NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|269784766|ref|NP_001028413|]
View 

uncharacterized protein LOC211208 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
KH-I super family cl00098
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 789-853 1.62e-23

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.


The actual alignment was detected with superfamily member cd22414:

Pssm-ID: 469614  Cd Length: 66  Bit Score: 95.06  E-value: 1.62e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784766  789 DDSILINRRFHHYFVMRRGQLLKEMAEDYGGVVITFSYSGRQNTKVTIRGAKPCVEAAKKHIKEI 853
Cdd:cd22414     1 EDEMTVDPKHHRHFVARRGQVLREIADEYGGVMVSFPRSGTQSDKVTLKGAKDCVEGAKKRILEI 65
KH-I super family cl00098
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 957-1033 2.69e-23

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.


The actual alignment was detected with superfamily member cd22416:

Pssm-ID: 469614 [Multi-domain]  Cd Length: 78  Bit Score: 94.60  E-value: 2.69e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269784766  957 PVTTEVHVPLHLQPYIIGHKGSGLRKLVKEYEVHMQVSQPGKNSDIISIMGLSANVEQAKIKLQKRVKSLQMEVEDR 1033
Cdd:cd22416     1 PVTEEVNVPFDLHRFIIGQKGADVRKMMDEFDVNISIPPAELQSDIIKITGPPANVERAKAALLERVKELEAEKEDR 77
KH-I super family cl00098
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 494-560 3.32e-23

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.


The actual alignment was detected with superfamily member cd22410:

Pssm-ID: 469614  Cd Length: 67  Bit Score: 93.88  E-value: 3.32e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269784766  494 EYSQDIIIKHQFHHILIGQKGERVREICKKFPDVILNFPHPAEKSDIVQLIGPRYESEKCAQYLENM 560
Cdd:cd22410     1 EKTKDIIIEQRFHRTIIGQKGEKIREIRDKFPQVQITFPDPGSKSDVVTLRGPKDEVDKCYKYLKKL 67
KH-I super family cl00098
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 1112-1177 5.37e-19

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.


The actual alignment was detected with superfamily member cd22418:

Pssm-ID: 469614 [Multi-domain]  Cd Length: 69  Bit Score: 81.93  E-value: 5.37e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269784766 1112 ISKEITLNQQVRGNVIGVRGKTINKIMDQYQVDIRLPPKGLYNPN-ITVTGLADNVEKAIEHILNLE 1177
Cdd:cd22418     1 VTEEVEIDSRVHPRLIGARGKAIRKIMEDFKVDIRFPRSGDADPNlVTITGLEENVEECKDHLLNLE 67
KH-I super family cl00098
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 352-420 2.23e-18

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.


The actual alignment was detected with superfamily member cd22409:

Pssm-ID: 469614 [Multi-domain]  Cd Length: 70  Bit Score: 80.32  E-value: 2.23e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784766  352 YIASSIFAPSWLHRFIIGTKGEEISEITECVPKVQIHFT-AKDKITLKGPIDDVNYAQEKFDIIVKDLMS 420
Cdd:cd22409     1 VVVAEVSAPSWLHRFIIGKKGANIKKITQDLPKVHIEFTeGEDKIELEGPPEEVEVVREQLEAIVKELVA 70
KH-I super family cl00098
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 1038-1110 5.04e-18

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.


The actual alignment was detected with superfamily member cd22417:

Pssm-ID: 469614 [Multi-domain]  Cd Length: 72  Bit Score: 79.56  E-value: 5.04e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269784766 1038 FKLMFNLDPKYQAKITGHKGLLITQICTEHDVTIHFPKKGThDMQEQITITGYKENTLAARDAIMRLLHKIEK 1110
Cdd:cd22417     1 FTLTVEVDPKYHPKIIGRKGAVITKLRDDHDVNIQFPDKGD-ENDDEITITGYEKNAEAAKDAILKIVQELES 72
KH-I super family cl00098
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 866-952 2.17e-17

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.


The actual alignment was detected with superfamily member cd22415:

Pssm-ID: 469614 [Multi-domain]  Cd Length: 92  Bit Score: 78.50  E-value: 2.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784766  866 VLPHSFQPFIMGPISSRIQQIARDYKVEIKFPDieKPALNMDLGTHEKGKEKWKRTAKEIAPNSPRKGDTIFISGQVENC 945
Cdd:cd22415     5 VIPQKFHRTVMGAKGSRVQQITSEFDVQIKFPD--RESNQPAPAENGEGNGGEGVEGEAVDDNSPRKCDIIIITGKKENC 82


                  ....*..
gi 269784766  946 KAATEAL 952
Cdd:cd22415    83 EAAKEAL 89
KH-I super family cl00098
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 713-777 1.04e-16

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.


The actual alignment was detected with superfamily member cd22413:

Pssm-ID: 469614 [Multi-domain]  Cd Length: 66  Bit Score: 75.37  E-value: 1.04e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784766  713 KNYSETLHIKSKYHQFLLNKNGGNISKICDETGTCVFFPNPTNKDQETITITGTEESVKEVQKQL 777
Cdd:cd22413     1 NSFTVEIRAKPEYHRFLIGRGGANIRKIRDNTGARIIFPTARDEDQELITIIGTKEAVEKAKEEL 65
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 570-631 5.37e-16

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: 73.39  E-value: 5.37e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 269784766  570 SISVPIIKKLHKRIIGKGVSNIRKISEATNTKITFPPESCNSEEFIITGYPENCEIARNWIL 631
Cdd:cd22411     1 SIKVPIFKQFHKNIIGKGGATIKKIREETNTRIDLPEENSDSDVITITGKKEDVEKARERIL 62
KH-I super family cl00098
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 641-709 5.64e-16

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.


The actual alignment was detected with superfamily member cd22412:

Pssm-ID: 469614  Cd Length: 70  Bit Score: 73.48  E-value: 5.64e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269784766  641 AEEEIIIPANLYKHLTNPKECLLNSIIEECGKIHLHFPKGKSNLNKIIIMGTIENVEKAKTKLLKLSEE 709
Cdd:cd22412     2 VEVEVEIPAKLHNSLIGAKGRLIRSIMEECGGVHIHFPPEGSGSDKVTIRGPKEDVEKAKKQLLELANE 70
KH-I super family cl00098
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 71-136 2.37e-12

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.


The actual alignment was detected with superfamily member cd22405:

Pssm-ID: 469614  Cd Length: 69  Bit Score: 63.08  E-value: 2.37e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269784766   71 TRIFHVLLEEEKYLT---QFGEGTLAKFYAHIMENTGVNLESSFVKDQGLYVTVFGNPEAVTNAENEIF 136
Cdd:cd22405     1 TQVFHVPLEERRYKEsnqQFGEGEQAKICKDIMQKTGATIELSSAKDQSLTIMVTGKQSAVMKARREVL 69
KH-I super family cl00098
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 422-489 2.68e-10

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.


The actual alignment was detected with superfamily member cd02394:

Pssm-ID: 469614 [Multi-domain]  Cd Length: 68  Bit Score: 57.20  E-value: 2.68e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269784766  422 MEYTEINSDSKFYKYLTGNNGEILNRITEKNQVSITMfPENESNYS-IRIEGESLGVHQAKKELLDLAN 489
Cdd:cd02394     1 MAFTTIEIDPKFHGHIIGKGGANIKRIREESGVSIRI-PDDEANSDeIRIEGSPEGVKKAKAEILELVD 68
 
Name Accession Description Interval E-value
KH-I_Vigilin_rpt11 cd22414
eleventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 789-853 1.62e-23

eleventh 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 eleventh one.


Pssm-ID: 411842  Cd Length: 66  Bit Score: 95.06  E-value: 1.62e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784766  789 DDSILINRRFHHYFVMRRGQLLKEMAEDYGGVVITFSYSGRQNTKVTIRGAKPCVEAAKKHIKEI 853
Cdd:cd22414     1 EDEMTVDPKHHRHFVARRGQVLREIADEYGGVMVSFPRSGTQSDKVTLKGAKDCVEGAKKRILEI 65
KH-I_Vigilin_rpt13 cd22416
thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 957-1033 2.69e-23

thirteenth 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 thirteenth one.


Pssm-ID: 411844 [Multi-domain]  Cd Length: 78  Bit Score: 94.60  E-value: 2.69e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269784766  957 PVTTEVHVPLHLQPYIIGHKGSGLRKLVKEYEVHMQVSQPGKNSDIISIMGLSANVEQAKIKLQKRVKSLQMEVEDR 1033
Cdd:cd22416     1 PVTEEVNVPFDLHRFIIGQKGADVRKMMDEFDVNISIPPAELQSDIIKITGPPANVERAKAALLERVKELEAEKEDR 77
KH-I_Vigilin_rpt7 cd22410
seventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 494-560 3.32e-23

seventh 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 seventh one.


Pssm-ID: 411838  Cd Length: 67  Bit Score: 93.88  E-value: 3.32e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269784766  494 EYSQDIIIKHQFHHILIGQKGERVREICKKFPDVILNFPHPAEKSDIVQLIGPRYESEKCAQYLENM 560
Cdd:cd22410     1 EKTKDIIIEQRFHRTIIGQKGEKIREIRDKFPQVQITFPDPGSKSDVVTLRGPKDEVDKCYKYLKKL 67
KH-I_Vigilin_rpt15 cd22418
fifteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 1112-1177 5.37e-19

fifteenth 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 fifteenth one.


Pssm-ID: 411846 [Multi-domain]  Cd Length: 69  Bit Score: 81.93  E-value: 5.37e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269784766 1112 ISKEITLNQQVRGNVIGVRGKTINKIMDQYQVDIRLPPKGLYNPN-ITVTGLADNVEKAIEHILNLE 1177
Cdd:cd22418     1 VTEEVEIDSRVHPRLIGARGKAIRKIMEDFKVDIRFPRSGDADPNlVTITGLEENVEECKDHLLNLE 67
KH-I_Vigilin_rpt5 cd22409
fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 352-420 2.23e-18

fifth 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 fifth one.


Pssm-ID: 411837 [Multi-domain]  Cd Length: 70  Bit Score: 80.32  E-value: 2.23e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784766  352 YIASSIFAPSWLHRFIIGTKGEEISEITECVPKVQIHFT-AKDKITLKGPIDDVNYAQEKFDIIVKDLMS 420
Cdd:cd22409     1 VVVAEVSAPSWLHRFIIGKKGANIKKITQDLPKVHIEFTeGEDKIELEGPPEEVEVVREQLEAIVKELVA 70
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 1038-1110 5.04e-18

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: 79.56  E-value: 5.04e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269784766 1038 FKLMFNLDPKYQAKITGHKGLLITQICTEHDVTIHFPKKGThDMQEQITITGYKENTLAARDAIMRLLHKIEK 1110
Cdd:cd22417     1 FTLTVEVDPKYHPKIIGRKGAVITKLRDDHDVNIQFPDKGD-ENDDEITITGYEKNAEAAKDAILKIVQELES 72
KH-I_Vigilin_rpt12 cd22415
twelfth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 866-952 2.17e-17

twelfth 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 twelfth one.


