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Conserved domains on  [gi|1907200786|ref|XP_036011246|]
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cAMP-regulated phosphoprotein 21 isoform X6 [Mus musculus]

Protein Classification

R3H_encore_like and SUZ domain-containing protein( domain architecture ID 12927641)

protein containing domains R3H_encore_like, SUZ, and PAT1

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
R3H_encore_like cd02642
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the ...
162-223 1.40e-25

R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the germline exit after four mitotic divisions, by facilitating SCF-ubiquitin-proteasome-dependent proteolysis. Maize DBF1-interactor protein 1 (DIP1) containing an R3H domain is a potential regulator of DBF1 activity in stress responses. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


:

Pssm-ID: 100071  Cd Length: 63  Bit Score: 99.98  E-value: 1.40e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907200786 162 DRMILLKMEQEMIDFIADSNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG-KSVIINKT 223
Cdd:cd02642     1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
SUZ pfam12752
SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched ...
244-298 6.38e-12

SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched in positively charged amino acids. It was first characterized in the C.elegans protein Szy-20 where it has been shown to bind RNA and allow their localization to the centrosome. Warning- the domain has a compositionally biased character.


:

Pssm-ID: 463689 [Multi-domain]  Cd Length: 56  Bit Score: 61.18  E-value: 6.38e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907200786 244 ESQKRFILKRDNSSIDKEDNQNRM-HPFRDDRRSKSIEEREEEYQRVRERIFAHDS 298
Cdd:pfam12752   1 PPPKMKILRRPSSGSSSSSSAGSSgASSSSGSDSKTLEEREAEYAEARARIFGSSE 56
PAT1 super family cl37801
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
568-797 1.19e-05

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


The actual alignment was detected with superfamily member pfam09770:

Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 48.88  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786 568 QLSMSRQssgdtpEPPSGTVYPASLLPQTAQPQSYVITSAGQQLS----TG--GFSDSGPPISQQVLQA----PPSPQGF 637
Cdd:pfam09770  99 QVRFNRQ------QPAARAAQSSAQPPASSLPQYQYASQQSQQPSkpvrTGyeKYKEPEPIPDLQVDASlwgvAPKKAAA 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786 638 VQQPPPAQMSvyyypsgqyPTSTSQQYRPLASVQY--SAQRSQQIPQTTQQA-------GYQPVLSGQQGFQGMMGVQQS 708
Cdd:pfam09770 173 PAPAPQPAAQ---------PASLPAPSRKMMSLEEveAAMRAQAKKPAQQPApapaqppAAPPAQQAQQQQQFPPQIQQQ 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786 709 AHSQGVMSSQQGAPVHGVMVS---YPTMSSYQVPMTQGSQAVPQQTYQPP--IMLPSQAGQ--GSLPATGMPVYCNVTPP 781
Cdd:pfam09770 244 QQPQQQPQQPQQHPGQGHPVTilqRPQSPQPDPAQPSIQPQAQQFHQQPPpvPVQPTQILQnpNRLSAARVGYPQNPQPG 323
                         250
                  ....*....|....*.
gi 1907200786 782 NPQNNLRLMGPHCPSS 797
Cdd:pfam09770 324 VQPAPAHQAHRQQGSF 339
 
Name Accession Description Interval E-value
R3H_encore_like cd02642
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the ...
162-223 1.40e-25

R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the germline exit after four mitotic divisions, by facilitating SCF-ubiquitin-proteasome-dependent proteolysis. Maize DBF1-interactor protein 1 (DIP1) containing an R3H domain is a potential regulator of DBF1 activity in stress responses. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100071  Cd Length: 63  Bit Score: 99.98  E-value: 1.40e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907200786 162 DRMILLKMEQEMIDFIADSNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG-KSVIINKT 223
Cdd:cd02642     1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
146-223 7.85e-13

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 64.24  E-value: 7.85e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786  146 IDLHGFLINTLKNNSRDRMILLKMEQEMIDFIAdSNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG--KSVIINKT 223
Cdd:smart00393   1 ADFLPVTLDALSYRPRRREELIELELEIARFVK-STKESVELPPMNSYERKIVHELAEKYGLESESFGEGpkRRVVISKK 79
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ...
164-222 5.50e-12

R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.


