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Conserved domains on  [gi|1593795325|ref|NP_001356026|]
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activating signal cointegrator 1 complex subunit 1 isoform 7 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AKAP7_NLS pfam10469
AKAP7 2'5' RNA ligase-like domain; AKAP7_NLS is the N-terminal domain of the cyclic ...
 133-319 5.15e-63

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


:

Pssm-ID: 402204 [Multi-domain]  Cd Length: 207  Bit Score: 199.42  E-value: 5.15e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795325 133 FTHFLAFFLNEVEVQEGFLRFQEEVLAKCSmdhGVDSSIFQNPKKLHLTIGMLVLLSEEEIQQTCEMLQQCKEEFINDIS 212
Cdd:pfam10469   1 PTHFLSIPLNSPELRKRLEEFQESVLKQLP---GLDESLFIPPEKLHITLLVLVLLDDEEVARAKEALRECREEIKDILN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795325 213 GgKPLEVEMAGIEYMNDDPGMVDVLYAKVHMKDGSNRLQELVDRVLERFQASGLIVKEWNS-VKLHATVMNTLFRKDPNa 291
Cdd:pfam10469  78 G-NPLSLRFKGLETFNDDPSAVRVLYAKVEEDDHSPKLQELADRIIRRFQEAGLLVKENNSrVKLHMTLMNTRYRKKKY- 155

                         170       180
                  ....*....|....*....|....*...
gi 1593795325 292 egrynlytaegkyiFKERESFDGRNILK 319
Cdd:pfam10469 156 --------------AKSKESFDAREILD 169
KH-I_ASCC1 cd22419
type I K homology (KH) RNA-binding domain found in activating signal cointegrator 1 complex ...
 59-124 2.34e-30

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: 109.97  E-value: 2.34e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1593795325  59 FRSTLRAPSLLYKHIVGKRGDTRKKIEMETKTSISIPKPGQDGEIVITGQHRNGVISARTRIDVLL 124
Cdd:cd22419     1 FRLSLDVPSALFKFIIGKKGETKKRLESETKTQIRIPRQGKEGDIVITGKDRSGVDSARTRIEVLV 66
 
Name Accession Description Interval E-value
AKAP7_NLS pfam10469
AKAP7 2'5' RNA ligase-like domain; AKAP7_NLS is the N-terminal domain of the cyclic ...
 133-319 5.15e-63

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


Pssm-ID: 402204 [Multi-domain]  Cd Length: 207  Bit Score: 199.42  E-value: 5.15e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795325 133 FTHFLAFFLNEVEVQEGFLRFQEEVLAKCSmdhGVDSSIFQNPKKLHLTIGMLVLLSEEEIQQTCEMLQQCKEEFINDIS 212
Cdd:pfam10469   1 PTHFLSIPLNSPELRKRLEEFQESVLKQLP---GLDESLFIPPEKLHITLLVLVLLDDEEVARAKEALRECREEIKDILN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795325 213 GgKPLEVEMAGIEYMNDDPGMVDVLYAKVHMKDGSNRLQELVDRVLERFQASGLIVKEWNS-VKLHATVMNTLFRKDPNa 291
Cdd:pfam10469  78 G-NPLSLRFKGLETFNDDPSAVRVLYAKVEEDDHSPKLQELADRIIRRFQEAGLLVKENNSrVKLHMTLMNTRYRKKKY- 155

                         170       180
                  ....*....|....*....|....*...
gi 1593795325 292 egrynlytaegkyiFKERESFDGRNILK 319
Cdd:pfam10469 156 --------------AKSKESFDAREILD 169
KH-I_ASCC1 cd22419
type I K homology (KH) RNA-binding domain found in activating signal cointegrator 1 complex ...
 59-124 2.34e-30

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: 109.97  E-value: 2.34e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1593795325  59 FRSTLRAPSLLYKHIVGKRGDTRKKIEMETKTSISIPKPGQDGEIVITGQHRNGVISARTRIDVLL 124
Cdd:cd22419     1 FRLSLDVPSALFKFIIGKKGETKKRLESETKTQIRIPRQGKEGDIVITGKDRSGVDSARTRIEVLV 66
PLN00108 PLN00108
unknown protein; Provisional
 129-333 8.84e-14

unknown protein; Provisional


Pssm-ID: 177724  Cd Length: 257  Bit Score: 70.48  E-value: 8.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795325 129 RKQPFTHFLAFFLN-EVEVQEGFLRFQEEVLAKCSMD----------HGVDSSIFQNPKKLHLTIGMLVLLSEEEIQQTC 197
Cdd:PLN00108   32 HREVFTHFVSLPLAiYPDLKKNIEAFQNSVLGNNDKDplkfqstlaeMGIEKSIFVSPKTFHLTVVMLKLENNESVVKAQ 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795325 198 EMLQQCKEEfINDISGGKPLEVEMAGIEYMNDDPGMVDVLYAKVHMKDGSNRLQELVDRVLERFQASGLIVKEWNS-VKL 276
Cdd:PLN00108  112 NILKSICSN-VRQALKDRPVFIRLRGLDCMNGSLDKTRVLYAPVEEVGHEGRLLNACHVIIDAFENAGFAGKDAKSrLKL 190

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1593795325 277 HATVMNTLFRKDPNAEgrynLYTAEGKYIFKERESFDGRNILkVSLMHILRAYQENP 333
Cdd:PLN00108  191 HATLMNASYRKDKSKK----MDTFDAREIHKEFENKDWGTYL-IREAHISQRYKYDP 242
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 62-120 4.15e-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: 43.81  E-value: 4.15e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1593795325  62 TLRAPSLLYKHIVGKRGDTRKKIEMETKTSISIPKP---GQDGEIVITGQhRNGVISARTRI 120
Cdd:pfam00013   3 EILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSeseGNERIVTITGT-PEAVEAAKALI 63
KH smart00322
K homology RNA-binding domain;
60-120 2.31e-04

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 38.82  E-value: 2.31e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1593795325   60 RSTLRAPSLLYKHIVGKRGDTRKKIEMETKTSISIPKPG-QDGEIVITGqHRNGVISARTRI 120
Cdd:smart00322   4 TIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGsEERVVEITG-PPENVEKAAELI 64
ThpR COG1514
RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA ligase) [Translation, ribosomal structure and ...
 136-260 8.83e-04

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


Pssm-ID: 441123 [Multi-domain]  Cd Length: 181  Bit Score: 39.63  E-value: 8.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795325 136 FLAFFLNEvEVQEGFLRFQEEVLAKCSMDhgvdssiFQNPKKLHLTIGMLVLLSEEEIQQTCEMLQQCKEEFindisggK 215
Cdd:COG1514     4 FIALPPPE-ELREALAALRARLKAAPGGR-------WVRPENLHLTLAFLGEVDEERLEALAEALARAAAGA-------P 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1593795325 216 PLEVEMAGIEYM-NDDPGmvdVLYAKVHMKDGSNRLQELVDRVLER 260
Cdd:COG1514    69 PFELRLDGLGAFpRPRPR---VLWLGVEPSPELLALHRRLRAALAR 111
 
Name Accession Description Interval E-value
AKAP7_NLS pfam10469
AKAP7 2'5' RNA ligase-like domain; AKAP7_NLS is the N-terminal domain of the cyclic ...
 133-319 5.15e-63

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


Pssm-ID: 402204 [Multi-domain]  Cd Length: 207  Bit Score: 199.42  E-value: 5.15e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795325 133 FTHFLAFFLNEVEVQEGFLRFQEEVLAKCSmdhGVDSSIFQNPKKLHLTIGMLVLLSEEEIQQTCEMLQQCKEEFINDIS 212
Cdd:pfam10469   1 PTHFLSIPLNSPELRKRLEEFQESVLKQLP---GLDESLFIPPEKLHITLLVLVLLDDEEVARAKEALRECREEIKDILN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795325 213 GgKPLEVEMAGIEYMNDDPGMVDVLYAKVHMKDGSNRLQELVDRVLERFQASGLIVKEWNS-VKLHATVMNTLFRKDPNa 291
Cdd:pfam10469  78 G-NPLSLRFKGLETFNDDPSAVRVLYAKVEEDDHSPKLQELADRIIRRFQEAGLLVKENNSrVKLHMTLMNTRYRKKKY- 155

                         170       180
                  ....*....|....*....|....*...
gi 1593795325 292 egrynlytaegkyiFKERESFDGRNILK 319
Cdd:pfam10469 156 --------------AKSKESFDAREILD 169
KH-I_ASCC1 cd22419
type I K homology (KH) RNA-binding domain found in activating signal cointegrator 1 complex ...
 59-124 2.34e-30

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: 109.97  E-value: 2.34e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1593795325  59 FRSTLRAPSLLYKHIVGKRGDTRKKIEMETKTSISIPKPGQDGEIVITGQHRNGVISARTRIDVLL 124
Cdd:cd22419     1 FRLSLDVPSALFKFIIGKKGETKKRLESETKTQIRIPRQGKEGDIVITGKDRSGVDSARTRIEVLV 66
PLN00108 PLN00108
unknown protein; Provisional
 129-333 8.84e-14

unknown protein; Provisional


Pssm-ID: 177724  Cd Length: 257  Bit Score: 70.48  E-value: 8.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795325 129 RKQPFTHFLAFFLN-EVEVQEGFLRFQEEVLAKCSMD----------HGVDSSIFQNPKKLHLTIGMLVLLSEEEIQQTC 197
Cdd:PLN00108   32 HREVFTHFVSLPLAiYPDLKKNIEAFQNSVLGNNDKDplkfqstlaeMGIEKSIFVSPKTFHLTVVMLKLENNESVVKAQ 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795325 198 EMLQQCKEEfINDISGGKPLEVEMAGIEYMNDDPGMVDVLYAKVHMKDGSNRLQELVDRVLERFQASGLIVKEWNS-VKL 276
Cdd:PLN00108  112 NILKSICSN-VRQALKDRPVFIRLRGLDCMNGSLDKTRVLYAPVEEVGHEGRLLNACHVIIDAFENAGFAGKDAKSrLKL 190

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1593795325 277 HATVMNTLFRKDPNAEgrynLYTAEGKYIFKERESFDGRNILkVSLMHILRAYQENP 333
Cdd:PLN00108  191 HATLMNASYRKDKSKK----MDTFDAREIHKEFENKDWGTYL-IREAHISQRYKYDP 242
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 69-120 1.91e-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: 1.91e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1593795325  69 LYKHIVGKRGDTRKKIEMETKTSISIPKPG-QDGEIVITGQHrNGVISARTRI 120
Cdd:cd02394    12 FHGHIIGKGGANIKRIREESGVSIRIPDDEaNSDEIRIEGSP-EGVKKAKAEI 63
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 66-121 2.43e-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: 47.29  E-value: 2.43e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1593795325  66 PSLLYKHIVGKRGDTRKKIEMETKTSISIPKPG---QDGEIVITGqHRNGVISARTRID 121
Cdd:cd00105     6 PSELVGLIIGKGGSTIKEIEEETGARIQIPKEGegsGERVVTITG-TPEAVEKAKELIE 63
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 71-120 4.43e-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: 46.43  E-value: 4.43e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1593795325  71 KHIVGKRGDTRKKIEMETKTSISIPKPG-QDGEIVITGQHRNgVISARTRI 120
Cdd:cd22411    12 KNIIGKGGATIKKIREETNTRIDLPEENsDSDVITITGKKED-VEKARERI 61
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 62-120 4.15e-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: 43.81  E-value: 4.15e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1593795325  62 TLRAPSLLYKHIVGKRGDTRKKIEMETKTSISIPKP---GQDGEIVITGQhRNGVISARTRI 120
Cdd:pfam00013   3 EILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSeseGNERIVTITGT-PEAVEAAKALI 63
KH-I_Vigilin_rpt2 cd22406
second type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 60-120 1.48e-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: 1.48e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1593795325  60 RSTLRAPSLLYKHIVGKRGDTRKKIEMETKTSISIPKPGQD-GEIVITGQhRNGVISARTRI 120
Cdd:cd22406     6 SVTVNIPKEHHRFILGKKGKKLQELELKTATKIVIPRQEDNsDEIKITGT-KEGIEKARHEI 66
KH-I_ScSCP160_rpt6 cd22451
sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 66-120 9.56e-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: 40.13  E-value: 9.56e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1593795325  66 PSLLYKHIVGKRGDTRKKIEMETKTSISIP-KPGQDGEIVITGQhRNGVISARTRI 120
Cdd:cd22451     8 PKEYHRAIIGKGGAVLRELEAETGCRIQVPkKDDPSGKIRITGA-RDGVEAATAKI 62
KH smart00322
K homology RNA-binding domain;
60-120 2.31e-04

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 38.82  E-value: 2.31e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1593795325   60 RSTLRAPSLLYKHIVGKRGDTRKKIEMETKTSISIPKPG-QDGEIVITGqHRNGVISARTRI 120
Cdd:smart00322   4 TIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGsEERVVEITG-PPENVEKAAELI 64
ThpR COG1514
RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA ligase) [Translation, ribosomal structure and ...
 136-260 8.83e-04

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


Pssm-ID: 441123 [Multi-domain]  Cd Length: 181  Bit Score: 39.63  E-value: 8.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593795325 136 FLAFFLNEvEVQEGFLRFQEEVLAKCSMDhgvdssiFQNPKKLHLTIGMLVLLSEEEIQQTCEMLQQCKEEFindisggK 215
Cdd:COG1514     4 FIALPPPE-ELREALAALRARLKAAPGGR-------WVRPENLHLTLAFLGEVDEERLEALAEALARAAAGA-------P 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1593795325 216 PLEVEMAGIEYM-NDDPGmvdVLYAKVHMKDGSNRLQELVDRVLER 260
Cdd:COG1514    69 PFELRLDGLGAFpRPRPR---VLWLGVEPSPELLALHRRLRAALAR 111
KH-I_Vigilin_rpt3 cd22407
third type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 61-120 1.13e-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: 36.80  E-value: 1.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1593795325  61 STLRAPSLLYKHIVGKRGDTRKKIEMETKTSISIPKPG-QDGEIVITGQhRNGVISARTRI 120
Cdd:cd22407     2 ERLDIPKVYHPFIAGPNNENVKELQEETGVRINIPPPSvNKDEIVVSGE-KEGVAQAVAKI 61
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 71-120 1.37e-03

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


Pssm-ID: 411836 [Multi-domain]  Cd Length: 62  Bit Score: 36.76  E-value: 1.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1593795325  71 KHIVGKRGDTRKKIEMETKTSISIPKPGQDGE-IVITGQHRNgVISARTRI 120
Cdd:cd22408    12 RFVIGPRGSTIQEILEETGCSVEVPPNDSDSEtITLRGPADK-LGAALTLV 61
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 59-120 4.53e-03

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: 35.26  E-value: 4.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1593795325  59 FRSTLRAPSLLYKHIVGKRGDTRKKIEMETKTSISIPKPGQDG--EIVITGqHRNGVISARTRI 120
Cdd:cd22417     1 FTLTVEVDPKYHPKIIGRKGAVITKLRDDHDVNIQFPDKGDENddEITITG-YEKNAEAAKDAI 63
KH-I_Dim2p_like_rpt1 cd22389
first type I K homology (KH) RNA-binding domain found in Pyrococcus horikoshii Dim2p and ...
 73-123 9.85e-03

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


Pssm-ID: 411817 [Multi-domain]  Cd Length: 70  Bit Score: 34.48  E-value: 9.85e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1593795325  73 IVGKRGDTRKKIEMETKTSISIpkPGQDGEIVITGQHRNGVISARTRIDVL 123
Cdd:cd22389    13 LIGKKGETKREIEERTGVKITV--DSETGEVIIEPEDEEDPLNVMKAREVV 61
 
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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