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Conserved domains on  [gi|1958755001|ref|XP_038959720|]
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regulation of nuclear pre-mRNA domain-containing protein 2 isoform X4 [Rattus norvegicus]

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

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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; ...
27-146 7.84e-85

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: 268.32  E-value: 7.84e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001  27 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSTYPHRLNLFYLANDVIQNCKRKNAIIFRESFADVLPE 106
Cdd:cd17001     6 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSAYPHRLNLFYLANDVIQNCKRKNAIVFRESFAEVLPE 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958755001 107 AAALVKDPSVSKSIERIFKIWEDRNVYPEDMIVALREALS 146
Cdd:cd17001    86 AAALVKDASVSKSVERIFKIWEERNVYPEETIAALKEALS 125
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
319-645 6.26e-06

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: 50.30  E-value: 6.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 319 SPVPSPSMDAPSPTgSESPFQGMGGEESQSPTMESDKSATPEPVTDNRDvedmelsdveddgskiivedrkekpvEKPAV 398
Cdd:pfam05109 475 SPTPAGTTSGASPV-TPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATS--------------------------PTPAV 527
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 399 STGVVTKSTENISKTSPCAPPSVPT-TAAPPLPkplntSLLSPSPTLVLPNLANVD---LAKISSILSSLTSVMKNTGVS 474
Cdd:pfam05109 528 TTPTPNATSPTLGKTSPTSAVTTPTpNATSPTP-----AVTTPTPNATIPTLGKTSptsAVTTPTPNATSPTVGETSPQA 602
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 475 SASRPSPGTPTSPSSLSSGLKTPAPA-TTPSHNPLANILSKVEITPESILSALSKTQTQSAPALQGLSSLLQSVTGNPV- 552
Cdd:pfam05109 603 NTTNHTLGGTSSTPVVTSPPKNATSAvTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHPTGGENIt 682
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 553 ---PASEAASQSTAASPASTTGSAVKGRNLLSNTQSFISKSFNYSPNSSTSEVSSTSASKASVGQSPVLPSTTFKLPSSS 629
Cdd:pfam05109 683 qvtPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTSTGGKANSTT 762
                         330
                  ....*....|....*..
gi 1958755001 630 LG-FTGTHNTSPAAPPT 645
Cdd:pfam05109 763 GGkHTTGHGARTSTEPT 779
PRK03918 super family cl35229
DNA double-strand break repair ATPase Rad50;
142-318 6.81e-04

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: 43.51  E-value: 6.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 142 REALSTTFKTQKQLKENLNKQpNKQWKKSQTStnpKAALKSKIVaEFRSQalIEELlmyKRSEDQIELKEKQLSTMRVDV 221
Cdd:PRK03918  223 LEKLEKEVKELEELKEEIEEL-EKELESLEGS---KRKLEEKIR-ELEER--IEEL---KKEIEELEEKVKELKELKEKA 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 222 CSTETLKCLKDKTggKKFSKEFEEASSKLEEFVNGLDKQVKNGPSLTEALENagifYEAQYKEVKVVANAYKTFA---NR 298
Cdd:PRK03918  293 EEYIKLSEFYEEY--LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE----LKKKLKELEKRLEELEERHelyEE 366
                         170       180
                  ....*....|....*....|..
gi 1958755001 299 VNNLKKKLDQLKSTLPD--PEE 318
Cdd:PRK03918  367 AKAKKEELERLKKRLTGltPEK 388
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
495-818 9.04e-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: 43.37  E-value: 9.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 495 KTPAPATTPSHNPlanILSKveiTPESILSA--LSKTQTQSAPALQGLSSLLQSVTGNPVPASEAASQSTAASPASTTGS 572
Cdd:pfam05109 407 RTATNATTTTHKV---IFSK---APESTTTSptLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSPTPAG 480
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 573 AVKGRNLLSNTQSfisksfnyspnsstsEVSSTSASKASVGQSPVLPSTTFKLPSSSLGFTGTHNTSPAAPPTEVAMCQS 652
Cdd:pfam05109 481 TTSGASPVTPSPS---------------PRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPT 545
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 653 SEVSKPKPESES-----TSPSLEMKIHNFLKGNPGfSGLNLNIPILSS--LGSSAPSEGHSSDFQRGPTSTSVDNidgTP 725
Cdd:pfam05109 546 SAVTTPTPNATSptpavTTPTPNATIPTLGKTSPT-SAVTTPTPNATSptVGETSPQANTTNHTLGGTSSTPVVT---SP 621
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 726 VRDERSGTPTQDEMMdkpTSSSVDTMSL----LSKIISPGSSTPSSIRSP------PAGGdESYPQEPPSSVSTYrpfgl 795
Cdd:pfam05109 622 PKNATSAVTTGQHNI---TSSSTSSMSLrpssISETLSPSTSDNSTSHMPlltsahPTGG-ENITQVTPASTSTH----- 692
                         330       340
                  ....*....|....*....|...
gi 1958755001 796 gggspYKQSSSAVERPSSLMDSS 818
Cdd:pfam05109 693 -----HVSTSSPAPRPGTTSQAS 710
 