Pssm-ID: 411843 [Multi-domain]  Cd Length: 92  Bit Score: 78.50  E-value: 2.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784766  866 VLPHSFQPFIMGPISSRIQQIARDYKVEIKFPDieKPALNMDLGTHEKGKEKWKRTAKEIAPNSPRKGDTIFISGQVENC 945
Cdd:cd22415     5 VIPQKFHRTVMGAKGSRVQQITSEFDVQIKFPD--RESNQPAPAENGEGNGGEGVEGEAVDDNSPRKCDIIIITGKKENC 82


                  ....*..
gi 269784766  946 KAATEAL 952
Cdd:cd22415    83 EAAKEAL 89
KH-I_Vigilin_rpt10 cd22413
tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 713-777 1.04e-16

tenth 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 tenth one.


Pssm-ID: 411841 [Multi-domain]  Cd Length: 66  Bit Score: 75.37  E-value: 1.04e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784766  713 KNYSETLHIKSKYHQFLLNKNGGNISKICDETGTCVFFPNPTNKDQETITITGTEESVKEVQKQL 777
Cdd:cd22413     1 NSFTVEIRAKPEYHRFLIGRGGANIRKIRDNTGARIIFPTARDEDQELITIIGTKEAVEKAKEEL 65
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 570-631 5.37e-16

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: 73.39  E-value: 5.37e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 269784766  570 SISVPIIKKLHKRIIGKGVSNIRKISEATNTKITFPPESCNSEEFIITGYPENCEIARNWIL 631
Cdd:cd22411     1 SIKVPIFKQFHKNIIGKGGATIKKIREETNTRIDLPEENSDSDVITITGKKEDVEKARERIL 62
KH-I_Vigilin_rpt9 cd22412
ninth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 641-709 5.64e-16

ninth 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 ninth one.


Pssm-ID: 411840  Cd Length: 70  Bit Score: 73.48  E-value: 5.64e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269784766  641 AEEEIIIPANLYKHLTNPKECLLNSIIEECGKIHLHFPKGKSNLNKIIIMGTIENVEKAKTKLLKLSEE 709
Cdd:cd22412     2 VEVEVEIPAKLHNSLIGAKGRLIRSIMEECGGVHIHFPPEGSGSDKVTIRGPKEDVEKAKKQLLELANE 70
KH-I_Vigilin_rpt1 cd22405
first type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 71-136 2.37e-12

first 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 first one.


Pssm-ID: 411833  Cd Length: 69  Bit Score: 63.08  E-value: 2.37e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269784766   71 TRIFHVLLEEEKYLT---QFGEGTLAKFYAHIMENTGVNLESSFVKDQGLYVTVFGNPEAVTNAENEIF 136
Cdd:cd22405     1 TQVFHVPLEERRYKEsnqQFGEGEQAKICKDIMQKTGATIELSSAKDQSLTIMVTGKQSAVMKARREVL 69
KH smart00322
K homology RNA-binding domain;
567-633 2.81e-12

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 63.08  E-value: 2.81e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269784766    567 NNYSISVPIIKKLHKRIIGKGVSNIRKISEATNTKITFPPESCNSEEFIITGYPENCEIARNWILSL 633
Cdd:smart00322    1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERVVEITGPPENVEKAAELILEI 67
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 716-779 5.50e-11

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: 59.22  E-value: 5.50e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784766   716 SETLHIKSKYHQFLLNKNGGNISKICDETGTCVFFP-NPTNKDQETITITGTEESVKEVQKQLDD 779
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPpSESEGNERIVTITGTPEAVEAAKALIEE 65
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 569-632 1.31e-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: 58.06  E-value: 1.31e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 269784766   569 YSISVPiiKKLHKRIIGKGVSNIRKISEATNTKITFPPES--CNSEEFIITGYPENCEIARNWILS 632
Cdd:pfam00013    2 VEILVP--SSLVGLIIGKGGSNIKEIREETGAKIQIPPSEseGNERIVTITGTPEAVEAAKALIEE 65
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 422-489 2.68e-10

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: 57.20  E-value: 2.68e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269784766  422 MEYTEINSDSKFYKYLTGNNGEILNRITEKNQVSITMfPENESNYS-IRIEGESLGVHQAKKELLDLAN 489
Cdd:cd02394     1 MAFTTIEIDPKFHGHIIGKGGANIKRIREESGVSIRI-PDDEANSDeIRIEGSPEGVKKAKAEILELVD 68
KH smart00322
K homology RNA-binding domain;
1112-1176 8.36e-10

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 56.15  E-value: 8.36e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784766   1112 ISKEITLNQQVRGNVIGVRGKTINKIMDQYQVDIRLPPKGLYNPNITVTGLADNVEKAIEHILNL 1176
Cdd:smart00322    3 VTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERVVEITGPPENVEKAAELILEI 67
KH smart00322
K homology RNA-binding domain;
957-1023 1.08e-09

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 55.76  E-value: 1.08e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269784766    957 PVTTEVHVPLHLQPYIIGHKGSGLRKLVKEYEVHMQVSQPGKNSDIISIMGLSANVEQAKIKLQKRV 1023
Cdd:smart00322    2 PVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERVVEITGPPENVEKAAELILEIL 68
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 1113-1175 6.50e-09

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: 53.44  E-value: 6.50e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784766  1113 SKEITLNQQVRGNVIGVRGKTINKIMDQYQVDIRLPPKGLYNPN--ITVTGLADNVEKAIEHILN 1175
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNEriVTITGTPEAVEAAKALIEE 65
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 959-1021 1.37e-07

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: 49.59  E-value: 1.37e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784766   959 TTEVHVPLHLQPYIIGHKGSGLRKLVKEYEVHMQV--SQPGKNSDIISIMGLSANVEQAKIKLQK 1021
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIppSESEGNERIVTITGTPEAVEAAKALIEE 65
KH smart00322
K homology RNA-binding domain;
713-781 5.14e-07

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 48.06  E-value: 5.14e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269784766    713 KNYSETLHIKSKYHQFLLNKNGGNISKICDETGTCVFFPNPTNKDqETITITGTEESVKEVQKQLDDLV 781
Cdd:smart00322    1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEE-RVVEITGPPENVEKAAELILEIL 68
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 1042-1102 1.59e-05

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: 43.81  E-value: 1.59e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 269784766  1042 FNLDPKYQAKITGHKGLLITQICTEHDVTIHFPKKGTHDMQEQITITGYKENTLAARDAIM 1102
Cdd:pfam00013    4 ILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNERIVTITGTPEAVEAAKALIE 64
KH smart00322
K homology RNA-binding domain;
493-561 3.06e-05

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 43.05  E-value: 3.06e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269784766    493 EEYSQDIIIKHQFHHILIGQKGERVREICKKFpDVILNFPHPAEKSDIVQLIGPRYESEKCAQYLENML 561
Cdd:smart00322    1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEET-GVKIDIPGPGSEERVVEITGPPENVEKAAELILEIL 68
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 642-705 9.96e-05

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: 41.50  E-value: 9.96e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784766   642 EEEIIIPANLYKHLTNPKECLLNSIIEECG-KIHLHFPKGKSNLNKIIIMGTIENVEKAKTKLLK 705
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGaKIQIPPSESEGNERIVTITGTPEAVEAAKALIEE 65
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 791-852 1.42e-04

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: 41.11  E-value: 1.42e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269784766   791 SILINRRFHHYFVMRRGQLLKEMAEDYG-GVVITFSYSGRQNTKVTIRGAKPCVEAAKKHIKE 852
Cdd:pfam00013    3 EILVPSSLVGLIIGKGGSNIKEIREETGaKIQIPPSESEGNERIVTITGTPEAVEAAKALIEE 65
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
 1077-1176 2.02e-04

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 45.81  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784766 1077 GTHD----MQEQITITGYKENTLA-----ARDAIMRLLHKIEKTISKE-------------ITLNQQVRGNVIGVRGKTI 1134
Cdd:PRK11824  497 GTRDgitaLQMDIKIDGITREILEealeqAKEGRLHILGKMNEAISEPraelspyaprietIKIPPDKIRDVIGPGGKTI 576

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 269784766 1135 NKIMDQYQVDIRLPPKGlynpNITVTGL-ADNVEKAIEHILNL 1176
Cdd:PRK11824  577 REITEETGAKIDIEDDG----TVKIAATdGEAAEAAKERIEGI 615
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 496-559 5.73e-04

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: 39.19  E-value: 5.73e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 269784766   496 SQDIIIKHQFHHILIGQKGERVREICKKFpDVILNFPHPA--EKSDIVQLIGPRYESEKCAQYLEN 559
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREET-GAKIQIPPSEseGNERIVTITGTPEAVEAAKALIEE 65
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 425-486 6.44e-04

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: 39.19  E-value: 6.44e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269784766   425 TEINSDSKFYKYLTGNNGEILNRITEKNQVSITMFPENESNYS--IRIEGESLGVHQAKKELLD 486
Cdd:pfam00013    2 VEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNEriVTITGTPEAVEAAKALIEE 65
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 356-410 1.72e-03

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: 38.03  E-value: 1.72e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 269784766   356 SIFAPSWLHRFIIGTKGEEISEITECVpKVQIHF------TAKDKITLKGPIDDVNYAQEK 410
Cdd:pfam00013    3 EILVPSSLVGLIIGKGGSNIKEIREET-GAKIQIppseseGNERIVTITGTPEAVEAAKAL 62
KH smart00322
K homology RNA-binding domain;
642-706 2.36e-03

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 37.66  E-value: 2.36e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784766    642 EEEIIIPANLYKHLTNPKECLLNSIIEECGKiHLHFPKGKSNLNKIIIMGTIENVEKAKTKLLKL 706
Cdd:smart00322    4 TIEVLIPADKVGLIIGKGGSTIKKIEEETGV-KIDIPGPGSEERVVEITGPPENVEKAAELILEI 67
 
Name Accession Description Interval E-value
KH-I_Vigilin_rpt11 cd22414
eleventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 789-853 1.62e-23

eleventh 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 eleventh one.


