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Conserved domains on  [gi|578804201|ref|XP_005247059|]
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vigilin isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KH-I_Vigilin_rpt12 cd22415
twelfth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
875-970 6.55e-45

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: 157.08  E-value: 6.55e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  875 TLECAIPQKFHRSVMGPKGSRIQQITRDFSVQIKFPDREENAVHSTEPvvqeNGDEAGEGREAKDCDPGSPRRCDIIIIS 954
Cdd:cd22415     1 TIECVIPQKFHRTVMGAKGSRVQQITSEFDVQIKFPDRESNQPAPAEN----GEGNGGEGVEGEAVDDNSPRKCDIIIIT 76
                          90
                  ....*....|....*.
gi 578804201  955 GRKEKCEAAKEALEAL 970
Cdd:cd22415    77 GKKENCEAAKEALLAL 92
KH-I_Vigilin_rpt13 cd22416
thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
972-1049 2.48e-40

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: 143.14  E-value: 2.48e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201  972 PVTIEVEVPFDLHRYVIGQKGSGIRKMMDEFEVNIHVPAPELQSDIIAITGLAANLDRAKAGLLERVKELQAEQEDRA 1049
Cdd:cd22416     1 PVTEEVNVPFDLHRFIIGQKGADVRKMMDEFDVNISIPPAELQSDIIKITGPPANVERAKAALLERVKELEAEKEDRE 78
KH-I_Vigilin_rpt11 cd22414
eleventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
802-867 3.19e-39

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: 139.75  E-value: 3.19e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201  802 EDSMLVDPKHHRHFVIRRGQVLREIAEEYGGVMVSFPRSGTQSDKVTLKGAKDCVEAAKKRIQEII 867
Cdd:cd22414     1 EDEMTVDPKHHRHFVARRGQVLREIADEYGGVMVSFPRSGTQSDKVTLKGAKDCVEGAKKRILEIV 66
KH-I_Vigilin_rpt9 cd22412
ninth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
653-722 4.00e-39

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: 139.74  E-value: 4.00e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  653 IAEVEVSIPAKLHNSLIGTKGRLIRSIMEECGGVHIHFPVEGSGSDTVVIRGPSSDVEKAKKQLLHLAEE 722
Cdd:cd22412     1 IVEVEVEIPAKLHNSLIGAKGRLIRSIMEECGGVHIHFPPEGSGSDKVTIRGPKEDVEKAKKQLLELANE 70
KH-I_Vigilin_rpt7 cd22410
seventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
507-573 7.48e-38

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: 135.87  E-value: 7.48e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201  507 ERTKDLIIEQRFHRTIIGQKGERIREIRDKFPEVIINFPDPAQKSDIVQLRGPKNEVEKCTKYMQKM 573
Cdd:cd22410     1 EKTKDIIIEQRFHRTIIGQKGEKIREIRDKFPQVQITFPDPGSKSDVVTLRGPKDEVDKCYKYLKKL 67
KH-I_Vigilin_rpt2 cd22406
second type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
147-221 2.16e-37

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: 134.75  E-value: 2.16e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201  147 LQTQASATVAIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPDDPSNQIKITGTKEGIEKARHEVLLISAEQDK 221
Cdd:cd22406     1 LQTQASVTVNIPKEHHRFILGKKGKKLQELELKTATKIVIPRQEDNSDEIKITGTKEGIEKARHEIQLISDEQAK 75
KH-I_Vigilin_rpt1 cd22405
first type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
77-144 1.34e-35

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: 129.34  E-value: 1.34e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201   77 TQVFHVPLEERKYKDMN-QFGEGEQAKICLEIMQRTGAHLELSLAKDQGLSIMVSGKLDAVMKARKDIV 144
Cdd:cd22405     1 TQVFHVPLEERRYKESNqQFGEGEQAKICKDIMQKTGATIELSSAKDQSLTIMVTGKQSAVMKARREVL 69
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1053-1126 2.84e-35

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: 128.48  E-value: 2.84e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804201 1053 FKLSVTVDPKYHPKIIGRKGAVITQIRLEHDVNIQFPDKDDGNqpQDQITITGYEKNTEAARDAILRIVGELEQ 1126
Cdd:cd22417     1 FTLTVEVDPKYHPKIIGRKGAVITKLRDDHDVNIQFPDKGDEN--DDEITITGYEKNAEAAKDAILKIVQELES 72
KH-I_Vigilin_rpt15 cd22418
fifteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1128-1196 2.18e-34

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: 125.84  E-value: 2.18e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201 1128 VSEDVPLDHRVHARIIGARGKAIRKIMDEFKVDIRFPQSGAPDPNCVTVTGLPENVEEAIDHILNLEEE 1196
Cdd:cd22418     1 VTEEVEIDSRVHPRLIGARGKAIRKIMEDFKVDIRFPRSGDADPNLVTITGLEENVEECKDHLLNLEEE 69
KH-I_Vigilin_rpt5 cd22409
fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
364-433 4.44e-34

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: 125.00  E-value: 4.44e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  364 FTVSSVAAPSWLHRFIIGKKGQNLAKITQQMPKVHIEFTEGEDKITLEGPTEDVNVAQEQIEGMVKDLIN 433
Cdd:cd22409     1 VVVAEVSAPSWLHRFIIGKKGANIKKITQDLPKVHIEFTEGEDKIELEGPPEEVEVVREQLEAIVKELVA 70
KH-I_Vigilin_rpt10 cd22413
tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
726-791 3.91e-32

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: 119.29  E-value: 3.91e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201  726 KSFTVDIRAKPEYHKFLIGKGGGKIRKVRDSTGARVIFPAAEDKDQDLITIIGKEDAVREAQKELE 791
Cdd:cd22413     1 NSFTVEIRAKPEYHRFLIGRGGANIRKIRDNTGARIIFPTARDEDQELITIIGTKEAVEKAKEELE 66
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
583-644 5.37e-30

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: 113.07  E-value: 5.37e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804201  583 SISVPIFKQFHKNIIGKGGANIKKIREESNTKIDLPAENSNSETIIITGKRANCEAARSRIL 644
Cdd:cd22411     1 SIKVPIFKQFHKNIIGKGGATIKKIREETNTRIDLPEENSDSDVITITGKKEDVEKARERIL 62
KH-I_Vigilin_rpt3 cd22407
third type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
224-283 4.65e-27

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: 104.98  E-value: 4.65e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  224 VERLEVEKAFHPFIAGPYNRLVGEIMQETGTRINIPPPSVNRTEIVFTGEKEQLAQAVAR 283
Cdd:cd22407     1 TERLDIPKVYHPFIAGPNNENVKELQEETGVRINIPPPSVNKDEIVVSGEKEGVAQAVAK 60
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
297-358 7.19e-27

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: 104.17  E-value: 7.19e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804201  297 TIAVEVKKSQHKYVIGPKGNSLQEILERTGVSVEIPPSDSISETVILRGEPEKLGQALTEVY 358
Cdd:cd22408     1 TVSVEVPKSQHRFVIGPRGSTIQEILEETGCSVEVPPNDSDSETITLRGPADKLGAALTLVY 62
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
435-502 5.33e-26

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: 101.88  E-value: 5.33e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201  435 MDYVEINIDHKFHRHLIGKSGANINRIKDQYKVSVRIPPDSEKSNLIRIEGDPQGVQQAKRELLELAS 502
Cdd:cd02394     1 MAFTTIEIDPKFHGHIIGKGGANIKRIREESGVSIRIPDDEANSDEIRIEGSPEGVKKAKAEILELVD 68
 
Name Accession Description Interval E-value
KH-I_Vigilin_rpt12 cd22415
twelfth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
875-970 6.55e-45

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: 157.08  E-value: 6.55e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  875 TLECAIPQKFHRSVMGPKGSRIQQITRDFSVQIKFPDREENAVHSTEPvvqeNGDEAGEGREAKDCDPGSPRRCDIIIIS 954
Cdd:cd22415     1 TIECVIPQKFHRTVMGAKGSRVQQITSEFDVQIKFPDRESNQPAPAEN----GEGNGGEGVEGEAVDDNSPRKCDIIIIT 76
                          90
                  ....*....|....*.
gi 578804201  955 GRKEKCEAAKEALEAL 970
Cdd:cd22415    77 GKKENCEAAKEALLAL 92
KH-I_Vigilin_rpt13 cd22416
thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
972-1049 2.48e-40

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: 143.14  E-value: 2.48e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201  972 PVTIEVEVPFDLHRYVIGQKGSGIRKMMDEFEVNIHVPAPELQSDIIAITGLAANLDRAKAGLLERVKELQAEQEDRA 1049
Cdd:cd22416     1 PVTEEVNVPFDLHRFIIGQKGADVRKMMDEFDVNISIPPAELQSDIIKITGPPANVERAKAALLERVKELEAEKEDRE 78
KH-I_Vigilin_rpt11 cd22414
eleventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
802-867 3.19e-39

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: 139.75  E-value: 3.19e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201  802 EDSMLVDPKHHRHFVIRRGQVLREIAEEYGGVMVSFPRSGTQSDKVTLKGAKDCVEAAKKRIQEII 867
Cdd:cd22414     1 EDEMTVDPKHHRHFVARRGQVLREIADEYGGVMVSFPRSGTQSDKVTLKGAKDCVEGAKKRILEIV 66
KH-I_Vigilin_rpt9 cd22412
ninth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
653-722 4.00e-39

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: 139.74  E-value: 4.00e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  653 IAEVEVSIPAKLHNSLIGTKGRLIRSIMEECGGVHIHFPVEGSGSDTVVIRGPSSDVEKAKKQLLHLAEE 722
Cdd:cd22412     1 IVEVEVEIPAKLHNSLIGAKGRLIRSIMEECGGVHIHFPPEGSGSDKVTIRGPKEDVEKAKKQLLELANE 70
KH-I_Vigilin_rpt7 cd22410
seventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
507-573 7.48e-38

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: 135.87  E-value: 7.48e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201  507 ERTKDLIIEQRFHRTIIGQKGERIREIRDKFPEVIINFPDPAQKSDIVQLRGPKNEVEKCTKYMQKM 573
Cdd:cd22410     1 EKTKDIIIEQRFHRTIIGQKGEKIREIRDKFPQVQITFPDPGSKSDVVTLRGPKDEVDKCYKYLKKL 67
KH-I_Vigilin_rpt2 cd22406
second type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
147-221 2.16e-37

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: 134.75  E-value: 2.16e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201  147 LQTQASATVAIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPDDPSNQIKITGTKEGIEKARHEVLLISAEQDK 221
Cdd:cd22406     1 LQTQASVTVNIPKEHHRFILGKKGKKLQELELKTATKIVIPRQEDNSDEIKITGTKEGIEKARHEIQLISDEQAK 75
KH-I_Vigilin_rpt1 cd22405
first type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
77-144 1.34e-35

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: 129.34  E-value: 1.34e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201   77 TQVFHVPLEERKYKDMN-QFGEGEQAKICLEIMQRTGAHLELSLAKDQGLSIMVSGKLDAVMKARKDIV 144
Cdd:cd22405     1 TQVFHVPLEERRYKESNqQFGEGEQAKICKDIMQKTGATIELSSAKDQSLTIMVTGKQSAVMKARREVL 69
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1053-1126 2.84e-35

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: 128.48  E-value: 2.84e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804201 1053 FKLSVTVDPKYHPKIIGRKGAVITQIRLEHDVNIQFPDKDDGNqpQDQITITGYEKNTEAARDAILRIVGELEQ 1126
Cdd:cd22417     1 FTLTVEVDPKYHPKIIGRKGAVITKLRDDHDVNIQFPDKGDEN--DDEITITGYEKNAEAAKDAILKIVQELES 72
KH-I_Vigilin_rpt15 cd22418
fifteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1128-1196 2.18e-34

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: 125.84  E-value: 2.18e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201 1128 VSEDVPLDHRVHARIIGARGKAIRKIMDEFKVDIRFPQSGAPDPNCVTVTGLPENVEEAIDHILNLEEE 1196
Cdd:cd22418     1 VTEEVEIDSRVHPRLIGARGKAIRKIMEDFKVDIRFPRSGDADPNLVTITGLEENVEECKDHLLNLEEE 69
KH-I_Vigilin_rpt5 cd22409
fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
364-433 4.44e-34

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: 125.00  E-value: 4.44e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  364 FTVSSVAAPSWLHRFIIGKKGQNLAKITQQMPKVHIEFTEGEDKITLEGPTEDVNVAQEQIEGMVKDLIN 433
Cdd:cd22409     1 VVVAEVSAPSWLHRFIIGKKGANIKKITQDLPKVHIEFTEGEDKIELEGPPEEVEVVREQLEAIVKELVA 70
KH-I_Vigilin_rpt10 cd22413
tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
726-791 3.91e-32

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: 119.29  E-value: 3.91e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201  726 KSFTVDIRAKPEYHKFLIGKGGGKIRKVRDSTGARVIFPAAEDKDQDLITIIGKEDAVREAQKELE 791
Cdd:cd22413     1 NSFTVEIRAKPEYHRFLIGRGGANIRKIRDNTGARIIFPTARDEDQELITIIGTKEAVEKAKEELE 66
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
583-644 5.37e-30

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: 113.07  E-value: 5.37e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804201  583 SISVPIFKQFHKNIIGKGGANIKKIREESNTKIDLPAENSNSETIIITGKRANCEAARSRIL 644
Cdd:cd22411     1 SIKVPIFKQFHKNIIGKGGATIKKIREETNTRIDLPEENSDSDVITITGKKEDVEKARERIL 62
KH-I_Vigilin_rpt3 cd22407
third type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
224-283 4.65e-27

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: 104.98  E-value: 4.65e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  224 VERLEVEKAFHPFIAGPYNRLVGEIMQETGTRINIPPPSVNRTEIVFTGEKEQLAQAVAR 283
Cdd:cd22407     1 TERLDIPKVYHPFIAGPNNENVKELQEETGVRINIPPPSVNKDEIVVSGEKEGVAQAVAK 60
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
297-358 7.19e-27

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: 104.17  E-value: 7.19e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804201  297 TIAVEVKKSQHKYVIGPKGNSLQEILERTGVSVEIPPSDSISETVILRGEPEKLGQALTEVY 358
Cdd:cd22408     1 TVSVEVPKSQHRFVIGPRGSTIQEILEETGCSVEVPPNDSDSETITLRGPADKLGAALTLVY 62
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
435-502 5.33e-26

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: 101.88  E-value: 5.33e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201  435 MDYVEINIDHKFHRHLIGKSGANINRIKDQYKVSVRIPPDSEKSNLIRIEGDPQGVQQAKRELLELAS 502
Cdd:cd02394     1 MAFTTIEIDPKFHGHIIGKGGANIKRIREESGVSIRIPDDEANSDEIRIEGSPEGVKKAKAEILELVD 68
KH smart00322
K homology RNA-binding domain;
580-646 1.54e-13

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 66.55  E-value: 1.54e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201    580 NSYSISVPIFKQFHKNIIGKGGANIKKIREESNTKIDLPAENSNSETIIITGKRANCEAARSRILSI 646
Cdd:smart00322    1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERVVEITGPPENVEKAAELILEI 67
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
583-645 1.14e-12

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: 63.84  E-value: 1.14e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201   583 SISVPIFKQFHKNIIGKGGANIKKIREESNTKIDLPAENS--NSETIIITGKRANCEAARSRILS 645
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESegNERIVTITGTPEAVEAAKALIEE 65
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
152-213 1.24e-12

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: 63.84  E-value: 1.24e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804201   152 SATVAIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPDDPSNQ--IKITGTKEGIEKARHEVL 213
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNEriVTITGTPEAVEAAKALIE 64
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
438-499 9.34e-12

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: 61.53  E-value: 9.34e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804201   438 VEINIDHKFHRHLIGKSGANINRIKDQYKVSVRIPPDSEKSN--LIRIEGDPQGVQQAKRELLE 499
Cdd:pfam00013    2 VEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNerIVTITGTPEAVEAAKALIEE 65
KH smart00322
K homology RNA-binding domain;
149-215 1.17e-11

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 61.16  E-value: 1.17e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201    149 TQASATVAIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPDDPSNQIKITGTKEGIEKARHEVLLI 215
Cdd:smart00322    1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERVVEITGPPENVEKAAELILEI 67
KH smart00322
K homology RNA-binding domain;
655-717 1.36e-11

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 61.16  E-value: 1.36e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201    655 EVEVSIPAKLHNSLIGTKGRLIRSIMEECgGVHIHFPVEGSGSDTVVIRGPSSDVEKAKKQLL 717
Cdd:smart00322    4 TIEVLIPADKVGLIIGKGGSTIKKIEEET-GVKIDIPGPGSEERVVEITGPPENVEKAAELIL 65
KH smart00322
K homology RNA-binding domain;
438-500 1.82e-11

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 60.77  E-value: 1.82e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201    438 VEINIDHKFHRHLIGKSGANINRIKDQYKVSVRIPPDSEKSNLIRIEGDPQGVQQAKRELLEL 500
Cdd:smart00322    5 IEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERVVEITGPPENVEKAAELILEI 67
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
729-792 2.41e-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: 60.37  E-value: 2.41e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201   729 TVDIRAKPEYHKFLIGKGGGKIRKVRDSTGARVIFPAAEDKDQD-LITIIGKEDAVREAQKELEA 792
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNErIVTITGTPEAVEAAKALIEE 65
KH smart00322
K homology RNA-binding domain;
972-1038 6.18e-11

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 59.23  E-value: 6.18e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201    972 PVTIEVEVPFDLHRYVIGQKGSGIRKMMDEFEVNIHVPAPELQSDIIAITGLAANLDRAKAGLLERV 1038
Cdd:smart00322    2 PVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERVVEITGPPENVEKAAELILEIL 68
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
1054-1118 8.02e-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: 58.83  E-value: 8.02e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201  1054 KLSVTVDPKYHPKIIGRKGAVITQIRLEHDVNIQFPDKDDgNQPQDQITITGYEKNTEAARDAIL 1118
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSES-EGNERIVTITGTPEAVEAAKALIE 64
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
1129-1192 1.29e-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: 1.29e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201  1129 SEDVPLDHRVHARIIGARGKAIRKIMDEFKVDIRFPQSGAPDPNC-VTVTGLPENVEEAIDHILN 1192
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNERiVTITGTPEAVEAAKALIEE 65
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
655-717 1.36e-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: 1.36e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201   655 EVEVSIPAKLHNSLIGTKGRLIRSIMEECgGVHIHFPVEGS--GSDTVVIRGPSSDVEKAKKQLL 717
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREET-GAKIQIPPSESegNERIVTITGTPEAVEAAKALIE 64
KH smart00322
K homology RNA-binding domain;
1054-1121 1.73e-09

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 54.99  E-value: 1.73e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201   1054 KLSVTVDPKYHPKIIGRKGAVITQIRLEHDVNIQFPDKDDGNqpqDQITITGYEKNTEAARDAILRIV 1121
Cdd:smart00322    4 TIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEE---RVVEITGPPENVEKAAELILEIL 68
KH smart00322
K homology RNA-binding domain;
1128-1193 2.30e-09

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 54.61  E-value: 2.30e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201   1128 VSEDVPLDHRVHARIIGARGKAIRKIMDEFKVDIRFPQSGAPDpNCVTVTGLPENVEEAIDHILNL 1193
Cdd:smart00322    3 VTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEE-RVVEITGPPENVEKAAELILEI 67
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
974-1036 4.21e-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: 53.82  E-value: 4.21e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201   974 TIEVEVPFDLHRYVIGQKGSGIRKMMDEFEVNIHVPAPE--LQSDIIAITGLAANLDRAKAGLLE 1036
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSEseGNERIVTITGTPEAVEAAKALIEE 65
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
297-359 3.29e-08

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: 51.51  E-value: 3.29e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201   297 TIAVEVKKSQHKYVIGPKGNSLQEILERTGVSVEIPPSDSI--SETVILRGEPEKLGQALTEVYA 359
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEgnERIVTITGTPEAVEAAKALIEE 65
KH smart00322
K homology RNA-binding domain;
506-574 5.87e-08

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 50.76  E-value: 5.87e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201    506 NERTKDLIIEQRFHRTIIGQKGERIREIRDKFpEVIINFPDPAQKSDIVQLRGPKNEVEKCTKYMQKMV 574
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 ...
509-572 5.97e-08

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: 50.74  E-value: 5.97e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201   509 TKDLIIEQRFHRTIIGQKGERIREIRDKFpEVIINFPDPA--QKSDIVQLRGPKNEVEKCTKYMQK 572
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREET-GAKIQIPPSEseGNERIVTITGTPEAVEAAKALIEE 65
KH smart00322
K homology RNA-binding domain;
799-867 6.53e-08

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 50.76  E-value: 6.53e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201    799 NVVEDSMLVDPKHHRHFVIRRGQVLREIAEEYgGVMVSFPRSGTQSDKVTLKGAKDCVEAAKKRIQEII 867
Cdd:smart00322    1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEET-GVKIDIPGPGSEERVVEITGPPENVEKAAELILEIL 68
KH smart00322
K homology RNA-binding domain;
296-360 8.51e-08

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 50.37  E-value: 8.51e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201    296 TTIAVEVKKSQHKYVIGPKGNSLQEILERTGVSVEIPPSDSISETVILRGEPEKLGQALTEVYAK 360
Cdd:smart00322    3 VTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERVVEITGPPENVEKAAELILEI 67
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
875-969 2.52e-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: 48.82  E-value: 2.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201   875 TLECAIPQKFHRSVMGPKGSRIQQITRDFSVQIKFPDREENAVHstepvvqengdeagegreakdcdpgsprrcDIIIIS 954
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNE------------------------------RIVTIT 50
                           90
                   ....*....|....*
gi 578804201   955 GRKEKCEAAKEALEA 969
Cdd:pfam00013   51 GTPEAVEAAKALIEE 65
KH smart00322
K homology RNA-binding domain;
726-794 3.01e-07

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 48.83  E-value: 3.01e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201    726 KSFTVDIRAKPEYHKFLIGKGGGKIRKVRDSTGARVIFPAAEDKDqDLITIIGKEDAVREAQKELEALI 794
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 ...
372-425 1.53e-06

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: 46.51  E-value: 1.53e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201   372 PSWLHRFIIGKKGQNLAKITQQMpKVHIEF-----TEGEDKITLEGPTEDVNVAQEQIE 425
Cdd:pfam00013    7 PSSLVGLIIGKGGSNIKEIREET-GAKIQIppsesEGNERIVTITGTPEAVEAAKALIE 64
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
594-658 2.11e-06

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 51.97  E-value: 2.11e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201  594 KNIIGKGGANIKKIREESNTKIDLpaenSNSETIIITGK-RANCEAARSRILSIqkdlanIAEVEV 658
Cdd:PRK11824  566 RDVIGPGGKTIREITEETGAKIDI----EDDGTVKIAATdGEAAEAAKERIEGI------TAEPEV 621
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
802-865 2.89e-06

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: 45.74  E-value: 2.89e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201   802 EDSMLVDPKHHRHFVIRRGQVLREIAEEYGgVMVSFPR--SGTQSDKVTLKGAKDCVEAAKKRIQE 865
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETG-AKIQIPPseSEGNERIVTITGTPEAVEAAKALIEE 65
KH smart00322
K homology RNA-binding domain;
369-428 2.98e-06

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 45.75  E-value: 2.98e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201    369 VAAPSWLHRFIIGKKGQNLAKITQQMpKVHIEF---TEGEDKITLEGPTEDVNVAQEQIEGMV 428
Cdd:smart00322    7 VLIPADKVGLIIGKGGSTIKKIEEET-GVKIDIpgpGSEERVVEITGPPENVEKAAELILEIL 68
KH smart00322
K homology RNA-binding domain;
872-971 3.63e-06