Name Accession Description Interval E-value
CID_RPRD2 cd17001
CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing protein 2; ...
27-146 7.84e-85

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: 268.32  E-value: 7.84e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001  27 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSTYPHRLNLFYLANDVIQNCKRKNAIIFRESFADVLPE 106
Cdd:cd17001     6 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSAYPHRLNLFYLANDVIQNCKRKNAIVFRESFAEVLPE 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958755001 107 AAALVKDPSVSKSIERIFKIWEDRNVYPEDMIVALREALS 146
Cdd:cd17001    86 AAALVKDASVSKSVERIFKIWEERNVYPEETIAALKEALS 125
CID pfam04818
CID domain; This domain binds to the phosphorylated C-terminal domain (CTD) of RNA polymerase ...
27-138 2.71e-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: 150.05  E-value: 2.71e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001  27 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSTYPHRLNLFYLANDVIQNCKRKNAIIFRESFADVLPE 106
Cdd:pfam04818   3 LEKKLSSLNNSQESIQTLSKWILFHRKHAKAIVEVWEKYLKKAKPEKKLHLLYLANDVLQNSRKKGKSEFADAFEPVLPE 82
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958755001 107 AAALV---KDPSVSKSIERIFKIWEDRNVYPEDMI 138
Cdd:pfam04818  83 AFASAykkCDEKLKKKLERLLNIWEERNVFSPEVI 117
RPR smart00582
domain present in proteins, which are involved in regulation of nuclear pre-mRNA;
27-145 2.77e-31

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


Pssm-ID: 214731  Cd Length: 124  Bit Score: 118.92  E-value: 2.77e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001   27 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSTYPHRLNLFYLANDVIQNCKRKNAIIFRESFADVLPE 106
Cdd:smart00582   2 FEQKLESLNNSQESIQTLTKWAIEHASHAKEIVELWEKYIKKAPVPRKLPLLYLLDSIVQNSKRKYGSEFGDELGPVFQD 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1958755001  107 AAALVKDPSVS---KSIERIFKIWEDRNVYPEDMIVALREAL 145
Cdd:smart00582  82 ALRRVLGAAPEelkKKIRRLLNIWEERGIFPPEVLRPLREKL 123
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
319-645 6.26e-06