Pssm-ID: 411842  Cd Length: 66  Bit Score: 95.06  E-value: 1.62e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784766  789 DDSILINRRFHHYFVMRRGQLLKEMAEDYGGVVITFSYSGRQNTKVTIRGAKPCVEAAKKHIKEI 853
Cdd:cd22414     1 EDEMTVDPKHHRHFVARRGQVLREIADEYGGVMVSFPRSGTQSDKVTLKGAKDCVEGAKKRILEI 65
KH-I_Vigilin_rpt13 cd22416
thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 957-1033 2.69e-23

thirteenth 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 thirteenth one.


Pssm-ID: 411844 [Multi-domain]  Cd Length: 78  Bit Score: 94.60  E-value: 2.69e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269784766  957 PVTTEVHVPLHLQPYIIGHKGSGLRKLVKEYEVHMQVSQPGKNSDIISIMGLSANVEQAKIKLQKRVKSLQMEVEDR 1033
Cdd:cd22416     1 PVTEEVNVPFDLHRFIIGQKGADVRKMMDEFDVNISIPPAELQSDIIKITGPPANVERAKAALLERVKELEAEKEDR 77
KH-I_Vigilin_rpt7 cd22410
seventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 494-560 3.32e-23

seventh 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 seventh one.


Pssm-ID: 411838  Cd Length: 67  Bit Score: 93.88  E-value: 3.32e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269784766  494 EYSQDIIIKHQFHHILIGQKGERVREICKKFPDVILNFPHPAEKSDIVQLIGPRYESEKCAQYLENM 560
Cdd:cd22410     1 EKTKDIIIEQRFHRTIIGQKGEKIREIRDKFPQVQITFPDPGSKSDVVTLRGPKDEVDKCYKYLKKL 67
KH-I_Vigilin_rpt15 cd22418
fifteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 1112-1177 5.37e-19

fifteenth 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 fifteenth one.


Pssm-ID: 411846 [Multi-domain]  Cd Length: 69  Bit Score: 81.93  E-value: 5.37e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269784766 1112 ISKEITLNQQVRGNVIGVRGKTINKIMDQYQVDIRLPPKGLYNPN-ITVTGLADNVEKAIEHILNLE 1177
Cdd:cd22418     1 VTEEVEIDSRVHPRLIGARGKAIRKIMEDFKVDIRFPRSGDADPNlVTITGLEENVEECKDHLLNLE 67
KH-I_Vigilin_rpt5 cd22409
fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 352-420 2.23e-18

fifth 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 fifth one.


Pssm-ID: 411837 [Multi-domain]  Cd Length: 70  Bit Score: 80.32  E-value: 2.23e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784766  352 YIASSIFAPSWLHRFIIGTKGEEISEITECVPKVQIHFT-AKDKITLKGPIDDVNYAQEKFDIIVKDLMS 420
Cdd:cd22409     1 VVVAEVSAPSWLHRFIIGKKGANIKKITQDLPKVHIEFTeGEDKIELEGPPEEVEVVREQLEAIVKELVA 70
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 1038-1110 5.04e-18

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: 79.56  E-value: 5.04e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269784766 1038 FKLMFNLDPKYQAKITGHKGLLITQICTEHDVTIHFPKKGThDMQEQITITGYKENTLAARDAIMRLLHKIEK 1110
Cdd:cd22417     1 FTLTVEVDPKYHPKIIGRKGAVITKLRDDHDVNIQFPDKGD-ENDDEITITGYEKNAEAAKDAILKIVQELES 72
KH-I_Vigilin_rpt12 cd22415
twelfth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 866-952 2.17e-17

twelfth 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 twelfth one.


Pssm-ID: 411843 [Multi-domain]  Cd Length: 92  Bit Score: 78.50  E-value: 2.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784766  866 VLPHSFQPFIMGPISSRIQQIARDYKVEIKFPDieKPALNMDLGTHEKGKEKWKRTAKEIAPNSPRKGDTIFISGQVENC 945
Cdd:cd22415     5 VIPQKFHRTVMGAKGSRVQQITSEFDVQIKFPD--RESNQPAPAENGEGNGGEGVEGEAVDDNSPRKCDIIIITGKKENC 82


                  ....*..
gi 269784766  946 KAATEAL 952
Cdd:cd22415    83 EAAKEAL 89
KH-I_Vigilin_rpt10 cd22413
tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 713-777 1.04e-16

tenth 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 tenth one.


Pssm-ID: 411841 [Multi-domain]  Cd Length: 66  Bit Score: 75.37  E-value: 1.04e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784766  713 KNYSETLHIKSKYHQFLLNKNGGNISKICDETGTCVFFPNPTNKDQETITITGTEESVKEVQKQL 777
Cdd:cd22413     1 NSFTVEIRAKPEYHRFLIGRGGANIRKIRDNTGARIIFPTARDEDQELITIIGTKEAVEKAKEEL 65
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 570-631 5.37e-16

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: 73.39  E-value: 5.37e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 269784766  570 SISVPIIKKLHKRIIGKGVSNIRKISEATNTKITFPPESCNSEEFIITGYPENCEIARNWIL 631
Cdd:cd22411     1 SIKVPIFKQFHKNIIGKGGATIKKIREETNTRIDLPEENSDSDVITITGKKEDVEKARERIL 62
KH-I_Vigilin_rpt9 cd22412
ninth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 641-709 5.64e-16

ninth 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 ninth one.


Pssm-ID: 411840  Cd Length: 70  Bit Score: 73.48  E-value: 5.64e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269784766  641 AEEEIIIPANLYKHLTNPKECLLNSIIEECGKIHLHFPKGKSNLNKIIIMGTIENVEKAKTKLLKLSEE 709
Cdd:cd22412     2 VEVEVEIPAKLHNSLIGAKGRLIRSIMEECGGVHIHFPPEGSGSDKVTIRGPKEDVEKAKKQLLELANE 70
KH-I_Vigilin_rpt1 cd22405
first type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 71-136 2.37e-12

first 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 first one.


Pssm-ID: 411833  Cd Length: 69  Bit Score: 63.08  E-value: 2.37e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269784766   71 TRIFHVLLEEEKYLT---QFGEGTLAKFYAHIMENTGVNLESSFVKDQGLYVTVFGNPEAVTNAENEIF 136
Cdd:cd22405     1 TQVFHVPLEERRYKEsnqQFGEGEQAKICKDIMQKTGATIELSSAKDQSLTIMVTGKQSAVMKARREVL 69
KH smart00322
K homology RNA-binding domain;
567-633 2.81e-12

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 63.08  E-value: 2.81e-12
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269784766    567 NNYSISVPIIKKLHKRIIGKGVSNIRKISEATNTKITFPPESCNSEEFIITGYPENCEIARNWILSL 633
Cdd:smart00322    1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERVVEITGPPENVEKAAELILEI 67
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 716-779 5.50e-11

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: 59.22  E-value: 5.50e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784766   716 SETLHIKSKYHQFLLNKNGGNISKICDETGTCVFFP-NPTNKDQETITITGTEESVKEVQKQLDD 779
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPpSESEGNERIVTITGTPEAVEAAKALIEE 65
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 570-631 9.21e-11

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: 58.34  E-value: 9.21e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 269784766  570 SISVPIIKKLHKRIIGKGVSNIRKISEATNTKITFPPESCNSEEFIITGYPENCEIARNWIL 631
Cdd:cd22408     1 TVSVEVPKSQHRFVIGPRGSTIQEILEETGCSVEVPPNDSDSETITLRGPADKLGAALTLVY 62
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 569-632 1.31e-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: 58.06  E-value: 1.31e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 269784766   569 YSISVPiiKKLHKRIIGKGVSNIRKISEATNTKITFPPES--CNSEEFIITGYPENCEIARNWILS 632
Cdd:pfam00013    2 VEILVP--SSLVGLIIGKGGSNIKEIREETGAKIQIPPSEseGNERIVTITGTPEAVEAAKALIEE 65
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 422-489 2.68e-10

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: 57.20  E-value: 2.68e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269784766  422 MEYTEINSDSKFYKYLTGNNGEILNRITEKNQVSITMfPENESNYS-IRIEGESLGVHQAKKELLDLAN 489
Cdd:cd02394     1 MAFTTIEIDPKFHGHIIGKGGANIKRIREESGVSIRI-PDDEANSDeIRIEGSPEGVKKAKAEILELVD 68
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 569-639 5.96e-10

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: 56.45  E-value: 5.96e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 269784766  569 YSISVPIIKKLHKRIIGKGVSNIRKISEATNTKITFPP-ESCNSEEFIITGYPENCEIARNWILSLQQELAD 639
Cdd:cd22417     1 FTLTVEVDPKYHPKIIGRKGAVITKLRDDHDVNIQFPDkGDENDDEITITGYEKNAEAAKDAILKIVQELES 72
KH smart00322
K homology RNA-binding domain;
1112-1176 8.36e-10

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 56.15  E-value: 8.36e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784766   1112 ISKEITLNQQVRGNVIGVRGKTINKIMDQYQVDIRLPPKGLYNPNITVTGLADNVEKAIEHILNL 1176
Cdd:smart00322    3 VTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERVVEITGPPENVEKAAELILEI 67
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 571-631 1.04e-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: 55.38  E-value: 1.04e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269784766  571 ISVPIIKKLHKRIIGKGVSNIRKISEATNTKITFPPESCNSEE--FIITGYPENCEIARNWIL 631
Cdd:cd00105     1 EEIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSGErvVTITGTPEAVEKAKELIE 63
KH smart00322
K homology RNA-binding domain;
957-1023 1.08e-09

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 55.76  E-value: 1.08e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269784766    957 PVTTEVHVPLHLQPYIIGHKGSGLRKLVKEYEVHMQVSQPGKNSDIISIMGLSANVEQAKIKLQKRV 1023
Cdd:smart00322    2 PVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERVVEITGPPENVEKAAELILEIL 68
KH-I_BICC1_rpt3 cd22422
third type I K homology (KH) RNA-binding domain found in protein bicaudal C homolog 1 (BICC1) ...
 716-777 1.18e-09

third type I K homology (KH) RNA-binding domain found in protein bicaudal C homolog 1 (BICC1) and similar proteins; BICC1, also called Bic-C, is a mammalian homologue of Drosophila Bicaudal-C (dBic-C). BICC1 functions as an RNA-binding protein that represses the translation of selected mRNAs to control development. It regulates gene expression and modulates cell proliferation and apoptosis. BICC1 is a negative regulator of Wnt signaling. Increased levels of BICC1 may be associated with depression. Besides, BICC1 is a genetic determinant of osteoblastogenesis and bone mineral density. BICC1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411850  Cd Length: 67  Bit Score: 55.42  E-value: 1.18e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269784766  716 SETLHIKSKYHQFLLNKNGGNISKICDETGTCVFFPNPTNKDQE--TITITGTEESVKEVQKQL 777
Cdd:cd22422     3 SMQLEIAPQHHLFMLGRNGSNIKHIMQRTGAQIHFPDPNNPPQRksTVFISGSIDSVYLARQQL 66
KH-I_Vigilin_rpt2 cd22406
second type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 569-638 1.31e-09