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 45.75  E-value: 3.63e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201    872 AQVTLECAIPQKFHRSVMGPKGSRIQQITRDFSVQIKFPDREENavhstepvvqengdeagegreakdcdpgsprrCDII 951
Cdd:smart00322    1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSE--------------------------------ERVV 48
                            90       100
                    ....*....|....*....|
gi 578804201    952 IISGRKEKCEAAKEALEALV 971
Cdd:smart00322   49 EITGPPENVEKAAELILEIL 68
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
224-283 6.22e-06

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: 44.96  E-value: 6.22e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804201   224 VERLEVEKAFHPFIAGPYNRLVGEIMQETGTRINIPPPSVNRTE--IVFTGEKEQLAQAVAR 283
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNEriVTITGTPEAVEAAKAL 62
KH smart00322
K homology RNA-binding domain;
221-283 1.01e-05

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 44.59  E-value: 1.01e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201    221 KRAVERLEVEKAFHPFIAGPYNRLVGEIMQETGTRINIPPPSVNRTEIVFTGEKEQLAQAVAR 283
Cdd:smart00322    1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERVVEITGPPENVEKAAEL 63
COG5166 COG5166
Uncharacterized conserved protein [Function unknown];
450-736 1.46e-03

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 227495 [Multi-domain]  Cd Length: 657  Bit Score: 43.04  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  450 LIGKSGANINRIKDQYKVSVR---IPPDS---------EKSNLIRIEGdpqgvQQAKRELLELASRMENERTK--DLIIE 515
Cdd:COG5166   237 LVGKAFSSTAGMKATESINIYtlpFCSDKiprlqtypaLNSSKIIITG-----QSEILQRLEISFYYAEMHLKlfTHVTE 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  516 QRFHRTIIGqkgerIREIRDKFPEVIINFPDPAQKSDIVqLRGPKN-----------EVEKCTKYMQKMVADLVENSYSI 584
Cdd:COG5166   312 ISFVKLFIF-----LAYNMDIMEENSSFIRFPEYFKEGV-ETTPENskvkiygssiaNSEKTALRIAKLASKYVQGKTQF 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  585 SVPIFKQFhknIIGKGGANIKKIREESNTKIDLPAENSNSETIIITGkrANCEAARSRILSIQKDlANIAEVEVSIPAKL 664
Cdd:COG5166   386 GVEDNEDF---LRGKKNGKATRIMKGVSCSELSSIVSSTGSIVETNG--IGEKMSFSKKLSIPPT-EFPAEIAFIIMESG 459
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  665 HNSLIGTKGRLIRSIMEECgGVHIHFPVE-----GSGSDTVVIRGPSSDVEK---AKKQLLHLAEEKQTKSFTVDIRAKP 736
Cdd:COG5166   460 HEMIIGTGGIEIQENMVKH-AVDIAFKNFykfgqSQWHDNVLIEAPRKNQDNisgKKNDKLDKVKQQCRFNLKGDIRFCP 538
 
Name Accession Description Interval E-value
KH-I_Vigilin_rpt12 cd22415
twelfth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
875-970 6.55e-45

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: 157.08  E-value: 6.55e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  875 TLECAIPQKFHRSVMGPKGSRIQQITRDFSVQIKFPDREENAVHSTEPvvqeNGDEAGEGREAKDCDPGSPRRCDIIIIS 954
Cdd:cd22415     1 TIECVIPQKFHRTVMGAKGSRVQQITSEFDVQIKFPDRESNQPAPAEN----GEGNGGEGVEGEAVDDNSPRKCDIIIIT 76
                          90
                  ....*....|....*.
gi 578804201  955 GRKEKCEAAKEALEAL 970
Cdd:cd22415    77 GKKENCEAAKEALLAL 92
KH-I_Vigilin_rpt13 cd22416
thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
972-1049 2.48e-40

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: 143.14  E-value: 2.48e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201  972 PVTIEVEVPFDLHRYVIGQKGSGIRKMMDEFEVNIHVPAPELQSDIIAITGLAANLDRAKAGLLERVKELQAEQEDRA 1049
Cdd:cd22416     1 PVTEEVNVPFDLHRFIIGQKGADVRKMMDEFDVNISIPPAELQSDIIKITGPPANVERAKAALLERVKELEAEKEDRE 78
KH-I_Vigilin_rpt11 cd22414
eleventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
802-867 3.19e-39

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: 139.75  E-value: 3.19e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201  802 EDSMLVDPKHHRHFVIRRGQVLREIAEEYGGVMVSFPRSGTQSDKVTLKGAKDCVEAAKKRIQEII 867
Cdd:cd22414     1 EDEMTVDPKHHRHFVARRGQVLREIADEYGGVMVSFPRSGTQSDKVTLKGAKDCVEGAKKRILEIV 66
KH-I_Vigilin_rpt9 cd22412
ninth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
653-722 4.00e-39

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: 139.74  E-value: 4.00e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  653 IAEVEVSIPAKLHNSLIGTKGRLIRSIMEECGGVHIHFPVEGSGSDTVVIRGPSSDVEKAKKQLLHLAEE 722
Cdd:cd22412     1 IVEVEVEIPAKLHNSLIGAKGRLIRSIMEECGGVHIHFPPEGSGSDKVTIRGPKEDVEKAKKQLLELANE 70
KH-I_Vigilin_rpt7 cd22410
seventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
507-573 7.48e-38

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: 135.87  E-value: 7.48e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201  507 ERTKDLIIEQRFHRTIIGQKGERIREIRDKFPEVIINFPDPAQKSDIVQLRGPKNEVEKCTKYMQKM 573
Cdd:cd22410     1 EKTKDIIIEQRFHRTIIGQKGEKIREIRDKFPQVQITFPDPGSKSDVVTLRGPKDEVDKCYKYLKKL 67
KH-I_Vigilin_rpt2 cd22406
second type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
147-221 2.16e-37

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: 134.75  E-value: 2.16e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201  147 LQTQASATVAIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPDDPSNQIKITGTKEGIEKARHEVLLISAEQDK 221
Cdd:cd22406     1 LQTQASVTVNIPKEHHRFILGKKGKKLQELELKTATKIVIPRQEDNSDEIKITGTKEGIEKARHEIQLISDEQAK 75
KH-I_Vigilin_rpt1 cd22405
first type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
77-144 1.34e-35

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: 129.34  E-value: 1.34e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201   77 TQVFHVPLEERKYKDMN-QFGEGEQAKICLEIMQRTGAHLELSLAKDQGLSIMVSGKLDAVMKARKDIV 144
Cdd:cd22405     1 TQVFHVPLEERRYKESNqQFGEGEQAKICKDIMQKTGATIELSSAKDQSLTIMVTGKQSAVMKARREVL 69
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1053-1126 2.84e-35

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: 128.48  E-value: 2.84e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804201 1053 FKLSVTVDPKYHPKIIGRKGAVITQIRLEHDVNIQFPDKDDGNqpQDQITITGYEKNTEAARDAILRIVGELEQ 1126
Cdd:cd22417     1 FTLTVEVDPKYHPKIIGRKGAVITKLRDDHDVNIQFPDKGDEN--DDEITITGYEKNAEAAKDAILKIVQELES 72
KH-I_Vigilin_rpt15 cd22418
fifteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1128-1196 2.18e-34

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: 125.84  E-value: 2.18e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201 1128 VSEDVPLDHRVHARIIGARGKAIRKIMDEFKVDIRFPQSGAPDPNCVTVTGLPENVEEAIDHILNLEEE 1196
Cdd:cd22418     1 VTEEVEIDSRVHPRLIGARGKAIRKIMEDFKVDIRFPRSGDADPNLVTITGLEENVEECKDHLLNLEEE 69
KH-I_Vigilin_rpt5 cd22409
fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
364-433 4.44e-34

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: 125.00  E-value: 4.44e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  364 FTVSSVAAPSWLHRFIIGKKGQNLAKITQQMPKVHIEFTEGEDKITLEGPTEDVNVAQEQIEGMVKDLIN 433
Cdd:cd22409     1 VVVAEVSAPSWLHRFIIGKKGANIKKITQDLPKVHIEFTEGEDKIELEGPPEEVEVVREQLEAIVKELVA 70
KH-I_Vigilin_rpt10 cd22413
tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
726-791 3.91e-32

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: 119.29  E-value: 3.91e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201  726 KSFTVDIRAKPEYHKFLIGKGGGKIRKVRDSTGARVIFPAAEDKDQDLITIIGKEDAVREAQKELE 791
Cdd:cd22413     1 NSFTVEIRAKPEYHRFLIGRGGANIRKIRDNTGARIIFPTARDEDQELITIIGTKEAVEKAKEELE 66
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
583-644 5.37e-30

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: 113.07  E-value: 5.37e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804201  583 SISVPIFKQFHKNIIGKGGANIKKIREESNTKIDLPAENSNSETIIITGKRANCEAARSRIL 644
Cdd:cd22411     1 SIKVPIFKQFHKNIIGKGGATIKKIREETNTRIDLPEENSDSDVITITGKKEDVEKARERIL 62
KH-I_Vigilin_rpt3 cd22407
third type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
224-283 4.65e-27

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: 104.98  E-value: 4.65e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  224 VERLEVEKAFHPFIAGPYNRLVGEIMQETGTRINIPPPSVNRTEIVFTGEKEQLAQAVAR 283
Cdd:cd22407     1 TERLDIPKVYHPFIAGPNNENVKELQEETGVRINIPPPSVNKDEIVVSGEKEGVAQAVAK 60
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
297-358 7.19e-27

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: 104.17  E-value: 7.19e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804201  297 TIAVEVKKSQHKYVIGPKGNSLQEILERTGVSVEIPPSDSISETVILRGEPEKLGQALTEVY 358
Cdd:cd22408     1 TVSVEVPKSQHRFVIGPRGSTIQEILEETGCSVEVPPNDSDSETITLRGPADKLGAALTLVY 62
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
435-502 5.33e-26

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: 101.88  E-value: 5.33e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201  435 MDYVEINIDHKFHRHLIGKSGANINRIKDQYKVSVRIPPDSEKSNLIRIEGDPQGVQQAKRELLELAS 502
Cdd:cd02394     1 MAFTTIEIDPKFHGHIIGKGGANIKRIREESGVSIRIPDDEANSDEIRIEGSPEGVKKAKAEILELVD 68
KH-I_ScSCP160_rpt6 cd22451
sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
151-219 2.08e-18

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: 80.58  E-value: 2.08e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201  151 ASATVAIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPDDPSNQIKITGTKEGIEKARHEVLLISAEQ 219
Cdd:cd22451     1 ASIDIDIPKEYHRAIIGKGGAVLRELEAETGCRIQVPKKDDPSGKIRITGARDGVEAATAKILNISDEE 69
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
585-646 9.99e-16

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: 72.60  E-value: 9.99e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804201  585 SVPIFKQFHKNIIGKGGANIKKIREESNTKIDLPAENSNSETIIITGKRANCEAARSRILSI 646
Cdd:cd02394     5 TIEIDPKFHGHIIGKGGANIKRIREESGVSIRIPDDEANSDEIRIEGSPEGVKKAKAEILEL 66
KH smart00322
K homology RNA-binding domain;
580-646 1.54e-13

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 66.55  E-value: 1.54e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201    580 NSYSISVPIFKQFHKNIIGKGGANIKKIREESNTKIDLPAENSNSETIIITGKRANCEAARSRILSI 646
Cdd:smart00322    1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERVVEITGPPENVEKAAELILEI 67
KH-I_Vigilin_rpt9 cd22412
ninth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
800-869 3.69e-13

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: 65.39  E-value: 3.69e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  800 VVEDSMLVDPKHHRHFVIRRGQVLREIAEEYGGVMVSFPRSGTQSDKVTLKGAKDCVEAAKKRIQEIIED 869
Cdd:cd22412     1 IVEVEVEIPAKLHNSLIGAKGRLIRSIMEECGGVHIHFPPEGSGSDKVTIRGPKEDVEKAKKQLLELANE 70
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
582-650 4.75e-13

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: 65.31  E-value: 4.75e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  582 YSISVPIFKQFHKNIIGKGGANIKKIREESNTKIDLPAENS-NSETIIITGKRANCEAARSRILSIQKDL 650
Cdd:cd22417     1 FTLTVEVDPKYHPKIIGRKGAVITKLRDDHDVNIQFPDKGDeNDDEITITGYEKNAEAAKDAILKIVQEL 70
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
583-645 1.14e-12

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: 63.84  E-value: 1.14e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201   583 SISVPIFKQFHKNIIGKGGANIKKIREESNTKIDLPAENS--NSETIIITGKRANCEAARSRILS 645
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESegNERIVTITGTPEAVEAAKALIEE 65
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
152-213 1.24e-12

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: 63.84  E-value: 1.24e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804201   152 SATVAIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPDDPSNQ--IKITGTKEGIEKARHEVL 213
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNEriVTITGTPEAVEAAKALIE 64
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
583-644 2.39e-12

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: 62.96  E-value: 2.39e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804201  583 SISVPIFKQFHKNIIGKGGANIKKIREESNTKIDLPAENSNSETIIITGKRANCEAARSRIL 644
Cdd:cd22408     1 TVSVEVPKSQHRFVIGPRGSTIQEILEETGCSVEVPPNDSDSETITLRGPADKLGAALTLVY 62
KH-I_Vigilin_rpt2 cd22406
second type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
581-651 3.41e-12

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: 63.10  E-value: 3.41e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578804201  581 SYSISVPIFKQFHKNIIGKGGANIKKIREESNTKIDLPAENSNSETIIITGKRANCEAARSRILSIQKDLA 651
Cdd:cd22406     4 QASVTVNIPKEHHRFILGKKGKKLQELELKTATKIVIPRQEDNSDEIKITGTKEGIEKARHEIQLISDEQA 74
KH-I_Vigilin_rpt15 cd22418
fifteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
439-501 6.09e-12

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: 61.90  E-value: 6.09e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804201  439 EINIDHKFHRHLIGKSGANINRIKDQYKVSVRIP-PDSEKSNLIRIEGDPQGVQQAKRELLELA 501
Cdd:cd22418     4 EVEIDSRVHPRLIGARGKAIRKIMEDFKVDIRFPrSGDADPNLVTITGLEENVEECKDHLLNLE 67
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
438-499 9.34e-12

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: 61.53  E-value: 9.34e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804201   438 VEINIDHKFHRHLIGKSGANINRIKDQYKVSVRIPPDSEKSN--LIRIEGDPQGVQQAKRELLE 499
Cdd:pfam00013    2 VEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNerIVTITGTPEAVEAAKALIEE 65
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
1056-1121 9.73e-12

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: 61.43  E-value: 9.73e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201 1056 SVTVDPKYHPKIIGRKGAVITQIRLEHDVNIQFPDKDDGNqpqDQITITGYEKNTEAARDAILRIV 1121
Cdd:cd02394     5 TIEIDPKFHGHIIGKGGANIKRIREESGVSIRIPDDEANS---DEIRIEGSPEGVKKAKAEILELV 67
KH smart00322
K homology RNA-binding domain;
149-215 1.17e-11

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 61.16  E-value: 1.17e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201    149 TQASATVAIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPDDPSNQIKITGTKEGIEKARHEVLLI 215
Cdd:smart00322    1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERVVEITGPPENVEKAAELILEI 67
KH-I_Vigilin_rpt13 cd22416
thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1131-1205 1.32e-11

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: 61.48  E-value: 1.32e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201 1131 DVPLDHrvHARIIGARGKAIRKIMDEFKVDIRFPQSGAPDpNCVTVTGLPENVEEAIDHILNLEEEYLADVVDSE 1205
Cdd:cd22416     7 NVPFDL--HRFIIGQKGADVRKMMDEFDVNISIPPAELQS-DIIKITGPPANVERAKAALLERVKELEAEKEDRE 78
KH smart00322
K homology RNA-binding domain;
655-717 1.36e-11

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 61.16  E-value: 1.36e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201    655 EVEVSIPAKLHNSLIGTKGRLIRSIMEECgGVHIHFPVEGSGSDTVVIRGPSSDVEKAKKQLL 717
Cdd:smart00322    4 TIEVLIPADKVGLIIGKGGSTIKKIEEET-GVKIDIPGPGSEERVVEITGPPENVEKAAELIL 65
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
152-213 1.51e-11

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: 60.68  E-value: 1.51e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804201  152 SATVAIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPDDPSNQIKITGTKEGIEKARHEVL 213
Cdd:cd22411     1 SIKVPIFKQFHKNIIGKGGATIKKIREETNTRIDLPEENSDSDVITITGKKEDVEKARERIL 62
KH smart00322
K homology RNA-binding domain;
438-500 1.82e-11

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 60.77  E-value: 1.82e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201    438 VEINIDHKFHRHLIGKSGANINRIKDQYKVSVRIPPDSEKSNLIRIEGDPQGVQQAKRELLEL 500
Cdd:smart00322    5 IEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERVVEITGPPENVEKAAELILEI 67
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
972-1039 1.84e-11

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: 60.66  E-value: 1.84e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201  972 PVTIEVEVPFDLHRYVIGQKGSGIRKMMDEFEVNIHVPAPELQSDIIAITGLAANLDRAKAGLLERVK 1039
Cdd:cd02394     1 MAFTTIEIDPKFHGHIIGKGGANIKRIREESGVSIRIPDDEANSDEIRIEGSPEGVKKAKAEILELVD 68
KH-I_Vigilin_rpt13 cd22416
thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
438-508 1.89e-11

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: 61.09  E-value: 1.89e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578804201  438 VEINIDHKFHRHLIGKSGANINRIKDQYKVSVRIPPDSEKSNLIRIEGDPQGVQQAKRELLELASRMENER 508
Cdd:cd22416     4 EEVNVPFDLHRFIIGQKGADVRKMMDEFDVNISIPPAELQSDIIKITGPPANVERAKAALLERVKELEAEK 74
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
729-792 2.41e-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: 60.37  E-value: 2.41e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201   729 TVDIRAKPEYHKFLIGKGGGKIRKVRDSTGARVIFPAAEDKDQD-LITIIGKEDAVREAQKELEA 792
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNErIVTITGTPEAVEAAKALIEE 65
KH-I_ScSCP160_rpt3 cd22448
third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
439-500 2.47e-11

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: 60.62  E-value: 2.47e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201  439 EINIDHKFHRHLIGKSGANINRIKDQYKVSVRIPPDSEKSNL-----------IRIEGDPQGVQQAKRELLEL 500
Cdd:cd22448     6 ILKIPVQFHGSLIGQQGKYVNRLQEKYGVKINFPRENSSSNDtetkkpqapdeVTIRGGKKGVAEAKQELLEL 78
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
584-644 3.75e-11

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: 59.62  E-value: 3.75e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201  584 ISVPIFKQFHKNIIGKGGANIKKIREESNTKIDLPAENSNSE--TIIITGKRANCEAARSRIL 644
Cdd:cd00105     1 EEIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSGerVVTITGTPEAVEKAKELIE 63
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
152-213 4.44e-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: 59.49  E-value: 4.44e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804201  152 SATVAIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPDDPSNQIKITGTKEGIEKARHEVL 213
Cdd:cd22408     1 TVSVEVPKSQHRFVIGPRGSTIQEILEETGCSVEVPPNDSDSETITLRGPADKLGAALTLVY 62
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
804-871 4.86e-11

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: 59.53  E-value: 4.86e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201  804 SMLVDPKHHRHFVIRRGQVLREIAEEYGgVMVSFPRSGTQ-SDKVTLKGAKDCVEAAKKRIQEIIEDLE 871
Cdd:cd22417     4 TVEVDPKYHPKIIGRKGAVITKLRDDHD-VNIQFPDKGDEnDDEITITGYEKNAEAAKDAILKIVQELE 71
KH smart00322
K homology RNA-binding domain;
972-1038 6.18e-11

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 59.23  E-value: 6.18e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201    972 PVTIEVEVPFDLHRYVIGQKGSGIRKMMDEFEVNIHVPAPELQSDIIAITGLAANLDRAKAGLLERV 1038
Cdd:smart00322    2 PVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERVVEITGPPENVEKAAELILEIL 68
KH-I_Vigilin_rpt5 cd22409
fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
516-579 6.65e-11

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: 59.13  E-value: 6.65e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804201  516 QRFHRTIIGQKGERIREIRDKFPEVIINFPDpaqKSDIVQLRGPKNEVEKCTKYMQKMVADLVE 579
Cdd:cd22409    10 SWLHRFIIGKKGANIKKITQDLPKVHIEFTE---GEDKIELEGPPEEVEVVREQLEAIVKELVA 70
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
154-213 7.01e-11

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: 58.85  E-value: 7.01e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804201  154 TVAIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPDDPSNQ--IKITGTKEGIEKARHEVL 213
Cdd:cd00105     2 EIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSGErvVTITGTPEAVEKAKELIE 63
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
1054-1118 8.02e-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: 58.83  E-value: 8.02e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201  1054 KLSVTVDPKYHPKIIGRKGAVITQIRLEHDVNIQFPDKDDgNQPQDQITITGYEKNTEAARDAIL 1118
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSES-EGNERIVTITGTPEAVEAAKALIE 64
KH-I_Vigilin_rpt11 cd22414
eleventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
655-717 1.11e-10

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: 58.47  E-value: 1.11e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201  655 EVEVSIPAKLHNSLIGTKGRLIRSIMEECGGVHIHFPVEGSGSDTVVIRGPSSDVEKAKKQLL 717
Cdd:cd22414     1 EDEMTVDPKHHRHFVARRGQVLREIADEYGGVMVSFPRSGTQSDKVTLKGAKDCVEGAKKRIL 63
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
1129-1192 1.29e-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: 1.29e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201  1129 SEDVPLDHRVHARIIGARGKAIRKIMDEFKVDIRFPQSGAPDPNC-VTVTGLPENVEEAIDHILN 1192
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, ...
511-573 1.31e-10

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: 58.46  E-value: 1.31e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201  511 DLIIEQRFHRTIIGQKGERIREIRDKFPEVIINFPDPAQKSDIVQLRGPKNEVEKCTKYMQKM 573
Cdd:cd22412     5 EVEIPAKLHNSLIGAKGRLIRSIMEECGGVHIHFPPEGSGSDKVTIRGPKEDVEKAKKQLLEL 67
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
655-717 1.36e-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: 1.36e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201   655 EVEVSIPAKLHNSLIGTKGRLIRSIMEECgGVHIHFPVEGS--GSDTVVIRGPSSDVEKAKKQLL 717
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREET-GAKIQIPPSESegNERIVTITGTPEAVEAAKALIE 64
KH-I_ScSCP160_rpt6 cd22451
sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
583-646 1.70e-10

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: 57.85  E-value: 1.70e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804201  583 SISVPIFKQFHKNIIGKGGANIKKIREESNTKIDLPAENSNSETIIITGKRANCEAARSRILSI 646
Cdd:cd22451     2 SIDIDIPKEYHRAIIGKGGAVLRELEAETGCRIQVPKKDDPSGKIRITGARDGVEAATAKILNI 65
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
511-577 1.76e-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: 57.99  E-value: 1.76e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201  511 DLIIEQRFHRTIIGQKGERIREIRDKFpEVIINFPDP-AQKSDIVQLRGPKNEVEKCTKYMQKMVADL 577
Cdd:cd22417     4 TVEVDPKYHPKIIGRKGAVITKLRDDH-DVNIQFPDKgDENDDEITITGYEKNAEAAKDAILKIVQEL 70
KH-I_ScSCP160_rpt5 cd22450
fifth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
798-869 2.19e-10

fifth 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 fifth one.