Pssm-ID: 460206  Cd Length: 60  Bit Score: 61.35  E-value: 5.50e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907200786 164 MILLKMEQEMIDFIADSNNHYKkFPQMSSYQRMLVHRVAAYFGLDHNV--DQTGKSVIINK 222
Cdd:pfam01424   1 EFLEQLAEKLAEFVKDTGKSLE-LPPMSSYERRIIHELAQKYGLESESegEEPNRRVVVYK 60
SUZ pfam12752
SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched ...
244-298 6.38e-12

SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched in positively charged amino acids. It was first characterized in the C.elegans protein Szy-20 where it has been shown to bind RNA and allow their localization to the centrosome. Warning- the domain has a compositionally biased character.


Pssm-ID: 463689 [Multi-domain]  Cd Length: 56  Bit Score: 61.18  E-value: 6.38e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907200786 244 ESQKRFILKRDNSSIDKEDNQNRM-HPFRDDRRSKSIEEREEEYQRVRERIFAHDS 298
Cdd:pfam12752   1 PPPKMKILRRPSSGSSSSSSAGSSgASSSSGSDSKTLEEREAEYAEARARIFGSSE 56
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
568-797 1.19e-05

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 48.88  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786 568 QLSMSRQssgdtpEPPSGTVYPASLLPQTAQPQSYVITSAGQQLS----TG--GFSDSGPPISQQVLQA----PPSPQGF 637
Cdd:pfam09770  99 QVRFNRQ------QPAARAAQSSAQPPASSLPQYQYASQQSQQPSkpvrTGyeKYKEPEPIPDLQVDASlwgvAPKKAAA 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786 638 VQQPPPAQMSvyyypsgqyPTSTSQQYRPLASVQY--SAQRSQQIPQTTQQA-------GYQPVLSGQQGFQGMMGVQQS 708
Cdd:pfam09770 173 PAPAPQPAAQ---------PASLPAPSRKMMSLEEveAAMRAQAKKPAQQPApapaqppAAPPAQQAQQQQQFPPQIQQQ 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786 709 AHSQGVMSSQQGAPVHGVMVS---YPTMSSYQVPMTQGSQAVPQQTYQPP--IMLPSQAGQ--GSLPATGMPVYCNVTPP 781
Cdd:pfam09770 244 QQPQQQPQQPQQHPGQGHPVTilqRPQSPQPDPAQPSIQPQAQQFHQQPPpvPVQPTQILQnpNRLSAARVGYPQNPQPG 323
                         250
                  ....*....|....*.
gi 1907200786 782 NPQNNLRLMGPHCPSS 797
Cdd:pfam09770 324 VQPAPAHQAHRQQGSF 339
PRK10927 PRK10927
cell division protein FtsN;
572-723 5.62e-04

cell division protein FtsN;


Pssm-ID: 236797 [Multi-domain]  Cd Length: 319  Bit Score: 42.74  E-value: 5.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786 572 SRQSSGDTPEPPSG---TVYPASLLPQTAQPQSYVITSAGQQ---LSTGGFSDSGPPISQQVLQAPPSPQGFVQQPPPAQ 645
Cdd:PRK10927   91 SRQPGVRAPTEPSAggeVKTPEQLTPEQRQLLEQMQADMRQQptqLVEVPWNEQTPEQRQQTLQRQRQAQQLAEQQRLAQ 170
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907200786 646 MSVYYYPSGQYPTSTSQQyrplasvQYSAQRSQQIPQTTQQAGYQPVLsgqqgfqgmmgvQQSAHSQGVMSSQQGAPV 723
Cdd:PRK10927  171 QSRTTEQSWQQQTRTSQA-------APVQAQPRQSKPASTQQPYQDLL------------QTPAHTTAQSKPQQAAPV 229
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
559-696 1.19e-03

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 42.49  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786 559 REELAAQFSQLSM-SRQSSGDTPEPPSgtvYPASLLPQTAQPQSYvitsAGQQLstgGFSDSGPPISQQVLQAPPSPQGF 637
Cdd:TIGR01628 368 RAHLQDQFMQLQPrMRQLPMGSPMGGA---MGQPPYYGQGPQQQF----NGQPL---GWPRMSMMPTPMGPGGPLRPNGL 437
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200786 638 VQQPPPAQMSVYYYPSGQYPTSTSQQYRPLASVQYSAQRSQQIPQTTQQAGYQPVLSGQ 696
Cdd:TIGR01628 438 APMNAVRAPSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQV 496
SP1-4_arthropods_N cd22553
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ...
532-765 6.90e-03

N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in the chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. One SP is clade SP1-4, which is expressed ubiquitously throughout development. SP1-4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. This model represents the N-terminal domain of SP1-4 from arthropods.