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: 55.78  E-value: 1.31e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784766  569 YSISVPIIKKLHKRIIGKGVSNIRKISEATNTKITFPPESCNSEEFIITGYPENCEIARNWILSLQQELA 638
Cdd:cd22406     5 ASVTVNIPKEHHRFILGKKGKKLQELELKTATKIVIPRQEDNSDEIKITGTKEGIEKARHEIQLISDEQA 74
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 958-1026 3.08e-09

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: 54.52  E-value: 3.08e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784766  958 VTTEVHVPLHLQPYIIGHKGSGLRKLVKEYEVHMQVSQPGK-NSDIISIMGLSANVEQAKIKLQKRVKSL 1026
Cdd:cd22417     1 FTLTVEVDPKYHPKIIGRKGAVITKLRDDHDVNIQFPDKGDeNDDEITITGYEKNAEAAKDAILKIVQEL 70
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 572-633 3.31e-09

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: 54.11  E-value: 3.31e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 269784766  572 SVPIIKKLHKRIIGKGVSNIRKISEATNTKITFPPESCNSEEFIITGYPENCEIARNWILSL 633
Cdd:cd02394     5 TIEIDPKFHGHIIGKGGANIKRIREESGVSIRIPDDEANSDEIRIEGSPEGVKKAKAEILEL 66
KH-I_Vigilin_rpt13 cd22416
thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 1126-1175 4.12e-09

thirteenth 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 thirteenth one.


Pssm-ID: 411844 [Multi-domain]  Cd Length: 78  Bit Score: 54.16  E-value: 4.12e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 269784766 1126 VIGVRGKTINKIMDQYQVDIRLPPKGLYNPNITVTGLADNVEKAIEHILN 1175
Cdd:cd22416    16 IIGQKGADVRKMMDEFDVNISIPPAELQSDIIKITGPPANVERAKAALLE 65
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 1113-1175 6.50e-09

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: 53.44  E-value: 6.50e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784766  1113 SKEITLNQQVRGNVIGVRGKTINKIMDQYQVDIRLPPKGLYNPN--ITVTGLADNVEKAIEHILN 1175
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNEriVTITGTPEAVEAAKALIEE 65
KH-I_Vigilin_rpt9 cd22412
ninth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 788-853 1.34e-08

ninth 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 ninth one.


Pssm-ID: 411840  Cd Length: 70  Bit Score: 52.68  E-value: 1.34e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 269784766  788 VDDSILINRRFHHYFVMRRGQLLKEMAEDYGGVVITFSYSGRQNTKVTIRGAKPCVEAAKKHIKEI 853
Cdd:cd22412     2 VEVEVEIPAKLHNSLIGAKGRLIRSIMEECGGVHIHFPPEGSGSDKVTIRGPKEDVEKAKKQLLEL 67
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 1114-1174 2.67e-08

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: 51.53  E-value: 2.67e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269784766 1114 KEITLNQQVRGNVIGVRGKTINKIMDQYQVDIRLPPKGLYNPN--ITVTGLADNVEKAIEHIL 1174
Cdd:cd00105     1 EEIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSGErvVTITGTPEAVEKAKELIE 63
KH-I_Vigilin_rpt7 cd22410
seventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 787-853 5.23e-08

seventh 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 seventh one.


Pssm-ID: 411838  Cd Length: 67  Bit Score: 50.74  E-value: 5.23e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269784766  787 EVDDSILINRRFHHYFVMRRGQLLKEMAEDYGGVVITFSYSGRQNTKVTIRGAKPCVEAAKKHIKEI 853
Cdd:cd22410     1 EKTKDIIIEQRFHRTIIGQKGEKIREIRDKFPQVQITFPDPGSKSDVVTLRGPKDEVDKCYKYLKKL 67
KH-I_Vigilin_rpt15 cd22418
fifteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 569-636 5.28e-08

fifteenth 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 fifteenth one.


Pssm-ID: 411846 [Multi-domain]  Cd Length: 69  Bit Score: 50.73  E-value: 5.28e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269784766  569 YSISVPIIKKLHKRIIGKGVSNIRKISEATNTKITFP-PESCNSEEFIITGYPENCEIARNWILSLQQE 636
Cdd:cd22418     1 VTEEVEIDSRVHPRLIGARGKAIRKIMEDFKVDIRFPrSGDADPNLVTITGLEENVEECKDHLLNLEEE 69
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 717-782 9.51e-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: 50.26  E-value: 9.51e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 269784766  717 ETLHIKSKYHQFLLNKNGGNISKICDETGTCVFFPNPTNKDQEtITITGTEESVKEVQKQLDDLVK 782
Cdd:cd02394     4 TTIEIDPKFHGHIIGKGGANIKRIREESGVSIRIPDDEANSDE-IRIEGSPEGVKKAKAEILELVD 68
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 717-778 1.17e-07

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: 49.60  E-value: 1.17e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269784766  717 ETLHIKSKYHQFLLNKNGGNISKICDETGTCVFFPNPTNKDQE-TITITGTEESVKEVQKQLD 778
Cdd:cd00105     1 EEIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSGErVVTITGTPEAVEKAKELIE 63
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 959-1021 1.37e-07

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: 49.59  E-value: 1.37e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784766   959 TTEVHVPLHLQPYIIGHKGSGLRKLVKEYEVHMQV--SQPGKNSDIISIMGLSANVEQAKIKLQK 1021
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIppSESEGNERIVTITGTPEAVEAAKALIEE 65
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 1123-1180 2.52e-07

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: 49.13  E-value: 2.52e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 269784766 1123 RGNVIGVRGKTINKIMDQYQVDIRLPPKGLYNPN-ITVTGLADNVEKAIEHILNLEKYY 1180
Cdd:cd22417    12 HPKIIGRKGAVITKLRDDHDVNIQFPDKGDENDDeITITGYEKNAEAAKDAILKIVQEL 70
KH-I_Vigilin_rpt13 cd22416
thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 571-643 2.96e-07

thirteenth 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 thirteenth one.


Pssm-ID: 411844 [Multi-domain]  Cd Length: 78  Bit Score: 49.15  E-value: 2.96e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269784766  571 ISVPIikKLHKRIIGKGVSNIRKISEATNTKITFPPESCNSEEFIITGYPENCEIARNWILSLQQELADTAEE 643
Cdd:cd22416     6 VNVPF--DLHRFIIGQKGADVRKMMDEFDVNISIPPAELQSDIIKITGPPANVERAKAALLERVKELEAEKED 76
KH-I_Vigilin_rpt7 cd22410
seventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 363-405 3.49e-07

seventh 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 seventh one.


Pssm-ID: 411838  Cd Length: 67  Bit Score: 48.43  E-value: 3.49e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 269784766  363 LHRFIIGTKGEEISEITECVPKVQIHF----TAKDKITLKGPIDDVN 405
Cdd:cd22410    12 FHRTIIGQKGEKIREIRDKFPQVQITFpdpgSKSDVVTLRGPKDEVD 58
KH-I_Vigilin_rpt5 cd22409
fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 958-1028 4.08e-07

fifth 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 fifth one.


Pssm-ID: 411837 [Multi-domain]  Cd Length: 70  Bit Score: 48.35  E-value: 4.08e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 269784766  958 VTTEVHVPLHLQPYIIGHKGSGLRKLVKEYE-VHMQVSqpgKNSDIISIMGLSANVEQAKIKLQKRVKSLQM 1028
Cdd:cd22409     2 VVAEVSAPSWLHRFIIGKKGANIKKITQDLPkVHIEFT---EGEDKIELEGPPEEVEVVREQLEAIVKELVA 70
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 1114-1176 4.34e-07

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: 48.34  E-value: 4.34e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269784766 1114 KEITLNQQVRGNVIGVRGKTINKIMDQYQVDIRLPPKGLYNPNITVTGLADNVEKAIEHILNL 1176
Cdd:cd02394     4 TTIEIDPKFHGHIIGKGGANIKRIREESGVSIRIPDDEANSDEIRIEGSPEGVKKAKAEILEL 66
KH smart00322
K homology RNA-binding domain;
713-781 5.14e-07

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 48.06  E-value: 5.14e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269784766    713 KNYSETLHIKSKYHQFLLNKNGGNISKICDETGTCVFFPNPTNKDqETITITGTEESVKEVQKQLDDLV 781
Cdd:smart00322    1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEE-RVVEITGPPENVEKAAELILEIL 68
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 1126-1174 6.94e-07

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: 47.55  E-value: 6.94e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 269784766 1126 VIGVRGKTINKIMDQYQVDIRLPPKGLYNPNITVTGLADNVEKAIEHIL 1174
Cdd:cd22408    14 VIGPRGSTIQEILEETGCSVEVPPNDSDSETITLRGPADKLGAALTLVY 62
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 718-786 1.32e-06

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: 47.20  E-value: 1.32e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269784766  718 TLHIKSKYHQFLLNKNGGNISKICDETGTCVFFPNPTNKDQETITITGTEESVKEVQKQLDDLVKDFEN 786
Cdd:cd22417     4 TVEVDPKYHPKIIGRKGAVITKLRDDHDVNIQFPDKGDENDDEITITGYEKNAEAAKDAILKIVQELES 72
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 1113-1174 1.32e-06

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: 46.81  E-value: 1.32e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 269784766 1113 SKEITLNQQVRGNVIGVRGKTINKIMDQYQVDIRLPPKGLYNPNITVTGLADNVEKAIEHIL 1174
Cdd:cd22411     1 SIKVPIFKQFHKNIIGKGGATIKKIREETNTRIDLPEENSDSDVITITGKKEDVEKARERIL 62
KH-I_Vigilin_rpt10 cd22413
tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 578-627 2.69e-06

tenth 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 tenth one.


