 FIALPP-PEELREALAALRARLKAA-----PGGRWVRPENLHLTLAFLGEVDEERLEALAEALaRAAAGA-----PPFEL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193909766 230 KIKGLEIMNDDPSatKVLYAHVE-SPNLQVFADKCLNYFQSTGLcatdNIERDSIKLHMTVlnARYRKEKVnnndrncfD 308
Cdd:COG1514   73 RLDGLGAFPRPRP--RVLWLGVEpSPELLALHRRLRAALARAGL----PPERRPFVPHVTL--ARGKRPAP--------P 136

                        170       180       190
                 ....*....|....*....|....*....|
gi 193909766 309 AREILKRFGDFDFGTAQCNEVHmcvLKSSR 338
Cdd:COG1514  137 LAPALAELRDFEFPEFTVDEFV---LYESE 163
KH-I_ScSCP160_rpt3 cd22448
third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 75-117 1.96e-05

third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411876  Cd Length: 81  Bit Score: 42.51  E-value: 1.96e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 193909766  75 LALHVPKSFYGGLIGFKGSTKRRIETESQTEIHVPRQNDSSND 117
Cdd:cd22448    5 LILKIPVQFHGSLIGQQGKYVNRLQEKYGVKINFPRENSSSND 47
KH-I_ScSCP160_rpt1 cd22446
first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 75-139 5.24e-05

first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411874 [Multi-domain]  Cd Length: 86  Bit Score: 41.24  E-value: 5.24e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193909766  75 LALHVPKSFYGGLIGFKGSTKRRIETESQTEIHVPRQNDSSNDL---------IIQSNDRKNVCAALRKIRLLV 139
Cdd:cd22446    9 ITISVPSSVRGAIIGSRGKNLKSIQDKTGTKIQIPKRNEEGNYDeddddetveISIEGDAEGVELAKKEIEAIV 82
KH-I_Vigilin_rpt3 cd22407
third type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 77-136 7.84e-05

third type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the third one.


Pssm-ID: 411835 [Multi-domain]  Cd Length: 62  Bit Score: 40.27  E-value: 7.84e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 193909766  77 LHVPKSFYGGLIGFKGSTKRRIETESQTEIHVPRQNDSSNDLIIqSNDRKNVCAALRKIR 136
Cdd:cd22407    4 LDIPKVYHPFIAGPNNENVKELQEETGVRINIPPPSVNKDEIVV-SGEKEGVAQAVAKIK 62
KH-I_Mextli_like cd22454
type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic ...
 71-135 9.68e-05

type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic translation initiation factor 4E-binding protein Mextli and similar proteins; Mextli is a novel eukaryotic translation initiation factor 4E-binding protein that promotes translation in Drosophila melanogaster.


Pssm-ID: 411882 [Multi-domain]  Cd Length: 71  Bit Score: 39.99  E-value: 9.68e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193909766  71 GNYKLALHVPKSFYGGLIGFKGSTKRRIETESQTEIHVPRQN-DSSNDLIIQSNDRKNVCAALRKI 135
Cdd:cd22454    2 GQTTIEVVIPNADVGKVIGKGGETIKRIEALTDTVITFERVNgGSPNREVQITGSPDNVAAAKRLI 67
KH-I_ScSCP160_rpt6 cd22451
sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 79-135 1.03e-04

sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the sixth one.


Pssm-ID: 411879 [Multi-domain]  Cd Length: 69  Bit Score: 40.13  E-value: 1.03e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 193909766  79 VPKSFYGGLIGFKGSTKRRIETESQTEIHVPRQNDSSNDLIIqSNDRKNVCAALRKI 135
Cdd:cd22451    7 IPKEYHRAIIGKGGAVLRELEAETGCRIQVPKKDDPSGKIRI-TGARDGVEAATAKI 62
KH-I_MER1_like cd22458
type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae meiotic ...
 74-136 1.78e-04

type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae meiotic recombination 1 protein (MER1) and similar proteins; MER1 is required for chromosome pairing and genetic recombination. It may function to bring the axial elements of the synaptonemal complex corresponding to homologous chromosomes together by initiating recombination. MER1 might be responsible for regulating the MER2 gene and/or gene product.