Pssm-ID: 411878  Cd Length: 80  Bit Score: 58.06  E-value: 2.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  798 DNVVEDSMLVDPKHHRHFVIRRGQVLREIAEEYGGV--------MVSFPRSGTQSDKVTLKGAKDCVEAAKKRIQEIIED 869
Cdd:cd22450     1 EDEVTRTIKVDRKYHRTIIGPGGSTLRELISKAGGPtdrqeqarLVRFPNQNSESDEVVIRGPKKIVEKIIAEIEKIVEE 80
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
151-215 2.64e-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: 57.58  E-value: 2.64e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201  151 ASATVAIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPDDPSNQIKITGTKEGIEKARHEVLLI 215
Cdd:cd02394     2 AFTTIEIDPKFHGHIIGKGGANIKRIREESGVSIRIPDDEANSDEIRIEGSPEGVKKAKAEILEL 66
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
438-498 3.62e-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.


Pssm-ID: 411802 [Multi-domain]  Cd Length: 63  Bit Score: 56.92  E-value: 3.62e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201  438 VEINIDHKFHRHLIGKSGANINRIKDQYKVSVRIPPDSEKS--NLIRIEGDPQGVQQAKRELL 498
Cdd:cd00105     1 EEIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSgeRVVTITGTPEAVEKAKELIE 63
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1131-1197 3.71e-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: 57.22  E-value: 3.71e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201 1131 DVPLDHRVHARIIGARGKAIRKIMDEFKVDIRFPQSGAPDPNCVTVTGLPENVEEAIDHILNLEEEY 1197
Cdd:cd22417     4 TVEVDPKYHPKIIGRKGAVITKLRDDHDVNIQFPDKGDENDDEITITGYEKNAEAAKDAILKIVQEL 70
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
1055-1118 4.24e-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.


Pssm-ID: 411802 [Multi-domain]  Cd Length: 63  Bit Score: 56.54  E-value: 4.24e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804201 1055 LSVTVDPKYHPKIIGRKGAVITQIRLEHDVNIQFPDKDDGNQPqDQITITGYEKNTEAARDAIL 1118
Cdd:cd00105     1 EEIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSGE-RVVTITGTPEAVEKAKELIE 63
KH-I_Vigilin_rpt13 cd22416
thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
655-722 4.55e-10

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: 57.24  E-value: 4.55e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201  655 EVEVSIPAKLHNSLIGTKGRLIRSIMEECgGVHIHFPVEGSGSDTVVIRGPSSDVEKAKKQLLHLAEE 722
Cdd:cd22416     3 TEEVNVPFDLHRFIIGQKGADVRKMMDEF-DVNISIPPAELQSDIIKITGPPANVERAKAALLERVKE 69
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
728-799 5.17e-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: 56.83  E-value: 5.17e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804201  728 FTVDIRAKPEYHKFLIGKGGGKIRKVRDSTGARVIFPAAEDKDQDLITIIGKEDAVREAQKELEALIQNLDN 799
Cdd:cd22417     1 FTLTVEVDPKYHPKIIGRKGAVITKLRDDHDVNIQFPDKGDENDDEITITGYEKNAEAAKDAILKIVQELES 72
KH-I_Vigilin_rpt13 cd22416
thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
152-223 5.32e-10

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: 56.85  E-value: 5.32e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201  152 SATVAIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPDDPSNQIKITGTKEGIEKARH----EVLLISAEQDKRA 223
Cdd:cd22416     3 TEEVNVPFDLHRFIIGQKGADVRKMMDEFDVNISIPPAELQSDIIKITGPPANVERAKAalleRVKELEAEKEDRE 78
KH-I_Vigilin_rpt12 cd22415
twelfth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1057-1118 7.13e-10

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: 56.92  E-value: 7.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201 1057 VTVDPKYHPKIIGRKGAVITQIRLEHDVNIQFPDKDDGNQ-------------------------PQDQITITGYEKNTE 1111
Cdd:cd22415     4 CVIPQKFHRTVMGAKGSRVQQITSEFDVQIKFPDRESNQPapaengegnggegvegeavddnsprKCDIIIITGKKENCE 83

                  ....*..
gi 578804201 1112 AARDAIL 1118
Cdd:cd22415    84 AAKEALL 90
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
438-506 7.28e-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: 7.28e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  438 VEINIDHKFHRHLIGKSGANINRIKDQYKVSVRIPP-DSEKSNLIRIEGDPQGVQQAKRELLELASRMEN 506
Cdd:cd22417     3 LTVEVDPKYHPKIIGRKGAVITKLRDDHDVNIQFPDkGDENDDEITITGYEKNAEAAKDAILKIVQELES 72
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
653-721 8.98e-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: 56.04  E-value: 8.98e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201  653 IAEVEVSIPAKLHNSLIGTKGRLIRSIMEECGgVHIHFPVEGSGSDTVVIRGPSSDVEKAKKQLLHLAE 721
Cdd:cd02394     1 MAFTTIEIDPKFHGHIIGKGGANIKRIREESG-VSIRIPDDEANSDEIRIEGSPEGVKKAKAEILELVD 68
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
736-795 9.33e-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: 55.65  E-value: 9.33e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  736 PEYHKFLIGKGGGKIRKVRDSTGARVIFPAAEDKDqDLITIIGKEDAVREAQKELEALIQ 795
Cdd:cd02394    10 PKFHGHIIGKGGANIKRIREESGVSIRIPDDEANS-DEIRIEGSPEGVKKAKAEILELVD 68
KH-I_Vigilin_rpt10 cd22413
tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
580-643 1.47e-09

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: 55.34  E-value: 1.47e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201  580 NSYSISVPIFKQFHKNIIGKGGANIKKIREESNTKIDLP-AENSNSETIIITGKRANCEAARSRI 643
Cdd:cd22413     1 NSFTVEIRAKPEYHRFLIGRGGANIRKIRDNTGARIIFPtARDEDQELITIIGTKEAVEKAKEEL 65
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
579-648 1.50e-09

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: 55.35  E-value: 1.50e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  579 ENSYSISVPIFKQFHKNIIGKGGANIKKIREESNTKIDLpAENSNSETIIITGKRANCEAARSRILSIQK 648
Cdd:cd22449     1 ENGYTVKFDVPAKYVPHIIGKKGANINKLREEYGVKIDF-EDKTGEGNVEIKGSKKNVEEAKKRILSQID 69
KH smart00322
K homology RNA-binding domain;
1054-1121 1.73e-09

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 54.99  E-value: 1.73e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201   1054 KLSVTVDPKYHPKIIGRKGAVITQIRLEHDVNIQFPDKDDGNqpqDQITITGYEKNTEAARDAILRIV 1121
Cdd:smart00322    4 TIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEE---RVVEITGPPENVEKAAELILEIL 68
KH-I_Vigilin_rpt5 cd22409
fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
438-506 1.88e-09

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: 54.89  E-value: 1.88e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  438 VEINIDHKFHRHLIGKSGANINRIKDQY-KVSVRIPpdsEKSNLIRIEGDPQGVQQAKRELLELASRMEN 506
Cdd:cd22409     4 AEVSAPSWLHRFIIGKKGANIKKITQDLpKVHIEFT---EGEDKIELEGPPEEVEVVREQLEAIVKELVA 70
KH-I_Vigilin_rpt15 cd22418
fifteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
655-722 2.19e-09

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: 54.97  E-value: 2.19e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201  655 EVEVSIPAKLHNSLIGTKGRLIRSIMEECgGVHIHFPVEGSG-SDTVVIRGPSSDVEKAKKQLLHLAEE 722
Cdd:cd22418     2 TEEVEIDSRVHPRLIGARGKAIRKIMEDF-KVDIRFPRSGDAdPNLVTITGLEENVEECKDHLLNLEEE 69
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
974-1031 2.22e-09

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: 54.48  E-value: 2.22e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201  974 TIEVEVPFDLHRYVIGQKGSGIRKMMDEFEVNIHVPAPELQSDIIAITGLAANLDRAK 1031
Cdd:cd22408     1 TVSVEVPKSQHRFVIGPRGSTIQEILEETGCSVEVPPNDSDSETITLRGPADKLGAAL 58
KH smart00322
K homology RNA-binding domain;
1128-1193 2.30e-09

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 54.61  E-value: 2.30e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201   1128 VSEDVPLDHRVHARIIGARGKAIRKIMDEFKVDIRFPQSGAPDpNCVTVTGLPENVEEAIDHILNL 1193
Cdd:smart00322    3 VTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEE-RVVEITGPPENVEKAAELILEI 67
KH-I_Vigilin_rpt13 cd22416
thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
584-650 2.31e-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: 54.93  E-value: 2.31e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201  584 ISVPIfkQFHKNIIGKGGANIKKIREESNTKIDLPAENSNSETIIITGKRANCEAARSRILSIQKDL 650
Cdd:cd22416     6 VNVPF--DLHRFIIGQKGADVRKMMDEFDVNISIPPAELQSDIIKITGPPANVERAKAALLERVKEL 70
KH-I_ASCC1 cd22419
type I K homology (KH) RNA-binding domain found in activating signal cointegrator 1 complex ...
154-215 2.99e-09

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: 54.50  E-value: 2.99e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201  154 TVAIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPDDpSNQIKITGT-KEGIEKARHEVLLI 215
Cdd:cd22419     4 SLDVPSALFKFIIGKKGETKKRLESETKTQIRIPRQGK-EGDIVITGKdRSGVDSARTRIEVL 65
KH-I_Vigilin_rpt10 cd22413
tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
438-497 3.00e-09

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: 54.19  E-value: 3.00e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578804201  438 VEINIDHKFHRHLIGKSGANINRIKDQYKVSVRIPPDSEK-SNLIRIEGDPQGVQQAKREL 497
Cdd:cd22413     5 VEIRAKPEYHRFLIGRGGANIRKIRDNTGARIIFPTARDEdQELITIIGTKEAVEKAKEEL 65
KH-I_ASCC1 cd22419
type I K homology (KH) RNA-binding domain found in activating signal cointegrator 1 complex ...
582-646 3.02e-09

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: 54.50  E-value: 3.02e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201  582 YSISVPIFKQFHKNIIGKGGANIKKIREESNTKIDLPAENSNSEtIIITGK-RANCEAARSRILSI 646
Cdd:cd22419     1 FRLSLDVPSALFKFIIGKKGETKKRLESETKTQIRIPRQGKEGD-IVITGKdRSGVDSARTRIEVL 65
KH-I_Vigilin_rpt15 cd22418
fifteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
973-1036 3.08e-09

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: 54.58  E-value: 3.08e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201  973 VTIEVEVPFDLHRYVIGQKGSGIRKMMDEFEVNIHVPAPEL-QSDIIAITGLAANLDRAKAGLLE 1036
Cdd:cd22418     1 VTEEVEIDSRVHPRLIGARGKAIRKIMEDFKVDIRFPRSGDaDPNLVTITGLEENVEECKDHLLN 65
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1054-1118 3.37e-09

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: 54.13  E-value: 3.37e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201 1054 KLSVTVDPKYHPKIIGRKGAVITQIRLEHDVNIQFPDKddgNQPQDQITITGYEKNTEAARDAIL 1118
Cdd:cd22411     1 SIKVPIFKQFHKNIIGKGGATIKKIREETNTRIDLPEE---NSDSDVITITGKKEDVEKARERIL 62
KH-I_Vigilin_rpt13 cd22416
thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
517-577 3.87e-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: 54.54  E-value: 3.87e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578804201  517 RFHRTIIGQKGERIREIRDKFpEVIINFPDPAQKSDIVQLRGPKNEVEKCTKYMQKMVADL 577
Cdd:cd22416    11 DLHRFIIGQKGADVRKMMDEF-DVNISIPPAELQSDIIKITGPPANVERAKAALLERVKEL 70
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
655-722 3.95e-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: 54.13  E-value: 3.95e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201  655 EVEVSIPAKLHNSLIGTKGRLIRSIMEEcGGVHIHFPVEGS-GSDTVVIRGPSSDVEKAKKQLLHLAEE 722
Cdd:cd22417     2 TLTVEVDPKYHPKIIGRKGAVITKLRDD-HDVNIQFPDKGDeNDDEITITGYEKNAEAAKDAILKIVQE 69
KH-I_Vigilin_rpt9 cd22412
ninth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
1128-1196 4.20e-09

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: 54.22  E-value: 4.20e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201 1128 VSEDVPLDHRVHARIIGARGKAIRKIMDEF-KVDIRFPQSGAPDpNCVTVTGLPENVEEAIDHILNLEEE 1196
Cdd:cd22412     2 VEVEVEIPAKLHNSLIGAKGRLIRSIMEECgGVHIHFPPEGSGS-DKVTIRGPKEDVEKAKKQLLELANE 70
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
974-1036 4.21e-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: 53.82  E-value: 4.21e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201   974 TIEVEVPFDLHRYVIGQKGSGIRKMMDEFEVNIHVPAPE--LQSDIIAITGLAANLDRAKAGLLE 1036
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSEseGNERIVTITGTPEAVEAAKALIEE 65
KH-I_Vigilin_rpt13 cd22416
thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1057-1126 4.94e-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: 4.94e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201 1057 VTVDPKYHPKIIGRKGAVITQIRLEHDVNIQFPDKDdgnQPQDQITITGYEKNTEAARDAILRIVGELEQ 1126
Cdd:cd22416     6 VNVPFDLHRFIIGQKGADVRKMMDEFDVNISIPPAE---LQSDIIKITGPPANVERAKAALLERVKELEA 72
KH-I_ScSCP160_rpt5 cd22450
fifth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
651-722 5.00e-09

fifth 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 fifth one.


Pssm-ID: 411878  Cd Length: 80  Bit Score: 54.21  E-value: 5.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  651 ANIAEVEVSIPAKLHNSLIGTKGRLIRSIMEECGGVH--------IHFPVEGSGSDTVVIRGPSSDVEKAKKQLLHLAEE 722
Cdd:cd22450     1 EDEVTRTIKVDRKYHRTIIGPGGSTLRELISKAGGPTdrqeqarlVRFPNQNSESDEVVIRGPKKIVEKIIAEIEKIVEE 80
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
874-971 5.90e-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: 53.75  E-value: 5.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  874 VTLECAIPQKFHRSVMGPKGSRIQQITRDFSVQIKFPDREenavhstepvvqENGDeagegreakdcdpgsprrcDIIII 953
Cdd:cd22417     1 FTLTVEVDPKYHPKIIGRKGAVITKLRDDHDVNIQFPDKG------------DEND-------------------DEITI 49
                          90
                  ....*....|....*...
gi 578804201  954 SGRKEKCEAAKEALEALV 971
Cdd:cd22417    50 TGYEKNAEAAKDAILKIV 67
KH-I_ScSCP160_rpt7 cd22452
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
593-644 6.75e-09

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: 53.48  E-value: 6.75e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578804201  593 HKNIIGKGGANIKKIREESNTKIDLPAENSNSETIIITGKRANCEAARSRIL 644
Cdd:cd22452    13 FGRIIGPGGSNINQIREKSGCFINVPKKNKESDVITLRGTKEGVEKAEEMIK 64
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
1050-1123 6.83e-09

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: 53.43  E-value: 6.83e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201 1050 LRSFKLSVTVDPKYHPKIIGRKGAVITQIRLEHDVNIQFPDKD-DGNqpqdqITITGYEKNTEAARDAILRIVGE 1123
Cdd:cd22449     1 ENGYTVKFDVPAKYVPHIIGKKGANINKLREEYGVKIDFEDKTgEGN-----VEIKGSKKNVEEAKKRILSQIDE 70
KH-I_Vigilin_rpt5 cd22409
fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
656-722 1.02e-08

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: 52.97  E-value: 1.02e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201  656 VEVSIPAKLHNSLIGTKGRLIRSIMEECGGVHIHFPvegSGSDTVVIRGPSSDVEKAKKQLLHLAEE 722
Cdd:cd22409     4 AEVSAPSWLHRFIIGKKGANIKKITQDLPKVHIEFT---EGEDKIELEGPPEEVEVVREQLEAIVKE 67
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
655-717 1.18e-08

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: 52.56  E-value: 1.18e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201  655 EVEVSIPAKLHNSLIGTKGRLIRSIMEECGgVHIHFPVEGSGSDTVVIRGPSSDVEKAKKQLL 717
Cdd:cd22408     1 TVSVEVPKSQHRFVIGPRGSTIQEILEETG-CSVEVPPNDSDSETITLRGPADKLGAALTLVY 62
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
1130-1191 1.23e-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: 52.69  E-value: 1.23e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201 1130 EDVPLDHRVHARIIGARGKAIRKIMDEFKVDIRFPQSG-APDPNCVTVTGLPENVEEAIDHIL 1191
Cdd:cd00105     1 EEIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGeGSGERVVTITGTPEAVEKAKELIE 63
KH-I_Vigilin_rpt12 cd22415
twelfth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
509-645 1.23e-08

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: 53.46  E-value: 1.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  509 TKDLIIEQRFHRTIIGQKGERIREIRDKFpEVIINFPDpaqksdivqlrgpKNEVEkctkymqkmVADLVENsysisvpi 588
Cdd:cd22415     1 TIECVIPQKFHRTVMGAKGSRVQQITSEF-DVQIKFPD-------------RESNQ---------PAPAENG-------- 49
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201  589 fkqfhkNIIGKGGANIKKIREESNTKIDLpaensnsetIIITGKRANCEAARSRILS 645
Cdd:cd22415    50 ------EGNGGEGVEGEAVDDNSPRKCDI---------IIITGKKENCEAAKEALLA 91
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
438-498 1.37e-08

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


Pssm-ID: 411839 [Multi-domain]  Cd Length: 62  Bit Score: 52.21  E-value: 1.37e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578804201  438 VEINIDHKFHRHLIGKSGANINRIKDQYKVSVRIPPDSEKSNLIRIEGDPQGVQQAKRELL 498
Cdd:cd22411     2 IKVPIFKQFHKNIIGKGGATIKKIREETNTRIDLPEENSDSDVITITGKKEDVEKARERIL 62
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
656-717 1.41e-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: 52.30  E-value: 1.41e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804201  656 VEVSIPAKLHNSLIGTKGRLIRSIMEECgGVHIHFP--VEGSGSDTVVIRGPSSDVEKAKKQLL 717
Cdd:cd00105     1 EEIEVPSELVGLIIGKGGSTIKEIEEET-GARIQIPkeGEGSGERVVTITGTPEAVEKAKELIE 63
KH-I_Vigilin_rpt5 cd22409
fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
973-1043 2.03e-08

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: 52.20  E-value: 2.03e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578804201  973 VTIEVEVPFDLHRYVIGQKGSGIRKMMDEFEvNIHVPAPELQsDIIAITGLAANLDRAKAGLLERVKELQA 1043
Cdd:cd22409     2 VVAEVSAPSWLHRFIIGKKGANIKKITQDLP-KVHIEFTEGE-DKIELEGPPEEVEVVREQLEAIVKELVA 70
KH-I_ScSCP160_rpt3 cd22448
third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
657-721 2.58e-08

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: 52.14  E-value: 2.58e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201  657 EVSIPAKLHNSLIGTKGRLIRSiMEECGGVHIHFPVEGSGS-----------DTVVIRGPSSDVEKAKKQLLHLAE 721
Cdd:cd22448     6 ILKIPVQFHGSLIGQQGKYVNR-LQEKYGVKINFPRENSSSndtetkkpqapDEVTIRGGKKGVAEAKQELLELLE 80
KH-I_ScSCP160_rpt5 cd22450
fifth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
505-576 3.05e-08

fifth 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 fifth one.


Pssm-ID: 411878  Cd Length: 80  Bit Score: 51.89  E-value: 3.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  505 ENERTKDLIIEQRFHRTIIGQKGERIREI---------RDKFPEvIINFPDPAQKSDIVQLRGPKNEVEKCTKYMQKMVA 575
Cdd:cd22450     1 EDEVTRTIKVDRKYHRTIIGPGGSTLRELiskaggptdRQEQAR-LVRFPNQNSESDEVVIRGPKKIVEKIIAEIEKIVE 79

                  .
gi 578804201  576 D 576
Cdd:cd22450    80 E 80
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
297-359 3.29e-08

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: 51.51  E-value: 3.29e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201   297 TIAVEVKKSQHKYVIGPKGNSLQEILERTGVSVEIPPSDSI--SETVILRGEPEKLGQALTEVYA 359
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEgnERIVTITGTPEAVEAAKALIEE 65
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
1127-1193 3.42e-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: 51.42  E-value: 3.42e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201 1127 MVSEDVPLDHRVHARIIGARGKAIRKIMDEFKVDIRFPQSGAPDpNCVTVTGLPENVEEAIDHILNL 1193
Cdd:cd02394     1 MAFTTIEIDPKFHGHIIGKGGANIKRIREESGVSIRIPDDEANS-DEIRIEGSPEGVKKAKAEILEL 66
KH-I_Vigilin_rpt10 cd22413
tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
1052-1117 4.09e-08

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: 51.11  E-value: 4.09e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201 1052 SFKLSVTVDPKYHPKIIGRKGAVITQIRLEHDVNIQFPDKDDgnQPQDQITITGYEKNTEAARDAI 1117
Cdd:cd22413     2 SFTVEIRAKPEYHRFLIGRGGANIRKIRDNTGARIIFPTARD--EDQELITIIGTKEAVEKAKEEL 65
KH-I_Vigilin_rpt9 cd22412
ninth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
438-502 4.53e-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: 51.14  E-value: 4.53e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201  438 VEINIDHKFHRHLIGKSGANINRIKDQY-KVSVRIPPDSEKSNLIRIEGDPQGVQQAKRELLELAS 502
Cdd:cd22412     4 VEVEIPAKLHNSLIGAKGRLIRSIMEECgGVHIHFPPEGSGSDKVTIRGPKEDVEKAKKQLLELAN 69
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
736-791 5.02e-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: 50.76  E-value: 5.02e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201  736 PEYHKFLIGKGGGKIRKVRDSTGARVIFPAAEDKDQD-LITIIGKEDAVREAQKELE 791
Cdd:cd00105     7 SELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSGErVVTITGTPEAVEKAKELIE 63
KH smart00322
K homology RNA-binding domain;
506-574 5.87e-08

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 50.76  E-value: 5.87e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201    506 NERTKDLIIEQRFHRTIIGQKGERIREIRDKFpEVIINFPDPAQKSDIVQLRGPKNEVEKCTKYMQKMV 574
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 ...
509-572 5.97e-08

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: 50.74  E-value: 5.97e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201   509 TKDLIIEQRFHRTIIGQKGERIREIRDKFpEVIINFPDPA--QKSDIVQLRGPKNEVEKCTKYMQK 572
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREET-GAKIQIPPSEseGNERIVTITGTPEAVEAAKALIEE 65
KH-I_ScSCP160_rpt6 cd22451
sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
1056-1123 6.07e-08

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: 50.92  E-value: 6.07e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201 1056 SVTVD-PK-YHPKIIGRKGAVITQIRLEHDVNIQFPDKDDgnqPQDQITITGYEKNTEAARDAILRIVGE 1123
Cdd:cd22451     2 SIDIDiPKeYHRAIIGKGGAVLRELEAETGCRIQVPKKDD---PSGKIRITGARDGVEAATAKILNISDE 68
KH-I_Vigilin_rpt7 cd22410
seventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
804-866 6.33e-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: 6.33e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201  804 SMLVDPKHHRHFVIRRGQVLREIAEEYGGVMVSFPRSGTQSDKVTLKGAKDCVEAAKKRIQEI 866
Cdd:cd22410     5 DIIIEQRFHRTIIGQKGEKIREIRDKFPQVQITFPDPGSKSDVVTLRGPKDEVDKCYKYLKKL 67
KH-I_ScSCP160_rpt3 cd22448
third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
873-971 6.41e-08

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: 50.99  E-value: 6.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  873 QVTLECAIPQKFHRSVMGPKGSRIQQITRDFSVQIKFPdREENavhstepvvqengdeagegrEAKDCDPGSPRRCDIII 952
Cdd:cd22448     2 ETTLILKIPVQFHGSLIGQQGKYVNRLQEKYGVKINFP-RENS--------------------SSNDTETKKPQAPDEVT 60
                          90
                  ....*....|....*....
gi 578804201  953 ISGRKEKCEAAKEALEALV 971
Cdd:cd22448    61 IRGGKKGVAEAKQELLELL 79
KH smart00322
K homology RNA-binding domain;
799-867 6.53e-08

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 50.76  E-value: 6.53e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201    799 NVVEDSMLVDPKHHRHFVIRRGQVLREIAEEYgGVMVSFPRSGTQSDKVTLKGAKDCVEAAKKRIQEII 867
Cdd:smart00322    1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEET-GVKIDIPGPGSEERVVEITGPPENVEKAAELILEIL 68
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
729-786 6.57e-08

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: 50.25  E-value: 6.57e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201  729 TVDIRAKPEYHKFLIGKGGGKIRKVRDSTGARVIFPaAEDKDQDLITIIGKEDAVREA 786
Cdd:cd22408     1 TVSVEVPKSQHRFVIGPRGSTIQEILEETGCSVEVP-PNDSDSETITLRGPADKLGAA 57
KH-I_ScSCP160_rpt3 cd22448
third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
506-565 6.60e-08

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: 50.99  E-value: 6.60e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578804201  506 NERTKDLIIEQRFHRTIIGQKGERIREIRDKFpEVIINFP-----------DPAQKSDIVQLRGPKNEVEK 565
Cdd:cd22448     1 DETTLILKIPVQFHGSLIGQQGKYVNRLQEKY-GVKINFPrensssndtetKKPQAPDEVTIRGGKKGVAE 70
KH smart00322
K homology RNA-binding domain;
296-360 8.51e-08

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 50.37  E-value: 8.51e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201    296 TTIAVEVKKSQHKYVIGPKGNSLQEILERTGVSVEIPPSDSISETVILRGEPEKLGQALTEVYAK 360
Cdd:smart00322    3 VTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERVVEITGPPENVEKAAELILEI 67
KH-I_BICC1_rpt3 cd22422
third type I K homology (KH) RNA-binding domain found in protein bicaudal C homolog 1 (BICC1) ...
152-213 1.04e-07

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: 50.03  E-value: 1.04e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201  152 SATVAIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPDDPS---NQIKITGTKEGIEKARHEVL 213
Cdd:cd22422     3 SMQLEIAPQHHLFMLGRNGSNIKHIMQRTGAQIHFPDPNNPPqrkSTVFISGSIDSVYLARQQLM 67
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
975-1032 1.14e-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: 1.14e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  975 IEVEVPFDLHRYVIGQKGSGIRKMMDEFEVNIHVP--APELQSDIIAITGLAANLDRAKA 1032
Cdd:cd00105     1 EEIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPkeGEGSGERVVTITGTPEAVEKAKE 60
KH-I_ScSCP160_rpt5 cd22450
fifth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
148-218 1.31e-07

fifth 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 fifth one.