Pssm-ID: 411778 [Multi-domain]  Cd Length: 384  Bit Score: 39.62  E-value: 6.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786 532 SQSVQYPAVSFPPQHLLPMSPTQHFPLREELAAQFSQLSMSRQSS--GDTPEPPSGTVYPASLLPQTAQP---QSYVITS 606
Cdd:cd22553    88 ANSGLLQTNNQQAIQLAPGGTQAILANQQTLIRPNTVQGQANASNvlQNIAQIASGGNAVQLPLNNMTQTipvQVPVSTA 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786 607 AGQ------QLSTGGFSDSGPPISQQVLQAPPSPQgfVQQPPPAQMSVYYYPSGQ-----YPTSTSQQyRPLASVQYSAQ 675
Cdd:cd22553   168 NGQtvyqtiQVPIQAIQSGNAGGGNQALQAQVIPQ--LAQAAQLQPQQLAQVSSQgyiqqIPANASQQ-QPQMVQQGPNQ 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786 676 RSQQIPQTTQQAGYQPVLSGQQGFQGMMGvqqsahSQGVMSSQQGAPVHGV----MVSYPTMSSYQVPMTQGSQAVPQQT 751
Cdd:cd22553   245 SGQIIGQVASASSIQAAAIPLTVYTGALA------GQNGSNQQQVGQIVTSpiqgMTQGLTAPASSSIPTVVQQQAIQGN 318
                         250
                  ....*....|....
gi 1907200786 752 YQPPIMLPSQAGQG 765
Cdd:cd22553   319 PLPPGTQIIAAGQQ 332
 
Name Accession Description Interval E-value
R3H_encore_like cd02642
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the ...
162-223 1.40e-25

R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the germline exit after four mitotic divisions, by facilitating SCF-ubiquitin-proteasome-dependent proteolysis. Maize DBF1-interactor protein 1 (DIP1) containing an R3H domain is a potential regulator of DBF1 activity in stress responses. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100071  Cd Length: 63  Bit Score: 99.98  E-value: 1.40e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907200786 162 DRMILLKMEQEMIDFIADSNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG-KSVIINKT 223
Cdd:cd02642     1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
146-223 7.85e-13

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 64.24  E-value: 7.85e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786  146 IDLHGFLINTLKNNSRDRMILLKMEQEMIDFIAdSNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG--KSVIINKT 223
Cdd:smart00393   1 ADFLPVTLDALSYRPRRREELIELELEIARFVK-STKESVELPPMNSYERKIVHELAEKYGLESESFGEGpkRRVVISKK 79
R3H cd02325
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most ...
166-222 3.50e-12

R3H domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. R3H domains are found in proteins together with ATPase domains, SF1 helicase domains, SF2 DEAH helicase domains, Cys-rich repeats, ring-type zinc fingers, and KH domains. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100064  Cd Length: 59  Bit Score: 61.86  E-value: 3.50e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200786 166 LLKMEQEMIDFIADSNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG--KSVIINK 222
Cdd:cd02325     1 REEREEELEAFAKDAAGKSLELPPMNSYERKLIHDLAEYYGLKSESEGEGpnRRVVITK 59
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ...
164-222 5.50e-12

R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.


Pssm-ID: 460206  Cd Length: 60  Bit Score: 61.35  E-value: 5.50e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907200786 164 MILLKMEQEMIDFIADSNNHYKkFPQMSSYQRMLVHRVAAYFGLDHNV--DQTGKSVIINK 222
Cdd:pfam01424   1 EFLEQLAEKLAEFVKDTGKSLE-LPPMSSYERRIIHELAQKYGLESESegEEPNRRVVVYK 60
SUZ pfam12752
SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched ...
244-298 6.38e-12

SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched in positively charged amino acids. It was first characterized in the C.elegans protein Szy-20 where it has been shown to bind RNA and allow their localization to the centrosome. Warning- the domain has a compositionally biased character.


