NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1908918734|ref|NP_001374047|]
View 

regulation of nuclear pre-mRNA domain-containing protein 2 isoform 8 [Homo sapiens]

Protein Classification

epsin; LCP family protein( domain architecture ID 13017359)

epsin plays an important role as an accessory protein in clathrin-mediated endocytosis| LytR-CpsA-Psr (LCP) family protein is implicated in the attachment of anionic polymers to cell wall peptidoglycan in bacteria

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CID_RPRD2 cd17001
CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing protein 2; ...
 27-145 1.27e-84

CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing protein 2; Regulation of nuclear pre-mRNA domain-containing protein 2 (RPRD2) is a CID (CTD-Interacting Domain) domain containing protein that co-purifies with RNA polymerase (Pol) II (RNAP II) and three other RNAP II-associated proteins, RPAP2, GRINL1A and RECQL5, but not with the Mediator complex. CID binds tightly to the carboxy-terminal domain (CTD) of RNAP II. During transcription, RNAP II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing through the CTD, which consists of up to 52 repeats of the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. CID contains eight alpha-helices in a right-handed superhelical arrangement, which closely resembles that of the VHS domains and ARM (Armadillo) repeat proteins, except for its two amino-terminal helices.


:

Pssm-ID: 340798  Cd Length: 125  Bit Score: 271.40  E-value: 1.27e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734   27 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSAYPHRLNLFYLANDVIQNCKRKNAIIFRESFADVLPE 106
Cdd:cd17001      6 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSAYPHRLNLFYLANDVIQNCKRKNAIVFRESFAEVLPE 85

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1908918734  107 AAALVKDPSVSKSVERIFKIWEDRNVYPEEMIVALREAL 145
Cdd:cd17001     86 AAALVKDASVSKSVERIFKIWEERNVYPEETIAALKEAL 124
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 293-610 2.89e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 45.29  E-value: 2.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734  293 SPVPSPSMDAPSPTgSESPFQGMGGEESQSPTMESEKSATPEPVTDnrdvedmelsdveddgskiivedrkeKPAEKSAV 372
Cdd:pfam05109  475 SPTPAGTTSGASPV-TPSPSPRDNGTESKAPDMTSPTSAVTTPTPN--------------------------ATSPTPAV 527

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734  373 STSVPTKPTENISKASsctPVPVTMTATPPLPKPVNTSLSPSPALALPNLANVdlAKISSILSSLTSVMKNTGLSSLLQS 452
Cdd:pfam05109  528 TTPTPNATSPTLGKTS---PTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKT--SPTSAVTTPTPNATSPTVGETSPQA 602

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734  453 VTGNPVPASEAASQSTSASPANTTVSTIKGR-NLPSSAQPFI---PKSFNYSPNSSTSEVSSTSASKASIGQSPGLPSTT 528
Cdd:pfam05109  603 NTTNHTLGGTSSTPVVTSPPKNATSAVTTGQhNITSSSTSSMslrPSSISETLSPSTSDNSTSHMPLLTSAHPTGGENIT 682

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734  529 FKLPSNslgfTATHNTSPAAP-PTEVTicqSSEVSKPKLESESTSPSLEmkihNFLKGNP--------GFSGLNLNIPIL 599
Cdd:pfam05109  683 QVTPAS----TSTHHVSTSSPaPRPGT---TSQASGPGNSSTSTKPGEV----NVTKGTPpknatspqAPSGQKTAVPTV 751

                          330
                   ....*....|.
gi 1908918734  600 SSLGSSAPSES 610
Cdd:pfam05109  752 TSTGGKANSTT 762
PRK03918 super family cl35229
DNA double-strand break repair ATPase Rad50;
98-292 1.40e-03

DNA double-strand break repair ATPase Rad50;


The actual alignment was detected with superfamily member PRK03918:

Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734   98 ESFADVLPEAAALVKD-PSVSKSVERIFKIWEDRNVYPEEmIVALREALTSTN-PKAALKSKIVaEFRSQalIEELllyK 175
Cdd:PRK03918   200 KELEEVLREINEISSElPELREELEKLEKEVKELEELKEE-IEELEKELESLEgSKRKLEEKIR-ELEER--IEEL---K 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734  176 RSEDQIELKEKQLSTMRVDVCSTETLKCLKDKTggKKFSKEFEEASSKLEEFVNGLDKQVKNGPSLTEALENagifYEAQ 255
Cdd:PRK03918   273 KEIEELEEKVKELKELKEKAEEYIKLSEFYEEY--LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE----LKKK 346

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1908918734  256 YKEVKVVANAYKTFA---NRVNNLKKKLDQLKSTLPD--PEE 292
Cdd:PRK03918   347 LKELEKRLEELEERHelyEEAKAKKEELERLKKRLTGltPEK 388
 
Name Accession Description Interval E-value
CID_RPRD2 cd17001
CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing protein 2; ...
 27-145 1.27e-84

CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing protein 2; Regulation of nuclear pre-mRNA domain-containing protein 2 (RPRD2) is a CID (CTD-Interacting Domain) domain containing protein that co-purifies with RNA polymerase (Pol) II (RNAP II) and three other RNAP II-associated proteins, RPAP2, GRINL1A and RECQL5, but not with the Mediator complex. CID binds tightly to the carboxy-terminal domain (CTD) of RNAP II. During transcription, RNAP II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing through the CTD, which consists of up to 52 repeats of the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. CID contains eight alpha-helices in a right-handed superhelical arrangement, which closely resembles that of the VHS domains and ARM (Armadillo) repeat proteins, except for its two amino-terminal helices.


Pssm-ID: 340798  Cd Length: 125  Bit Score: 271.40  E-value: 1.27e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734   27 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSAYPHRLNLFYLANDVIQNCKRKNAIIFRESFADVLPE 106
Cdd:cd17001      6 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSAYPHRLNLFYLANDVIQNCKRKNAIVFRESFAEVLPE 85

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1908918734  107 AAALVKDPSVSKSVERIFKIWEDRNVYPEEMIVALREAL 145
Cdd:cd17001     86 AAALVKDASVSKSVERIFKIWEERNVYPEETIAALKEAL 124
CID pfam04818
CID domain; This domain binds to the phosphorylated C-terminal domain (CTD) of RNA polymerase ...
 27-138 6.38e-42

CID domain; This domain binds to the phosphorylated C-terminal domain (CTD) of RNA polymerase II. This domain is known as the CTD-interacting domain (CID).


Pssm-ID: 461442  Cd Length: 117  Bit Score: 149.28  E-value: 6.38e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734   27 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSAYPHRLNLFYLANDVIQNCKRKNAIIFRESFADVLPE 106
Cdd:pfam04818    3 LEKKLSSLNNSQESIQTLSKWILFHRKHAKAIVEVWEKYLKKAKPEKKLHLLYLANDVLQNSRKKGKSEFADAFEPVLPE 82

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1908918734  107 AAALV---KDPSVSKSVERIFKIWEDRNVYPEEMI 138
Cdd:pfam04818   83 AFASAykkCDEKLKKKLERLLNIWEERNVFSPEVI 117
RPR smart00582
domain present in proteins, which are involved in regulation of nuclear pre-mRNA;
27-145 4.88e-31

domain present in proteins, which are involved in regulation of nuclear pre-mRNA;


Pssm-ID: 214731  Cd Length: 124  Bit Score: 118.53  E-value: 4.88e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734    27 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSAYPHRLNLFYLANDVIQNCKRKNAIIFRESFADVLPE 106
Cdd:smart00582    2 FEQKLESLNNSQESIQTLTKWAIEHASHAKEIVELWEKYIKKAPVPRKLPLLYLLDSIVQNSKRKYGSEFGDELGPVFQD 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 1908918734   107 AAALVKDPSVS---KSVERIFKIWEDRNVYPEEMIVALREAL 145
Cdd:smart00582   82 ALRRVLGAAPEelkKKIRRLLNIWEERGIFPPEVLRPLREKL 123
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 293-610 2.89e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 45.29  E-value: 2.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734  293 SPVPSPSMDAPSPTgSESPFQGMGGEESQSPTMESEKSATPEPVTDnrdvedmelsdveddgskiivedrkeKPAEKSAV 372
Cdd:pfam05109  475 SPTPAGTTSGASPV-TPSPSPRDNGTESKAPDMTSPTSAVTTPTPN--------------------------ATSPTPAV 527

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734  373 STSVPTKPTENISKASsctPVPVTMTATPPLPKPVNTSLSPSPALALPNLANVdlAKISSILSSLTSVMKNTGLSSLLQS 452
Cdd:pfam05109  528 TTPTPNATSPTLGKTS---PTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKT--SPTSAVTTPTPNATSPTVGETSPQA 602

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734  453 VTGNPVPASEAASQSTSASPANTTVSTIKGR-NLPSSAQPFI---PKSFNYSPNSSTSEVSSTSASKASIGQSPGLPSTT 528
Cdd:pfam05109  603 NTTNHTLGGTSSTPVVTSPPKNATSAVTTGQhNITSSSTSSMslrPSSISETLSPSTSDNSTSHMPLLTSAHPTGGENIT 682

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734  529 FKLPSNslgfTATHNTSPAAP-PTEVTicqSSEVSKPKLESESTSPSLEmkihNFLKGNP--------GFSGLNLNIPIL 599
Cdd:pfam05109  683 QVTPAS----TSTHHVSTSSPaPRPGT---TSQASGPGNSSTSTKPGEV----NVTKGTPpknatspqAPSGQKTAVPTV 751

                          330
                   ....*....|.
gi 1908918734  600 SSLGSSAPSES 610
Cdd:pfam05109  752 TSTGGKANSTT 762
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
98-292 1.40e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734   98 ESFADVLPEAAALVKD-PSVSKSVERIFKIWEDRNVYPEEmIVALREALTSTN-PKAALKSKIVaEFRSQalIEELllyK 175
Cdd:PRK03918   200 KELEEVLREINEISSElPELREELEKLEKEVKELEELKEE-IEELEKELESLEgSKRKLEEKIR-ELEER--IEEL---K 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734  176 RSEDQIELKEKQLSTMRVDVCSTETLKCLKDKTggKKFSKEFEEASSKLEEFVNGLDKQVKNGPSLTEALENagifYEAQ 255
Cdd:PRK03918   273 KEIEELEEKVKELKELKEKAEEYIKLSEFYEEY--LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE----LKKK 346

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1908918734  256 YKEVKVVANAYKTFA---NRVNNLKKKLDQLKSTLPD--PEE 292
Cdd:PRK03918   347 LKELEKRLEELEERHelyEEAKAKKEELERLKKRLTGltPEK 388
 
Name Accession Description Interval E-value
CID_RPRD2 cd17001
CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing protein 2; ...
 27-145 1.27e-84

CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing protein 2; Regulation of nuclear pre-mRNA domain-containing protein 2 (RPRD2) is a CID (CTD-Interacting Domain) domain containing protein that co-purifies with RNA polymerase (Pol) II (RNAP II) and three other RNAP II-associated proteins, RPAP2, GRINL1A and RECQL5, but not with the Mediator complex. CID binds tightly to the carboxy-terminal domain (CTD) of RNAP II. During transcription, RNAP II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing through the CTD, which consists of up to 52 repeats of the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. CID contains eight alpha-helices in a right-handed superhelical arrangement, which closely resembles that of the VHS domains and ARM (Armadillo) repeat proteins, except for its two amino-terminal helices.


Pssm-ID: 340798  Cd Length: 125  Bit Score: 271.40  E-value: 1.27e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734   27 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSAYPHRLNLFYLANDVIQNCKRKNAIIFRESFADVLPE 106
Cdd:cd17001      6 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSAYPHRLNLFYLANDVIQNCKRKNAIVFRESFAEVLPE 85

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1908918734  107 AAALVKDPSVSKSVERIFKIWEDRNVYPEEMIVALREAL 145
Cdd:cd17001     86 AAALVKDASVSKSVERIFKIWEERNVYPEETIAALKEAL 124
CID_RPRD_like cd16981
CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing proteins; ...
 27-145 7.11e-57

CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing proteins; This family is composed of Regulation of nuclear pre-mRNA domain-containing proteins 1A (RPRD1A), 1B (RPRD1B), 2 (RPRD2), yeast Rtt103, and similar proteins. RPRD1A, RPRD1B, and RPRD2 are CID (CTD-Interacting Domain) containing proteins that co-purify with RNA polymerase (Pol) II (RNAP II) and three other RNAP II-associated proteins, RPAP2, GRINL1A and RECQL5, but not with the Mediator complex. Yeast transcription termination factor Rtt103 is a CID containing protein that functions in DNA damage response. CID binds tightly to the carboxy-terminal domain (CTD) of RNAP II. During transcription, RNAP II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing through the CTD, which consists of up to 52 repeats of the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. CID contains eight alpha-helices in a right-handed superhelical arrangement, which closely resembles that of the VHS domains and ARM (Armadillo) repeat proteins, except for its two amino-terminal helices.


Pssm-ID: 340778  Cd Length: 125  Bit Score: 192.41  E-value: 7.11e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734   27 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSAYPHRLNLFYLANDVIQNCKRKNAIIFRESFADVLPE 106
Cdd:cd16981      4 LEKKLRSLNNTQQSIQTLSLWCLFHKKHAKQIVKIWLKELKKAKPERKLTLLYLANDVLQNSRRKGAPEFVEAFKKVLPE 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1908918734  107 AAALVK---DPSVSKSVERIFKIWEDRNVYPEEMIVALREAL 145
Cdd:cd16981     84 ALALVRsegDESVRKKVLRVLNIWEERNVFGSEFLAELRAIL 125
CID pfam04818
CID domain; This domain binds to the phosphorylated C-terminal domain (CTD) of RNA polymerase ...
 27-138 6.38e-42

CID domain; This domain binds to the phosphorylated C-terminal domain (CTD) of RNA polymerase II. This domain is known as the CTD-interacting domain (CID).


Pssm-ID: 461442  Cd Length: 117  Bit Score: 149.28  E-value: 6.38e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734   27 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSAYPHRLNLFYLANDVIQNCKRKNAIIFRESFADVLPE 106
Cdd:pfam04818    3 LEKKLSSLNNSQESIQTLSKWILFHRKHAKAIVEVWEKYLKKAKPEKKLHLLYLANDVLQNSRKKGKSEFADAFEPVLPE 82

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1908918734  107 AAALV---KDPSVSKSVERIFKIWEDRNVYPEEMI 138
Cdd:pfam04818   83 AFASAykkCDEKLKKKLERLLNIWEERNVFSPEVI 117
CID_RPRD1 cd17002
CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing protein 1 and ...
 27-147 1.53e-35

CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing protein 1 and similar proteins; This subfamily contains Regulation of nuclear pre-mRNA domain-containing proteins 1A (RPRD1A) and 1B (RPRD1B) from jawed vertebrates, CID domain-containing protein 1 (CIDS1 or cids-1) from Caenorhabditis elegans, and similar proteins. RPRD1A and RPRD1B are CID (CTD-Interacting Domain) containing proteins that co-purify with RNA polymerase (Pol) II (RNAP II) and three other RNAP II-associated proteins, RPAP2, GRINL1A and RECQL5, but not with the Mediator complex. CID binds tightly to the carboxy-terminal domain (CTD) of RNAP II. During transcription, RNAP II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing through the CTD, which consists of up to 52 repeats of the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. RPRD1A and RPRD1B form homodimers and heterodimers through their coiled-coil domains. Both associate directly with RPAP2 phosphatase and serve as CTD scaffolds to coordinate the dephosphorylation of phospho-S5 by RPAP2. The function of CIDS1 is not yet known. CID contains eight alpha-helices in a right-handed superhelical arrangement, which closely resembles that of the VHS domains and ARM (Armadillo) repeat proteins, except for its two amino-terminal helices.


Pssm-ID: 340799  Cd Length: 128  Bit Score: 131.61  E-value: 1.53e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734   27 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSAYPHRLNLFYLANDVIQNCKRKNAiIFRESFADVLPE 106
Cdd:cd17002      6 LEKKLAELSNSQQSIQTLSLWLIHHRKHAKTIVRVWLKELRKEKPSKKLTLLYLANDVIQNSRKKGP-EFTKEFAPVLED 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1908918734  107 AAALV---KDPSVSKSVERIFKIWEDRNVYPEEMIVALREALTS 147
Cdd:cd17002     85 AFKHVaklTDSEVLKALERILNIWKERQVYEKDFIEQLRAALRK 128
RPR smart00582
domain present in proteins, which are involved in regulation of nuclear pre-mRNA;
27-145 4.88e-31

domain present in proteins, which are involved in regulation of nuclear pre-mRNA;


Pssm-ID: 214731  Cd Length: 124  Bit Score: 118.53  E-value: 4.88e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734    27 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSAYPHRLNLFYLANDVIQNCKRKNAIIFRESFADVLPE 106
Cdd:smart00582    2 FEQKLESLNNSQESIQTLTKWAIEHASHAKEIVELWEKYIKKAPVPRKLPLLYLLDSIVQNSKRKYGSEFGDELGPVFQD 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 1908918734   107 AAALVKDPSVS---KSVERIFKIWEDRNVYPEEMIVALREAL 145
Cdd:smart00582   82 ALRRVLGAAPEelkKKIRRLLNIWEERGIFPPEVLRPLREKL 123
CID_Rtt103 cd17003
CID (CTD-Interacting Domain) of yeast transcription termination factor Rtt103 and similar ...
 30-145 1.25e-25

CID (CTD-Interacting Domain) of yeast transcription termination factor Rtt103 and similar proteins; Yeast transcription termination factor Rtt103 is a CID (CTD-Interacting Domain) containing protein that functions in DNA damage response. It associates with sites of DNA breaks and is essential for recovery from DNA double strand breaks in the chromosome. CID binds tightly to the carboxy-terminal domain (CTD) of RNA polymerase (Pol) II (RNAP II). Rtt103 CID preferentially interacts with CTD phosphorylated at Ser2. During transcription, RNAP II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing through the CTD, which consists of up to 52 repeats of the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. CID contains eight alpha-helices in a right-handed superhelical arrangement, which closely resembles that of the VHS domains and ARM (Armadillo) repeat proteins, except for its two amino-terminal helices.


Pssm-ID: 340800  Cd Length: 127  Bit Score: 103.07  E-value: 1.25e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734   30 KFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSAY--PHRLNLFYLANDVIQNCKRKNAIIFRESFADVLPEA 107
Cdd:cd17003      7 KLNALNETQESIVSISQWVLFHYRHADEIAEIWSDYLLKSSVnsRRKLLLIYLANDVVQQAKAKKKTEFIDAFSKVLPEV 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1908918734  108 AALVK---DPSVSKSVERIFKIWEDRNVYPEEMIVALREAL 145
Cdd:cd17003     87 LEKIYpslPSDIKKKIKRVVNVWKQRQIFSKDVIDDIEERL 127
CID_RPRD1A cd17011
CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing protein 1A; ...
 27-145 6.75e-25

CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing protein 1A; Regulation of nuclear pre-mRNA domain-containing protein 1A (RPRD1A) is also called Cyclin-dependent kinase inhibitor 2B-related protein or p15INK4B-related protein (P15RS). RPRD1A is a CID (CTD-Interacting Domain) containing protein that co-purifies with RNA polymerase (Pol) II (RNAP II) and three other RNAP II-associated proteins, RPAP2, GRINL1A and RECQL5, but not with the Mediator complex. CID binds tightly to the carboxy-terminal domain (CTD) of RNAP II. During transcription, RNAP II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing through the CTD, which consists of up to 52 repeats of the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. RPRD1A form homodimers and heterodimers with RPRD1B through their coiled-coil domains. Both RPRD1A and RPRD1B associate directly with RPAP2 phosphatase and serve as CTD scaffolds to coordinate the dephosphorylation of phospho-S5 by RPAP2. CID contains eight alpha-helices in a right-handed superhelical arrangement, which closely resembles that of the VHS domains and ARM (Armadillo) repeat proteins, except for its two amino-terminal helices.


Pssm-ID: 340808  Cd Length: 128  Bit Score: 101.27  E-value: 6.75e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734   27 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSAYPHRLNLFYLANDVIQNCKRKNAiIFRESFADVLPE 106
Cdd:cd17011      6 LEKKLSELSNSQQSVQTLSLWLIHHRKHSRPIVTVWERELRKAKPNRKLTFLYLANDVIQNSKRKGP-EFTKDFAPVIVE 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1908918734  107 AAALVK---DPSVSKSVERIFKIWEDRNVYPEEMIVALREAL 145
Cdd:cd17011     85 AFKHVSsetDESCKKHLGRVLSIWEERSVYENDVLEQLKQAL 126
CID_RPRD1B cd17012
CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing protein 1B; ...
 27-142 1.05e-23

CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing protein 1B; Regulation of nuclear pre-mRNA domain-containing protein 1B (RPRD1B) is also called Cell cycle-related and expression-elevated protein in tumor (CREPT). RPRD1B is a CID (CTD-Interacting Domain) containing protein that co-purifies with RNA polymerase (Pol) II (RNAP II) and three other RNAP II-associated proteins, RPAP2, GRINL1A and RECQL5, but not with the Mediator complex. CID binds tightly to the carboxy-terminal domain (CTD) of RNAP II. During transcription, RNAP II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing through the CTD, which consists of up to 52 repeats of the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. RPRD1B form homodimers and heterodimers with RPRD1A through their coiled-coil domains. Both RPRD1A and RPRD1B associate directly with RPAP2 phosphatase and serve as CTD scaffolds to coordinate the dephosphorylation of phospho-S5 by RPAP2. RPRD1B is highly expressed during tumorigenesis and in endometrial cancer, has been shown to promote tumor growth by accelerating the cell cycle. CID contains eight alpha-helices in a right-handed superhelical arrangement, which closely resembles that of the VHS domains and ARM (Armadillo) repeat proteins, except for its two amino-terminal helices.


Pssm-ID: 340809  Cd Length: 129  Bit Score: 97.77  E-value: 1.05e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734   27 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSAYPHRLNLFYLANDVIQNCKRKNAIIFREsFADVLPE 106
Cdd:cd17012      7 LEKKLSELSNSQQSVQTLSLWLIHHRKHAGPIVSVWHRELRKAKSSRKLTFLYLANDVIQNSKRKGPEFTRE-FESVLVD 85

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1908918734  107 AAALVK---DPSVSKSVERIFKIWEDRNVYPEEMIVALR 142
Cdd:cd17012     86 AFSHVAreaDEGCKKPLERLLNIWQERSVYGGDFIQQLK 124
CID cd03562
CID (CTD-Interacting Domain) family; The CTD-Interacting Domain (CID) is present in several ...
 36-144 1.30e-13

CID (CTD-Interacting Domain) family; The CTD-Interacting Domain (CID) is present in several eukaryotic RNA-processing factors including yeast proteins, Pcf11 and Nrd1, and vertebrate proteins, CTD-associated factors 8 (SCAF8) and Regulation of nuclear pre-mRNA domain-containing proteins (such as RPRD1 and RPRD2). Pcf11 is a conserved and essential subunit of the yeast cleavage factor IA, which is required for polyadenylation-dependent 3'-RNA processing and transcription termination. Nrd1 is implicated in polyadenylation-independent 3'-RNA processing. CID binds tightly to the carboxy-terminal domain (CTD) of RNA polymerase (Pol) II (RNAP II). During transcription, RNAP II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing through the CTD, which consists of up to 52 repeats of the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. CID contains eight alpha-helices in a right-handed superhelical arrangement, which closely resembles that of the VHS domains and ARM (Armadillo) repeat proteins, except for its two amino-terminal helices.


Pssm-ID: 340766  Cd Length: 123  Bit Score: 68.70  E-value: 1.30e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734   36 NTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSAYPHRLNLFYLANDVIQNCKRKNAiIFRESFADVLPEA---AALVK 112
Cdd:cd03562     13 LSQQSITTLTKWAIHHIKHSRPIVTVIEREIRKCKPNRKLTFLYLIDSIIRNSKRKGP-EFTKDFSPVIVELfkhVYSET 91

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1908918734  113 DPSVSKSVERIFKIWEDRNVYPEEMIVALREA 144
Cdd:cd03562     92 DEDCKKKLGRVLSIWEERNVFENSVLEQLKQA 123
CID_SCAF8_like cd16983
CID (CTD-Interacting Domain) of SR-related and CTD-associated factor 8 and similar proteins; ...
 41-144 3.32e-08

CID (CTD-Interacting Domain) of SR-related and CTD-associated factor 8 and similar proteins; This subfamily includes SR-related and CTD-associated factors 8 (SCAF8) and 4 (SCAF4), and similar proteins. SCAF4 is also called Splicing factor arginine serine rich 15 (SFRS15). Members may play roles in mRNA processing. Both SCAF4 and SCAF8 contains a CTD-interacting domain (CID) at the amino terminus and a Ser/Arg-rich domain followed by an RNA recognition motif. CID binds tightly to the carboxy-terminal domain (CTD) of RNA polymerase (Pol) II (RNAP II). During transcription, RNAP II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing through the CTD, which consists of up to 52 repeats of the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. CID contains eight alpha-helices in a right-handed superhelical arrangement, which closely resembles that of the VHS domains and ARM (Armadillo) repeat proteins, except for its two amino-terminal helices.


Pssm-ID: 340780  Cd Length: 131  Bit Score: 53.38  E-value: 3.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734   41 IQGLSSWCIENKKHHSTIVYHWMKWLRRSAYPHRLNLFYLANDVIQNCKRKNAII---FRESFADVL-PEAAALVKDPSV 116
Cdd:cd16983     22 INAITKLAIKAIKFYKHVVQSVEKFIQKCKPEYKLPGLYVIDSIIRQSRHQYGKEkdvYAPRFAKNLsKTFLNLLKCPEK 101

                           90       100
                   ....*....|....*....|....*....
gi 1908918734  117 SKS-VERIFKIWEDRNVYPEEMIVALREA 144
Cdd:cd16983    102 DKPkVKRVLNLWQKNGVFPKEIIQPLLDA 130
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 293-610 2.89e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 45.29  E-value: 2.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734  293 SPVPSPSMDAPSPTgSESPFQGMGGEESQSPTMESEKSATPEPVTDnrdvedmelsdveddgskiivedrkeKPAEKSAV 372
Cdd:pfam05109  475 SPTPAGTTSGASPV-TPSPSPRDNGTESKAPDMTSPTSAVTTPTPN--------------------------ATSPTPAV 527

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734  373 STSVPTKPTENISKASsctPVPVTMTATPPLPKPVNTSLSPSPALALPNLANVdlAKISSILSSLTSVMKNTGLSSLLQS 452
Cdd:pfam05109  528 TTPTPNATSPTLGKTS---PTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKT--SPTSAVTTPTPNATSPTVGETSPQA 602

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734  453 VTGNPVPASEAASQSTSASPANTTVSTIKGR-NLPSSAQPFI---PKSFNYSPNSSTSEVSSTSASKASIGQSPGLPSTT 528
Cdd:pfam05109  603 NTTNHTLGGTSSTPVVTSPPKNATSAVTTGQhNITSSSTSSMslrPSSISETLSPSTSDNSTSHMPLLTSAHPTGGENIT 682

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734  529 FKLPSNslgfTATHNTSPAAP-PTEVTicqSSEVSKPKLESESTSPSLEmkihNFLKGNP--------GFSGLNLNIPIL 599
Cdd:pfam05109  683 QVTPAS----TSTHHVSTSSPaPRPGT---TSQASGPGNSSTSTKPGEV----NVTKGTPpknatspqAPSGQKTAVPTV 751

                          330
                   ....*....|.
gi 1908918734  600 SSLGSSAPSES 610
Cdd:pfam05109  752 TSTGGKANSTT 762
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
98-292 1.40e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734   98 ESFADVLPEAAALVKD-PSVSKSVERIFKIWEDRNVYPEEmIVALREALTSTN-PKAALKSKIVaEFRSQalIEELllyK 175
Cdd:PRK03918   200 KELEEVLREINEISSElPELREELEKLEKEVKELEELKEE-IEELEKELESLEgSKRKLEEKIR-ELEER--IEEL---K 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1908918734  176 RSEDQIELKEKQLSTMRVDVCSTETLKCLKDKTggKKFSKEFEEASSKLEEFVNGLDKQVKNGPSLTEALENagifYEAQ 255
Cdd:PRK03918   273 KEIEELEEKVKELKELKEKAEEYIKLSEFYEEY--LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE----LKKK 346

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1908918734  256 YKEVKVVANAYKTFA---NRVNNLKKKLDQLKSTLPD--PEE 292
Cdd:PRK03918   347 LKELEKRLEELEERHelyEEAKAKKEELERLKKRLTGltPEK 388
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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