Pssm-ID: 411878  Cd Length: 80  Bit Score: 50.35  E-value: 1.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  148 QTQASATVAIPKEHHRFVIGKNGEKLQDL---------ELKTATKIQIPRPDDPSNQIKITGTKEGIEKARHEVLLISAE 218
Cdd:cd22450     1 EDEVTRTIKVDRKYHRTIIGPGGSTLRELiskaggptdRQEQARLVRFPNQNSESDEVVIRGPKKIVEKIIAEIEKIVEE 80
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
737-788 1.68e-07

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: 49.12  E-value: 1.68e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578804201  737 EYHKFLIGKGGGKIRKVRDSTGARVIFPaAEDKDQDLITIIGKEDAVREAQK 788
Cdd:cd22411     9 QFHKNIIGKGGATIKKIREETNTRIDLP-EENSDSDVITITGKKEDVEKARE 59
KH-I_HNRNPK_rpt3 cd22434
third type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ...
581-631 1.78e-07

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: 49.63  E-value: 1.78e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578804201  581 SYSISVPIFKQFHKNIIGKGGANIKKIREESNT--KIDLPAENSNSETIIITG 631
Cdd:cd22434     1 TTTTQVTIPKDLAGSIIGKGGQRIRQIRHESGAsiKIDEPLPGSEDRIITITG 53
KH-I_Vigilin_rpt11 cd22414
eleventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
511-574 1.88e-07

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: 49.22  E-value: 1.88e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804201  511 DLIIEQRFHRTIIGQKGERIREIRDKFPEVIINFPDPAQKSDIVQLRGPKNEVEKCTKYMQKMV 574
Cdd:cd22414     3 EMTVDPKHHRHFVARRGQVLREIADEYGGVMVSFPRSGTQSDKVTLKGAKDCVEGAKKRILEIV 66
KH-I_Vigilin_rpt15 cd22418
fifteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
509-573 1.95e-07

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: 49.19  E-value: 1.95e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201  509 TKDLIIEQRFHRTIIGQKGERIREIRDKFpEVIINFP-DPAQKSDIVQLRGPKNEVEKCTKYMQKM 573
Cdd:cd22418     2 TEEVEIDSRVHPRLIGARGKAIRKIMEDF-KVDIRFPrSGDADPNLVTITGLEENVEECKDHLLNL 66
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
974-1032 2.06e-07

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: 49.12  E-value: 2.06e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201  974 TIEVEVPFDLHRYVIGQKGSGIRKMMDEFEVNIHVPAPELQSDIIAITGLAANLDRAKA 1032
Cdd:cd22411     1 SIKVPIFKQFHKNIIGKGGATIKKIREETNTRIDLPEENSDSDVITITGKKEDVEKARE 59
KH-I_Vigilin_rpt10 cd22413
tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
153-212 2.12e-07

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: 49.18  E-value: 2.12e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578804201  153 ATVAIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPDDP-SNQIKITGTKEGIEKARHEV 212
Cdd:cd22413     5 VEIRAKPEYHRFLIGRGGANIRKIRDNTGARIIFPTARDEdQELITIIGTKEAVEKAKEEL 65
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
583-646 2.42e-07

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: 49.34  E-value: 2.42e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804201  583 SISVPIFKQFHKNIIGKGGANIKKIREESNTKIDLPAENSNSET----------IIITGKRANCEAARSRILSI 646
Cdd:cd22447     5 NLTVPIPASTRARIIGKKGANLKQIREKTGVRIDIPPRDADAAPadedddtmveVTITGDEFNVQHAKQRIEEI 78
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
875-969 2.52e-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: 48.82  E-value: 2.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201   875 TLECAIPQKFHRSVMGPKGSRIQQITRDFSVQIKFPDREENAVHstepvvqengdeagegreakdcdpgsprrcDIIIIS 954
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNE------------------------------RIVTIT 50
                           90
                   ....*....|....*
gi 578804201   955 GRKEKCEAAKEALEA 969
Cdd:pfam00013   51 GTPEAVEAAKALIEE 65
KH-I_ScSCP160_rpt7 cd22452
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
728-792 2.58e-07

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: 48.86  E-value: 2.58e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201  728 FTVDIRAKPEYHKFLIGKGGGKIRKVRDSTGARVIFPAAeDKDQDLITIIGKEDAVREAQKELEA 792
Cdd:cd22452     2 FRGWIKVSPRYFGRIIGPGGSNINQIREKSGCFINVPKK-NKESDVITLRGTKEGVEKAEEMIKK 65
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
801-868 2.62e-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: 48.72  E-value: 2.62e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201  801 VEDSMLVDPKHHRHFVIRRGQVLREIAEEYgGVMVSFPRSGTQSDKVTLKGAKDCVEAAKKRIQEIIE 868
Cdd:cd02394     2 AFTTIEIDPKFHGHIIGKGGANIKRIREES-GVSIRIPDDEANSDEIRIEGSPEGVKKAKAEILELVD 68
KH smart00322
K homology RNA-binding domain;
726-794 3.01e-07

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 48.83  E-value: 3.01e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201    726 KSFTVDIRAKPEYHKFLIGKGGGKIRKVRDSTGARVIFPAAEDKDqDLITIIGKEDAVREAQKELEALI 794
Cdd:smart00322    1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEE-RVVEITGPPENVEKAAELILEIL 68
KH-I_Vigilin_rpt3 cd22407
third type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
585-643 4.37e-07

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: 47.97  E-value: 4.37e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201  585 SVPIFKQFHKNIIGKGGANIKKIREESNTKIDLPAENSNSETIIITGKRANCEAARSRI 643
Cdd:cd22407     3 RLDIPKVYHPFIAGPNNENVKELQEETGVRINIPPPSVNKDEIVVSGEKEGVAQAVAKI 61
KH-I_Vigilin_rpt3 cd22407
third type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
439-497 4.45e-07

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: 47.97  E-value: 4.45e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201  439 EINIDHKFHRHLIGKSGANINRIKDQYKVSVRIPPDSEKSNLIRIEGDPQGVQQAKREL 497
Cdd:cd22407     3 RLDIPKVYHPFIAGPNNENVKELQEETGVRINIPPPSVNKDEIVVSGEKEGVAQAVAKI 61
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
509-579 4.53e-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: 4.53e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578804201  509 TKDLIIEQRFHRTIIGQKGERIREIRDKFpEVIINFPDPAQKSDIVQLRGPKNEVEKCtkymQKMVADLVE 579
Cdd:cd02394     3 FTTIEIDPKFHGHIIGKGGANIKRIREES-GVSIRIPDDEANSDEIRIEGSPEGVKKA----KAEILELVD 68
KH-I_ScSCP160_rpt6 cd22451
sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
973-1035 5.44e-07

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: 48.22  E-value: 5.44e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201  973 VTIEVEVPFDLHRYVIGQKGSGIRKMMDEFEVNIHVPAPELQSDIIAITGLAANLDRAKAGLL 1035
Cdd:cd22451     1 ASIDIDIPKEYHRAIIGKGGAVLRELEAETGCRIQVPKKDDPSGKIRITGARDGVEAATAKIL 63
KH-I_Vigilin_rpt9 cd22412
ninth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
973-1040 5.61e-07

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: 48.06  E-value: 5.61e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201  973 VTIEVEVPFDLHRYVIGQKGSGIRKMMDEFE-VNIHVPAPELQSDIIAITGLAANLDRAKAGLLERVKE 1040
Cdd:cd22412     2 VEVEVEIPAKLHNSLIGAKGRLIRSIMEECGgVHIHFPPEGSGSDKVTIRGPKEDVEKAKKQLLELANE 70
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1055-1118 5.78e-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: 5.78e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804201 1055 LSVTVDPKYHPKIIGRKGAVITQIRLEHDVNIQFPDKDDgnqPQDQITITGYEKNTEAARDAIL 1118
Cdd:cd22408     2 VSVEVPKSQHRFVIGPRGSTIQEILEETGCSVEVPPNDS---DSETITLRGPADKLGAALTLVY 62
KH-I_BICC1_rpt2 cd22421
second type I K homology (KH) RNA-binding domain found in protein bicaudal C homolog 1 (BICC1) ...
973-1032 6.93e-07

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: 47.72  E-value: 6.93e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201  973 VTIEVEVPFDLHRYVIGQKGSGIRKMMDEFEVNIHVP-----APELQSDIIAITGLAANLDRAKA 1032
Cdd:cd22421     3 VTLKMDVSHTDHSHVIGKGGNNIKKVMEDTGCHIHFPdsnrtSQAEKSNQVSIAGQPAGVESARA 67
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
300-362 7.85e-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: 47.57  E-value: 7.85e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201  300 VEVKKSQHKYVIGPKGNSLQEILERTGVSVEIPPSDSISETVILRGEPEKLGQALTEVYAKAN 362
Cdd:cd02394     6 IEIDPKFHGHIIGKGGANIKRIREESGVSIRIPDDEANSDEIRIEGSPEGVKKAKAEILELVD 68
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
154-221 9.12e-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: 47.59  E-value: 9.12e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201  154 TVAIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPDDP-SNQIKITGTKEGIEKARHEVLLISAEQDK 221
Cdd:cd22417     4 TVEVDPKYHPKIIGRKGAVITKLRDDHDVNIQFPDKGDEnDDEITITGYEKNAEAAKDAILKIVQELES 72
KH-I_ScSCP160_rpt1 cd22446
first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
153-219 1.24e-06

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: 47.79  E-value: 1.24e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201  153 ATVAIPKEHHRFVIGKNGEKLQDLELKTATKIQIPR----------PDDPSNQIKITGTKEGIEKARHEVLLISAEQ 219
Cdd:cd22446     9 ITISVPSSVRGAIIGSRGKNLKSIQDKTGTKIQIPKrneegnydedDDDETVEISIEGDAEGVELAKKEIEAIVKER 85
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
1054-1122 1.24e-06

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: 47.41  E-value: 1.24e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201 1054 KLSVTVDPKYHPKIIGRKGAVITQIRLEHDVNIQFPDKDDGNQPQD-------QITITGYEKNTEAARDAILRIVG 1122
Cdd:cd22447     5 NLTVPIPASTRARIIGKKGANLKQIREKTGVRIDIPPRDADAAPADedddtmvEVTITGDEFNVQHAKQRIEEIIS 80
KH-I_IGF2BP_rpt2 cd22401
second type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
593-664 1.25e-06

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: 47.22  E-value: 1.25e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201  593 HKN----IIGKGGANIKKIREESNTKIDLpaenSNSETIIItgkrANCEaarsRILSIQKDLANIAEVEVSIPAKL 664
Cdd:cd22401     7 HNNlcgrLIGKDGRNIKKIMEDTNTKITI----SSLQDLTS----YNPE----RTITIKGSLEAMSEAESLISEKL 70
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
372-425 1.53e-06

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: 46.51  E-value: 1.53e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201   372 PSWLHRFIIGKKGQNLAKITQQMpKVHIEF-----TEGEDKITLEGPTEDVNVAQEQIE 425
Cdd:pfam00013    7 PSSLVGLIIGKGGSNIKEIREET-GAKIQIppsesEGNERIVTITGTPEAVEAAKALIE 64
KH-I_Vigilin_rpt15 cd22418
fifteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
728-793 1.57e-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: 46.88  E-value: 1.57e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201  728 FTVDIRAKPEYHKFLIGKGGGKIRKVRDSTGARVIFPAAEDKDQDLITIIGKEDAVREAQKELEAL 793
Cdd:cd22418     1 VTEEVEIDSRVHPRLIGARGKAIRKIMEDFKVDIRFPRSGDADPNLVTITGLEENVEECKDHLLNL 66
KH-I_IGF2BP_rpt1 cd22400
first type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
596-646 1.86e-06

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: 46.50  E-value: 1.86e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578804201  596 IIGKGGANIKKIREESNTKIDL--PAENSNSETII-ITGKRANCEAARSRILSI 646
Cdd:cd22400    14 IIGKGGATIRQITQQTGARIDIhrKENAGAAEKAItIYGTPEGCSSACKQILEI 67
KH-I_Vigilin_rpt7 cd22410
seventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
983-1036 2.09e-06

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: 46.50  E-value: 2.09e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578804201  983 LHRYVIGQKGSGIRKMMDEF-EVNIHVPAPELQSDIIAITGLAANLDRAKAGLLE 1036
Cdd:cd22410    12 FHRTIIGQKGEKIREIRDKFpQVQITFPDPGSKSDVVTLRGPKDEVDKCYKYLKK 66
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
594-658 2.11e-06

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 51.97  E-value: 2.11e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201  594 KNIIGKGGANIKKIREESNTKIDLpaenSNSETIIITGK-RANCEAARSRILSIqkdlanIAEVEV 658
Cdd:PRK11824  566 RDVIGPGGKTIREITEETGAKIDI----EDDGTVKIAATdGEAAEAAKERIEGI------TAEPEV 621
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
741-794 2.49e-06

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: 46.64  E-value: 2.49e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201  741 FLIGKGGGKIRKVRDSTGARVIFP--------AAEDKDQDL-ITIIGKEDAVREAQKELEALI 794
Cdd:cd22447    17 RIIGKKGANLKQIREKTGVRIDIPprdadaapADEDDDTMVeVTITGDEFNVQHAKQRIEEII 79
KH-I_BICC1_rpt2 cd22421
second type I K homology (KH) RNA-binding domain found in protein bicaudal C homolog 1 (BICC1) ...
433-497 2.68e-06

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: 46.18  E-value: 2.68e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  433 NRMDyVEINIDHKFHRHLIGKSGANINRIKDQYKVSVRIP-----PDSEKSNLIRIEGDPQGVQQAKREL 497
Cdd:cd22421     1 NRVT-LKMDVSHTDHSHVIGKGGNNIKKVMEDTGCHIHFPdsnrtSQAEKSNQVSIAGQPAGVESARAQI 69
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
802-865 2.89e-06

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: 45.74  E-value: 2.89e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201   802 EDSMLVDPKHHRHFVIRRGQVLREIAEEYGgVMVSFPR--SGTQSDKVTLKGAKDCVEAAKKRIQE 865
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETG-AKIQIPPseSEGNERIVTITGTPEAVEAAKALIEE 65
KH smart00322
K homology RNA-binding domain;
369-428 2.98e-06

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 45.75  E-value: 2.98e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201    369 VAAPSWLHRFIIGKKGQNLAKITQQMpKVHIEF---TEGEDKITLEGPTEDVNVAQEQIEGMV 428
Cdd:smart00322    7 VLIPADKVGLIIGKGGSTIKKIEEET-GVKIDIpgpGSEERVVEITGPPENVEKAAELILEIL 68
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
438-498 3.12e-06

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: 45.62  E-value: 3.12e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578804201  438 VEINIDHKFHRHLIGKSGANINRIKDQYKVSVRIPPDSEKSNLIRIEGDPQGVQQAKRELL 498
Cdd:cd22408     2 VSVEVPKSQHRFVIGPRGSTIQEILEETGCSVEVPPNDSDSETITLRGPADKLGAALTLVY 62
KH smart00322
K homology RNA-binding domain;
872-971 3.63e-06

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 45.75  E-value: 3.63e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201    872 AQVTLECAIPQKFHRSVMGPKGSRIQQITRDFSVQIKFPDREENavhstepvvqengdeagegreakdcdpgsprrCDII 951
Cdd:smart00322    1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSE--------------------------------ERVV 48
                            90       100
                    ....*....|....*....|
gi 578804201    952 IISGRKEKCEAAKEALEALV 971
Cdd:smart00322   49 EITGPPENVEKAAELILEIL 68
KH-I_ScSCP160_rpt7 cd22452
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
509-572 3.63e-06

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: 45.77  E-value: 3.63e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804201  509 TKDLIIEQRFHRTIIGQKGERIREIRDKFpEVIINFPDPAQKSDIVQLRGPKNEVEKCTKYMQK 572
Cdd:cd22452     3 RGWIKVSPRYFGRIIGPGGSNINQIREKS-GCFINVPKKNKESDVITLRGTKEGVEKAEEMIKK 65
KH-I_ScSCP160_rpt3 cd22448
third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
150-213 4.14e-06

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: 45.98  E-value: 4.14e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201  150 QASATVAIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPDDPSN-----------QIKITGTKEGIEKARHEVL 213
Cdd:cd22448     2 ETTLILKIPVQFHGSLIGQQGKYVNRLQEKYGVKINFPRENSSSNdtetkkpqapdEVTIRGGKKGVAEAKQELL 76
KH-I_ScSCP160_rpt6 cd22451
sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
727-794 5.03e-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: 45.52  E-value: 5.03e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201  727 SFTVDIRAkpEYHKFLIGKGGGKIRKVRDSTGARVIFPAAEDKDQDlITIIGKEDAVREAQKELEALI 794
Cdd:cd22451     2 SIDIDIPK--EYHRAIIGKGGAVLRELEAETGCRIQVPKKDDPSGK-IRITGARDGVEAATAKILNIS 66
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
803-864 5.24e-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: 44.98  E-value: 5.24e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804201  803 DSMLVDPKHHRHFVIRRGQVLREIaEEYGGVMVSFPR--SGTQSDKVTLKGAKDCVEAAKKRIQ 864
Cdd:cd00105     1 EEIEVPSELVGLIIGKGGSTIKEI-EEETGARIQIPKegEGSGERVVTITGTPEAVEKAKELIE 63
KH-I_Vigilin_rpt2 cd22406
second type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
973-1045 5.35e-06

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: 45.38  E-value: 5.35e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201  973 VTIEVEVPFDLHRYVIGQKGSGIRKMMDEFEVNIHVPAPELQSDIIAITGLAANLDRAKagllERVKELQAEQ 1045
Cdd:cd22406     5 ASVTVNIPKEHHRFILGKKGKKLQELELKTATKIVIPRQEDNSDEIKITGTKEGIEKAR----HEIQLISDEQ 73
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
223-283 5.36e-06

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: 45.25  E-value: 5.36e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578804201  223 AVERLEVEKAFHPFIAGPYNRLVGEIMQETGTRINIPPPSVNRTEIVFTGEKEQLAQAVAR 283
Cdd:cd02394     2 AFTTIEIDPKFHGHIIGKGGANIKRIREESGVSIRIPDDEANSDEIRIEGSPEGVKKAKAE 62
KH-I_BICC1_rpt2 cd22421
second type I K homology (KH) RNA-binding domain found in protein bicaudal C homolog 1 (BICC1) ...
593-643 5.48e-06

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: 45.41  E-value: 5.48e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201  593 HKNIIGKGGANIKKIREESNTKIDLPAENSNSET-----IIITGKRANCEAARSRI 643
Cdd:cd22421    14 HSHVIGKGGNNIKKVMEDTGCHIHFPDSNRTSQAeksnqVSIAGQPAGVESARAQI 69
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
224-283 6.22e-06

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: 44.96  E-value: 6.22e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804201   224 VERLEVEKAFHPFIAGPYNRLVGEIMQETGTRINIPPPSVNRTE--IVFTGEKEQLAQAVAR 283
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNEriVTITGTPEAVEAAKAL 62
KH-I_Vigilin_rpt10 cd22413
tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
1128-1190 7.08e-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: 44.94  E-value: 7.08e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201 1128 VSEDVPLDHRVHARIIGARGKAIRKIMDEFKVDIRFPQSGAPDPNCVTVTGLPENVEEAIDHI 1190
Cdd:cd22413     3 FTVEIRAKPEYHRFLIGRGGANIRKIRDNTGARIIFPTARDEDQELITIIGTKEAVEKAKEEL 65
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1129-1191 7.53e-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: 44.50  E-value: 7.53e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201 1129 SEDVPLDHRVHARIIGARGKAIRKIMDEFKVDIRFPQSGApDPNCVTVTGLPENVEEAIDHIL 1191
Cdd:cd22411     1 SIKVPIFKQFHKNIIGKGGATIKKIREETNTRIDLPEENS-DSDVITITGKKEDVEKARERIL 62
KH-I_Vigilin_rpt11 cd22414
eleventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
439-500 8.11e-06