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: 50.30  E-value: 6.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 319 SPVPSPSMDAPSPTgSESPFQGMGGEESQSPTMESDKSATPEPVTDNRDvedmelsdveddgskiivedrkekpvEKPAV 398
Cdd:pfam05109 475 SPTPAGTTSGASPV-TPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATS--------------------------PTPAV 527
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 399 STGVVTKSTENISKTSPCAPPSVPT-TAAPPLPkplntSLLSPSPTLVLPNLANVD---LAKISSILSSLTSVMKNTGVS 474
Cdd:pfam05109 528 TTPTPNATSPTLGKTSPTSAVTTPTpNATSPTP-----AVTTPTPNATIPTLGKTSptsAVTTPTPNATSPTVGETSPQA 602
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 475 SASRPSPGTPTSPSSLSSGLKTPAPA-TTPSHNPLANILSKVEITPESILSALSKTQTQSAPALQGLSSLLQSVTGNPV- 552
Cdd:pfam05109 603 NTTNHTLGGTSSTPVVTSPPKNATSAvTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHPTGGENIt 682
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 553 ---PASEAASQSTAASPASTTGSAVKGRNLLSNTQSFISKSFNYSPNSSTSEVSSTSASKASVGQSPVLPSTTFKLPSSS 629
Cdd:pfam05109 683 qvtPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTSTGGKANSTT 762
                         330
                  ....*....|....*..
gi 1958755001 630 LG-FTGTHNTSPAAPPT 645
Cdd:pfam05109 763 GGkHTTGHGARTSTEPT 779
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
142-318 6.81e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 6.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 142 REALSTTFKTQKQLKENLNKQpNKQWKKSQTStnpKAALKSKIVaEFRSQalIEELlmyKRSEDQIELKEKQLSTMRVDV 221
Cdd:PRK03918  223 LEKLEKEVKELEELKEEIEEL-EKELESLEGS---KRKLEEKIR-ELEER--IEEL---KKEIEELEEKVKELKELKEKA 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 222 CSTETLKCLKDKTggKKFSKEFEEASSKLEEFVNGLDKQVKNGPSLTEALENagifYEAQYKEVKVVANAYKTFA---NR 298
Cdd:PRK03918  293 EEYIKLSEFYEEY--LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE----LKKKLKELEKRLEELEERHelyEE 366
                         170       180
                  ....*....|....*....|..
gi 1958755001 299 VNNLKKKLDQLKSTLPD--PEE 318
Cdd:PRK03918  367 AKAKKEELERLKKRLTGltPEK 388
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
495-818 9.04e-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: 43.37  E-value: 9.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 495 KTPAPATTPSHNPlanILSKveiTPESILSA--LSKTQTQSAPALQGLSSLLQSVTGNPVPASEAASQSTAASPASTTGS 572
Cdd:pfam05109 407 RTATNATTTTHKV---IFSK---APESTTTSptLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSPTPAG 480
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 573 AVKGRNLLSNTQSfisksfnyspnsstsEVSSTSASKASVGQSPVLPSTTFKLPSSSLGFTGTHNTSPAAPPTEVAMCQS 652
Cdd:pfam05109 481 TTSGASPVTPSPS---------------PRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPT 545
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 653 SEVSKPKPESES-----TSPSLEMKIHNFLKGNPGfSGLNLNIPILSS--LGSSAPSEGHSSDFQRGPTSTSVDNidgTP 725
Cdd:pfam05109 546 SAVTTPTPNATSptpavTTPTPNATIPTLGKTSPT-SAVTTPTPNATSptVGETSPQANTTNHTLGGTSSTPVVT---SP 621
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 726 VRDERSGTPTQDEMMdkpTSSSVDTMSL----LSKIISPGSSTPSSIRSP------PAGGdESYPQEPPSSVSTYrpfgl 795
Cdd:pfam05109 622 PKNATSAVTTGQHNI---TSSSTSSMSLrpssISETLSPSTSDNSTSHMPlltsahPTGG-ENITQVTPASTSTH----- 692
                         330       340
                  ....*....|....*....|...
gi 1958755001 796 gggspYKQSSSAVERPSSLMDSS 818
Cdd:pfam05109 693 -----HVSTSSPAPRPGTTSQAS 710
PHA03247 PHA03247
large tegument protein UL36; Provisional
314-577 1.10e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001  314 PDPEESPVPSPSMDAP-SPTGSESPFQGMGGEESQSPTMESDKSATPEPVTDNRDVEDMELSDVEDDGSKiivedrkeKP 392
Cdd:PHA03247  2733 PALPAAPAPPAVPAGPaTPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPW--------DP 2804
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001  393 VEKPAVSTGVVTKSTENISKTSPCAPPSVPTTAAPPLPKPLNTSLLSPSPTLVlpnlANVDLAKISSILSSLTSVMKNT- 471
Cdd:PHA03247  2805 ADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA----PGGDVRRRPPSRSPAAKPAAPAr 2880
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001  472 -GVSSASRP----SPGTPTSPSSLSSGLKTPAPATTPSHNPLANILSKVEITPEsilsalskTQTQSAPALQglssllqs 546
Cdd:PHA03247  2881 pPVRRLARPavsrSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPP--------PPPRPQPPLA-------- 2944
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1958755001  547 vtgnPVPASEAASQSTAASPASTTGSAVKGR 577
Cdd:PHA03247  2945 ----PTTDPAGAGEPSGAVPQPWLGALVPGR 2971
 