Pssm-ID: 463689 [Multi-domain]  Cd Length: 56  Bit Score: 61.18  E-value: 6.38e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907200786 244 ESQKRFILKRDNSSIDKEDNQNRM-HPFRDDRRSKSIEEREEEYQRVRERIFAHDS 298
Cdd:pfam12752   1 PPPKMKILRRPSSGSSSSSSAGSSgASSSSGSDSKTLEEREAEYAEARARIFGSSE 56
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
568-797 1.19e-05

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 48.88  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786 568 QLSMSRQssgdtpEPPSGTVYPASLLPQTAQPQSYVITSAGQQLS----TG--GFSDSGPPISQQVLQA----PPSPQGF 637
Cdd:pfam09770  99 QVRFNRQ------QPAARAAQSSAQPPASSLPQYQYASQQSQQPSkpvrTGyeKYKEPEPIPDLQVDASlwgvAPKKAAA 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786 638 VQQPPPAQMSvyyypsgqyPTSTSQQYRPLASVQY--SAQRSQQIPQTTQQA-------GYQPVLSGQQGFQGMMGVQQS 708
Cdd:pfam09770 173 PAPAPQPAAQ---------PASLPAPSRKMMSLEEveAAMRAQAKKPAQQPApapaqppAAPPAQQAQQQQQFPPQIQQQ 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786 709 AHSQGVMSSQQGAPVHGVMVS---YPTMSSYQVPMTQGSQAVPQQTYQPP--IMLPSQAGQ--GSLPATGMPVYCNVTPP 781
Cdd:pfam09770 244 QQPQQQPQQPQQHPGQGHPVTilqRPQSPQPDPAQPSIQPQAQQFHQQPPpvPVQPTQILQnpNRLSAARVGYPQNPQPG 323
                         250
                  ....*....|....*.
gi 1907200786 782 NPQNNLRLMGPHCPSS 797
Cdd:pfam09770 324 VQPAPAHQAHRQQGSF 339
PRK10927 PRK10927
cell division protein FtsN;
572-723 5.62e-04

cell division protein FtsN;


Pssm-ID: 236797 [Multi-domain]  Cd Length: 319  Bit Score: 42.74  E-value: 5.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786 572 SRQSSGDTPEPPSG---TVYPASLLPQTAQPQSYVITSAGQQ---LSTGGFSDSGPPISQQVLQAPPSPQGFVQQPPPAQ 645
Cdd:PRK10927   91 SRQPGVRAPTEPSAggeVKTPEQLTPEQRQLLEQMQADMRQQptqLVEVPWNEQTPEQRQQTLQRQRQAQQLAEQQRLAQ 170
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907200786 646 MSVYYYPSGQYPTSTSQQyrplasvQYSAQRSQQIPQTTQQAGYQPVLsgqqgfqgmmgvQQSAHSQGVMSSQQGAPV 723
Cdd:PRK10927  171 QSRTTEQSWQQQTRTSQA-------APVQAQPRQSKPASTQQPYQDLL------------QTPAHTTAQSKPQQAAPV 229
PHA03247 PHA03247
large tegument protein UL36; Provisional
401-748 1.03e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786  401 SRTHPQSTALTSSVAAGSPGCMAYSENGMGGQVPPSSTSYILLPLESATGIPPGSillnphtgqpfVNPDGTPAIYNPPG 480
Cdd:PHA03247  2699 ADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGG-----------PARPARPPTTAGPP 2767
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786  481 SQQTLRGTVGGQPQQPPQQQPSPQPQQQVQASQPQMAGPlVTQSVQSLQPSSQSVQYPAVSFPPqhllpmsPTQHFPLRE 560
Cdd:PHA03247  2768 APAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPAD-PPAAVLAPAAALPPAASPAGPLPP-------PTSAQPTAP 2839
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786  561 ELAAQFSQlsmsrqssgdTPEPPSGTVYPASLLPQTAQPQSYVITSAgqqlstggfSDSGPPISQQVLQAPPSPQGFVQQ 640
Cdd:PHA03247  2840 PPPPGPPP----------PSLPLGGSVAPGGDVRRRPPSRSPAAKPA---------APARPPVRRLARPAVSRSTESFAL 2900
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786  641 PPPAQmsvyyypsgQYPTSTSQQYRPLASVQYSAQRSQQiPQTTQQAGYQPVLSGQQGFQGmmgvqQSAHSQGVMSSQQG 720
Cdd:PHA03247  2901 PPDQP---------ERPPQPQAPPPPQPQPQPPPPPQPQ-PPPPPPPRPQPPLAPTTDPAG-----AGEPSGAVPQPWLG 2965
                          330       340
                   ....*....|....*....|....*...
gi 1907200786  721 APVHGvmvsyptmsSYQVPMTQGSQAVP 748
Cdd:PHA03247  2966 ALVPG---------RVAVPRFRVPQPAP 2984
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
559-696 1.19e-03

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 42.49  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786 559 REELAAQFSQLSM-SRQSSGDTPEPPSgtvYPASLLPQTAQPQSYvitsAGQQLstgGFSDSGPPISQQVLQAPPSPQGF 637
Cdd:TIGR01628 368 RAHLQDQFMQLQPrMRQLPMGSPMGGA---MGQPPYYGQGPQQQF----NGQPL---GWPRMSMMPTPMGPGGPLRPNGL 437
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200786 638 VQQPPPAQMSVYYYPSGQYPTSTSQQYRPLASVQYSAQRSQQIPQTTQQAGYQPVLSGQ 696
Cdd:TIGR01628 438 APMNAVRAPSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQV 496
PRK10263 PRK10263
DNA translocase FtsK; Provisional
559-781 1.36e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.38  E-value: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786  559 REELAAQFSQLSMSR---QSSGDTPEPP--SGTVYPASLLPQTAQPQsyvitsagQQLSTGGFSDSGPPISQQVLQAPPS 633
Cdd:PRK10263   661 QDELARQFAQTQQQRygeQYQHDVPVNAedADAAAEAELARQFAQTQ--------QQRYSGEQPAGANPFSLDDFEFSPM 732
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786  634 pQGFVQQPPPAQMsvyyYPSGQYPTSTSQQyRPLASVQYSAQRSQQIPQTTQQAGYQPVLSGQQGFQGMMGVQQSAHSQG 713
Cdd:PRK10263   733 -KALLDDGPHEPL----FTPIVEPVQQPQQ-PVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQ 806
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786  714 VMSSQQGAPvhgvmvsyptmsSYQVPMtqgSQAVPQQTYQPPIMLPSQAGQGSL----------------PATGMPVYCN 777
Cdd:PRK10263   807 PQQPVAPQP------------QYQQPQ---QPVAPQPQYQQPQQPVAPQPQDTLlhpllmrngdsrplhkPTTPLPSLDL 871

                   ....
gi 1907200786  778 VTPP 781
Cdd:PRK10263   872 LTPP 875
PRK10263 PRK10263
DNA translocase FtsK; Provisional
545-741 2.22e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.61  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786  545 QHLLPMSPTQHFPLRE-ELAAQFSQLSMSRQSSgdtpEPPSGTvYPASLLPQTAQPQSYVITSAGQQLStggFSDSGPPI 623
Cdd:PRK10263   681 QHDVPVNAEDADAAAEaELARQFAQTQQQRYSG----EQPAGA-NPFSLDDFEFSPMKALLDDGPHEPL---FTPIVEPV 752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786  624 SQQVLQAPPSPQGFVQQPPPAQMSVYYYPsgQYPTSTSQQYR-PLASVQYSAQRSQ-QIPQTTQQAGYQPvlsgQQGFQG 701
Cdd:PRK10263   753 QQPQQPVAPQQQYQQPQQPVAPQPQYQQP--QQPVAPQPQYQqPQQPVAPQPQYQQpQQPVAPQPQYQQP----QQPVAP 826
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1907200786  702 MMGVQQsaHSQGVMSSQQGAPVHGVMVSYPTMSSYQVPMT 741
Cdd:PRK10263   827 QPQYQQ--PQQPVAPQPQDTLLHPLLMRNGDSRPLHKPTT 864
R3H_sperm-antigen cd02636
R3H domain of a group of metazoan proteins that is related to the sperm-associated antigen 7. ...
168-207 2.96e-03