Pssm-ID: 411841 [Multi-domain]  Cd Length: 66  Bit Score: 46.10  E-value: 2.69e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 269784766  578 KLHKRIIGKGVSNIRKISEATNTKITFPPESCNSEEFI-ITGYPENCEIAR 627
Cdd:cd22413    12 EYHRFLIGRGGANIRKIRDNTGARIIFPTARDEDQELItIIGTKEAVEKAK 62
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 961-1020 3.13e-06

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: 45.75  E-value: 3.13e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 269784766  961 EVHVPLHLQPYIIGHKGSGLRKLVKEYEVHMQVSQPGKNSD--IISIMGLSANVEQAKIKLQ 1020
Cdd:cd00105     2 EIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSGerVVTITGTPEAVEKAKELIE 63
KH-I_ScSCP160_rpt6 cd22451
sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 570-636 3.66e-06

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: 45.91  E-value: 3.66e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269784766  570 SISVPIIKKLHKRIIGKGVSNIRKISEATNTKITFPPESCNSEEFIITGYPENCEIARNWILSLQQE 636
Cdd:cd22451     2 SIDIDIPKEYHRAIIGKGGAVLRELEAETGCRIQVPKKDDPSGKIRITGARDGVEAATAKILNISDE 68
KH-I_Vigilin_rpt9 cd22412
ninth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 356-407 5.26e-06

ninth 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 ninth one.


Pssm-ID: 411840  Cd Length: 70  Bit Score: 45.36  E-value: 5.26e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 269784766  356 SIFAPSWLHRFIIGTKGEEISEITECVPKVQIHF----TAKDKITLKGPIDDVNYA 407
Cdd:cd22412     5 EVEIPAKLHNSLIGAKGRLIRSIMEECGGVHIHFppegSGSDKVTIRGPKEDVEKA 60
KH-I_Vigilin_rpt13 cd22416
thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 505-566 5.47e-06

thirteenth 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 thirteenth one.


Pssm-ID: 411844 [Multi-domain]  Cd Length: 78  Bit Score: 45.30  E-value: 5.47e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 269784766  505 FHHILIGQKGERVREICKKFpDVILNFPHPAEKSDIVQLIGPRYESEKCAQYLENMLTDIKE 566
Cdd:cd22416    12 LHRFIIGQKGADVRKMMDEF-DVNISIPPAELQSDIIKITGPPANVERAKAALLERVKELEA 72
KH-I_Vigilin_rpt15 cd22418
fifteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 958-1016 5.88e-06

fifteenth 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 fifteenth one.


Pssm-ID: 411846 [Multi-domain]  Cd Length: 69  Bit Score: 44.95  E-value: 5.88e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784766  958 VTTEVHVPLHLQPYIIGHKGSGLRKLVKEYEVHMQVSQPG-KNSDIISIMGLSANVEQAK 1016
Cdd:cd22418     1 VTEEVEIDSRVHPRLIGARGKAIRKIMEDFKVDIRFPRSGdADPNLVTITGLEENVEECK 60
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 1042-1102 8.77e-06

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: 44.60  E-value: 8.77e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 269784766 1042 FNLDPKYQAKITGHKGLLITQICTEHDVTIHFPKKGTHDMQEQITITGYKENTLAARDAIM 1102
Cdd:cd00105     3 IEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSGERVVTITGTPEAVEKAKELIE 63
KH-I_ScSCP160_rpt3 cd22448
third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 426-487 1.10e-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: 44.82  E-value: 1.10e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269784766  426 EINSDSKFYKYLTGNNGEILNRITEKNQVSITMFPENESNYS-----------IRIEGESLGVHQAKKELLDL 487
Cdd:cd22448     6 ILKIPVQFHGSLIGQQGKYVNRLQEKYGVKINFPRENSSSNDtetkkpqapdeVTIRGGKKGVAEAKQELLEL 78
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 959-1018 1.29e-05

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: 44.08  E-value: 1.29e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784766  959 TTEVHVPLHLQPYIIGHKGSGLRKLVKEYEVHMQVSQPGKNSDIISIMGLSANVEQAKIK 1018
Cdd:cd22408     1 TVSVEVPKSQHRFVIGPRGSTIQEILEETGCSVEVPPNDSDSETITLRGPADKLGAALTL 60
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 1042-1102 1.59e-05

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: 43.81  E-value: 1.59e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 269784766  1042 FNLDPKYQAKITGHKGLLITQICTEHDVTIHFPKKGTHDMQEQITITGYKENTLAARDAIM 1102
Cdd:pfam00013    4 ILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNERIVTITGTPEAVEAAKALIE 64
KH-I_IGF2BP_rpt2 cd22401
second type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
 582-630 1.68e-05

second type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 mRNA-binding protein (IGF2BP) family; The IGF2BP family includes three members: IGF2BP1/IMP-1/ CRD-BP/ VICKZ1, IGF2BP2/IMP-2/ VICKZ2, and IGF2BP3/IMP-3/VICKZ3, which are RNA-binding factors that recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). They function by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. IGF2BP proteins contain 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 second one.


Pssm-ID: 411829 [Multi-domain]  Cd Length: 72  Bit Score: 43.75  E-value: 1.68e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 269784766  582 RIIGKGVSNIRKISEATNTKITF----PPESCNSEEFI-ITGYPENCEIARNWI 630
Cdd:cd22401    13 RLIGKDGRNIKKIMEDTNTKITIsslqDLTSYNPERTItIKGSLEAMSEAESLI 66
KH-I_Vigilin_rpt15 cd22418
fifteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 715-777 1.87e-05

fifteenth 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 fifteenth one.


Pssm-ID: 411846 [Multi-domain]  Cd Length: 69  Bit Score: 43.79  E-value: 1.87e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269784766  715 YSETLHIKSKYHQFLLNKNGGNISKICDETGTCVFFPNPTNKDQETITITGTEESVKEVQKQL 777
Cdd:cd22418     1 VTEEVEIDSRVHPRLIGARGKAIRKIMEDFKVDIRFPRSGDADPNLVTITGLEENVEECKDHL 63
KH smart00322
K homology RNA-binding domain;
493-561 3.06e-05

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 43.05  E-value: 3.06e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269784766    493 EEYSQDIIIKHQFHHILIGQKGERVREICKKFpDVILNFPHPAEKSDIVQLIGPRYESEKCAQYLENML 561
Cdd:smart00322    1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEET-GVKIDIPGPGSEERVVEITGPPENVEKAAELILEIL 68
KH-I_Vigilin_rpt15 cd22418
fifteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 495-560 3.30e-05

fifteenth 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 fifteenth one.


Pssm-ID: 411846 [Multi-domain]  Cd Length: 69  Bit Score: 43.02  E-value: 3.30e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269784766  495 YSQDIIIKHQFHHILIGQKGERVREICKKFpDVILNFPHP-AEKSDIVQLIGPRYESEKCAQYLENM 560
Cdd:cd22418     1 VTEEVEIDSRVHPRLIGARGKAIRKIMEDF-KVDIRFPRSgDADPNLVTITGLEENVEECKDHLLNL 66
KH-I_ScSCP160_rpt7 cd22452
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 1124-1174 3.42e-05

seventh 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 seventh one.


Pssm-ID: 411880 [Multi-domain]  Cd Length: 65  Bit Score: 42.69  E-value: 3.42e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 269784766 1124 GNVIGVRGKTINKIMDQYQVDIRLPPKGLYNPNITVTGLADNVEKAIEHIL 1174
Cdd:cd22452    14 GRIIGPGGSNINQIREKSGCFINVPKKNKESDVITLRGTKEGVEKAEEMIK 64
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 716-777 3.90e-05

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: 42.58  E-value: 3.90e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 269784766  716 SETLHIKSKYHQFLLNKNGGNISKICDETGTCVFFPNpTNKDQETITITGTEESVKEVQKQL 777
Cdd:cd22411     1 SIKVPIFKQFHKNIIGKGGATIKKIREETNTRIDLPE-ENSDSDVITITGKKEDVEKARERI 61
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 570-630 3.95e-05

second 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 second one.


Pssm-ID: 411875 [Multi-domain]  Cd Length: 80  Bit Score: 43.18  E-value: 3.95e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 269784766  570 SISVPIIKKLHKRIIGKGVSNIRKISEATNTKITFPPESCNSE----------EFIITGYPENCEIARNWI 630
Cdd:cd22447     5 NLTVPIPASTRARIIGKKGANLKQIREKTGVRIDIPPRDADAApadedddtmvEVTITGDEFNVQHAKQRI 75
KH-I_Vigilin_rpt3 cd22407
third type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 424-484 4.55e-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: 42.20  E-value: 4.55e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 269784766  424 YTEINSDSKFYKYLTGNNGEILNRITEKNQVSITMFPENESNYSIRIEGESLGVHQAKKEL 484
Cdd:cd22407     1 TERLDIPKVYHPFIAGPNNENVKELQEETGVRINIPPPSVNKDEIVVSGEKEGVAQAVAKI 61
KH-I_IGF2BP_rpt1 cd22400
first type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
 582-631 4.56e-05

first type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 mRNA-binding protein (IGF2BP) family; The IGF2BP family includes three members: IGF2BP1/IMP-1/ CRD-BP/ VICKZ1, IGF2BP2/IMP-2/ VICKZ2, and IGF2BP3/IMP-3/VICKZ3, which are RNA-binding factors that recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). They function by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. IGF2BP proteins contain 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: 411828 [Multi-domain]  Cd Length: 68  Bit Score: 42.64  E-value: 4.56e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 269784766  582 RIIGKGVSNIRKISEATNTKITF--PPESCNSEEFI-ITGYPENCEIARNWIL 631
Cdd:cd22400    13 AIIGKGGATIRQITQQTGARIDIhrKENAGAAEKAItIYGTPEGCSSACKQIL 65
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 957-1016 5.19e-05

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: 42.56  E-value: 5.19e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784766  957 PVTTEVHVPLHLQPYIIGHKGSGLRKLVKEYEVHMQVSQPGKNSDIISIMGLSANVEQAK 1016
Cdd:cd02394     1 MAFTTIEIDPKFHGHIIGKGGANIKRIREESGVSIRIPDDEANSDEIRIEGSPEGVKKAK 60
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 718-773 6.78e-05

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: 41.77  E-value: 6.78e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 269784766  718 TLHIKSKYHQFLLNKNGGNISKICDETGTCVFFPnPTNKDQETITITGTEESVKEV 773
Cdd:cd22408     3 SVEVPKSQHRFVIGPRGSTIQEILEETGCSVEVP-PNDSDSETITLRGPADKLGAA 57
KH-I_ScSCP160_rpt6 cd22451
sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 641-710 7.15e-05

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: 42.06  E-value: 7.15e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784766  641 AEEEIIIPANLYKHLTNPKECLLNSIIEECGkIHLHFPKGKSNLNKIIIMGTIENVEKAKTKLLKLSEEE 710
Cdd:cd22451     1 ASIDIDIPKEYHRAIIGKGGAVLRELEAETG-CRIQVPKKDDPSGKIRITGARDGVEAATAKILNISDEE 69
KH-I_Vigilin_rpt2 cd22406
second type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 711-782 7.22e-05

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: 42.30  E-value: 7.22e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 269784766  711 QAKNYSETLHIKSKYHQFLLNKNGGNISKICDETGTCVFFPNPTnKDQETITITGTEESV----KEVQKQLDDLVK 782
Cdd:cd22406     1 LQTQASVTVNIPKEHHRFILGKKGKKLQELELKTATKIVIPRQE-DNSDEIKITGTKEGIekarHEIQLISDEQAK 75
KH-I_ScSCP160_rpt7 cd22452
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 722-771 7.51e-05

seventh 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 seventh one.