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: 44.60  E-value: 8.11e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201  439 EINIDHKFHRHLIGKSGANINRIKDQY-KVSVRIPPDSEKSNLIRIEGDPQGVQQAKRELLEL 500
Cdd:cd22414     3 EMTVDPKHHRHFVARRGQVLREIADEYgGVMVSFPRSGTQSDKVTLKGAKDCVEGAKKRILEI 65
KH-I_Vigilin_rpt11 cd22414
eleventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1056-1121 9.13e-06

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: 44.60  E-value: 9.13e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201 1056 SVTVDPKYHPKIIGRKGAVITQIRLEH-DVNIQFPDKDDGNqpqDQITITGYEKNTEAARDAILRIV 1121
Cdd:cd22414     3 EMTVDPKHHRHFVARRGQVLREIADEYgGVMVSFPRSGTQS---DKVTLKGAKDCVEGAKKRILEIV 66
KH-I_Vigilin_rpt15 cd22418
fifteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
582-649 9.18e-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: 44.57  E-value: 9.18e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201  582 YSISVPIFKQFHKNIIGKGGANIKKIREESNTKIDLPA-ENSNSETIIITGKRANCEAARSRILSIQKD 649
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, ...
874-971 9.28e-06

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: 44.48  E-value: 9.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  874 VTLECAIPQKFHRSVMGPKGSRIQQITRDFSVQIKFPDREENAvhstepvvqengdeagegreakdcdpgsprrcDIIII 953
Cdd:cd02394     2 AFTTIEIDPKFHGHIIGKGGANIKRIREESGVSIRIPDDEANS--------------------------------DEIRI 49
                          90
                  ....*....|....*...
gi 578804201  954 SGRKEKCEAAKEALEALV 971
Cdd:cd02394    50 EGSPEGVKKAKAEILELV 67
KH-I_Vigilin_rpt5 cd22409
fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
812-872 9.52e-06

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: 44.49  E-value: 9.52e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578804201  812 HRHFVIRRGQVLREIAEEYGGVMVSFPRSGtqsDKVTLKGAKDCVEAAKKRIQEIIEDLEA 872
Cdd:cd22409    13 HRFIIGKKGANIKKITQDLPKVHIEFTEGE---DKIELEGPPEEVEVVREQLEAIVKELVA 70
KH smart00322
K homology RNA-binding domain;
221-283 1.01e-05

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 44.59  E-value: 1.01e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201    221 KRAVERLEVEKAFHPFIAGPYNRLVGEIMQETGTRINIPPPSVNRTEIVFTGEKEQLAQAVAR 283
Cdd:smart00322    1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERVVEITGPPENVEKAAEL 63
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
368-431 1.15e-05

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: 44.50  E-value: 1.15e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201  368 SVAAPSWLHRFIIGKKGQNLAKItQQMPKVHIEF----TEGEDKITLEGPTEDVNVAQEQIEGMVKDL 431
Cdd:cd22417     4 TVEVDPKYHPKIIGRKGAVITKL-RDDHDVNIQFpdkgDENDDEITITGYEKNAEAAKDAILKIVQEL 70
KH-I_ScSCP160_rpt6 cd22451
sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
1131-1196 1.29e-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: 44.37  E-value: 1.29e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201 1131 DVPLDHrvHARIIGARGKAIRKIMDEFKVDIRFPQSGAPDPNcVTVTGLPENVEEAIDHILNLEEE 1196
Cdd:cd22451     6 DIPKEY--HRAIIGKGGAVLRELEAETGCRIQVPKKDDPSGK-IRITGARDGVEAATAKILNISDE 68
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
300-357 1.44e-05

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: 43.83  E-value: 1.44e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  300 VEVKKSQHKYVIGPKGNSLQEILERTGVSVEIPPSDSISE--TVILRGEPEKLGQALTEV 357
Cdd:cd00105     3 IEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSGerVVTITGTPEAVEKAKELI 62
KH-I_Vigilin_rpt7 cd22410
seventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1129-1186 1.47e-05

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: 43.80  E-value: 1.47e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201 1129 SEDVPLDHRVHARIIGARGKAIRKIMDEF-KVDIRFPQSGApDPNCVTVTGLPENVEEA 1186
Cdd:cd22410     3 TKDIIIEQRFHRTIIGQKGEKIREIRDKFpQVQITFPDPGS-KSDVVTLRGPKDEVDKC 60
KH-I_ASCC1 cd22419
type I K homology (KH) RNA-binding domain found in activating signal cointegrator 1 complex ...
440-501 1.49e-05

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: 43.72  E-value: 1.49e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201  440 INIDHKFHRHLIGKSGANINRIKDQYKVSVRIPPdSEKSNLIRIEG-DPQGVQQAKRELLELA 501
Cdd:cd22419     5 LDVPSALFKFIIGKKGETKKRLESETKTQIRIPR-QGKEGDIVITGkDRSGVDSARTRIEVLV 66
KH-I_ScSCP160_rpt6 cd22451
sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
654-723 1.67e-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: 43.98  E-value: 1.67e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  654 AEVEVSIPAKLHNSLIGTKGRLIRSIMEECgGVHIHFPVEGSGSDTVVIRGPSSDVEKAKKQLLHLAEEK 723
Cdd:cd22451     1 ASIDIDIPKEYHRAIIGKGGAVLRELEAET-GCRIQVPKKDDPSGKIRITGARDGVEAATAKILNISDEE 69
KH-I_PCBP_rpt1 cd22438
first type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
596-635 1.68e-05

first type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding proteins (PCBPs); The PCBP family, also known as hnRNP E family, comprises four members, PCBP1-4, which are RNA-binding proteins that interact in a sequence-specific manner with single-stranded poly(C) sequences. They are mainly involved in various posttranscriptional regulations, including mRNA stabilization or translational activation/silencing. Besides, PCBPs may share iron chaperone activity. PCBPs contain three K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411866 [Multi-domain]  Cd Length: 67  Bit Score: 43.79  E-value: 1.68e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 578804201  596 IIGKGGANIKKIREESNTKIDLpAENSNSETII-ITGKRAN 635
Cdd:cd22438    13 IIGKKGETIKKFREESGARINI-SDGSCPERIVtVTGTTDA 52
KH-I_BICC1_rpt2 cd22421
second type I K homology (KH) RNA-binding domain found in protein bicaudal C homolog 1 (BICC1) ...
1131-1190 1.73e-05

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: 43.87  E-value: 1.73e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804201 1131 DVPldHRVHARIIGARGKAIRKIMDEFKVDIRFPQSG----APDPNCVTVTGLPENVEEAIDHI 1190
Cdd:cd22421     8 DVS--HTDHSHVIGKGGNNIKKVMEDTGCHIHFPDSNrtsqAEKSNQVSIAGQPAGVESARAQI 69
KH-I_Vigilin_rpt13 cd22416
thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
737-803 1.76e-05

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: 44.14  E-value: 1.76e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201  737 EYHKFLIGKGGGKIRKVRDSTGARVIFPAAEDKdQDLITIIGKEDAVREAQKELEALIQNLDNVVED 803
Cdd:cd22416    11 DLHRFIIGQKGADVRKMMDEFDVNISIPPAELQ-SDIIKITGPPANVERAKAALLERVKELEAEKED 76
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
874-921 1.80e-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: 43.95  E-value: 1.80e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 578804201  874 VTLECAIPQKFHRSVMGPKGSRIQQITRDFSVQIKFPDREENAVHSTE 921
Cdd:cd22447     4 QNLTVPIPASTRARIIGKKGANLKQIREKTGVRIDIPPRDADAAPADE 51
KH-I_BICC1_rpt3 cd22422
third type I K homology (KH) RNA-binding domain found in protein bicaudal C homolog 1 (BICC1) ...
727-790 1.89e-05

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: 43.48  E-value: 1.89e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201  727 SFTVDIraKPEYHKFLIGKGGGKIRKVRDSTGARVIFPAAEDKDQ--DLITIIGKEDAVREAQKEL 790
Cdd:cd22422     3 SMQLEI--APQHHLFMLGRNGSNIKHIMQRTGAQIHFPDPNNPPQrkSTVFISGSIDSVYLARQQL 66
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
802-863 1.98e-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: 43.31  E-value: 1.98e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804201  802 EDSMLVDPKHHRHFVIRRGQVLREIAEEYgGVMVSFPRSGTQSDKVTLKGAKDCVEAAKKRI 863
Cdd:cd22408     1 TVSVEVPKSQHRFVIGPRGSTIQEILEET-GCSVEVPPNDSDSETITLRGPADKLGAALTLV 61
KH-I_Vigilin_rpt2 cd22406
second type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
438-497 2.09e-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: 43.84  E-value: 2.09e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  438 VEINIDHKFHRHLIGKSGANINRIKDQYKVSVRIPPDSEKSNLIRIEGDPQGVQQAKREL 497
Cdd:cd22406     7 VTVNIPKEHHRFILGKKGKKLQELELKTATKIVIPRQEDNSDEIKITGTKEGIEKARHEI 66
KH-I_PNPase cd02393
type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase ...
596-649 2.36e-05

type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase (PNPase) and similar proteins; PNPase, also called polynucleotide phosphorylase, is a polyribonucleotide nucleotidyl transferase that degrades mRNA in prokaryotes and plant chloroplasts. It catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. It is also involved, along with RNase II, in tRNA processing. The C-terminal region of PNPase contains domains homologous to those in other RNA binding proteins: a KH domain and an S1 domain. The model corresponds to the KH domain.


Pssm-ID: 411803 [Multi-domain]  Cd Length: 70  Bit Score: 43.62  E-value: 2.36e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578804201  596 IIGKGGANIKKIREESNTKIDLpaenSNSETIIITGK-RANCEAARSRILSIQKD 649
Cdd:cd02393    18 VIGPGGKTIRAIIEETGAKIDI----EDDGTVTIFATdKESAEAAKAMIEDIVAE 68
KH-I_BICC1_rpt2 cd22421
second type I K homology (KH) RNA-binding domain found in protein bicaudal C homolog 1 (BICC1) ...
660-716 2.58e-05

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: 43.49  E-value: 2.58e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804201  660 IPAKLHNSLIGTKGRLIRSIMEECgGVHIHFP-----VEGSGSDTVVIRGPSSDVEKAKKQL 716
Cdd:cd22421     9 VSHTDHSHVIGKGGNNIKKVMEDT-GCHIHFPdsnrtSQAEKSNQVSIAGQPAGVESARAQI 69
KH-I_Vigilin_rpt5 cd22409
fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
729-797 2.88e-05

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: 43.34  E-value: 2.88e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804201  729 TVDIRAKPEYHKFLIGKGGGKIRKVRDStgarviFPAAE---DKDQDLITIIGKEDAVREAQKELEALIQNL 797
Cdd:cd22409     3 VAEVSAPSWLHRFIIGKKGANIKKITQD------LPKVHiefTEGEDKIELEGPPEEVEVVREQLEAIVKEL 68
KH-I_Vigilin_rpt13 cd22416
thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
801-873 3.05e-05

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: 43.37  E-value: 3.05e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201  801 VEDSMLVDPKHHRHFVIRRGQVLREIAEEYGgVMVSFPRSGTQSDKVTLKGAKDCVEAAKKRIQEIIEDLEAQ 873
Cdd:cd22416     2 VTEEVNVPFDLHRFIIGQKGADVRKMMDEFD-VNISIPPAELQSDIIKITGPPANVERAKAALLERVKELEAE 73
KH-I_Vigilin_rpt12 cd22415
twelfth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
438-500 3.18e-05

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: 43.83  E-value: 3.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  438 VEINIDHKFHRHLIGKSGANINRIKDQYKVSVRIP----------------------------PDSEKSNLIRIEGDPQG 489
Cdd:cd22415     2 IECVIPQKFHRTVMGAKGSRVQQITSEFDVQIKFPdresnqpapaengegnggegvegeavddNSPRKCDIIIITGKKEN 81
                          90
                  ....*....|.
gi 578804201  490 VQQAKRELLEL 500
Cdd:cd22415    82 CEAAKEALLAL 92
KH-I_ScSCP160_rpt7 cd22452
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
162-213 3.87e-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: 3.87e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578804201  162 HRFVIGKNGEKLQDLELKTATKIQIPRPDDPSNQIKITGTKEGIEKARHEVL 213
Cdd:cd22452    13 FGRIIGPGGSNINQIREKSGCFINVPKKNKESDVITLRGTKEGVEKAEEMIK 64
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1131-1191 3.93e-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: 42.54  E-value: 3.93e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578804201 1131 DVPLDHRVHARIIGARGKAIRKIMDEFKVDIRFPQSGAPDPNcVTVTGLPENVEEAIDHIL 1191
Cdd:cd22408     3 SVEVPKSQHRFVIGPRGSTIQEILEETGCSVEVPPNDSDSET-ITLRGPADKLGAALTLVY 62
KH-I_CeGLD3_rpt1 cd22441
first type I K homology (KH) RNA-binding domain found in Caenorhabditis elegans defective in ...
1054-1114 4.11e-05

first type I K homology (KH) RNA-binding domain found in Caenorhabditis elegans defective in germ line development protein 3 (CeGLD-3) and similar proteins; CeGLD-3, also called germline development defective 3, is a Bicaudal-C (Bic-C) homolog that is involved in the translational control of germline-specific mRNAs during embryogenesis. It interacts with the cytoplasmic poly(A)-polymerase GLD-2. The two proteins cooperate to recognize target mRNAs and convert them into a polyadenylated, translationally active state. CeGLD-3 contains four K-homology (KH) RNA-binding domains, which are divergent KH domains that lacks the RNA-binding GXXG motif. The model corresponds to the first one.


Pssm-ID: 411869  Cd Length: 71  Bit Score: 42.97  E-value: 4.11e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201 1054 KLSVTVDPKYHPKIIGRKGA--VITQIRLEHDVNIQFPDKDD--GNQPQDQITITGYEKNTEAAR 1114
Cdd:cd22441     3 TLNMEFESQYHSLMTSDNGDheNIASIMAETSTLIQFPDRSVggPEPFANQVTITGYFVNVERAR 67
KH-I_ScSCP160_rpt7 cd22452
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
1057-1118 4.48e-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: 4.48e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804201 1057 VTVDPKYHPKIIGRKGAVITQIRLEHDVNIQFPDKDDGNqpqDQITITGYEKNTEAARDAIL 1118
Cdd:cd22452     6 IKVSPRYFGRIIGPGGSNINQIREKSGCFINVPKKNKES---DVITLRGTKEGVEKAEEMIK 64
KH-I_Vigilin_rpt7 cd22410
seventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
880-911 5.32e-05

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: 42.26  E-value: 5.32e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 578804201  880 IPQKFHRSVMGPKGSRIQQITRDFS-VQIKFPD 911
Cdd:cd22410     8 IEQRFHRTIIGQKGEKIREIRDKFPqVQITFPD 40
KH-I_Vigilin_rpt2 cd22406
second type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
724-793 5.62e-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: 42.68  E-value: 5.62e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  724 QTKSfTVDIRAKPEYHKFLIGKGGGKIRKVRDSTGARVIFPAAEDkDQDLITIIGKEDAVREAQKELEAL 793
Cdd:cd22406     2 QTQA-SVTVNIPKEHHRFILGKKGKKLQELELKTATKIVIPRQED-NSDEIKITGTKEGIEKARHEIQLI 69
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
438-503 5.89e-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: 42.26  E-value: 5.89e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201  438 VEINIDHKFHRHLIGKSGANINRIKDQYKVSVRIpPDSEKSNLIRIEGDPQGVQQAKRELLELASR 503
Cdd:cd22449     6 VKFDVPAKYVPHIIGKKGANINKLREEYGVKIDF-EDKTGEGNVEIKGSKKNVEEAKKRILSQIDE 70
KH-I_Vigilin_rpt3 cd22407
third type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
300-357 5.90e-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: 5.90e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201  300 VEVKKSQHKYVIGPKGNSLQEILERTGVSVEIPPSDSISETVILRGEPEKLGQALTEV 357
Cdd:cd22407     4 LDIPKVYHPFIAGPNNENVKELQEETGVRINIPPPSVNKDEIVVSGEKEGVAQAVAKI 61
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
372-425 6.21e-05

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: 41.90  E-value: 6.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201  372 PSWLHRFIIGKKGQNLAKItQQMPKVHIEF-----TEGEDKITLEGPTEDVNVAQEQIE 425
Cdd:cd00105     6 PSELVGLIIGKGGSTIKEI-EEETGARIQIpkegeGSGERVVTITGTPEAVEKAKELIE 63
KH-I_TDRKH_rpt1 cd22428
first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing ...
596-646 6.37e-05

first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing protein (TDRKH) and similar proteins; TDRKH, also called tudor domain-containing protein 2 (TDRD2), is a mitochondria-anchored RNA-binding protein that is required for spermatogenesis and involved in piRNA biogenesis. It specifically recruits MIWI, but not MILI, to engage the piRNA pathway. TDRKH contains two K-homology (KH) RNA-binding domains and one tudor domain, which are involved in binding to RNA or single-strand DNA. The model corresponds to the first one.


Pssm-ID: 411856 [Multi-domain]  Cd Length: 74  Bit Score: 42.32  E-value: 6.37e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578804201  596 IIGKGGANIKKIREESNTKIDLPAENSNSE----TIIITGKRANCEAARSRILSI 646
Cdd:cd22428    19 IIGRQGATIKQIQKETGARIDFKDEGSGGElperVLLIQGNPVQAQRAEEAIHQI 73
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
512-571 6.66e-05

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: 41.90  E-value: 6.66e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804201  512 LIIEQRFHRTIIGQKGERIREIRDKFpEVIINFPDPAQKSD--IVQLRGPKNEVEKCTKYMQ 571
Cdd:cd00105     3 IEVPSELVGLIIGKGGSTIKEIEEET-GARIQIPKEGEGSGerVVTITGTPEAVEKAKELIE 63
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
448-502 7.15e-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: 42.40  E-value: 7.15e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201  448 RHLIGKSGANINRIKDQYKVSVRIPP----------DSEKSNLIRIEGDPQGVQQAKRELLELAS 502
Cdd:cd22447    16 ARIIGKKGANLKQIREKTGVRIDIPPrdadaapadeDDDTMVEVTITGDEFNVQHAKQRIEEIIS 80
KH-I_Vigilin_rpt15 cd22418
fifteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
801-869 7.42e-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: 41.87  E-value: 7.42e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  801 VEDSMLVDPKHHRHFVIRRGQVLREIAEEYgGVMVSFPRSGT-QSDKVTLKGAKDCVEAAKKRIQEIIED 869
Cdd:cd22418     1 VTEEVEIDSRVHPRLIGARGKAIRKIMEDF-KVDIRFPRSGDaDPNLVTITGLEENVEECKDHLLNLEEE 69
KH-I_ScSCP160_rpt5 cd22450
fifth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
439-502 7.43e-05

fifth 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 fifth one.


Pssm-ID: 411878  Cd Length: 80  Bit Score: 42.26  E-value: 7.43e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201  439 EINIDHKFHRHLIGKSGANINRI---------KDQYKVSVRIPPDSEKSNLIRIEGDPQGVQQAKRELLELAS 502
Cdd:cd22450     7 TIKVDRKYHRTIIGPGGSTLRELiskaggptdRQEQARLVRFPNQNSESDEVVIRGPKKIVEKIIAEIEKIVE 79
KH-I_ScSCP160_rpt3 cd22448
third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
1057-1121 7.80e-05

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


Pssm-ID: 411876  Cd Length: 81  Bit Score: 42.51  E-value: 7.80e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201 1057 VTVDPKYHPKIIGRKGAVITQIRLEHDVNIQFPDKDDGN--------QPQDQITITGYEKNTEAARDAILRIV 1121
Cdd:cd22448     7 LKIPVQFHGSLIGQQGKYVNRLQEKYGVKINFPRENSSSndtetkkpQAPDEVTIRGGKKGVAEAKQELLELL 79
KH-I_BTR1_rpt2 cd22437
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 ...
596-644 8.98e-05

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: 41.82  E-value: 8.98e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578804201  596 IIGKGGANIKKIREESNTKI-----DLPAENSNSETIIITGKRANCEAARSRIL 644
Cdd:cd22437    13 IIGKGGSTIKELREDSNANIkispkDQLLPGSSERIVTITGSFDQVVKAVALIL 66
KH-I_Vigilin_rpt5 cd22409
fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
592-652 9.46e-05

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: 41.80  E-value: 9.46e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804201  592 FHKNIIGKGGANIKKIREE-SNTKIDLPAEnsnSETIIITGKRANCEAARSRILSIQKDLAN 652
Cdd:cd22409    12 LHRFIIGKKGANIKKITQDlPKVHIEFTEG---EDKIELEGPPEEVEVVREQLEAIVKELVA 70
KH-I_ScSCP160_rpt6 cd22451
sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
439-503 9.84e-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: 41.67  E-value: 9.84e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201  439 EINIDHKFHRHLIGKSGANINRIKDQYKVSVRIPPDSEKSNLIRIEGDPQGVQQAKRELLELASR 503
Cdd:cd22451     4 DIDIPKEYHRAIIGKGGAVLRELEAETGCRIQVPKKDDPSGKIRITGARDGVEAATAKILNISDE 68
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
876-968 1.10e-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: 41.52  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  876 LECAIPQKFHRSVMGPKGSRIQQITRDFSVQIKFPDREENAVHstepvvqengdeagegreakdcdpgsprrcDIIIISG 955
Cdd:cd00105     1 EEIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSGE------------------------------RVVTITG 50
                          90
                  ....*....|...
gi 578804201  956 RKEKCEAAKEALE 968
Cdd:cd00105    51 TPEAVEKAKELIE 63
KH-I_Vigilin_rpt7 cd22410
seventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
583-639 1.11e-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: 41.49  E-value: 1.11e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201  583 SISVPIFKQFHKNIIGKGGANIKKIREE-SNTKIDLPAENSNSETIIITGKRANCEAA 639
Cdd:cd22410     3 TKDIIIEQRFHRTIIGQKGEKIREIRDKfPQVQITFPDPGSKSDVVTLRGPKDEVDKC 60
KH-I_BTR1_rpt3 cd22514
third type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 and ...
152-210 1.11e-04

third 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 third one.


Pssm-ID: 411942 [Multi-domain]  Cd Length: 71  Bit Score: 41.64  E-value: 1.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804201  152 SATVAIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPDD-----PSNQIKITGTKEGIEKARH 210
Cdd:cd22514     2 SVTIGVPDEHIGAILGRGGRTINEIQQHSGARIKISDRGDfvsgtRNRKVTITGPQDAVQMAQY 65
KH-I_TDRKH_rpt1 cd22428
first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing ...
1067-1121 1.17e-04

first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing protein (TDRKH) and similar proteins; TDRKH, also called tudor domain-containing protein 2 (TDRD2), is a mitochondria-anchored RNA-binding protein that is required for spermatogenesis and involved in piRNA biogenesis. It specifically recruits MIWI, but not MILI, to engage the piRNA pathway. TDRKH contains two K-homology (KH) RNA-binding domains and one tudor domain, which are involved in binding to RNA or single-strand DNA. The model corresponds to the first one.