Name Accession Description Interval E-value
CID_RPRD2 cd17001
CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing protein 2; ...
27-146 7.84e-85

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: 268.32  E-value: 7.84e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001  27 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSTYPHRLNLFYLANDVIQNCKRKNAIIFRESFADVLPE 106
Cdd:cd17001     6 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSAYPHRLNLFYLANDVIQNCKRKNAIVFRESFAEVLPE 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958755001 107 AAALVKDPSVSKSIERIFKIWEDRNVYPEDMIVALREALS 146
Cdd:cd17001    86 AAALVKDASVSKSVERIFKIWEERNVYPEETIAALKEALS 125
CID_RPRD_like cd16981
CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing proteins; ...
27-145 4.43e-56

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: 189.33  E-value: 4.43e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001  27 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSTYPHRLNLFYLANDVIQNCKRKNAIIFRESFADVLPE 106
Cdd:cd16981     4 LEKKLRSLNNTQQSIQTLSLWCLFHKKHAKQIVKIWLKELKKAKPERKLTLLYLANDVLQNSRRKGAPEFVEAFKKVLPE 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958755001 107 AAALVK---DPSVSKSIERIFKIWEDRNVYPEDMIVALREAL 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 2.71e-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: 150.05  E-value: 2.71e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001  27 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSTYPHRLNLFYLANDVIQNCKRKNAIIFRESFADVLPE 106
Cdd:pfam04818   3 LEKKLSSLNNSQESIQTLSKWILFHRKHAKAIVEVWEKYLKKAKPEKKLHLLYLANDVLQNSRKKGKSEFADAFEPVLPE 82
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958755001 107 AAALV---KDPSVSKSIERIFKIWEDRNVYPEDMI 138
Cdd:pfam04818  83 AFASAykkCDEKLKKKLERLLNIWEERNVFSPEVI 117
CID_RPRD1 cd17002
CID (CTD-Interacting Domain) of Regulation of nuclear pre-mRNA domain-containing protein 1 and ...
27-145 6.09e-37

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: 135.08  E-value: 6.09e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001  27 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSTYPHRLNLFYLANDVIQNCKRKNAiIFRESFADVLPE 106
Cdd:cd17002     6 LEKKLAELSNSQQSIQTLSLWLIHHRKHAKTIVRVWLKELRKEKPSKKLTLLYLANDVIQNSRKKGP-EFTKEFAPVLED 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958755001 107 AAALV---KDPSVSKSIERIFKIWEDRNVYPEDMIVALREAL 145
Cdd:cd17002    85 AFKHVaklTDSEVLKALERILNIWKERQVYEKDFIEQLRAAL 126
RPR smart00582
domain present in proteins, which are involved in regulation of nuclear pre-mRNA;
27-145 2.77e-31

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


Pssm-ID: 214731  Cd Length: 124  Bit Score: 118.92  E-value: 2.77e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001   27 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSTYPHRLNLFYLANDVIQNCKRKNAIIFRESFADVLPE 106
Cdd:smart00582   2 FEQKLESLNNSQESIQTLTKWAIEHASHAKEIVELWEKYIKKAPVPRKLPLLYLLDSIVQNSKRKYGSEFGDELGPVFQD 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1958755001  107 AAALVKDPSVS---KSIERIFKIWEDRNVYPEDMIVALREAL 145
Cdd:smart00582  82 ALRRVLGAAPEelkKKIRRLLNIWEERGIFPPEVLRPLREKL 123
CID_Rtt103 cd17003
CID (CTD-Interacting Domain) of yeast transcription termination factor Rtt103 and similar ...
30-145 3.11e-26

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: 104.61  E-value: 3.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001  30 KFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSTY--PHRLNLFYLANDVIQNCKRKNAIIFRESFADVLPEA 107
Cdd:cd17003     7 KLNALNETQESIVSISQWVLFHYRHADEIAEIWSDYLLKSSVnsRRKLLLIYLANDVVQQAKAKKKTEFIDAFSKVLPEV 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958755001 108 AALVK---DPSVSKSIERIFKIWEDRNVYPEDMIVALREAL 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 8.09e-26

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: 103.58  E-value: 8.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001  27 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSTYPHRLNLFYLANDVIQNCKRKNAiIFRESFADVLPE 106
Cdd:cd17011     6 LEKKLSELSNSQQSVQTLSLWLIHHRKHSRPIVTVWERELRKAKPNRKLTFLYLANDVIQNSKRKGP-EFTKDFAPVIVE 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958755001 107 AAALVK---DPSVSKSIERIFKIWEDRNVYPEDMIVALREAL 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 4.42e-24

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: 98.54  E-value: 4.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001  27 LDRKFQSVTNTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSTYPHRLNLFYLANDVIQNCKRKNAIIFREsFADVLPE 106
Cdd:cd17012     7 LEKKLSELSNSQQSVQTLSLWLIHHRKHAGPIVSVWHRELRKAKSSRKLTFLYLANDVIQNSKRKGPEFTRE-FESVLVD 85
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958755001 107 AAALVK---DPSVSKSIERIFKIWEDRNVYPEDMIVALR 142
Cdd:cd17012    86 AFSHVAreaDEGCKKPLERLLNIWQERSVYGGDFIQQLK 124
CID cd03562
CID (CTD-Interacting Domain) family; The CTD-Interacting Domain (CID) is present in several ...
36-144 9.14e-14

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: 9.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001  36 NTMESIQGLSSWCIENKKHHSTIVYHWMKWLRRSTYPHRLNLFYLANDVIQNCKRKNAiIFRESFADVLPEA---AALVK 112
Cdd:cd03562    13 LSQQSITTLTKWAIHHIKHSRPIVTVIEREIRKCKPNRKLTFLYLIDSIIRNSKRKGP-EFTKDFSPVIVELfkhVYSET 91
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958755001 113 DPSVSKSIERIFKIWEDRNVYPEDMIVALREA 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 4.15e-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: 52.61  E-value: 4.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001  41 IQGLSSWCIENKKHHSTIVYHWMKWLRRSTYPHRLNLFYLANDVIQNCKRKNAII---FRESFADVL-PEAAALVKDPSV 116
Cdd:cd16983    22 INAITKLAIKAIKFYKHVVQSVEKFIQKCKPEYKLPGLYVIDSIIRQSRHQYGKEkdvYAPRFAKNLsKTFLNLLKCPEK 101
                          90       100
                  ....*....|....*....|....*....
gi 1958755001 117 SKS-IERIFKIWEDRNVYPEDMIVALREA 144
Cdd:cd16983   102 DKPkVKRVLNLWQKNGVFPKEIIQPLLDA 130
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
319-645 6.26e-06