Pssm-ID: 411880 [Multi-domain]  Cd Length: 65  Bit Score: 41.92  E-value: 7.51e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 269784766  722 KSKYHQFLLNKNGGNISKICDETGTCVFFPNpTNKDQETITITGTEESVK 771
Cdd:cd22452     9 SPRYFGRIIGPGGSNINQIREKSGCFINVPK-KNKESDVITLRGTKEGVE 57
KH-I_Vigilin_rpt9 cd22412
ninth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 498-557 7.59e-05

ninth 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 ninth one.


Pssm-ID: 411840  Cd Length: 70  Bit Score: 41.90  E-value: 7.59e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784766  498 DIIIKHQFHHILIGQKGERVREICKKFPDVILNFPHPAEKSDIVQLIGPRYESEKCAQYL 557
Cdd:cd22412     5 EVEIPAKLHNSLIGAKGRLIRSIMEECGGVHIHFPPEGSGSDKVTIRGPKEDVEKAKKQL 64
KH-I_Vigilin_rpt9 cd22412
ninth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 571-636 9.41e-05

ninth 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 ninth one.


Pssm-ID: 411840  Cd Length: 70  Bit Score: 41.90  E-value: 9.41e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269784766  571 ISVPIIKKLHKRIIGKGVSNIRKISE-ATNTKITFPPESCNSEEFIITGYPENCEIARNWILSLQQE 636
Cdd:cd22412     4 VEVEIPAKLHNSLIGAKGRLIRSIMEeCGGVHIHFPPEGSGSDKVTIRGPKEDVEKAKKQLLELANE 70
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 959-1024 9.67e-05

fourth 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 fourth one.


Pssm-ID: 411877 [Multi-domain]  Cd Length: 70  Bit Score: 41.87  E-value: 9.67e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 269784766  959 TTEVHVPLHLQPYIIGHKGSGLRKLVKEYEVHMQVSQPGKNSDiISIMGLSANVEQAKIKLQKRVK 1024
Cdd:cd22449     5 TVKFDVPAKYVPHIIGKKGANINKLREEYGVKIDFEDKTGEGN-VEIKGSKKNVEEAKKRILSQID 69
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 642-705 9.96e-05

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: 41.50  E-value: 9.96e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784766   642 EEEIIIPANLYKHLTNPKECLLNSIIEECG-KIHLHFPKGKSNLNKIIIMGTIENVEKAKTKLLK 705
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGaKIQIPPSESEGNERIVTITGTPEAVEAAKALIEE 65
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 791-852 1.42e-04

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: 41.11  E-value: 1.42e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269784766   791 SILINRRFHHYFVMRRGQLLKEMAEDYG-GVVITFSYSGRQNTKVTIRGAKPCVEAAKKHIKE 852
Cdd:pfam00013    3 EILVPSSLVGLIIGKGGSNIKEIREETGaKIQIPPSESEGNERIVTITGTPEAVEAAKALIEE 65
KH-I_Vigilin_rpt5 cd22409
fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 505-566 1.51e-04

fifth 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 fifth one.


Pssm-ID: 411837 [Multi-domain]  Cd Length: 70  Bit Score: 41.03  E-value: 1.51e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 269784766  505 FHHILIGQKGERVREICKKFPDVILNFPhpaEKSDIVQLIGPRYESEKCAQYLENMLTDIKE 566
Cdd:cd22409    12 LHRFIIGKKGANIKKITQDLPKVHIEFT---EGEDKIELEGPPEEVEVVREQLEAIVKELVA 70
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 1045-1101 1.99e-04

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: 40.63  E-value: 1.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 269784766 1045 DPKYQAKITGHKGLLITQICTEHDVTIHFPKKGTHDMqeQITITGYKENTLAARDAI 1101
Cdd:cd02394     9 DPKFHGHIIGKGGANIKRIREESGVSIRIPDDEANSD--EIRIEGSPEGVKKAKAEI 63
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
 1077-1176 2.02e-04

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 45.81  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784766 1077 GTHD----MQEQITITGYKENTLA-----ARDAIMRLLHKIEKTISKE-------------ITLNQQVRGNVIGVRGKTI 1134
Cdd:PRK11824  497 GTRDgitaLQMDIKIDGITREILEealeqAKEGRLHILGKMNEAISEPraelspyaprietIKIPPDKIRDVIGPGGKTI 576

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 269784766 1135 NKIMDQYQVDIRLPPKGlynpNITVTGL-ADNVEKAIEHILNL 1176
Cdd:PRK11824  577 REITEETGAKIDIEDDG----TVKIAATdGEAAEAAKERIEGI 615
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 495-566 2.14e-04

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: 40.65  E-value: 2.14e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269784766  495 YSQDIIIKHQFHHILIGQKGERVREICKKFpDVILNFPHP-AEKSDIVQLIGPRYESEKCAQYLENMLTDIKE 566
Cdd:cd22417     1 FTLTVEVDPKYHPKIIGRKGAVITKLRDDH-DVNIQFPDKgDENDDEITITGYEKNAEAAKDAILKIVQELES 72
KH-I_FUBP_rpt3 cd22398
third type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
 570-630 2.43e-04

third type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding proteins; The far upstream element-binding protein (FUBP) family includes FUBP1-3. FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP proteins contain four K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411826 [Multi-domain]  Cd Length: 67  Bit Score: 40.32  E-value: 2.43e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269784766  570 SISVPIIKKLHKRIIGKGVSNIRKISEATNTKITFPPESCNSEEFI--ITGYPENCEIARNWI 630
Cdd:cd22398     1 GMEVPVPRFAVGVVIGKGGEMIKKIQNETGARVQFKPDDGNSPDRIcvITGPPDQVQHAARMI 63
KH-I_Vigilin_rpt15 cd22418
fifteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 642-709 2.45e-04

fifteenth 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 fifteenth one.


Pssm-ID: 411846 [Multi-domain]  Cd Length: 69  Bit Score: 40.71  E-value: 2.45e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269784766  642 EEEIIIPANLYKHLTNPKECLLNSIIEECgKIHLHFPK-GKSNLNKIIIMGTIENVEKAKTKLLKLSEE 709
Cdd:cd22418     2 TEEVEIDSRVHPRLIGARGKAIRKIMEDF-KVDIRFPRsGDADPNLVTITGLEENVEECKDHLLNLEEE 69
KH-I_IGF2BP_rpt3 cd22402
third type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
 583-630 3.30e-04

third type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 mRNA-binding protein (IGF2BP) family; The IGF2BP family includes three members: IGF2BP1/IMP-1/ CRD-BP/ VICKZ1, IGF2BP2/IMP-2/ VICKZ2, and IGF2BP3/IMP-3/VICKZ3, which are RNA-binding factors that recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). They function by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. IGF2BP proteins contain 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 third one.


Pssm-ID: 411830 [Multi-domain]  Cd Length: 66  Bit Score: 39.93  E-value: 3.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 269784766  583 IIGKGVSNIRKISEATNTKITF-PPESCNSEE--FIITGYPENCEIARNWI 630
Cdd:cd22402    15 IIGTKGSHIRYIKRFSGASIKIaPADSPDAPErkVTITGPPEAQWKAQLCI 65
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 718-782 3.51e-04

second 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 second one.


Pssm-ID: 411875 [Multi-domain]  Cd Length: 80  Bit Score: 40.48  E-value: 3.51e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269784766  718 TLHIKSKYHQFLLNKNGGNISKICDETGTCVFFPN------PTNKDQET---ITITGTEESVKEVQKQLDDLVK 782
Cdd:cd22447     7 TVPIPASTRARIIGKKGANLKQIREKTGVRIDIPPrdadaaPADEDDDTmveVTITGDEFNVQHAKQRIEEIIS 80
KH-I_ScSCP160_rpt3 cd22448
third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 493-561 3.95e-04

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: 40.20  E-value: 3.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784766  493 EEYSQDIIIKHQFHHILIGQKGERVREICKKFpDVILNFP-----------HPAEKSDIVQLIGPRYESEKCAQYLENML 561
Cdd:cd22448     1 DETTLILKIPVQFHGSLIGQQGKYVNRLQEKY-GVKINFPrensssndtetKKPQAPDEVTIRGGKKGVAEAKQELLELL 79
KH-I_Vigilin_rpt13 cd22416
thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 716-790 4.16e-04

thirteenth 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 thirteenth one.


Pssm-ID: 411844 [Multi-domain]  Cd Length: 78  Bit Score: 40.29  E-value: 4.16e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784766  716 SETLHIKSKYHQFLLNKNGGNISKICDETGTCVFFPnPTNKDQETITITGTEESVKEVQKQLDDLVKDFENEVDD 790
Cdd:cd22416     3 TEEVNVPFDLHRFIIGQKGADVRKMMDEFDVNISIP-PAELQSDIIKITGPPANVERAKAALLERVKELEAEKED 76
KH-I_Vigilin_rpt3 cd22407
third type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 1043-1102 4.58e-04

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: 39.50  E-value: 4.58e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784766 1043 NLDPKYQAKITGHKGLLITQICTEHDVTIHFPKkgTHDMQEQITITGYKENTLAARDAIM 1102
Cdd:cd22407     5 DIPKVYHPFIAGPNNENVKELQEETGVRINIPP--PSVNKDEIVVSGEKEGVAQAVAKIK 62
KH-I_MEX3_rpt2 cd22424
second type I K homology (KH) RNA-binding domain found in the family of MEX-3 RNA-binding ...
 1112-1173 4.91e-04

second type I K homology (KH) RNA-binding domain found in the family of MEX-3 RNA-binding proteins; The MEX-3 protein family includes four members, MEX3A/RKHD4, MEX3B/RKHD3/RNF195, MEX3C/ RKHD2/RNF194, and MEX3D/RKHD1/RNF193/TINO. They are homologous of Caenorhabditis elegans MEX-3 protein, a translational regulator that specifies the posterior blastomere identity in the early embryo and contributes to the maintenance of the germline totipotency. Mex-3 proteins are RNA-binding phosphoproteins involved in post-transcriptional regulatory mechanisms. They are characterized by containing two K-homology (KH) RNA-binding domains and a C-terminal RING finger. They bind RNA through their KH domains and shuttle between the nucleus and the cytoplasm via the CRM1-dependent export pathway. The model corresponds to the second KH domain.