Pssm-ID: 411856 [Multi-domain]  Cd Length: 74  Bit Score: 41.55  E-value: 1.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201 1067 IIGRKGAVITQIRLEHDVNIQFPDKDDGNQPQDQI-TITGYEKNTEAARDAILRIV 1121
Cdd:cd22428    19 IIGRQGATIKQIQKETGARIDFKDEGSGGELPERVlLIQGNPVQAQRAEEAIHQII 74
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
154-212 1.24e-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: 41.63  E-value: 1.24e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201  154 TVAIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPD----------DPSNQIKITGTKEGIEKARHEV 212
Cdd:cd22447     7 TVPIPASTRARIIGKKGANLKQIREKTGVRIDIPPRDadaapadeddDTMVEVTITGDEFNVQHAKQRI 75
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
1128-1196 1.27e-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: 41.49  E-value: 1.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201 1128 VSEDVPLDHRvhARIIGARGKAIRKIMDEFKVDIRFPQsgAPDPNCVTVTGLPENVEEAIDHILNLEEE 1196
Cdd:cd22449     6 VKFDVPAKYV--PHIIGKKGANINKLREEYGVKIDFED--KTGEGNVEIKGSKKNVEEAKKRILSQIDE 70
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
297-348 1.30e-04

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: 41.03  E-value: 1.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578804201  297 TIAVEVKKSQHKYVIGPKGNSLQEILERTGVSVEIPPSDSISETVILRGEPE 348
Cdd:cd22411     1 SIKVPIFKQFHKNIIGKGGATIKKIREETNTRIDLPEENSDSDVITITGKKE 52
KH-I_BICC1_rpt3 cd22422
third type I K homology (KH) RNA-binding domain found in protein bicaudal C homolog 1 (BICC1) ...
583-644 1.49e-04

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: 41.17  E-value: 1.49e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201  583 SISVPIFKQFHKNIIGKGGANIKKIREESNTKIDLPAENSNSE---TIIITGKRANCEAARSRIL 644
Cdd:cd22422     3 SMQLEIAPQHHLFMLGRNGSNIKHIMQRTGAQIHFPDPNNPPQrksTVFISGSIDSVYLARQQLM 67
KH-I_Vigilin_rpt5 cd22409
fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
1064-1125 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 578804201 1064 HPKIIGRKGAVITQIRLE-HDVNIQFPDKddgnqpQDQITITGYEKNTEAARDAILRIVGELE 1125
Cdd:cd22409    13 HRFIIGKKGANIKKITQDlPKVHIEFTEG------EDKIELEGPPEEVEVVREQLEAIVKELV 69
KH-I_ScSCP160_rpt1 cd22446
first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
584-649 1.52e-04

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


Pssm-ID: 411874 [Multi-domain]  Cd Length: 86  Bit Score: 41.62  E-value: 1.52e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201  584 ISVPIFKQFHknIIGKGGANIKKIREESNTKIDLPAENSN----------SETIIITGKRANCEAARSRILSIQKD 649
Cdd:cd22446    11 ISVPSSVRGA--IIGSRGKNLKSIQDKTGTKIQIPKRNEEgnydeddddeTVEISIEGDAEGVELAKKEIEAIVKE 84
KH-I_Vigilin_rpt9 cd22412
ninth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
368-424 1.59e-04

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: 41.13  E-value: 1.59e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  368 SVAAPSWLHRFIIGKKGQNLAKITQQMPKVHIEFTEGE---DKITLEGPTEDVNVAQEQI 424
Cdd:cd22412     5 EVEIPAKLHNSLIGAKGRLIRSIMEECGGVHIHFPPEGsgsDKVTIRGPKEDVEKAKKQL 64
KH-I_BICC1_rpt2 cd22421
second type I K homology (KH) RNA-binding domain found in protein bicaudal C homolog 1 (BICC1) ...
1064-1117 1.62e-04

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: 41.17  E-value: 1.62e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201 1064 HPKIIGRKGAVITQIRLEHDVNIQFPDKDDGNQPQ--DQITITGYEKNTEAARDAI 1117
Cdd:cd22421    14 HSHVIGKGGNNIKKVMEDTGCHIHFPDSNRTSQAEksNQVSIAGQPAGVESARAQI 69
KH-I_BICC1_rpt2 cd22421
second type I K homology (KH) RNA-binding domain found in protein bicaudal C homolog 1 (BICC1) ...
157-212 1.78e-04

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: 41.17  E-value: 1.78e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578804201  157 IPKEHHRFVIGKNGEKLQDLELKTATKIQIP-----RPDDPSNQIKITGTKEGIEKARHEV 212
Cdd:cd22421     9 VSHTDHSHVIGKGGNNIKKVMEDTGCHIHFPdsnrtSQAEKSNQVSIAGQPAGVESARAQI 69
KH-I_Vigilin_rpt2 cd22406
second type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
297-357 1.86e-04

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: 41.14  E-value: 1.86e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578804201  297 TIAVEVKKSQHKYVIGPKGNSLQEILERTGVSVEIPPSDSISETVILRGEPEKLGQALTEV 357
Cdd:cd22406     6 SVTVNIPKEHHRFILGKKGKKLQELELKTATKIVIPRQEDNSDEIKITGTKEGIEKARHEI 66
KH-I_Vigilin_rpt2 cd22406
second type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
650-723 1.99e-04

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: 41.14  E-value: 1.99e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804201  650 LANIAEVEVSIPAKLHNSLIGTKGRLIRSImEECGGVHIHFPVEGSGSDTVVIRGPSSDVEKAKKQLLHLAEEK 723
Cdd:cd22406     1 LQTQASVTVNIPKEHHRFILGKKGKKLQEL-ELKTATKIVIPRQEDNSDEIKITGTKEGIEKARHEIQLISDEQ 73
KH-I_ScSCP160_rpt6 cd22451
sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
801-868 2.18e-04

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


Pssm-ID: 411879 [Multi-domain]  Cd Length: 69  Bit Score: 40.90  E-value: 2.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201  801 VEDSMLVDPKHHRHFVIRRGQVLREIAEEYGgVMVSFPRSGTQSDKVTLKGAKDCVEAAKKRIQEIIE 868
Cdd:cd22451     1 ASIDIDIPKEYHRAIIGKGGAVLRELEAETG-CRIQVPKKDDPSGKIRITGARDGVEAATAKILNISD 67
KH-I_FUBP_rpt1 cd22396
first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
438-497 2.21e-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: 40.70  E-value: 2.21e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804201  438 VEINIDHKFHRHLIGKSGANINRIKDQYKVSVRIPPDSEKSN--LIRIEGDPQGVQQAKREL 497
Cdd:cd22396     3 EEYKVPDKMVGLIIGRGGEQINRLQAESGAKIQIAPDSGGLPerPCTLTGTPDAIETAKRLI 64
KH-I_Vigilin_rpt5 cd22409
fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
1127-1199 2.43e-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: 40.64  E-value: 2.43e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804201 1127 MVSEDVPLDHRVHARIIGARGKAIRKIMDEF-KVDIRFPQSGapdpNCVTVTGLPENVEEAIDHILNLEEEYLA 1199
Cdd:cd22409     1 VVVAEVSAPSWLHRFIIGKKGANIKKITQDLpKVHIEFTEGE----DKIELEGPPEEVEVVREQLEAIVKELVA 70
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
651-722 2.49e-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: 40.72  E-value: 2.49e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804201  651 ANIAEVEVSIPAKLHNSLIGTKGRLIRSIMEECgGVHIHFpVEGSGSDTVVIRGPSSDVEKAKKQLLHLAEE 722
Cdd:cd22449     1 ENGYTVKFDVPAKYVPHIIGKKGANINKLREEY-GVKIDF-EDKTGEGNVEIKGSKKNVEEAKKRILSQIDE 70
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
368-429 2.51e-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: 40.86  E-value: 2.51e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804201  368 SVAAPSWLHRFIIGKKGQNLAKITQQM-PKVHI--------EFTEGEDK---ITLEGPTEDVNVAQEQIEGMVK 429
Cdd:cd22447     7 TVPIPASTRARIIGKKGANLKQIREKTgVRIDIpprdadaaPADEDDDTmveVTITGDEFNVQHAKQRIEEIIS 80
KH-I_ScSCP160_rpt5 cd22450
fifth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
584-649 2.60e-04

fifth 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 fifth one.


Pssm-ID: 411878  Cd Length: 80  Bit Score: 40.72  E-value: 2.60e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201  584 ISVPifKQFHKNIIGKGGANIKKI---------REESNTKIDLPAENSNSETIIITGKRANCEAARSRILSIQKD 649
Cdd:cd22450     8 IKVD--RKYHRTIIGPGGSTLRELiskaggptdRQEQARLVRFPNQNSESDEVVIRGPKKIVEKIIAEIEKIVEE 80
KH-I_ScSCP160_rpt1 cd22446
first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
656-723 2.82e-04

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: 40.85  E-value: 2.82e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201  656 VEVSIPAKLHNSLIGTKGRLIRSIMEECgGVHIHFPVEGSGSD----------TVVIRGPSSDVEKAKKQLLHLAEEK 723
Cdd:cd22446     9 ITISVPSSVRGAIIGSRGKNLKSIQDKT-GTKIQIPKRNEEGNydeddddetvEISIEGDAEGVELAKKEIEAIVKER 85
KH-I_ScSCP160_rpt7 cd22452
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
445-499 2.84e-04

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: 40.38  E-value: 2.84e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578804201  445 KFHRHLIGKSGANINRIKDQYKVSVRIPPDSEKSNLIRIEGDPQGVQQAKRELLE 499
Cdd:cd22452    11 RYFGRIIGPGGSNINQIREKSGCFINVPKKNKESDVITLRGTKEGVEKAEEMIKK 65
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
225-283 2.88e-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: 40.36  E-value: 2.88e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578804201  225 ERLEVEKAFHPFIAGPYNRLVGEIMQETGTRINIPPPSVNRTE--IVFTGEKEQLAQAVAR 283
Cdd:cd00105     1 EEIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSGErvVTITGTPEAVEKAKEL 61
KH-I_FUBP_rpt1 cd22396
first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
156-212 2.94e-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: 40.32  E-value: 2.94e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201  156 AIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPDDPSNQ--IKITGTKEGIEKARHEV 212
Cdd:cd22396     6 KVPDKMVGLIIGRGGEQINRLQAESGAKIQIAPDSGGLPErpCTLTGTPDAIETAKRLI 64
KH-I_Vigilin_rpt10 cd22413
tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
652-716 2.95e-04

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: 40.32  E-value: 2.95e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201  652 NIAEVEVSIPAKLHNSLIGTKGRLIRSIMEECGgVHIHFPVEG-SGSDTVVIRGPSSDVEKAKKQL 716
Cdd:cd22413     1 NSFTVEIRAKPEYHRFLIGRGGANIRKIRDNTG-ARIIFPTARdEDQELITIIGTKEAVEKAKEEL 65
KH-I_HNRNPK_rpt1 cd22432
first type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ...
596-636 3.08e-04

first 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 first one.


Pssm-ID: 411860 [Multi-domain]  Cd Length: 64  Bit Score: 40.24  E-value: 3.08e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 578804201  596 IIGKGGANIKKIREESNTKIDLPAENSNSETIIITGKRANC 636
Cdd:cd22432    16 IIGKGGENIKRLRTEYNASVSVPDSSGPERILTISADRETV 56
KH-I_CeGLD3_rpt1 cd22441
first type I K homology (KH) RNA-binding domain found in Caenorhabditis elegans defective in ...
583-643 3.16e-04

first type I K homology (KH) RNA-binding domain found in Caenorhabditis elegans defective in germ line development protein 3 (CeGLD-3) and similar proteins; CeGLD-3, also called germline development defective 3, is a Bicaudal-C (Bic-C) homolog that is involved in the translational control of germline-specific mRNAs during embryogenesis. It interacts with the cytoplasmic poly(A)-polymerase GLD-2. The two proteins cooperate to recognize target mRNAs and convert them into a polyadenylated, translationally active state. CeGLD-3 contains four K-homology (KH) RNA-binding domains, which are divergent KH domains that lacks the RNA-binding GXXG motif. The model corresponds to the first one.


Pssm-ID: 411869  Cd Length: 71  Bit Score: 40.28  E-value: 3.16e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201  583 SISVPIFKQFHKNIIGK--GGANIKKIREESNTKIDLPAENSN-----SETIIITGKRANCEAARSRI 643
Cdd:cd22441     3 TLNMEFESQYHSLMTSDngDHENIASIMAETSTLIQFPDRSVGgpepfANQVTITGYFVNVERARMRM 70
KH-I_ScSCP160_rpt3 cd22448
third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
1129-1195 3.85e-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: 40.59  E-value: 3.85e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201 1129 SEDVPLDHRVHARIIGARGKAIRKIMDEFKVDIRFP--QSGAPD--------PNCVTVTGLPENVEEAIDHILNLEE 1195
Cdd:cd22448     4 TLILKIPVQFHGSLIGQQGKYVNRLQEKYGVKINFPreNSSSNDtetkkpqaPDEVTIRGGKKGVAEAKQELLELLE 80
KH-I_ScSCP160_rpt7 cd22452
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
299-357 4.01e-04

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: 40.00  E-value: 4.01e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201  299 AVEVKKSQHKYVIGPKGNSLQEILERTGVSVEIPPSDSISETVILRGEPEKLGQALTEV 357
Cdd:cd22452     5 WIKVSPRYFGRIIGPGGSNINQIREKSGCFINVPKKNKESDVITLRGTKEGVEKAEEMI 63
KH-I_PEPPER_rpt1_like cd22459
first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
743-794 4.10e-04

first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH domain-containing protein PEPPER and similar proteins; The family includes a group of plant RNA-binding KH domain-containing proteins, such as PEPPER, flowering locus K homology domain protein (FLK), RNA-binding KH domain-containing protein RCF3 and KH domain-containing protein HEN4. PEPPER regulates vegetative and gynoecium development. It acts as a positive regulator of the central floral repressor FLOWERING LOCUS C. In concert with HUA2, PEPPER antagonizes FLK by positively regulating FLC probably at transcriptional and post-transcriptional levels, and thus acts as a negative regulator of flowering. FLK, also called flowering locus KH domain protein, regulates positively flowering by repressing FLC expression and post-transcriptional modification. PEPPER and FLK contain three K-homology (KH) RNA-binding domains. RCF3, also called protein ENHANCED STRESS RESPONSE 1 (ESR1), or protein HIGH OSMOTIC STRESS GENE EXPRESSION 5 (HOS5), or protein REGULATOR OF CBF GENE EXPRESSION 3, or protein SHINY 1 (SHI1), acts as negative regulator of osmotic stress-induced gene expression. It is involved in the regulation of thermotolerance responses under heat stress. It functions as an upstream regulator of heat stress transcription factor (HSF) genes. HEN4, also called protein HUA ENHANCER 4, plays a role in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. It functions in association with HUA1 and HUA2. RCF3 and HEN4 contain five KH RNA-binding domains. The model corresponds to the KH1 domain of PEPPER and FLK, as well as KH1 and KH3 domains of RCF3 and HEN4.


Pssm-ID: 411887 [Multi-domain]  Cd Length: 69  Bit Score: 39.90  E-value: 4.10e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578804201  743 IGKGGGKIRKVRDSTGARV-IFPAAEDKDQDLITIIGKEDAVREAQKELEALI 794
Cdd:cd22459    17 IGKGGEIIKQLRQETGARIkVEDGVPGTEERVITISSSEAPEAPVSPAQEALL 69
KH-I_Vigilin_rpt2 cd22406
second type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1055-1123 4.12e-04

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: 39.99  E-value: 4.12e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201 1055 LSVTVDPKYHPKIIGRKGAVITQIRLEHDVNIQFPDKDDGNqpqDQITITGYEKNTEAARDAILRIVGE 1123
Cdd:cd22406     7 VTVNIPKEHHRFILGKKGKKLQELELKTATKIVIPRQEDNS---DEIKITGTKEGIEKARHEIQLISDE 72
KH-I_ScSCP160_rpt7 cd22452
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
1137-1191 4.21e-04

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: 39.61  E-value: 4.21e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578804201 1137 RVHARIIGARGKAIRKIMDEFKVDIRFPQSGApDPNCVTVTGLPENVEEAIDHIL 1191
Cdd:cd22452    11 RYFGRIIGPGGSNINQIREKSGCFINVPKKNK-ESDVITLRGTKEGVEKAEEMIK 64
KH-I_Vigilin_rpt9 cd22412
ninth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
296-353 4.25e-04

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: 39.97  E-value: 4.25e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201  296 TTIAVEVKKSQHKYVIGPKGNSLQEILERT-GVSVEIPPSDSISETVILRGEPEKLGQA 353
Cdd:cd22412     2 VEVEVEIPAKLHNSLIGAKGRLIRSIMEECgGVHIHFPPEGSGSDKVTIRGPKEDVEKA 60
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
807-864 4.85e-04

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: 39.49  E-value: 4.85e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201  807 VDPKHHRHFVIRRGQVLREIAEEyGGVMVSFPRSGTQSDKVTLKGAKDCVEAAKKRIQ 864
Cdd:cd22411     6 IFKQFHKNIIGKGGATIKKIREE-TNTRIDLPEENSDSDVITITGKKEDVEKARERIL 62
KH-I_HNRNPK_rpt2 cd22433
second type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ...
596-646 4.97e-04

second 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 second one.


Pssm-ID: 411861 [Multi-domain]  Cd Length: 70  Bit Score: 39.54  E-value: 4.97e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578804201  596 IIGKGGANIKKIREESNTKIDL---PAENSNSETIIITGKRANCEAARSRILSI 646
Cdd:cd22433    16 IIGRAGFKIKELREKTGATIKVyseCCPRSTDRVVQIGGKPDKVVECIREILEL 69
KH-I_MUG60_like cd22453
type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe meiotically ...
654-710 4.98e-04

type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe meiotically up-regulated gene 60 protein (MUG60) and similar proteins; MUG60 is a KH domain-containing protein that has a role in meiosis. The family also contains Saccharomyces cerevisiae KH domain-containing protein YLL032C.


Pssm-ID: 411881 [Multi-domain]  Cd Length: 72  Bit Score: 39.66  E-value: 4.98e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804201  654 AEVEVSIPAKLHNSLIGTKGRLIRSIMEECgGVHIHFP-----VEGSGSDTVVIRGPSSDVE 710
Cdd:cd22453     2 AEISFYVPEKYHKRIIGKGGQNIQRIMKKY-NVFIKFSnandrADNYYPDNVVIRTPAKNAA 62
KH-I_ScSCP160_rpt1 cd22446
first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
372-430 5.07e-04

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: 40.08  E-value: 5.07e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578804201  372 PSWLHRFIIGKKGQNLAKITQ------QMPKVHIEFTEGED------KITLEGPTEDVNVAQEQIEGMVKD 430
Cdd:cd22446    14 PSSVRGAIIGSRGKNLKSIQDktgtkiQIPKRNEEGNYDEDdddetvEISIEGDAEGVELAKKEIEAIVKE 84
KH-I_Vigilin_rpt7 cd22410
seventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
729-793 5.10e-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: 39.57  E-value: 5.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201  729 TVDIRAKPEYHKFLIGKGGGKIRKVRDS-TGARVIFPAAeDKDQDLITIIGKEDAVREAQKELEAL 793
Cdd:cd22410     3 TKDIIIEQRFHRTIIGQKGEKIREIRDKfPQVQITFPDP-GSKSDVVTLRGPKDEVDKCYKYLKKL 67
KH-I_Vigilin_rpt13 cd22416
thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
297-353 5.18e-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: 39.91  E-value: 5.18e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201  297 TIAVEVKKSQHKYVIGPKGNSLQEILERTGVSVEIPPSDSISETVILRGEPEKLGQA 353
Cdd:cd22416     3 TEEVNVPFDLHRFIIGQKGADVRKMMDEFDVNISIPPAELQSDIIKITGPPANVERA 59
KH-I_Vigilin_rpt9 cd22412
ninth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
1055-1123 5.27e-04

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: 39.59  E-value: 5.27e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201 1055 LSVTVDPKYHPKIIGRKGAVITQIRLEHD-VNIQFPDKDDGNqpqDQITITGYEKNTEAARDAILRIVGE 1123
Cdd:cd22412     4 VEVEIPAKLHNSLIGAKGRLIRSIMEECGgVHIHFPPEGSGS---DKVTIRGPKEDVEKAKKQLLELANE 70
KH-I_ScSCP160_rpt3 cd22448
third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
729-795 5.48e-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: 39.82  E-value: 5.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201  729 TVDIRAKPEYHKFLIGKGGGKIRKVRDSTGARVIFPAAEDKDQ----------DLITIIGKEDAVREAQKELEALIQ 795
Cdd:cd22448     4 TLILKIPVQFHGSLIGQQGKYVNRLQEKYGVKINFPRENSSSNdtetkkpqapDEVTIRGGKKGVAEAKQELLELLE 80
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
297-336 5.76e-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: 39.71  E-value: 5.76e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 578804201  297 TIAVEVKKSQHKYVIGPKGNSLQEILERTGVSVEIPPSDS 336
Cdd:cd22447     5 NLTVPIPASTRARIIGKKGANLKQIREKTGVRIDIPPRDA 44
KH-I_Vigilin_rpt3 cd22407
third type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
736-791 5.94e-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: 39.11  E-value: 5.94e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201  736 PEYHKFLIGKGGGKIRKVRDSTGARV-IFPAAEDKDQdlITIIGKEDAVREAQKELE 791
Cdd:cd22407     8 KVYHPFIAGPNNENVKELQEETGVRInIPPPSVNKDE--IVVSGEKEGVAQAVAKIK 62
KH-I_DDX43_DDX53 cd22430
type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box ...
596-649 6.06e-04

type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box protein 53 (DDX53) and similar proteins; DDX43 (also called cancer/testis antigen 13, or DEAD box protein HAGE, or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 (also called cancer-associated gene protein, or cancer/testis antigen 26, or DEAD box protein CAGE) shows high expression level in various tumors and is involved in anti-cancer drug resistance. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation.