R3H domain of a group of metazoan proteins that is related to the sperm-associated antigen 7. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100065  Cd Length: 61  Bit Score: 36.54  E-value: 2.96e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1907200786 168 KMEQEMIDFIADSNNHYKKFPQMSSYQRMLVHRVAAYFGL 207
Cdd:cd02636     3 SMEKEVSKFIKDSVRTREKFQPMDKVERSIVHDVAEVAGL 42
PRK10263 PRK10263
DNA translocase FtsK; Provisional
587-775 4.26e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.84  E-value: 4.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786  587 VYPASLLPQTAQPQSYVITSAGQQLSTGGFSDSGPPISQQVLQapPSPQGFVQQPPPAQMSVYYYPSGQYPTSTSQQYRP 666
Cdd:PRK10263   332 SWAAPVEPVTQTPPVASVDVPPAQPTVAWQPVPGPQTGEPVIA--PAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYA 409
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786  667 LASVQYSAQrsQQIPQTTQQAGYQPVLSGQqgfqgmmgVQQSAHSQGVMSSQQGaPVHGVMVSYPTMSSYQVPMTQGSQA 746
Cdd:PRK10263   410 PAAEQPAQQ--PYYAPAPEQPAQQPYYAPA--------PEQPVAGNAWQAEEQQ-STFAPQSTYQTEQTYQQPAAQEPLY 478
                          170       180
                   ....*....|....*....|....*....
gi 1907200786  747 VPQQTYQPPIMLPSQAGQGSLPATGMPVY 775
Cdd:PRK10263   479 QQPQPVEQQPVVEPEPVVEETKPARPPLY 507
R3H_Smubp-2_like cd02641
R3H domain of Smubp-2_like proteins. Smubp-2_like proteins also contain a helicase_like and ...
176-220 6.19e-03

R3H domain of Smubp-2_like proteins. Smubp-2_like proteins also contain a helicase_like and an AN1-like Zinc finger domain and have been shown to bind single-stranded DNA. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA.


Pssm-ID: 100070  Cd Length: 60  Bit Score: 35.79  E-value: 6.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1907200786 176 FIADSNNHYKKFP-QMSSYQRMLVHRVAAYFGLDHNVDQTGKSVII 220
Cdd:cd02641    11 FMKDPKATELEFPpTLSSHDRLLVHELAEELGLRHESTGEGSDRVI 56
SP1-4_arthropods_N cd22553
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ...
532-765 6.90e-03

N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in the chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. One SP is clade SP1-4, which is expressed ubiquitously throughout development. SP1-4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. This model represents the N-terminal domain of SP1-4 from arthropods.


Pssm-ID: 411778 [Multi-domain]  Cd Length: 384  Bit Score: 39.62  E-value: 6.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786 532 SQSVQYPAVSFPPQHLLPMSPTQHFPLREELAAQFSQLSMSRQSS--GDTPEPPSGTVYPASLLPQTAQP---QSYVITS 606
Cdd:cd22553    88 ANSGLLQTNNQQAIQLAPGGTQAILANQQTLIRPNTVQGQANASNvlQNIAQIASGGNAVQLPLNNMTQTipvQVPVSTA 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786 607 AGQ------QLSTGGFSDSGPPISQQVLQAPPSPQgfVQQPPPAQMSVYYYPSGQ-----YPTSTSQQyRPLASVQYSAQ 675
Cdd:cd22553   168 NGQtvyqtiQVPIQAIQSGNAGGGNQALQAQVIPQ--LAQAAQLQPQQLAQVSSQgyiqqIPANASQQ-QPQMVQQGPNQ 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200786 676 RSQQIPQTTQQAGYQPVLSGQQGFQGMMGvqqsahSQGVMSSQQGAPVHGV----MVSYPTMSSYQVPMTQGSQAVPQQT 751
Cdd:cd22553   245 SGQIIGQVASASSIQAAAIPLTVYTGALA------GQNGSNQQQVGQIVTSpiqgMTQGLTAPASSSIPTVVQQQAIQGN 318
                         250
                  ....*....|....
gi 1907200786 752 YQPPIMLPSQAGQG 765
Cdd:cd22553   319 PLPPGTQIIAAGQQ 332
 
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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