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: 50.30  E-value: 6.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 319 SPVPSPSMDAPSPTgSESPFQGMGGEESQSPTMESDKSATPEPVTDNRDvedmelsdveddgskiivedrkekpvEKPAV 398
Cdd:pfam05109 475 SPTPAGTTSGASPV-TPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATS--------------------------PTPAV 527
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 399 STGVVTKSTENISKTSPCAPPSVPT-TAAPPLPkplntSLLSPSPTLVLPNLANVD---LAKISSILSSLTSVMKNTGVS 474
Cdd:pfam05109 528 TTPTPNATSPTLGKTSPTSAVTTPTpNATSPTP-----AVTTPTPNATIPTLGKTSptsAVTTPTPNATSPTVGETSPQA 602
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 475 SASRPSPGTPTSPSSLSSGLKTPAPA-TTPSHNPLANILSKVEITPESILSALSKTQTQSAPALQGLSSLLQSVTGNPV- 552
Cdd:pfam05109 603 NTTNHTLGGTSSTPVVTSPPKNATSAvTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHPTGGENIt 682
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 553 ---PASEAASQSTAASPASTTGSAVKGRNLLSNTQSFISKSFNYSPNSSTSEVSSTSASKASVGQSPVLPSTTFKLPSSS 629
Cdd:pfam05109 683 qvtPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTSTGGKANSTT 762
                         330
                  ....*....|....*..
gi 1958755001 630 LG-FTGTHNTSPAAPPT 645
Cdd:pfam05109 763 GGkHTTGHGARTSTEPT 779
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
142-318 6.81e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 6.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 142 REALSTTFKTQKQLKENLNKQpNKQWKKSQTStnpKAALKSKIVaEFRSQalIEELlmyKRSEDQIELKEKQLSTMRVDV 221
Cdd:PRK03918  223 LEKLEKEVKELEELKEEIEEL-EKELESLEGS---KRKLEEKIR-ELEER--IEEL---KKEIEELEEKVKELKELKEKA 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 222 CSTETLKCLKDKTggKKFSKEFEEASSKLEEFVNGLDKQVKNGPSLTEALENagifYEAQYKEVKVVANAYKTFA---NR 298
Cdd:PRK03918  293 EEYIKLSEFYEEY--LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE----LKKKLKELEKRLEELEERHelyEE 366
                         170       180
                  ....*....|....*....|..
gi 1958755001 299 VNNLKKKLDQLKSTLPD--PEE 318
Cdd:PRK03918  367 AKAKKEELERLKKRLTGltPEK 388
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
495-818 9.04e-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: 43.37  E-value: 9.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 495 KTPAPATTPSHNPlanILSKveiTPESILSA--LSKTQTQSAPALQGLSSLLQSVTGNPVPASEAASQSTAASPASTTGS 572
Cdd:pfam05109 407 RTATNATTTTHKV---IFSK---APESTTTSptLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSPTPAG 480
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 573 AVKGRNLLSNTQSfisksfnyspnsstsEVSSTSASKASVGQSPVLPSTTFKLPSSSLGFTGTHNTSPAAPPTEVAMCQS 652
Cdd:pfam05109 481 TTSGASPVTPSPS---------------PRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPT 545
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 653 SEVSKPKPESES-----TSPSLEMKIHNFLKGNPGfSGLNLNIPILSS--LGSSAPSEGHSSDFQRGPTSTSVDNidgTP 725
Cdd:pfam05109 546 SAVTTPTPNATSptpavTTPTPNATIPTLGKTSPT-SAVTTPTPNATSptVGETSPQANTTNHTLGGTSSTPVVT---SP 621
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001 726 VRDERSGTPTQDEMMdkpTSSSVDTMSL----LSKIISPGSSTPSSIRSP------PAGGdESYPQEPPSSVSTYrpfgl 795
Cdd:pfam05109 622 PKNATSAVTTGQHNI---TSSSTSSMSLrpssISETLSPSTSDNSTSHMPlltsahPTGG-ENITQVTPASTSTH----- 692
                         330       340
                  ....*....|....*....|...
gi 1958755001 796 gggspYKQSSSAVERPSSLMDSS 818
Cdd:pfam05109 693 -----HVSTSSPAPRPGTTSQAS 710
PHA03247 PHA03247
large tegument protein UL36; Provisional
314-577 1.10e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001  314 PDPEESPVPSPSMDAP-SPTGSESPFQGMGGEESQSPTMESDKSATPEPVTDNRDVEDMELSDVEDDGSKiivedrkeKP 392
Cdd:PHA03247  2733 PALPAAPAPPAVPAGPaTPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPW--------DP 2804
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001  393 VEKPAVSTGVVTKSTENISKTSPCAPPSVPTTAAPPLPKPLNTSLLSPSPTLVlpnlANVDLAKISSILSSLTSVMKNT- 471
Cdd:PHA03247  2805 ADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA----PGGDVRRRPPSRSPAAKPAAPAr 2880
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001  472 -GVSSASRP----SPGTPTSPSSLSSGLKTPAPATTPSHNPLANILSKVEITPEsilsalskTQTQSAPALQglssllqs 546
Cdd:PHA03247  2881 pPVRRLARPavsrSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPP--------PPPRPQPPLA-------- 2944
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1958755001  547 vtgnPVPASEAASQSTAASPASTTGSAVKGR 577
Cdd:PHA03247  2945 ----PTTDPAGAGEPSGAVPQPWLGALVPGR 2971
PHA03247 PHA03247
large tegument protein UL36; Provisional
314-844 1.66e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001  314 PDPEESPVPSPsmDAPSPTGSESP--FQGMGGEESQSPTM----------ESDKSATPEP--------VTDNRDVEDmel 373
Cdd:PHA03247  2496 PDPGGGGPPDP--DAPPAPSRLAPaiLPDEPVGEPVHPRMltwirgleelASDDAGDPPPplppaappAAPDRSVPP--- 2570
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001  374 SDVEDDGSKIIVEDRKEKPVEKPAVSTGVVTKSTENISKTSPCAPPSVPTTAAPPLPKPlntsllSPSP---TLVLPNLA 450
Cdd:PHA03247  2571 PRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPP------SPSPaanEPDPHPPP 2644
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001  451 NVDLAKISSILSSLTSVMKNTGVSSASRPS-----------PGTPTSPSSLSSGLKTPAPATTPSHNPLAnilskveITP 519
Cdd:PHA03247  2645 TVPPPERPRDDPAPGRVSRPRRARRLGRAAqassppqrprrRAARPTVGSLTSLADPPPPPPTPEPAPHA-------LVS 2717
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001  520 ESILSALSKTQTQSAPALQGLSSLLQSVTGNPVPASEA--ASQSTAASPASTTGSAVKGRNLLSNTQSFISKSFNYSPNS 597
Cdd:PHA03247  2718 ATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPArpARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRES 2797
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001  598 STSEVSSTSASKASVGQSPVLPSTTfkLPSsslgftgthntSPAAPPTEVAMCQSSEVSKPKPESESTSpslemkihnfl 677
Cdd:PHA03247  2798 LPSPWDPADPPAAVLAPAAALPPAA--SPA-----------GPLPPPTSAQPTAPPPPPGPPPPSLPLG----------- 2853
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001  678 kgnpgfsglnlnipilsslGSSAPseghSSDFQRGPTSTSVDNIDGTPVRdersgtPTQDEMMDKPTSSSVDTMSL---- 753
Cdd:PHA03247  2854 -------------------GSVAP----GGDVRRRPPSRSPAAKPAAPAR------PPVRRLARPAVSRSTESFALppdq 2904
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001  754 LSKIISPGSSTPSSIRSPPAGGDESYPQEPPSSVSTYRPFGLGGGSPYKQSSSAVERPSSLMDSSQEKLFPDTSFQEDED 833
Cdd:PHA03247  2905 PERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
                          570
                   ....*....|.
gi 1958755001  834 YRDFEYSGPPP 844
Cdd:PHA03247  2985 SREAPASSTPP 2995
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
307-442 5.30e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.92  E-value: 5.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755001  307 DQLKSTLPDPEESPVPSPSMDAPSPTGSESPFQGMGGEESQSPTMESDKSATPEPVTDNRDVEDMELSDVEDDGSKIIVE 386
Cdd:PHA03307   793 EAAFRRPGRLRRSGPAADAASRTASKRKSRSHTPDGGSESSGPARPPGAAARPPPARSSESSKSKPAAAGGRARGKNGRR 872
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958755001  387 -DRKEKPVEKPAVSTGvvtkstenisktSPCAPPSVPTTAAPPLPKPLNTSLLSPSP 442
Cdd:PHA03307   873 rPRPPEPRARPGAAAP------------PKAAAAAPPAGAPAPRPRPAPRVKLGPMP 917
 
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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