Pssm-ID: 411858 [Multi-domain]  Cd Length: 66  Bit Score: 39.19  E-value: 6.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578804201  596 IIGKGGANIKKIREESNTKIDLPAENSNSEtIIITGKRANCEAARSRILSIQKD 649
Cdd:cd22430    14 VIGRGGSKIRELEESTGSKIKIIKGGQEAE-VKIFGSDEAQQKAKELIDELVGR 66
KH-I_Vigilin_rpt13 cd22416
thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
369-431 6.12e-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: 39.52  E-value: 6.12e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201  369 VAAPSWLHRFIIGKKGQNLAKITQQMpKVHIEFTEGEDK---ITLEGPTEDVNVAQEQIEGMVKDL 431
Cdd:cd22416     6 VNVPFDLHRFIIGQKGADVRKMMDEF-DVNISIPPAELQsdiIKITGPPANVERAKAALLERVKEL 70
KH-I_MEX3_rpt2 cd22424
second type I K homology (KH) RNA-binding domain found in the family of MEX-3 RNA-binding ...
973-1031 6.31e-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: 6.31e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201  973 VTIEVEVPFDLHRYVIGQKGSGIRKMMDEFEVNIHVPAPELQSdIIAITGLAANLDRAK 1031
Cdd:cd22424     4 TTIQVRVPYRVVGLVVGPKGATIKRIQQQTHTYIVTPSRDKEP-VFEVTGMPENVERAR 61
KH-I_FUBP_rpt3 cd22398
third type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
155-210 6.59e-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: 39.16  E-value: 6.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201  155 VAIPKEHHRFVIGKNGEKLQDLELKTATKIQIpRPDDPSNQIK---ITGTKEGIEKARH 210
Cdd:cd22398     4 VPVPRFAVGVVIGKGGEMIKKIQNETGARVQF-KPDDGNSPDRicvITGPPDQVQHAAR 61
KH-I_PCBP4_rpt2 cd22520
second type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) ...
742-794 7.05e-04

second type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) and similar proteins; PCBP4, also called alpha-CP4, or heterogeneous nuclear ribonucleoprotein E4, or hnRNP E4, is a single-stranded nucleic acid binding protein that binds preferentially to oligo dC. It regulates both basal and stress-induced p21 expression through binding p21 3'-UTR and modulating p21 mRNA stability. It also plays a role in the cell cycle and is implicated in lung tumor suppression. PCBP4 contains three K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411948 [Multi-domain]  Cd Length: 72  Bit Score: 39.23  E-value: 7.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201  742 LIGKGGGKIRKVRDSTGARV-----IFPAAEDKDqdlITIIGKEDAVREAQKELEALI 794
Cdd:cd22520    16 LIGKAGSKIKEIRESTGAQVqvagdLLPNSTERA---VTVSGVPDAIIQCVRQICAVI 70
KH-I_Vigilin_rpt9 cd22412
ninth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
874-916 7.15e-04

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: 39.20  E-value: 7.15e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 578804201  874 VTLECAIPQKFHRSVMGPKGSRIQQITRDFS-VQIKFPDREENA 916
Cdd:cd22412     2 VEVEVEIPAKLHNSLIGAKGRLIRSIMEECGgVHIHFPPEGSGS 45
KH-I_FUBP_rpt1 cd22396
first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
741-794 7.19e-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: 7.19e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578804201  741 FLIGKGGGKIRKVRDSTGARVIFPAAEDKDQD-LITIIGKEDAVREAQKELEALI 794
Cdd:cd22396    14 LIIGRGGEQINRLQAESGAKIQIAPDSGGLPErPCTLTGTPDAIETAKRLIDQIV 68
KH-I_ScSCP160_rpt3 cd22448
third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
579-646 7.43e-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: 39.43  E-value: 7.43e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201  579 ENSYSISVPIfkQFHKNIIGKGGANIKKIREESNTKIDLPAENSNS-----------ETIIITGKRANCEAARSRILSI 646
Cdd:cd22448     2 ETTLILKIPV--QFHGSLIGQQGKYVNRLQEKYGVKINFPRENSSSndtetkkpqapDEVTIRGGKKGVAEAKQELLEL 78
KH-I_ScSCP160_rpt6 cd22451
sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
509-575 7.90e-04

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


Pssm-ID: 411879 [Multi-domain]  Cd Length: 69  Bit Score: 38.98  E-value: 7.90e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201  509 TKDLIIEQRFHRTIIGQKGERIREIRDKFpEVIINFPDPAQKSDIVQLRGPKNEVEKCTKYMQKMVA 575
Cdd:cd22451     2 SIDIDIPKEYHRAIIGKGGAVLRELEAET-GCRIQVPKKDDPSGKIRITGARDGVEAATAKILNISD 67
KH-I_ScSCP160_rpt5 cd22450
fifth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
295-348 8.19e-04

fifth 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 fifth one.


Pssm-ID: 411878  Cd Length: 80  Bit Score: 39.57  E-value: 8.19e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201  295 TTTIAVEVKKSQHKYVIGPKGNSLQEILERTGVS---------VEIPPSDSISETVILRGEPE 348
Cdd:cd22450     3 EVTRTIKVDRKYHRTIIGPGGSTLRELISKAGGPtdrqeqarlVRFPNQNSESDEVVIRGPKK 65
KH-I_Vigilin_rpt10 cd22413
tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
362-425 8.21e-04

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: 39.17  E-value: 8.21e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201  362 NSFTVSSVAAPSwLHRFIIGKKGQNLAKITQQMpKVHIEF----TEGEDKITLEGPTEDVNVAQEQIE 425
Cdd:cd22413     1 NSFTVEIRAKPE-YHRFLIGRGGANIRKIRDNT-GARIIFptarDEDQELITIIGTKEAVEKAKEELE 66
KH-I_HNRNPK_rpt3 cd22434
third type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ...
742-787 8.42e-04

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: 39.22  E-value: 8.42e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 578804201  742 LIGKGGGKIRKVRDSTGARVIF----PAAEDKdqdLITIIGKEDAVREAQ 787
Cdd:cd22434    16 IIGKGGQRIRQIRHESGASIKIdeplPGSEDR---IITITGTQDQIQNAQ 62
KH-I_PEPPER_rpt2_like cd22460
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
595-645 9.14e-04

second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH domain-containing protein PEPPER and similar proteins; The family includes a group of plant RNA-binding KH domain-containing proteins, such as PEPPER, flowering locus K homology domain protein (FLK), RNA-binding KH domain-containing protein RCF3 and KH domain-containing protein HEN4. PEPPER regulates vegetative and gynoecium development. It acts as a positive regulator of the central floral repressor FLOWERING LOCUS C. In concert with HUA2, PEPPER antagonizes FLK by positively regulating FLC probably at transcriptional and post-transcriptional levels, and thus acts as a negative regulator of flowering. FLK, also called flowering locus KH domain protein, regulates positively flowering by repressing FLC expression and post-transcriptional modification. PEPPER and FLK contain three K-homology (KH) RNA-binding domains. RCF3, also called protein ENHANCED STRESS RESPONSE 1 (ESR1), or protein HIGH OSMOTIC STRESS GENE EXPRESSION 5 (HOS5), or protein REGULATOR OF CBF GENE EXPRESSION 3, or protein SHINY 1 (SHI1), acts as negative regulator of osmotic stress-induced gene expression. It is involved in the regulation of thermotolerance responses under heat stress. It functions as an upstream regulator of heat stress transcription factor (HSF) genes. HEN4, also called protein HUA ENHANCER 4, plays a role in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. It functions in association with HUA1 and HUA2. RCF3 and HEN4 contain five KH RNA-binding domains. The model corresponds to the KH2 domain of PEPPER and FLK, as well as KH2 and KH4 domains of RCF3 and HEN4.


Pssm-ID: 411888 [Multi-domain]  Cd Length: 73  Bit Score: 39.14  E-value: 9.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201  595 NIIGKGGANIKKIREESNTKID-LPAE------NSNSETIIITGKRANCEAARSRILS 645
Cdd:cd22460    13 SLIGKGGAIIKQIREESGASVRiLPEEelppcaSPDDRVVQISGEAQAVKKALELVSS 70
KH-I_ANKHD1 cd22503
type I K homology (KH) RNA-binding domain found in ankyrin repeat and KH domain-containing ...
742-812 9.38e-04

type I K homology (KH) RNA-binding domain found in ankyrin repeat and KH domain-containing protein 1 (ANKHD1) and similar proteins; ANKHD1, also called HIV-1 Vpr-binding ankyrin repeat protein, or multiple ankyrin repeats single KH domain, or Hmask, is highly expressed in various cancer tissues and is involved in cancer progression, including proliferation and invasion. It acts as a scaffolding protein that may be associated with the abnormal phenotype of leukemia cells. It may play might have a role in MM cell proliferation and cell cycle progression by regulating expression of p21. It also regulates cell cycle progression and proliferation in multiple myeloma cells. ANKHD1 is a component of Hippo signaling pathway. It functions as a positive regulator of YAP1 and promotes cell growth and cell cycle progression through Cyclin A upregulation in prostate cancer cells.


Pssm-ID: 411931  Cd Length: 83  Bit Score: 39.35  E-value: 9.38e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804201  742 LIGKGGGKIRKVRDSTGARVIFPAAEDKD-QDLITIIGKEDAVREAQKELEALIQNLDNVVEDSMlvdPKHH 812
Cdd:cd22503    15 IMGRGGCNITAIQDVTGAHIDVDKQKDKNgERMITIRGGTESTRYAVQLINALIQDPAKELEDLI---PRNH 83
KH-I_ScSCP160_rpt7 cd22452
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
977-1030 1.06e-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: 38.46  E-value: 1.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578804201  977 VEVPFDLHRYVIGQKGSGIRKMMDEFEVNIHVPAPELQSDIIAITGLAANLDRA 1030
Cdd:cd22452     6 IKVSPRYFGRIIGPGGSNINQIREKSGCFINVPKKNKESDVITLRGTKEGVEKA 59
KH-I_Mextli_like cd22454
type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic ...
1066-1121 1.12e-03

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: 38.84  E-value: 1.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201 1066 KIIGRKGAVITQIRLEHDVNIQFpDKDDGNQPQDQITITGYEKNTEAARDAILRIV 1121
Cdd:cd22454    17 KVIGKGGETIKRIEALTDTVITF-ERVNGGSPNREVQITGSPDNVAAAKRLIEDTI 71
KH-I_PEPPER_rpt2_like cd22460
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
742-798 1.13e-03

second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH domain-containing protein PEPPER and similar proteins; The family includes a group of plant RNA-binding KH domain-containing proteins, such as PEPPER, flowering locus K homology domain protein (FLK), RNA-binding KH domain-containing protein RCF3 and KH domain-containing protein HEN4. PEPPER regulates vegetative and gynoecium development. It acts as a positive regulator of the central floral repressor FLOWERING LOCUS C. In concert with HUA2, PEPPER antagonizes FLK by positively regulating FLC probably at transcriptional and post-transcriptional levels, and thus acts as a negative regulator of flowering. FLK, also called flowering locus KH domain protein, regulates positively flowering by repressing FLC expression and post-transcriptional modification. PEPPER and FLK contain three K-homology (KH) RNA-binding domains. RCF3, also called protein ENHANCED STRESS RESPONSE 1 (ESR1), or protein HIGH OSMOTIC STRESS GENE EXPRESSION 5 (HOS5), or protein REGULATOR OF CBF GENE EXPRESSION 3, or protein SHINY 1 (SHI1), acts as negative regulator of osmotic stress-induced gene expression. It is involved in the regulation of thermotolerance responses under heat stress. It functions as an upstream regulator of heat stress transcription factor (HSF) genes. HEN4, also called protein HUA ENHANCER 4, plays a role in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. It functions in association with HUA1 and HUA2. RCF3 and HEN4 contain five KH RNA-binding domains. The model corresponds to the KH2 domain of PEPPER and FLK, as well as KH2 and KH4 domains of RCF3 and HEN4.


Pssm-ID: 411888 [Multi-domain]  Cd Length: 73  Bit Score: 38.76  E-value: 1.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201  742 LIGKGGGKIRKVRDSTGARV-IFPAAE-----DKDQDLITIIGKEDAVREAqkeLEALIQNLD 798
Cdd:cd22460    14 LIGKGGAIIKQIREESGASVrILPEEElppcaSPDDRVVQISGEAQAVKKA---LELVSSRLR 73
KH-I_Mextli_like cd22454
type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic ...
596-644 1.15e-03

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: 38.84  E-value: 1.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578804201  596 IIGKGGANIKKIREESNTKIDLPAENSNSET--IIITGKRANCEAARSRIL 644
Cdd:cd22454    18 VIGKGGETIKRIEALTDTVITFERVNGGSPNreVQITGSPDNVAAAKRLIE 68
KH-I_FUBP2_rpt1 cd22479
first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
450-503 1.26e-03

first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 2 (FUBP2) and similar proteins; 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. FUBP2 contains four K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411907 [Multi-domain]  Cd Length: 71  Bit Score: 38.77  E-value: 1.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201  450 LIGKSGANINRIKDQYKVSVRIPPDSE--KSNLIRIEGDPQGVQQAKRELLELASR 503
Cdd:cd22479    15 IIGRGGEQINKIQQDSGCKVQISPDSGglPERSVSLTGSPEAVQKAKMMLDDIVSR 70
KH-I_Vigilin_rpt15 cd22418
fifteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
874-970 1.32e-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: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  874 VTLECAIPQKFHRSVMGPKGSRIQQITRDFSVQIKFPdREENAvhstepvvqengdeagegreakdcDPgsprrcDIIII 953
Cdd:cd22418     1 VTEEVEIDSRVHPRLIGARGKAIRKIMEDFKVDIRFP-RSGDA------------------------DP------NLVTI 49
                          90
                  ....*....|....*..
gi 578804201  954 SGRKEKCEAAKEALEAL 970
Cdd:cd22418    50 TGLEENVEECKDHLLNL 66
KH-I_BICC1_rpt2 cd22421
second type I K homology (KH) RNA-binding domain found in protein bicaudal C homolog 1 (BICC1) ...
739-790 1.34e-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: 38.48  E-value: 1.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201  739 HKFLIGKGGGKIRKVRDSTGARVIFP------AAEDKDQdlITIIGKEDAVREAQKEL 790
Cdd:cd22421    14 HSHVIGKGGNNIKKVMEDTGCHIHFPdsnrtsQAEKSNQ--VSIAGQPAGVESARAQI 69
KH-I_Mextli_like cd22454
type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic ...
155-209 1.36e-03

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: 38.45  E-value: 1.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201  155 VAIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPDDPSNQ--IKITGTKEGIEKAR 209
Cdd:cd22454     8 VVIPNADVGKVIGKGGETIKRIEALTDTVITFERVNGGSPNreVQITGSPDNVAAAK 64
COG5166 COG5166
Uncharacterized conserved protein [Function unknown];
450-736 1.46e-03

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 227495 [Multi-domain]  Cd Length: 657  Bit Score: 43.04  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  450 LIGKSGANINRIKDQYKVSVR---IPPDS---------EKSNLIRIEGdpqgvQQAKRELLELASRMENERTK--DLIIE 515
Cdd:COG5166   237 LVGKAFSSTAGMKATESINIYtlpFCSDKiprlqtypaLNSSKIIITG-----QSEILQRLEISFYYAEMHLKlfTHVTE 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  516 QRFHRTIIGqkgerIREIRDKFPEVIINFPDPAQKSDIVqLRGPKN-----------EVEKCTKYMQKMVADLVENSYSI 584
Cdd:COG5166   312 ISFVKLFIF-----LAYNMDIMEENSSFIRFPEYFKEGV-ETTPENskvkiygssiaNSEKTALRIAKLASKYVQGKTQF 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  585 SVPIFKQFhknIIGKGGANIKKIREESNTKIDLPAENSNSETIIITGkrANCEAARSRILSIQKDlANIAEVEVSIPAKL 664
Cdd:COG5166   386 GVEDNEDF---LRGKKNGKATRIMKGVSCSELSSIVSSTGSIVETNG--IGEKMSFSKKLSIPPT-EFPAEIAFIIMESG 459
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  665 HNSLIGTKGRLIRSIMEECgGVHIHFPVE-----GSGSDTVVIRGPSSDVEK---AKKQLLHLAEEKQTKSFTVDIRAKP 736
Cdd:COG5166   460 HEMIIGTGGIEIQENMVKH-AVDIAFKNFykfgqSQWHDNVLIEAPRKNQDNisgKKNDKLDKVKQQCRFNLKGDIRFCP 538
KH-I_PCBP_rpt3 cd22439
third type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
742-787 1.53e-03

third type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding proteins (PCBPs); The PCBP family, also known as hnRNP E family, comprises four members, PCBP1-4, which are RNA-binding proteins that interact in a sequence-specific manner with single-stranded poly(C) sequences. They are mainly involved in various posttranscriptional regulations, including mRNA stabilization or translational activation/silencing. Besides, PCBPs may share iron chaperone activity. PCBPs contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411867 [Multi-domain]  Cd Length: 68  Bit Score: 38.37  E-value: 1.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 578804201  742 LIGKGGGKIRKVRDSTGARV-IFPAAEDKDQDLITIIGKEDAVREAQ 787
Cdd:cd22439    16 IIGKGGTKINEIRQLSGATIkIANSEDGSTERSVTITGTPEAVSLAQ 62
KH-I_RCF3_like_rpt5 cd22463
fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
742-794 1.55e-03

fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH domain-containing protein RCF3 and similar protein; RCF3, also called protein ENHANCED STRESS RESPONSE 1 (ESR1), or protein HIGH OSMOTIC STRESS GENE EXPRESSION 5 (HOS5), or protein REGULATOR OF CBF GENE EXPRESSION 3, or protein SHINY 1 (SHI1), acts as negative regulator of osmotic stress-induced gene expression. It is involved in the regulation of thermotolerance responses under heat stress. It functions as an upstream regulator of heat stress transcription factor (HSF) genes. HEN4, also called protein HUA ENHANCER 4, plays a role in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. It functions in association with HUA1 and HUA2. RCF3 contains five K-homology (KH) RNA-binding domains. The model corresponds to the KH5 domain of RCF3.


Pssm-ID: 411891 [Multi-domain]  Cd Length: 71  Bit Score: 38.57  E-value: 1.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201  742 LIGKGGGKIRKVRDSTGARVIF---PAAEDKDQDLITIIGKEDAVREAQKELEALI 794
Cdd:cd22463    16 IIGKSGNTIKQISERSGAFVAIvqdRYPLEETQKILRISGTEEQLKRAQSLVEGLI 71
KH-I_Vigilin_rpt2 cd22406
second type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
367-425 1.74e-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: 38.45  E-value: 1.74e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578804201  367 SSVAAPSWLHRFIIGKKGQNLAKITQQ-MPKVHI-EFTEGEDKITLEGPTEDVNVAQEQIE 425
Cdd:cd22406     7 VTVNIPKEHHRFILGKKGKKLQELELKtATKIVIpRQEDNSDEIKITGTKEGIEKARHEIQ 67
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
973-1032 1.83e-03

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: 38.55  E-value: 1.83e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  973 VTIEVEVPFDLHRYVIGQKGSGIRKMMDEFEVNIHVP------APELQSDI----IAITGLAANLDRAKA 1032
Cdd:cd22447     4 QNLTVPIPASTRARIIGKKGANLKQIREKTGVRIDIPprdadaAPADEDDDtmveVTITGDEFNVQHAKQ 73
KH-I_Vigilin_rpt10 cd22413
tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
973-1034 1.86e-03

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: 38.01  E-value: 1.86e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201  973 VTIEVEVPFDLHRYVIGQKGSGIRKMMDEFEVNIHVP-APELQSDIIAITGLAANLDRAKAGL 1034
Cdd:cd22413     3 FTVEIRAKPEYHRFLIGRGGANIRKIRDNTGARIIFPtARDEDQELITIIGTKEAVEKAKEEL 65
KH-I_FUBP_rpt3 cd22398
third type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
583-643 1.87e-03

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: 38.01  E-value: 1.87e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201  583 SISVPIFKQFHKNIIGKGGANIKKIREESNTKIDLPAENSNSETII--ITGKRANCEAARSRI 643
Cdd:cd22398     1 GMEVPVPRFAVGVVIGKGGEMIKKIQNETGARVQFKPDDGNSPDRIcvITGPPDQVQHAARMI 63
KH-I_Vigilin_rpt5 cd22409
fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
874-971 1.87e-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: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  874 VTLECAIPQKFHRSVMGPKGSRIQQITRDFS-VQIKFPDREenavhstepvvqengdeagegreakdcdpgsprrcDIII 952
Cdd:cd22409     2 VVAEVSAPSWLHRFIIGKKGANIKKITQDLPkVHIEFTEGE-----------------------------------DKIE 46
                          90
                  ....*....|....*....
gi 578804201  953 ISGRKEKCEAAKEALEALV 971
Cdd:cd22409    47 LEGPPEEVEVVREQLEAIV 65
KH-I_FUBP_rpt1 cd22396
first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
1128-1190 1.94e-03

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: 38.00  E-value: 1.94e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201 1128 VSEDVPLDHRVHARIIGARGKAIRKIMDEFKVDIRFPQ--SGAPDPNCvTVTGLPENVEEA---IDHI 1190
Cdd:cd22396     1 VTEEYKVPDKMVGLIIGRGGEQINRLQAESGAKIQIAPdsGGLPERPC-TLTGTPDAIETAkrlIDQI 67
KH-I_HNRNPK_rpt3 cd22434
third type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ...
150-210 2.27e-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: 38.07  E-value: 2.27e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201  150 QASATVAIPKEHHRFVIGKNGEKLQDLELKTATKIQI--PRPDDPSNQIKITGTKEGIEKARH 210
Cdd:cd22434     1 TTTTQVTIPKDLAGSIIGKGGQRIRQIRHESGASIKIdePLPGSEDRIITITGTQDQIQNAQY 63
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
1132-1190 2.32e-03

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: 38.17  E-value: 2.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201 1132 VPLDHRVHARIIGARGKAIRKIMDEFKVDIRFPQSGAPDPNC---------VTVTGLPENVEEAIDHI 1190
Cdd:cd22447     8 VPIPASTRARIIGKKGANLKQIREKTGVRIDIPPRDADAAPAdedddtmveVTITGDEFNVQHAKQRI 75
KH-I_ASCC1 cd22419
type I K homology (KH) RNA-binding domain found in activating signal cointegrator 1 complex ...
974-1022 2.62e-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: 2.62e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578804201  974 TIEVEVPFDLHRYVIGQKGSGIRKMMDEFEVNIHVPAPElQSDIIAITG 1022
Cdd:cd22419     2 RLSLDVPSALFKFIIGKKGETKKRLESETKTQIRIPRQG-KEGDIVITG 49
KH-I_Vigilin_rpt3 cd22407
third type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
976-1032 2.76e-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: 37.19  E-value: 2.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201  976 EVEVPFDLHRYVIGQKGSGIRKMMDEFEVNIHVPAPELQSDIIAITGLAANLDRAKA 1032
Cdd:cd22407     3 RLDIPKVYHPFIAGPNNENVKELQEETGVRINIPPPSVNKDEIVVSGEKEGVAQAVA 59
YbjL COG2985
Uncharacterized membrane protein YbjL, putative transporter [General function prediction only]; ...
956-1117 2.80e-03

Uncharacterized membrane protein YbjL, putative transporter [General function prediction only];


Pssm-ID: 442224 [Multi-domain]  Cd Length: 543  Bit Score: 42.03  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  956 RKEKCEAAKEALEA---LVPVTIEVEVPfdlhrYVIGQKGSGIRKM-MDEFEV-------NIHVPAPE--LQS-DIIAIT 1021
Cdd:COG2985   185 DAEAKKLEAGEGSAyppLVTRAYRVTNP-----NLVGKTVAELEALlGTRVVIsrirrggEIIVPTPDtvLQEgDIVLVV 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201 1022 GLAANLDRAKAGLLERVKElqAEQEDRALRSFKLSVTvdpkyHPKIIGRK----------GAVITQIR-------LEHDV 1084
Cdd:COG2985   260 GTREALEAAEALLGEEVDD--SELLDSDLDVRRIVVT-----NKEVAGKTlgelnlrnrfGVVITRVRrggvelpATPDT 332
                         170       180       190
                  ....*....|....*....|....*....|...
gi 578804201 1085 NIQFPDKddgnqpqdqITITGYEKNTEAARDAI 1117
Cdd:COG2985   333 VLQLGDR---------LTVVGPKEDVERVAKLL 356
KH-I_PCBP_rpt3 cd22439
third type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
596-631 2.87e-03

third type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding proteins (PCBPs); The PCBP family, also known as hnRNP E family, comprises four members, PCBP1-4, which are RNA-binding proteins that interact in a sequence-specific manner with single-stranded poly(C) sequences. They are mainly involved in various posttranscriptional regulations, including mRNA stabilization or translational activation/silencing. Besides, PCBPs may share iron chaperone activity. PCBPs contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411867 [Multi-domain]  Cd Length: 68  Bit Score: 37.59  E-value: 2.87e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 578804201  596 IIGKGGANIKKIREES--NTKIDLPAENSNSETIIITG 631
Cdd:cd22439    16 IIGKGGTKINEIRQLSgaTIKIANSEDGSTERSVTITG 53
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
974-1040 3.03e-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: 37.63  E-value: 3.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201  974 TIEVEVPFDLHRYVIGQKGSGIRKMMDEFEVNIHVPAPELQSDiIAITGLAANLDRAKAGLLERVKE 1040
Cdd:cd22449     5 TVKFDVPAKYVPHIIGKKGANINKLREEYGVKIDFEDKTGEGN-VEIKGSKKNVEEAKKRILSQIDE 70
KH-I_Vigilin_rpt7 cd22410
seventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1056-1105 3.05e-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: 37.25  E-value: 3.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578804201 1056 SVTVDPKYHPKIIGRKGAVITQIRLEH-DVNIQFPDKddgNQPQDQITITG 1105
Cdd:cd22410     5 DIIIEQRFHRTIIGQKGEKIREIRDKFpQVQITFPDP---GSKSDVVTLRG 52
KH-I_Vigilin_rpt12 cd22415
twelfth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
656-719 3.07e-03

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: 38.05  E-value: 3.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  656 VEVSIPAKLHNSLIGTKGRLIRSIMEECgGVHIHFP----------------------VEGSG------SDTVVIRGPSS 707
Cdd:cd22415     2 IECVIPQKFHRTVMGAKGSRVQQITSEF-DVQIKFPdresnqpapaengegnggegveGEAVDdnsprkCDIIIITGKKE 80
                          90
                  ....*....|..
gi 578804201  708 DVEKAKKQLLHL 719
Cdd:cd22415    81 NCEAAKEALLAL 92
KH-I_ANKRD17 cd22502
type I K homology (KH) RNA-binding domain found in ankyrin repeat domain-containing protein 17 ...
742-796 3.27e-03

type I K homology (KH) RNA-binding domain found in ankyrin repeat domain-containing protein 17 (ANKRD17) and similar proteins; ANKRD17, also called ankyrin repeat protein 17, or gene trap ankyrin repeat protein (GTAR), or serologically defined breast cancer antigen NY-BR-16, is a ubiquitously expressed ankyrin factor essential for the vascular integrity during embryogenesis. It may be directly involved in the DNA replication process and play pivotal roles in cell cycle and DNA regulation. It is also involved in innate immune defense against bacteria and viruses.


Pssm-ID: 411930 [Multi-domain]  Cd Length: 71  Bit Score: 37.43  E-value: 3.27e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201  742 LIGKGGGKIRKVRDSTGARVIFPAAEDKDQD-LITIIGKEDAVREAQKELEALIQN 796
Cdd:cd22502    15 VIGRGGCNINAIREFTGAHIDIDKQKDKTGDrIITIRGGTESTRQATQLINALIKD 70
KH-I_MEX3_rpt2 cd22424
second type I K homology (KH) RNA-binding domain found in the family of MEX-3 RNA-binding ...
596-645 3.45e-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: 37.32  E-value: 3.45e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 578804201  596 IIGKGGANIKKIREESNTKIDLPAENSNSeTIIITGKRANCEAARSRILS 645
Cdd:cd22424    18 VVGPKGATIKRIQQQTHTYIVTPSRDKEP-VFEVTGMPENVERAREEIEA 66
KH-I_MER1_like cd22458
type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae meiotic ...
300-355 3.45e-03

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


Pssm-ID: 411886 [Multi-domain]  Cd Length: 65  Bit Score: 37.04  E-value: 3.45e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201  300 VEVKKSQHKYVIGPKGNSLQEILERTGVSVE-IPPSDSISETVILRGEPEKLGQALT 355
Cdd:cd22458     5 IKLPQALCGRLIGAKGKNIKALSEKSGASIRlIPISNSSQQTIHLSGTDKQIALAIS 61
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
505-575 3.47e-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: 3.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578804201  505 ENERTKDLIIEQRFHRTIIGQKGERIREIRDKFpEVIINFPDPAQKSDIVqLRGPKNEVEKCTKYMQKMVA 575
Cdd:cd22449     1 ENGYTVKFDVPAKYVPHIIGKKGANINKLREEY-GVKIDFEDKTGEGNVE-IKGSKKNVEEAKKRILSQID 69
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
509-565 3.48e-03

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


Pssm-ID: 411836 [Multi-domain]  Cd Length: 62  Bit Score: 37.15  E-value: 3.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201  509 TKDLIIEQRFHRTIIGQKGERIREIRDKfPEVIINFPDPAQKSDIVQLRGPKNEVEK 565
Cdd:cd22408     1 TVSVEVPKSQHRFVIGPRGSTIQEILEE-TGCSVEVPPNDSDSETITLRGPADKLGA 56
KH-I_MER1_like cd22458
type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae meiotic ...
584-631 3.74e-03

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


Pssm-ID: 411886 [Multi-domain]  Cd Length: 65  Bit Score: 37.04  E-value: 3.74e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578804201  584 ISVPifKQFHKNIIGKGGANIKKIREESNTKIDL-PAENSNSETIIITG 631
Cdd:cd22458     5 IKLP--QALCGRLIGAKGKNIKALSEKSGASIRLiPISNSSQQTIHLSG 51
KH-I_Vigilin_rpt12 cd22415
twelfth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
1131-1193 3.81e-03

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: 38.05  E-value: 3.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201 1131 DVPLDHRVHARIIGARGKAIRKIMDEFKVDIRFP----QSGAPDPN-----------------------CVTVTGLPENV 1183
Cdd:cd22415     3 ECVIPQKFHRTVMGAKGSRVQQITSEFDVQIKFPdresNQPAPAENgegnggegvegeavddnsprkcdIIIITGKKENC 82
                          90
                  ....*....|
gi 578804201 1184 EEAIDHILNL 1193
Cdd:cd22415    83 EAAKEALLAL 92
KH-I_FUBP_rpt1 cd22396
first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
596-646 3.94e-03

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: 37.23  E-value: 3.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578804201  596 IIGKGGANIKKIREESNTKIDLPAENSNS--ETIIITGKRANCEAARSRILSI 646
Cdd:cd22396    15 IIGRGGEQINRLQAESGAKIQIAPDSGGLpeRPCTLTGTPDAIETAKRLIDQI 67
KH-I_DDX43_DDX53 cd22430
type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box ...
165-209 4.09e-03

type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box protein 53 (DDX53) and similar proteins; DDX43 (also called cancer/testis antigen 13, or DEAD box protein HAGE, or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 (also called cancer-associated gene protein, or cancer/testis antigen 26, or DEAD box protein CAGE) shows high expression level in various tumors and is involved in anti-cancer drug resistance. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation.


Pssm-ID: 411858 [Multi-domain]  Cd Length: 66  Bit Score: 36.88  E-value: 4.09e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 578804201  165 VIGKNGEKLQDLELKTATKIQIPRpDDPSNQIKITGTKEGIEKAR 209
Cdd:cd22430    14 VIGRGGSKIRELEESTGSKIKIIK-GGQEAEVKIFGSDEAQQKAK 57
KH-I_MUG60_like cd22453
type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe meiotically ...
880-909 4.11e-03

type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe meiotically up-regulated gene 60 protein (MUG60) and similar proteins; MUG60 is a KH domain-containing protein that has a role in meiosis. The family also contains Saccharomyces cerevisiae KH domain-containing protein YLL032C.


Pssm-ID: 411881 [Multi-domain]  Cd Length: 72  Bit Score: 37.35  E-value: 4.11e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 578804201  880 IPQKFHRSVMGPKGSRIQQITRDFSVQIKF 909
Cdd:cd22453     8 VPEKYHKRIIGKGGQNIQRIMKKYNVFIKF 37
KH-I_PCBP_rpt3 cd22439
third type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
150-208 4.13e-03

third type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding proteins (PCBPs); The PCBP family, also known as hnRNP E family, comprises four members, PCBP1-4, which are RNA-binding proteins that interact in a sequence-specific manner with single-stranded poly(C) sequences. They are mainly involved in various posttranscriptional regulations, including mRNA stabilization or translational activation/silencing. Besides, PCBPs may share iron chaperone activity. PCBPs contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411867 [Multi-domain]  Cd Length: 68  Bit Score: 37.21  E-value: 4.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578804201  150 QASATVAIPKEHHRFVIGKNGEKLQDLELKTATKIQIPRPDDPSN--QIKITGTKEGIEKA 208
Cdd:cd22439     1 QTTQEITIPNDLIGCIIGKGGTKINEIRQLSGATIKIANSEDGSTerSVTITGTPEAVSLA 61
KH-I_Vigilin_rpt2 cd22406
second type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
870-916 4.52e-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: 4.52e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 578804201  870 LEAQVTLECAIPQKFHRSVMGPKGSRIQQITRDFSVQIKFPDREENA 916
Cdd:cd22406     1 LQTQASVTVNIPKEHHRFILGKKGKKLQELELKTATKIVIPRQEDNS 47
KH-I_ASCC1 cd22419
type I K homology (KH) RNA-binding domain found in activating signal cointegrator 1 complex ...
1053-1121 4.54e-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: 36.79  E-value: 4.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201 1053 FKLSVTVDPKYHPKIIGRKGAVITQIRLEHDVNIQFPDKDDGnqpqDQITITGYEKN-TEAARDAILRIV 1121
Cdd:cd22419     1 FRLSLDVPSALFKFIIGKKGETKKRLESETKTQIRIPRQGKE----GDIVITGKDRSgVDSARTRIEVLV 66
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
879-965 5.25e-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: 5.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  879 AIPQKFHRSVMGPKGSRIQQITRDFSVQIKFPDREENAvhstepvvqengdeagegreakdcdpgsprrcDIIIISGRKE 958
Cdd:cd22411     5 PIFKQFHKNIIGKGGATIKKIREETNTRIDLPEENSDS--------------------------------DVITITGKKE 52

                  ....*..
gi 578804201  959 KCEAAKE 965
Cdd:cd22411    53 DVEKARE 59
KH-I_ScSCP160_rpt3 cd22448
third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
807-868 5.43e-03

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: 37.12  E-value: 5.43e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804201  807 VDPKHHRHFVIRRGQVLREIAEEYGgVMVSFPR-----------SGTQSDKVTLKGAKDCVEAAKKRIQEIIE 868
Cdd:cd22448     9 IPVQFHGSLIGQQGKYVNRLQEKYG-VKINFPRensssndtetkKPQAPDEVTIRGGKKGVAEAKQELLELLE 80
KH-I_FUBP3_rpt1 cd22480
first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
157-209 5.51e-03

first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 3 (FUBP3) and similar proteins; 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. FUBP3 contains four K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411908 [Multi-domain]  Cd Length: 71  Bit Score: 36.80  E-value: 5.51e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201  157 IPKEHHRFVIGKNGEKLQDLELKTATKIQIPrPDD---PSNQIKITGTKEGIEKAR 209
Cdd:cd22480     7 VPDKMVGFIIGRGGEQISRIQLESGCKIQIA-PDSggmPERPCVLTGTPESIEQAK 61
KH-I_ScSCP160_rpt7 cd22452
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
807-865 5.71e-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: 36.53  E-value: 5.71e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578804201  807 VDPKHHRHFVIRRGQVLREIAEEYGgVMVSFPRSGTQSDKVTLKGAKDCVEAAKKRIQE 865
Cdd:cd22452     8 VSPRYFGRIIGPGGSNINQIREKSG-CFINVPKKNKESDVITLRGTKEGVEKAEEMIKK 65
KH-I_MER1_like cd22458
type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae meiotic ...
728-791 5.82e-03

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


Pssm-ID: 411886 [Multi-domain]  Cd Length: 65  Bit Score: 36.66  E-value: 5.82e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804201  728 FTVDIRAKPEYHKFLIGKGGGKIRKVRDSTGARV-IFPAAEDKDQdLITIIGKEDAVREAQKELE 791
Cdd:cd22458     1 VTWEIKLPQALCGRLIGAKGKNIKALSEKSGASIrLIPISNSSQQ-TIHLSGTDKQIALAISSIE 64
KH-I_NOVA_rpt2 cd22436
second type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
596-645 5.87e-03

second type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ventral antigen (Nova); The family includes two related neuronal RNA-binding proteins, Nova-1 and Nova-2. Nova-1, also called onconeural ventral antigen 1, or paraneoplastic Ri antigen, or ventral neuron-specific protein 1, may regulate RNA splicing or metabolism in a specific subset of developing neurons. It interacts with RNA containing repeats of the YCAY sequence. It is a brain-enriched splicing factor regulating neuronal alternative splicing. Nova-1 is involved in neurological disorders and carcinogenesis. Nova-2, also called astrocytic NOVA1-like RNA-binding protein, is a neuronal RNA-binding protein expressed in a broader central nervous system (CNS) distribution than Nova-1. It functions in neuronal RNA metabolism. NOVA family proteins contain three K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411864 [Multi-domain]  Cd Length: 70  Bit Score: 36.83  E-value: 5.87e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578804201  596 IIGKGGANIKKIREESNTKIDL---PAENSNSETII-ITGKRANCEAARSRILS 645
Cdd:cd22436    15 IIGKGGATIKAIMEQSGARVQIsqkPESINLQERVVtVTGEPEANRKAVSLILQ 68
KH-I_MEX3_rpt1 cd22423
first type I K homology (KH) RNA-binding domain found in the family of MEX-3 RNA-binding ...
155-213 5.93e-03

first 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 first KH domain.


Pssm-ID: 411851  Cd Length: 73  Bit Score: 36.69  E-value: 5.93e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578804201  155 VAIP-KEHHRFVIGKNGEKLQDLELKTATKIQIP-RPDDPSnqIKITGTKEGIEKARHEVL 213
Cdd:cd22423     5 VPVPsSEHVAEIVGRQGCKIKALRAKTNTYIKTPvRGEEPV--FVVTGRKEDVAMAKREIL 63
KH-I_HNRNPK_rpt1 cd22432
first type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ...
450-486 6.19e-03

first 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 first one.


Pssm-ID: 411860 [Multi-domain]  Cd Length: 64  Bit Score: 36.39  E-value: 6.19e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 578804201  450 LIGKSGANINRIKDQYKVSVRIPPDSEKSNLIRIEGD 486
Cdd:cd22432    16 IIGKGGENIKRLRTEYNASVSVPDSSGPERILTISAD 52
KH-I_Mextli_like cd22454
type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic ...
656-717 6.41e-03

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: 36.52  E-value: 6.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804201  656 VEVSIPAKLHNSLIGTKGRLIRSIMEECGGVhIHF--PVEGSGSDTVVIRGPSSDVEKAKKQLL 717
Cdd:cd22454     6 IEVVIPNADVGKVIGKGGETIKRIEALTDTV-ITFerVNGGSPNREVQITGSPDNVAAAKRLIE 68
KH-I_FUBP_rpt1 cd22396
first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
1067-1121 6.51e-03

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: 36.46  E-value: 6.51e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578804201 1067 IIGRKGAVITQIRLEHDVNIQFPdKDDGNQPQDQITITGYEKNTEAARDAILRIV 1121
Cdd:cd22396    15 IIGRGGEQINRLQAESGAKIQIA-PDSGGLPERPCTLTGTPDAIETAKRLIDQIV 68
KH-I_KHDC4_rpt2 cd22386
first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein ...
438-500 7.46e-03

first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein 4 (KHDC4) and similar proteins; KHDC4, also called Brings lots of money 7 (Blom7), or pre-mRNA splicing factor protein KHDC4, is an RNA-binding protein involved in pre-mRNA splicing. It interacts with the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome. KHDC4 binds preferentially RNA with A/C rich sequences and poly-C stretches. KHDC4 contains two type I K homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411814 [Multi-domain]  Cd Length: 102  Bit Score: 37.15  E-value: 7.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804201  438 VEINIDH---KFH--RHLIGKSGANINRIKDQYKVSVRI---------PPDSEKSNL---IRIEG-DPQGVQQAKRELLE 499
Cdd:cd22386     7 VFVGLEHappGFNvrGKLIGPGGSNVKHIQQETGAKVQLrgkgsgfiePASGREADEplhLLISHpDPEGLQQAKKLCED 86

                  .
gi 578804201  500 L 500
Cdd:cd22386    87 L 87
KH-I_PCBP1_2_rpt3 cd22521
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) ...
596-643 8.12e-03

third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) and similar proteins; The family includes PCBP1 (also called alpha-CP1, or heterogeneous nuclear ribonucleoprotein E1, or hnRNP E1, or nucleic acid-binding protein SUB2.3) and PCBP2 (also called alpha-CP2, or heterogeneous nuclear ribonucleoprotein E2, or hnRNP E2). They are single-stranded nucleic acid binding proteins that bind preferentially to oligo dC. They act as iron chaperones for ferritin. In case of infection by poliovirus, PCBP1 plays a role in initiation of viral RNA replication in concert with the viral protein 3CD. PCBP2 is a major cellular poly(rC)-binding protein. It also binds poly(rU). PCBP2 negatively regulates cellular antiviral responses mediated by MAVS signaling. It acts as an adapter between MAVS and the E3 ubiquitin ligase ITCH, therefore triggering MAVS ubiquitination and degradation. PCBP2 forms a metabolon with the heme oxygenase 1/cytochrome P450 reductase complex for heme catabolism and iron transfer. Both PCBP1 and PCBP2 contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411949  Cd Length: 76  Bit Score: 36.57  E-value: 8.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 578804201  596 IIGKGGANIKKIREESNTKIDL--PAENSNSETIIITGKRANCEAARSRI 643
Cdd:cd22521    19 IIGRQGAKINEIRQMSGAQIKIanPVEGSTDRQVTITGSAASISLAQYLI 68
KH-I_PCBP3_rpt2 cd22519
second type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 3 (PCBP3) ...
742-790 8.38e-03

second type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 3 (PCBP3) and similar proteins; PCBP3, also called alpha-CP3, or PCBP3-overlapping transcript, or PCBP3-overlapping transcript 1, or heterogeneous nuclear ribonucleoprotein E3, or hnRNP E3, is a single-stranded nucleic acid binding protein that binds preferentially to oligo dC. It can function as a repressor dependent on binding to single-strand and double-stranded poly(C) sequences. PCBP3 contains three K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411947 [Multi-domain]  Cd Length: 79  Bit Score: 36.69  E-value: 8.38e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578804201  742 LIGKGGGKIRKVRDSTGARV-----IFPAAEDKdqdLITIIGKEDAVREAQKEL 790
Cdd:cd22519    20 LIGKGGSKIKEIRESTGAQVqvagdMLPNSTER---AVTISGTPDAIIQCVKQI 70
KH-I_MASK cd22404
type I K homology (KH) RNA-binding domain found in Mask family proteins; The Mask family ...
742-795 8.47e-03

type I K homology (KH) RNA-binding domain found in Mask family proteins; The Mask family includes Drosophila melanogaster ankyrin repeat and KH domain-containing protein Mask, and its mammalian homologues Mask1/ANKHD1 and Mask2/ANKRD17. Mask, also called multiple ankyrin repeat single KH domain-containing protein, is a large ankyrin repeat and KH domain-containing protein involved in Drosophila receptor tyrosine kinase signaling. It acts as a mediator of receptor tyrosine kinase (RTK) signaling and may act either downstream of MAPK or transduce signaling through a parallel branch of the RTK pathway. Mask is required for the development and organization of indirect flight muscle sarcomeres by regulating the formation of M line and H zone and the correct assembly of thick and thin filaments in the sarcomere. Mask1/ANKHD1, also called HIV-1 Vpr-binding ankyrin repeat protein, or multiple ankyrin repeats single KH domain, or Hmask, is highly expressed in various cancer tissues and is involved in cancer progression, including proliferation and invasion. Mask2/ANKRD17, also called ankyrin repeat protein 17, or gene trap ankyrin repeat protein (GTAR), or serologically defined breast cancer antigen NY-BR-16, is a ubiquitously expressed ankyrin factor essential for the vascular integrity during embryogenesis. It may be directly involved in the DNA replication process and play pivotal roles in cell cycle and DNA regulation. It is also involved in innate immune defense against bacteria and viruses.


Pssm-ID: 411832 [Multi-domain]  Cd Length: 71  Bit Score: 36.42  E-value: 8.47e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578804201  742 LIGKGGGKIRKVRDSTGARVIFPAAEDKDQD-LITIIGKEDAVREAQKELEALIQ 795
Cdd:cd22404    15 VIGRGGCNINAIREVSGAHIEIDKQKGEQGDrRITIKGSADATRQAAQLINALIK 69
KH-I_ScSCP160_rpt3 cd22448
third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
974-1036 8.78e-03

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: 36.74  E-value: 8.78e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578804201  974 TIEVEVPFDLHRYVIGQKGSGIRKMMDEFEVNIHVPAPELQS-----------DIIAITGLAANLDRAKAGLLE 1036
Cdd:cd22448     4 TLILKIPVQFHGSLIGQQGKYVNRLQEKYGVKINFPRENSSSndtetkkpqapDEVTIRGGKKGVAEAKQELLE 77
KH-I_AKAP1 cd22395
type I K homology (KH) RNA-binding domain found in mitochondrial A-kinase anchor protein 1 ...
596-639 9.22e-03

type I K homology (KH) RNA-binding domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; AKAP1, also called A-kinase anchor protein 149 kDa, or AKAP 149, or dual specificity A-kinase-anchoring protein 1, or D-AKAP-1, or protein kinase A-anchoring protein 1 (PRKA1), or spermatid A-kinase anchor protein 84, or S-AKAP84, is a novel developmentally regulated A kinase anchor protein of male germ cells. It binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane.


Pssm-ID: 411823 [Multi-domain]  Cd Length: 68  Bit Score: 35.96  E-value: 9.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 578804201  596 IIGKGGANIKKIREESNTKIDLPA--ENSNSETIIITGKRANCEAA 639
Cdd:cd22395    14 LIGKQGRNVKQLKQKSGAKIYIKPhpYTQNFQICSIEGTQQQIDKA 59
KH-I_FUBP1_rpt1 cd22478
first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
450-503 9.48e-03

first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 1 (FUBP1) and similar proteins; 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. FUBP1 contains four K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411906 [Multi-domain]  Cd Length: 75  Bit Score: 36.15  E-value: 9.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578804201  450 LIGKSGANINRIKDQYKVSVRIPPDS----EKSNLirIEGDPQGVQQAKRELLELASR 503
Cdd:cd22478    18 IIGRGGEQISRIQQESGCKIQIAPDSgglpERSCM--LTGTPESVQSAKRLLDQIVEK 73
KH-I_Vigilin_rpt9 cd22412
ninth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
154-218 9.49e-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: 36.12  E-value: 9.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804201  154 TVAIPKEHHRFVIGKNGEKLQDL-ELKTATKIQIPRPDDPSNQIKITGTKEGIEKARHEVLLISAE 218
Cdd:cd22412     5 EVEIPAKLHNSLIGAKGRLIRSImEECGGVHIHFPPEGSGSDKVTIRGPKEDVEKAKKQLLELANE 70
KH-I_PCBP_rpt2 cd02396
second type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
742-786 9.57e-03

second type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding proteins (PCBPs); The PCBP family, also known as hnRNP E family, comprises four members, PCBP1-4, which are RNA-binding proteins that interact in a sequence-specific manner with single-stranded poly(C) sequences. They are mainly involved in various posttranscriptional regulations, including mRNA stabilization or translational activation/silencing. Besides, PCBPs may share iron chaperone activity. PCBPs contain three K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411806 [Multi-domain]  Cd Length: 72  Bit Score: 36.09  E-value: 9.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 578804201  742 LIGKGGGKIRKVRDSTGARVIF-----PAAEDKdqdLITIIGKEDAVREA 786
Cdd:cd02396    16 LIGKGGSKIKEIRESTGASVQVasemlPNSTER---AVTISGSPEAITKC 62
KH-I_ScSCP160_rpt6 cd22451
sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
297-353 9.89e-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: 35.89  E-value: 9.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578804201  297 TIAVEVKKSQHKYVIGPKGNSLQEILERTGVSVEIPPSDSISETVILRGEPEKLGQA 353
Cdd:cd22451     2 SIDIDIPKEYHRAIIGKGGAVLRELEAETGCRIQVPKKDDPSGKIRITGARDGVEAA 58
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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