Pssm-ID: 411886 [Multi-domain]  Cd Length: 65  Bit Score: 39.35  E-value: 1.78e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193909766  74 KLALHVPKSFYGGLIGFKGSTKRRIETESQTEIHVPRQNDSSNDLIIQSNDRKNVCAALRKIR 136
Cdd:cd22458    2 TWEIKLPQALCGRLIGAKGKNIKALSEKSGASIRLIPISNSSQQTIHLSGTDKQIALAISSIE 64
KH-I_Dim2p_like_rpt1 cd22389
first type I K homology (KH) RNA-binding domain found in Pyrococcus horikoshii Dim2p and ...
 79-133 1.90e-04

first type I K homology (KH) RNA-binding domain found in Pyrococcus horikoshii Dim2p and similar proteins; The family includes a group of conserved KH domain-containing protein mainly from archaea, such as Dim2p homologues from Pyrococcus horikoshii and Aeropyrum pernix. Dim2p acts as a preribosomal RNA processing factor that has been identified as an essential protein for the maturation of 40S ribosomal subunit in Saccharomyces cerevisiae. It is required for the cleavage at processing site A2 to generate the pre-20S rRNA and for the dimethylation of the 18S rRNA by 18S rRNA dimethyltransferase, Dim1p. Dim2p contains two K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411817 [Multi-domain]  Cd Length: 70  Bit Score: 39.10  E-value: 1.90e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 193909766  79 VPKSFYGGLIGFKGSTKRRIETESQTEIHVprqNDSSNDLIIQSNDRKNVCAALR 133
Cdd:cd22389    5 IPKERIGVLIGKKGETKREIEERTGVKITV---DSETGEVIIEPEDEEDPLNVMK 56
KH-I_IGF2BP1_rpt1 cd22490
first type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 ...
 75-149 5.09e-04

first type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 mRNA-binding protein 1 (IGF2BP1) and similar proteins; IGF2BP1, also called IGF2 mRNA-binding protein 1 (IMP-1), or coding region determinant-binding protein (CRD-BP), or IGF-II mRNA-binding protein 1, or VICKZ family member 1 (VICKZ1), or zipcode-binding protein 1 (ZBP-1), is an RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). It functions by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. It regulates localized beta-actin/ACTB mRNA translation, a crucial process for cell polarity, cell migration and neurite outgrowth. IGF2BP1 can form homodimers and heterodimers with IGF2BP1 and IGF2BP3. It contains four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the first one.


Pssm-ID: 411918  Cd Length: 76  Bit Score: 38.15  E-value: 5.09e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193909766  75 LALHVPKSFYGGLIGFKGSTKRRIETESQTEIHVPR-QNDSSNDLIIQSNDRKNVCAAlrKIRLLVDSLRKRMKPT 149
Cdd:cd22490    2 LRLLVPTQYVGAIIGKEGATIRNITKQTQSKIDVHRkENAGAAEKAISIHSTPEGCSA--ACKMILEIMQKEAKDT 75
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 75-135 1.05e-03

fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fourth one.


Pssm-ID: 411836 [Multi-domain]  Cd Length: 62  Bit Score: 36.76  E-value: 1.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193909766  75 LALHVPKSFYGGLIGFKGSTKRRIETESQTEIHVPrQNDSSNDLIIQSNDRKNVCAALRKI 135
Cdd:cd22408    2 VSVEVPKSQHRFVIGPRGSTIQEILEETGCSVEVP-PNDSDSETITLRGPADKLGAALTLV 61
KH-I_BTR1_rpt2 cd22437
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 ...
 75-120 6.01e-03

second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 and similar proteins; BTR1, also called Binding to ToMV RNA 1, is a negative regulator of tomato mosaic virus (ToMV) multiplication but has no effect on the multiplication of cucumber mosaic virus (CMV). BTR1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411865 [Multi-domain]  Cd Length: 69  Bit Score: 34.89  E-value: 6.01e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 193909766  75 LALHVPKSFYGGLIGFKGSTKRRIETESQTEIHV---PRQNDSSNDLII 120
Cdd:cd22437    1 VRLLVPNSSCGLIIGKGGSTIKELREDSNANIKIspkDQLLPGSSERIV 49
 
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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