Pssm-ID: 411852 [Multi-domain]  Cd Length: 72  Bit Score: 39.63  E-value: 4.91e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 269784766 1112 ISKEITLNQQVRGNVIGVRGKTINKIMDQYQVDIRLPPKGLyNPNITVTGLADNVEKAIEHI 1173
Cdd:cd22424     4 TTIQVRVPYRVVGLVVGPKGATIKRIQQQTHTYIVTPSRDK-EPVFEVTGMPENVERAREEI 64
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 496-559 5.73e-04

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: 39.19  E-value: 5.73e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 269784766   496 SQDIIIKHQFHHILIGQKGERVREICKKFpDVILNFPHPA--EKSDIVQLIGPRYESEKCAQYLEN 559
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREET-GAKIQIPPSEseGNERIVTITGTPEAVEAAKALIEE 65
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 425-486 6.44e-04

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: 39.19  E-value: 6.44e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269784766   425 TEINSDSKFYKYLTGNNGEILNRITEKNQVSITMFPENESNYS--IRIEGESLGVHQAKKELLD 486
Cdd:pfam00013    2 VEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNEriVTITGTPEAVEAAKALIEE 65
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 566-636 7.17e-04

fourth 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 fourth one.


Pssm-ID: 411877 [Multi-domain]  Cd Length: 70  Bit Score: 39.17  E-value: 7.17e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 269784766  566 ENNYSISVPIIKKLHKRIIGKGVSNIRKISEATNTKITFpPESCNSEEFIITGYPENCEIARNWILSLQQE 636
Cdd:cd22449     1 ENGYTVKFDVPAKYVPHIIGKKGANINKLREEYGVKIDF-EDKTGEGNVEIKGSKKNVEEAKKRILSQIDE 70
KH-I_Vigilin_rpt3 cd22407
third type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 717-773 7.79e-04

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: 38.73  E-value: 7.79e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 269784766  717 ETLHIKSKYHQFLLNKNGGNISKICDETGTCVFFPNPTNKDQEtITITGTEESVKEV 773
Cdd:cd22407     2 ERLDIPKVYHPFIAGPNNENVKELQEETGVRINIPPPSVNKDE-IVVSGEKEGVAQA 57
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 1122-1173 7.93e-04

second 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 second one.


Pssm-ID: 411875 [Multi-domain]  Cd Length: 80  Bit Score: 39.32  E-value: 7.93e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 269784766 1122 VRGNVIGVRGKTINKIMDQYQVDIRLPPKGLYNP----------NITVTGLADNVEKAIEHI 1173
Cdd:cd22447    14 TRARIIGKKGANLKQIREKTGVRIDIPPRDADAApadedddtmvEVTITGDEFNVQHAKQRI 75
KH-I_Mextli_like cd22454
type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic ...
 566-633 8.34e-04

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: 39.22  E-value: 8.34e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784766  566 ENNYSISVPIIKKLHKRIIGKGVSNIRKISEATNTKITF--PPESCNSEEFIITGYPENCEIARNWILSL 633
Cdd:cd22454     1 TGQTTIEVVIPNADVGKVIGKGGETIKRIEALTDTVITFerVNGGSPNREVQITGSPDNVAAAKRLIEDT 70
KH-I_FUBP_rpt1 cd22396
first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
 582-630 8.46e-04

first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding proteins; The far upstream element-binding protein (FUBP) family includes FUBP1-3. FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP proteins contain four K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411824 [Multi-domain]  Cd Length: 68  Bit Score: 39.16  E-value: 8.46e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 269784766  582 RIIGKGVSNIRKISEATNTKITFPPESCNSEE--FIITGYPENCEIARNWI 630
Cdd:cd22396    14 LIIGRGGEQINRLQAESGAKIQIAPDSGGLPErpCTLTGTPDAIETAKRLI 64
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 643-704 9.14e-04

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: 38.82  E-value: 9.14e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269784766  643 EEIIIPANLYKHLTNPKECLLNSIIEECG-KIHLHFPKGKSNLNKIIIMGTIENVEKAKTKLL 704
Cdd:cd00105     1 EEIEVPSELVGLIIGKGGSTIKEIEEETGaRIQIPKEGEGSGERVVTITGTPEAVEKAKELIE 63
KH-I_Vigilin_rpt7 cd22410
seventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 971-1021 9.70e-04

seventh 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 seventh one.


Pssm-ID: 411838  Cd Length: 67  Bit Score: 38.80  E-value: 9.70e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 269784766  971 YIIGHKGSGLRKLVKEY-EVHMQVSQPGKNSDIISIMGLSANVEQAKIKLQK 1021
Cdd:cd22410    15 TIIGQKGEKIREIRDKFpQVQITFPDPGSKSDVVTLRGPKDEVDKCYKYLKK 66
KH-I_Vigilin_rpt9 cd22412
ninth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 1115-1176 1.05e-03

ninth 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 ninth one.


Pssm-ID: 411840  Cd Length: 70  Bit Score: 38.81  E-value: 1.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269784766 1115 EITLNQQVRGNVIGVRGKTINKIMDQY-QVDIRLPPKGLYNPNITVTGLADNVEKAIEHILNL 1176
Cdd:cd22412     5 EVEIPAKLHNSLIGAKGRLIRSIMEECgGVHIHFPPEGSGSDKVTIRGPKEDVEKAKKQLLEL 67
KH-I_Vigilin_rpt7 cd22410
seventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 1113-1176 1.06e-03

seventh 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 seventh one.


Pssm-ID: 411838  Cd Length: 67  Bit Score: 38.80  E-value: 1.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784766 1113 SKEITLNQQVRGNVIGVRGKTINKIMDQY-QVDIRLPPKGLYNPNITVTGLADNVEKAIEHILNL 1176
Cdd:cd22410     3 TKDIIIEQRFHRTIIGQKGEKIREIRDKFpQVQITFPDPGSKSDVVTLRGPKDEVDKCYKYLKKL 67
KH-I_Vigilin_rpt3 cd22407
third type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 572-618 1.08e-03

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: 38.34  E-value: 1.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 269784766  572 SVPIIKKLHKRIIGKGVSNIRKISEATNTKITFPPESCNSEEFIITG 618
Cdd:cd22407     3 RLDIPKVYHPFIAGPNNENVKELQEETGVRINIPPPSVNKDEIVVSG 49
KH-I_Vigilin_rpt15 cd22418
fifteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 788-855 1.37e-03

fifteenth 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 fifteenth one.


Pssm-ID: 411846 [Multi-domain]  Cd Length: 69  Bit Score: 38.40  E-value: 1.37e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269784766  788 VDDSILINRRFHHYFVMRRGQLLKEMAEDYGgVVITFSYSG-RQNTKVTIRGAKPCVEAAKKHIKEIFE 855
Cdd:cd22418     1 VTEEVEIDSRVHPRLIGARGKAIRKIMEDFK-VDIRFPRSGdADPNLVTITGLEENVEECKDHLLNLEE 68
KH-I_ScSCP160_rpt6 cd22451
sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 716-771 1.68e-03

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: 38.20  E-value: 1.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 269784766  716 SETLHIKSKYHQFLLNKNGGNISKICDETGTCVFFPnptNKDQE--TITITGTEESVK 771
Cdd:cd22451     2 SIDIDIPKEYHRAIIGKGGAVLRELEAETGCRIQVP---KKDDPsgKIRITGARDGVE 56
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 356-410 1.72e-03

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: 38.03  E-value: 1.72e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 269784766   356 SIFAPSWLHRFIIGTKGEEISEITECVpKVQIHF------TAKDKITLKGPIDDVNYAQEK 410
Cdd:pfam00013    3 EILVPSSLVGLIIGKGGSNIKEIREET-GAKIQIppseseGNERIVTITGTPEAVEAAKAL 62
KH-I_Vigilin_rpt5 cd22409
fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 579-637 1.83e-03

fifth 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 fifth one.


Pssm-ID: 411837 [Multi-domain]  Cd Length: 70  Bit Score: 37.95  E-value: 1.83e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784766  579 LHKRIIGKGVSNIRKISEAT-NTKITFPPESCnseEFIITGYPENCEIARNWILSLQQEL 637
Cdd:cd22409    12 LHRFIIGKKGANIKKITQDLpKVHIEFTEGED---KIELEGPPEEVEVVREQLEAIVKEL 68
KH-I_Vigilin_rpt9 cd22412
ninth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 958-1020 1.83e-03

ninth 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 ninth one.


Pssm-ID: 411840  Cd Length: 70  Bit Score: 38.04  E-value: 1.83e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269784766  958 VTTEVHVPLHLQPYIIGHKGSGLRKLVKEYE-VHMQVSQPGKNSDIISIMGLSANVEQAKIKLQ 1020
Cdd:cd22412     2 VEVEVEIPAKLHNSLIGAKGRLIRSIMEECGgVHIHFPPEGSGSDKVTIRGPKEDVEKAKKQLL 65
KH-I_ScSCP160_rpt6 cd22451
sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 1113-1175 1.92e-03

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: 38.20  E-value: 1.92e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269784766 1113 SKEITLNQQVRGNVIGVRGKTINKIMDQYQVDIRLPPKGLYNPNITVTGLADNVEKAIEHILN 1175
Cdd:cd22451     2 SIDIDIPKEYHRAIIGKGGAVLRELEAETGCRIQVPKKDDPSGKIRITGARDGVEAATAKILN 64
KH-I_Vigilin_rpt3 cd22407
third type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 1124-1173 2.02e-03

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: 37.57  E-value: 2.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 269784766 1124 GNVIGVRGKTINKIMDQYQVDIRLPPKGLYNPNITVTGLADNVEKAIEHI 1173
Cdd:cd22407    12 PFIAGPNNENVKELQEETGVRINIPPPSVNKDEIVVSGEKEGVAQAVAKI 61
KH-I_ScSCP160_rpt1 cd22446
first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 1107-1174 2.23e-03

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: 38.54  E-value: 2.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 269784766 1107 KIEKTISKEITLNQQVRGNVIGVRGKTINKIMDQYQVDIRLPPK---GLYNP-------NITVTGLADNVEKAIEHIL 1174
Cdd:cd22446     2 ELSPKVTITISVPSSVRGAIIGSRGKNLKSIQDKTGTKIQIPKRneeGNYDEddddetvEISIEGDAEGVELAKKEIE 79
KH smart00322
K homology RNA-binding domain;
642-706 2.36e-03

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 37.66  E-value: 2.36e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784766    642 EEEIIIPANLYKHLTNPKECLLNSIIEECGKiHLHFPKGKSNLNKIIIMGTIENVEKAKTKLLKL 706
Cdd:smart00322    4 TIEVLIPADKVGLIIGKGGSTIKKIEEETGV-KIDIPGPGSEERVVEITGPPENVEKAAELILEI 67
KH-I_ScSCP160_rpt6 cd22451
sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 958-1021 2.41e-03

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: 37.82  E-value: 2.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269784766  958 VTTEVHVPLHLQPYIIGHKGSGLRKLVKEYEVHMQVSQPGKNSDIISIMGLSANVEQAKIKLQK 1021
Cdd:cd22451     1 ASIDIDIPKEYHRAIIGKGGAVLRELEAETGCRIQVPKKDDPSGKIRITGARDGVEAATAKILN 64
KH-I_Vigilin_rpt5 cd22409
fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 643-712 2.53e-03

fifth 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 fifth one.


Pssm-ID: 411837 [Multi-domain]  Cd Length: 70  Bit Score: 37.56  E-value: 2.53e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784766  643 EEIIIPANLYKHLTNPKECLLNSIIEECGKIHLHFPKGKsnlNKIIIMGTIENVEKAKTKLLKLSEEEQA 712
Cdd:cd22409     4 AEVSAPSWLHRFIIGKKGANIKKITQDLPKVHIEFTEGE---DKIELEGPPEEVEVVREQLEAIVKELVA 70
KH-I_BICC1_rpt2 cd22421
second type I K homology (KH) RNA-binding domain found in protein bicaudal C homolog 1 (BICC1) ...
 580-630 2.67e-03

second type I K homology (KH) RNA-binding domain found in protein bicaudal C homolog 1 (BICC1) and similar proteins; BICC1, also called Bic-C, is a mammalian homologue of Drosophila Bicaudal-C (dBic-C). BICC1 functions as an RNA-binding protein that represses the translation of selected mRNAs to control development. It regulates gene expression and modulates cell proliferation and apoptosis. BICC1 is a negative regulator of Wnt signaling. Increased levels of BICC1 may be associated with depression. Besides, BICC1 is a genetic determinant of osteoblastogenesis and bone mineral density. BICC1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411849  Cd Length: 70  Bit Score: 37.71  E-value: 2.67e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 269784766  580 HKRIIGKGVSNIRKISEATNTKITFPpeSCN-------SEEFIITGYPENCEIARNWI 630
Cdd:cd22421    14 HSHVIGKGGNNIKKVMEDTGCHIHFP--DSNrtsqaekSNQVSIAGQPAGVESARAQI 69
KH-I_ASCC1 cd22419
type I K homology (KH) RNA-binding domain found in activating signal cointegrator 1 complex ...
 569-618 2.71e-03

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: 37.56  E-value: 2.71e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 269784766  569 YSISVPIIKKLHKRIIGKGVSNIRKISEATNTKITFPPESCNsEEFIITG 618
Cdd:cd22419     1 FRLSLDVPSALFKFIIGKKGETKKRLESETKTQIRIPRQGKE-GDIVITG 49
KH-I_ScSCP160_rpt7 cd22452
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 578-631 3.12e-03

seventh 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 seventh one.


Pssm-ID: 411880 [Multi-domain]  Cd Length: 65  Bit Score: 37.30  E-value: 3.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 269784766  578 KLHKRIIGKGVSNIRKISEATNTKITFPPESCNSEEFIITGYPENCEIARNWIL 631
Cdd:cd22452    11 RYFGRIIGPGGSNINQIREKSGCFINVPKKNKESDVITLRGTKEGVEKAEEMIK 64
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 1115-1176 3.70e-03

fourth 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 fourth one.


Pssm-ID: 411877 [Multi-domain]  Cd Length: 70  Bit Score: 37.25  E-value: 3.70e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 269784766 1115 EITLNQQVRGNVIGVRGKTINKIMDQYQVDIRLPPKGLYNpNITVTGLADNVEKAIEHILNL 1176
Cdd:cd22449     7 KFDVPAKYVPHIIGKKGANINKLREEYGVKIDFEDKTGEG-NVEIKGSKKNVEEAKKRILSQ 67
KH-I_Vigilin_rpt2 cd22406
second type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 958-1021 3.88e-03

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: 37.29  E-value: 3.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269784766  958 VTTEVHVPLHLQPYIIGHKGSGLRKLVKEYEVHMQVSQPGKNSDIISIMGLSANVEQAKIKLQK 1021
Cdd:cd22406     5 ASVTVNIPKEHHRFILGKKGKKLQELELKTATKIVIPRQEDNSDEIKITGTKEGIEKARHEIQL 68
KH-I_BTR1_rpt2 cd22437
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 ...
 1124-1175 5.12e-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: 36.81  E-value: 5.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 269784766 1124 GNVIGVRGKTINKIMDQYQVDIRLPPKGLYNPN-----ITVTGLADNVEKAIEHILN 1175
Cdd:cd22437    11 GLIIGKGGSTIKELREDSNANIKISPKDQLLPGsseriVTITGSFDQVVKAVALILE 67
KH-I_MEX3_rpt2 cd22424
second type I K homology (KH) RNA-binding domain found in the family of MEX-3 RNA-binding ...
 958-1016 5.84e-03

second type I K homology (KH) RNA-binding domain found in the family of MEX-3 RNA-binding proteins; The MEX-3 protein family includes four members, MEX3A/RKHD4, MEX3B/RKHD3/RNF195, MEX3C/ RKHD2/RNF194, and MEX3D/RKHD1/RNF193/TINO. They are homologous of Caenorhabditis elegans MEX-3 protein, a translational regulator that specifies the posterior blastomere identity in the early embryo and contributes to the maintenance of the germline totipotency. Mex-3 proteins are RNA-binding phosphoproteins involved in post-transcriptional regulatory mechanisms. They are characterized by containing two K-homology (KH) RNA-binding domains and a C-terminal RING finger. They bind RNA through their KH domains and shuttle between the nucleus and the cytoplasm via the CRM1-dependent export pathway. The model corresponds to the second KH domain.


Pssm-ID: 411852 [Multi-domain]  Cd Length: 72  Bit Score: 36.93  E-value: 5.84e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784766  958 VTTEVHVPLHLQPYIIGHKGSGLRKLvkEYEVHMQVSQPGKNSD-IISIMGLSANVEQAK 1016
Cdd:cd22424     4 TTIQVRVPYRVVGLVVGPKGATIKRI--QQQTHTYIVTPSRDKEpVFEVTGMPENVERAR 61
KH-I_ScSCP160_rpt1 cd22446
first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 568-636 5.95e-03

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: 37.00  E-value: 5.95e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269784766  568 NYSISVPIIKKLHkrIIGKGVSNIRKISEATNTKITFPPE----SCNSE------EFIITGYPENCEIARNWILSLQQE 636
Cdd:cd22446     8 TITISVPSSVRGA--IIGSRGKNLKSIQDKTGTKIQIPKRneegNYDEDdddetvEISIEGDAEGVELAKKEIEAIVKE 84
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 961-1020 6.18e-03

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: 36.41  E-value: 6.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784766  961 EVHVPLHLQPYIIGHKGSGLRKLVKEYEVHMQVSQPGKNSDIISIMGLSANVEQAKIKLQ 1020
Cdd:cd22411     3 KVPIFKQFHKNIIGKGGATIKKIREETNTRIDLPEENSDSDVITITGKKEDVEKARERIL 62
KH-I_Vigilin_rpt15 cd22418
fifteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 1043-1104 7.13e-03

fifteenth 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 fifteenth one.


Pssm-ID: 411846 [Multi-domain]  Cd Length: 69  Bit Score: 36.48  E-value: 7.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 269784766 1043 NLDPKYQAKITGHKGLLITQICTEHDVTIHFPKKGTHDmQEQITITGYKENTLAARDAIMRL 1104
Cdd:cd22418     6 EIDSRVHPRLIGARGKAIRKIMEDFKVDIRFPRSGDAD-PNLVTITGLEENVEECKDHLLNL 66
KH-I_ScSCP160_rpt6 cd22451
sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 1046-1103 7.77e-03

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: 36.28  E-value: 7.77e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 269784766 1046 PK-YQAKITGHKGLLITQICTEHDVTIHFPKKGthDMQEQITITGYKENTLAARDAIMR 1103
Cdd:cd22451     8 PKeYHRAIIGKGGAVLRELEAETGCRIQVPKKD--DPSGKIRITGARDGVEAATAKILN 64
KH-I_HNRNPK_rpt3 cd22434
third type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ...
 957-1028 8.93e-03

third type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ribonucleoprotein K (hnRNP K) and similar proteins; hnRNP K, also called transformation up-regulated nuclear protein (TUNP), is a pre-mRNA binding protein that binds tenaciously to poly(C) sequences. It may be involved in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. It can also bind poly(C) single-stranded DNA. hnRNP K plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. hnRNP K contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411862 [Multi-domain]  Cd Length: 74  Bit Score: 36.14  E-value: 8.93e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269784766  957 PVTTEVHVPLHLQPYIIGHKGSGLRKLVKEYEVHMQVSQPGKNSD--IISIMGLSANVEQAKIKLQKRVKSLQM 1028
Cdd:cd22434     1 TTTTQVTIPKDLAGSIIGKGGQRIRQIRHESGASIKIDEPLPGSEdrIITITGTQDQIQNAQYLLQNSVKQYSG 74
KH-I_HNRNPK_rpt3 cd22434
third type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ...
 568-617 9.57e-03

third type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ribonucleoprotein K (hnRNP K) and similar proteins; hnRNP K, also called transformation up-regulated nuclear protein (TUNP), is a pre-mRNA binding protein that binds tenaciously to poly(C) sequences. It may be involved in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. It can also bind poly(C) single-stranded DNA. hnRNP K plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. hnRNP K contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411862 [Multi-domain]  Cd Length: 74  Bit Score: 36.14  E-value: 9.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 269784766  568 NYSISVPIIKKLHKRIIGKGVSNIRKISEATNTKITFPPESCNSEEFIIT 617
Cdd:cd22434     1 TTTTQVTIPKDLAGSIIGKGGQRIRQIRHESGASIKIDEPLPGSEDRIIT 50
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH