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Conserved domains on  [gi|33621227|gb|AAQ23182|]
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poly(ADP)-ribose polymerase [Aspergillus nidulans]

Protein Classification

BRCT domain-containing protein( domain architecture ID 10032660)

BRCT (BRCA1 C-terminus) domain-containing protein may interact with DNA, and participate in DNA-damage checkpoint or DNA-repair pathways

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 306-673 5.99e-165

Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active. Poly(ADP-ribose)-like polymerases (PARPS 1-3, VPARP, tankyrase) catalyze the addition of up to 100 ADP_ribose units from NAD+. PARPs 1 and 2 are localized in the nucleaus, bind DNA, and are activated by DNA damage. VPARP is part of the vault ribonucleoprotein complex. Tankyrases regulates telomere length through interactions with telomere repeat binding factor 1.


:

Pssm-ID: 238717 [Multi-domain]  Cd Length: 347  Bit Score: 476.76  E-value: 5.99e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227 306 SKLPAPVQNVISFIFNQKYFLETMAQMSYDANKLPLGKLSKRTLMAGYETLKELAELATKPSmamskygmQLRPAMEQLS 385
Cdd:cd01437   2 SKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGS--------SQGSQLEELS 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227 386 NRYFTTIPHVFGRNRPPVLDNQAYIKREIELLETLTDMEITNSILKDaSKMEDANPLDSQYAGLGMQeMTPLDHASEEFR 465
Cdd:cd01437  74 NEFYTLIPHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKD-DEDDSDDPLDANYEKLKCK-IEPLDKDSEEYK 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227 466 ELEKYLSGTRGSTHGVKYKVIDIFRIERQGEHDRFKSSSyaglKNSNRRLLWHGSRSTNYGGILSQGLRIAPPEAPVSGY 545
Cdd:cd01437 152 IIEKYLKNTHAPTTEYTVEVQEIFRVEREGETDRFKPFK----KLGNRKLLWHGSRLTNFVGILSQGLRIAPPEAPVTGY 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227 546 MFGKGVYFADMSSKSANYCWSHNSDHKALLLLGDVELGDpIYELYDSDYNAGEnaKKEGKIATLGKGRSIPAGWKDagci 625
Cdd:cd01437 228 MFGKGIYFADMFSKSANYCHASASDPTGLLLLCEVALGK-MNELKKADYMAKE--LPKGKHSVKGLGKTAPDPSEF---- 300

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 33621227 626 HPHLKGIQVPDADSGTTDHKTDqGYLLYNEYIVYDVAQIRLRYLFFVD 673
Cdd:cd01437 301 EIDLDGVVVPLGKPVPSGHKTD-TSLLYNEYIVYDVAQVRLKYLLEVK 347
WGR_PARP cd07997
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ...
 185-282 3.91e-38

WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins and histones. Higher eukaryotes contain several PARPs and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. Poly-ADP-ribosylation was thought to be a reversible post-translational covalent modification that serves as a regulatory mechanism for protein substrates. However, it is now known that it plays important roles in many cellular processes including maintenance of genomic stability, transcriptional regulation, energy metabolism, cell death and survival, among others.


:

Pssm-ID: 153426  Cd Length: 102  Bit Score: 136.67  E-value: 3.91e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227 185 DDSGLIWDATLNLTVSAANNNKFYLIQILNSKDGSRYQTWTRWGRVGERGQSVLLGDGTLDSAKKQFEKKFKDKSGLAWK 264
Cdd:cd07997   4 GDIATVYDATLNQTDISNNNNKFYKIQILESKGPNTYALFTRWGRVGERGQSQLTPFGSLESAIKEFEKKFKDKTGNEWE 83

                        90
                ....*....|....*....
gi 33621227 265 DRLNSPK-NNKYTFIERNY 282
Cdd:cd07997  84 NRPLFKKqPGKYALVELDY 102
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 52-96 2.61e-06

C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage.


:

Pssm-ID: 349339 [Multi-domain]  Cd Length: 68  Bit Score: 45.43  E-value: 2.61e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 33621227  52 LKAIVERHGATFTSSVGTDCTHLIATQKEADKKGAK--------LSLDWLLDS 96
Cdd:cd00027  16 LKKLIEALGGKVSESLSSKVTHLIAKSPSGEKYYLAalawgipiVSPEWLLDC 68
 
Name Accession Description Interval E-value
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 306-673 5.99e-165

Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active. Poly(ADP-ribose)-like polymerases (PARPS 1-3, VPARP, tankyrase) catalyze the addition of up to 100 ADP_ribose units from NAD+. PARPs 1 and 2 are localized in the nucleaus, bind DNA, and are activated by DNA damage. VPARP is part of the vault ribonucleoprotein complex. Tankyrases regulates telomere length through interactions with telomere repeat binding factor 1.


Pssm-ID: 238717 [Multi-domain]  Cd Length: 347  Bit Score: 476.76  E-value: 5.99e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227 306 SKLPAPVQNVISFIFNQKYFLETMAQMSYDANKLPLGKLSKRTLMAGYETLKELAELATKPSmamskygmQLRPAMEQLS 385
Cdd:cd01437   2 SKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGS--------SQGSQLEELS 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227 386 NRYFTTIPHVFGRNRPPVLDNQAYIKREIELLETLTDMEITNSILKDaSKMEDANPLDSQYAGLGMQeMTPLDHASEEFR 465
Cdd:cd01437  74 NEFYTLIPHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKD-DEDDSDDPLDANYEKLKCK-IEPLDKDSEEYK 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227 466 ELEKYLSGTRGSTHGVKYKVIDIFRIERQGEHDRFKSSSyaglKNSNRRLLWHGSRSTNYGGILSQGLRIAPPEAPVSGY 545
Cdd:cd01437 152 IIEKYLKNTHAPTTEYTVEVQEIFRVEREGETDRFKPFK----KLGNRKLLWHGSRLTNFVGILSQGLRIAPPEAPVTGY 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227 546 MFGKGVYFADMSSKSANYCWSHNSDHKALLLLGDVELGDpIYELYDSDYNAGEnaKKEGKIATLGKGRSIPAGWKDagci 625
Cdd:cd01437 228 MFGKGIYFADMFSKSANYCHASASDPTGLLLLCEVALGK-MNELKKADYMAKE--LPKGKHSVKGLGKTAPDPSEF---- 300

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 33621227 626 HPHLKGIQVPDADSGTTDHKTDqGYLLYNEYIVYDVAQIRLRYLFFVD 673
Cdd:cd01437 301 EIDLDGVVVPLGKPVPSGHKTD-TSLLYNEYIVYDVAQVRLKYLLEVK 347
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 124-673 1.46e-155

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 463.93  E-value: 1.46e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  124 AKSEKKRSAKAVQDTDDDRSNKKpKQIMEDAQMITAEKaaKVRVRVDEYY----HSNEHTWQVFIDdsglIWDATLNLTV 199
Cdd:PLN03124 113 LESDVKVGSANGTGEDEKEKGGD-EEREKEEKIVTATK--KGRAVLDQWLpdhiKSNYHVLEEGDD----VYDAMLNQTN 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  200 SAANNNKFYLIQILNSKDGSRYQTWTRWGRVGERGQSVLLGDG-TLDSAKKQFEKKFKDKSGLAWKDRLN-SPKNNKYTF 277
Cdd:PLN03124 186 VGDNNNKFYVLQVLESDDGSKYMVYTRWGRVGVKGQDKLHGPYdSREPAIREFEKKFYDKTKNHWSDRKNfISHPKKYTW 265

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  278 IERNYEesDDEDEKSDNKLVKQPSNIPASKLPAPVQNVISFIFNQKYFLETMAQMSYDANKLPLGKLSKRTLMAGYETLK 357
Cdd:PLN03124 266 LEMDYE--DEEESKKDKPSVSSEDKNKQSKLDPRVAQFISLICDVSMMKQQMMEIGYNARKLPLGKLSKSTILKGYEVLK 343

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  358 ELAElatkpsmAMSKYGmqlRPAMEQLSNRYFTTIPHVFGRN--RPPVLDNQAYIKREIELLETLTDMEITNSILKDASK 435
Cdd:PLN03124 344 RIAE-------VISRSD---RETLEELSGEFYTVIPHDFGFKkmRQFTIDTPQKLKHKLEMVEALGEIEIATKLLKDDIG 413

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  436 MEDaNPLDSQYAGLGMqEMTPLDHASEEFRELEKYLSGTRGSTH-GVKYKVIDIFRIERQGEHDRFKSSSyaglKNSNRR 514
Cdd:PLN03124 414 EQD-DPLYAHYKRLNC-ELEPLDTDSEEFSMIAKYLENTHGQTHsGYTLEIVQIFKVSREGEDERFQKFS----STKNRM 487

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  515 LLWHGSRSTNYGGILSQGLRIAPPEAPVSGYMFGKGVYFADMSSKSANYCWSHNSDHKALLLLGDVELGDpIYELYDSDY 594
Cdd:PLN03124 488 LLWHGSRLTNWTGILSQGLRIAPPEAPSTGYMFGKGVYFADMFSKSANYCYASAANPDGVLLLCEVALGD-MNELLQADY 566

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  595 NAgeNAKKEGKIATLGKGRSIP----AGWKDAGCIHPHLKGIQVPDAdsgttdhktdQGYLLYNEYIVYDVAQIRLRYLF 670
Cdd:PLN03124 567 NA--NKLPPGKLSTKGVGRTVPdpseAKTLEDGVVVPLGKPVESPYS----------KGSLEYNEYIVYNVDQIRMRYVL 634


                 ...
gi 33621227  671 FVD 673
Cdd:PLN03124 635 QVK 637
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 461-672 1.58e-82

Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.


Pssm-ID: 395519 [Multi-domain]  Cd Length: 195  Bit Score: 258.80  E-value: 1.58e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227   461 SEEFRELEKYLSGTRGSTHGVKYKVIDIFRIERQGEHDRFKSSSyaglKNSNRRLLWHGSRSTNYGGILSQGLRIAPPEA 540
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDPTHGYPLFILEIFRVQRDGEWERFQPKK----KLRNRRLLWHGSRLTNFLGILSQGLRIAPPEA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227   541 PVSGYMFGKGVYFADMSSKSANYCWSHNSDHKALLLLGDVELGDpIYELYDSDYnagENAKKEGKIATLGKGRSIPagwk 620
Cdd:pfam00644  77 PVTGYMFGKGIYFADDASKSANYCPPSEAHGNGLMLLSEVALGD-MNELKKADY---AEKLPPGKHSVKGLGKTAP---- 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 33621227   621 dagCIHPHLKGiqVPDADSGTTDHKTDQgyLLYNEYIVYDVAQIRLRYLFFV 672
Cdd:pfam00644 149 ---ESFVDLDG--VPLGKLVATGYDSSV--LLYNEYVVYNVNQVRPKYLLEV 193
WGR_PARP cd07997
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ...
 185-282 3.91e-38

WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins and histones. Higher eukaryotes contain several PARPs and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. Poly-ADP-ribosylation was thought to be a reversible post-translational covalent modification that serves as a regulatory mechanism for protein substrates. However, it is now known that it plays important roles in many cellular processes including maintenance of genomic stability, transcriptional regulation, energy metabolism, cell death and survival, among others.


Pssm-ID: 153426  Cd Length: 102  Bit Score: 136.67  E-value: 3.91e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227 185 DDSGLIWDATLNLTVSAANNNKFYLIQILNSKDGSRYQTWTRWGRVGERGQSVLLGDGTLDSAKKQFEKKFKDKSGLAWK 264
Cdd:cd07997   4 GDIATVYDATLNQTDISNNNNKFYKIQILESKGPNTYALFTRWGRVGERGQSQLTPFGSLESAIKEFEKKFKDKTGNEWE 83

                        90
                ....*....|....*....
gi 33621227 265 DRLNSPK-NNKYTFIERNY 282
Cdd:cd07997  84 NRPLFKKqPGKYALVELDY 102
WGR smart00773
Proposed nucleic acid binding domain; This domain is named after its most conserved central ...
 186-270 1.56e-27

Proposed nucleic acid binding domain; This domain is named after its most conserved central motif. It is found in a variety of polyA polymerases as well as in molybdate metabolism regulators (e.g. in E.coli) and other proteins of unknown function. The domain is found in isolation in some proteins and is between 70 and 80 residues in length. It is proposed that it may be a nucleic acid binding domain.


Pssm-ID: 214814  Cd Length: 84  Bit Score: 106.22  E-value: 1.56e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227    186 DSGLIWDATLNLTVSAANNNKFYLIQILNSkDGSRYQTWTRWGRVGERGQSVLLGDGTLDSAKKQFEKKFKDKSGLAWKD 265
Cdd:smart00773   1 EGGEIYDVYLNFTDLASNNNKFYIIQLLED-DFGGYSVYRRWGRIGTKGQTKLKTFDSLEDAIKEFEKLFKEKTKNGYEE 79


                   ....*
gi 33621227    266 RLNSP 270
Cdd:smart00773  80 RGKFV 84
WGR pfam05406
WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli ...
 191-270 5.33e-24

WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli molybdate metabolism regulator Swiss:P33345 and other proteins of unknown function. I have called this domain WGR after the most conserved central motif of the domain. The domain is found in isolation in proteins such as Swiss:Q9JN21 and is between 70 and 80 residues in length. I propose that this may be a nucleic acid binding domain.


Pssm-ID: 398851  Cd Length: 79  Bit Score: 95.77  E-value: 5.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227   191 WDATLNLTVSAANNNKFYLIQILNsKDGSRYQTWTRWGRVGERGQSVLLGDGTLDSAKKQFEKKFKDKSGLAWKDRLNSP 270
Cdd:pfam05406   1 YDLYLEQTDAARNSNKFYEIQVED-DLFGGYSLFRRWGRIGTRGQTKLKSFDSLEEAIKEFEKLFAEKTKKGYRERGEFE 79
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 52-96 2.61e-06

C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage.


Pssm-ID: 349339 [Multi-domain]  Cd Length: 68  Bit Score: 45.43  E-value: 2.61e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 33621227  52 LKAIVERHGATFTSSVGTDCTHLIATQKEADKKGAK--------LSLDWLLDS 96
Cdd:cd00027  16 LKKLIEALGGKVSESLSSKVTHLIAKSPSGEKYYLAalawgipiVSPEWLLDC 68
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 28-96 1.60e-05

BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 43.44  E-value: 1.60e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33621227    28 DVQFLIEFFKSTTREltrhsyagDLKAIVERHGATFTSSVGTDCTHLIATQ-----KEADKKGAK-LSLDWLLDS 96
Cdd:pfam00533   8 GKTFVITGLDGLERD--------ELKELIEKLGGKVTDSLSKKTTHVIVEArtkkyLKAKELGIPiVTEEWLLDC 74
BRCT smart00292
breast cancer carboxy-terminal domain;
3-96 4.53e-04

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 39.28  E-value: 4.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227      3 PKLFKKLVIAVSGTFPGYRqgrnfcdvqflieffksttREltrhsyagDLKAIVERHGATFTSSV-GTDCTHLIATQKEA 81
Cdd:smart00292   1 PKLFKGKTFYITGSFDKEE-------------------RD--------ELKELIEALGGKVTSSLsSKTTTHVIVGSPEG 53

                           90       100
                   ....*....|....*....|....
gi 33621227     82 DKKGAKLSL---------DWLLDS 96
Cdd:smart00292  54 GKLELLKAIalgipivkeEWLLDC 77
WGR COG3831
WGR domain, predicted DNA-binding domain in MolR [Transcription];
195-258 3.19e-03

WGR domain, predicted DNA-binding domain in MolR [Transcription];


Pssm-ID: 443043  Cd Length: 83  Bit Score: 36.89  E-value: 3.19e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33621227 195 LNLTVSAANNNKFYLIQILNSKDGsryqTWT---RWGRVGERGQSVLLGDGTLDSAKKQFEKKFKDK 258
Cdd:COG3831   5 LERIDPAGNSARFYELEVEPDLFG----GWSltrRWGRIGTKGQTKTKTFASEEEALAALEKLVAEK 67
 
Name Accession Description Interval E-value
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 306-673 5.99e-165

Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active. Poly(ADP-ribose)-like polymerases (PARPS 1-3, VPARP, tankyrase) catalyze the addition of up to 100 ADP_ribose units from NAD+. PARPs 1 and 2 are localized in the nucleaus, bind DNA, and are activated by DNA damage. VPARP is part of the vault ribonucleoprotein complex. Tankyrases regulates telomere length through interactions with telomere repeat binding factor 1.


Pssm-ID: 238717 [Multi-domain]  Cd Length: 347  Bit Score: 476.76  E-value: 5.99e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227 306 SKLPAPVQNVISFIFNQKYFLETMAQMSYDANKLPLGKLSKRTLMAGYETLKELAELATKPSmamskygmQLRPAMEQLS 385
Cdd:cd01437   2 SKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGS--------SQGSQLEELS 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227 386 NRYFTTIPHVFGRNRPPVLDNQAYIKREIELLETLTDMEITNSILKDaSKMEDANPLDSQYAGLGMQeMTPLDHASEEFR 465
Cdd:cd01437  74 NEFYTLIPHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKD-DEDDSDDPLDANYEKLKCK-IEPLDKDSEEYK 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227 466 ELEKYLSGTRGSTHGVKYKVIDIFRIERQGEHDRFKSSSyaglKNSNRRLLWHGSRSTNYGGILSQGLRIAPPEAPVSGY 545
Cdd:cd01437 152 IIEKYLKNTHAPTTEYTVEVQEIFRVEREGETDRFKPFK----KLGNRKLLWHGSRLTNFVGILSQGLRIAPPEAPVTGY 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227 546 MFGKGVYFADMSSKSANYCWSHNSDHKALLLLGDVELGDpIYELYDSDYNAGEnaKKEGKIATLGKGRSIPAGWKDagci 625
Cdd:cd01437 228 MFGKGIYFADMFSKSANYCHASASDPTGLLLLCEVALGK-MNELKKADYMAKE--LPKGKHSVKGLGKTAPDPSEF---- 300

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 33621227 626 HPHLKGIQVPDADSGTTDHKTDqGYLLYNEYIVYDVAQIRLRYLFFVD 673
Cdd:cd01437 301 EIDLDGVVVPLGKPVPSGHKTD-TSLLYNEYIVYDVAQVRLKYLLEVK 347
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 124-673 1.46e-155

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 463.93  E-value: 1.46e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  124 AKSEKKRSAKAVQDTDDDRSNKKpKQIMEDAQMITAEKaaKVRVRVDEYY----HSNEHTWQVFIDdsglIWDATLNLTV 199
Cdd:PLN03124 113 LESDVKVGSANGTGEDEKEKGGD-EEREKEEKIVTATK--KGRAVLDQWLpdhiKSNYHVLEEGDD----VYDAMLNQTN 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  200 SAANNNKFYLIQILNSKDGSRYQTWTRWGRVGERGQSVLLGDG-TLDSAKKQFEKKFKDKSGLAWKDRLN-SPKNNKYTF 277
Cdd:PLN03124 186 VGDNNNKFYVLQVLESDDGSKYMVYTRWGRVGVKGQDKLHGPYdSREPAIREFEKKFYDKTKNHWSDRKNfISHPKKYTW 265

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  278 IERNYEesDDEDEKSDNKLVKQPSNIPASKLPAPVQNVISFIFNQKYFLETMAQMSYDANKLPLGKLSKRTLMAGYETLK 357
Cdd:PLN03124 266 LEMDYE--DEEESKKDKPSVSSEDKNKQSKLDPRVAQFISLICDVSMMKQQMMEIGYNARKLPLGKLSKSTILKGYEVLK 343

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  358 ELAElatkpsmAMSKYGmqlRPAMEQLSNRYFTTIPHVFGRN--RPPVLDNQAYIKREIELLETLTDMEITNSILKDASK 435
Cdd:PLN03124 344 RIAE-------VISRSD---RETLEELSGEFYTVIPHDFGFKkmRQFTIDTPQKLKHKLEMVEALGEIEIATKLLKDDIG 413

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  436 MEDaNPLDSQYAGLGMqEMTPLDHASEEFRELEKYLSGTRGSTH-GVKYKVIDIFRIERQGEHDRFKSSSyaglKNSNRR 514
Cdd:PLN03124 414 EQD-DPLYAHYKRLNC-ELEPLDTDSEEFSMIAKYLENTHGQTHsGYTLEIVQIFKVSREGEDERFQKFS----STKNRM 487

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  515 LLWHGSRSTNYGGILSQGLRIAPPEAPVSGYMFGKGVYFADMSSKSANYCWSHNSDHKALLLLGDVELGDpIYELYDSDY 594
Cdd:PLN03124 488 LLWHGSRLTNWTGILSQGLRIAPPEAPSTGYMFGKGVYFADMFSKSANYCYASAANPDGVLLLCEVALGD-MNELLQADY 566

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  595 NAgeNAKKEGKIATLGKGRSIP----AGWKDAGCIHPHLKGIQVPDAdsgttdhktdQGYLLYNEYIVYDVAQIRLRYLF 670
Cdd:PLN03124 567 NA--NKLPPGKLSTKGVGRTVPdpseAKTLEDGVVVPLGKPVESPYS----------KGSLEYNEYIVYNVDQIRMRYVL 634


                 ...
gi 33621227  671 FVD 673
Cdd:PLN03124 635 QVK 637
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
 184-672 1.07e-89

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 300.55  E-value: 1.07e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  184 IDDSGLIWDATLNLTVSAANNNKFYLIQILNSKDGSRYQTWTRWGRVG-ERGQSVLLGDGTLDSAKKQFEKKFKDKSG-- 260
Cdd:PLN03123 513 LEDGKSIYNTTLNMSDLSTGVNSYYILQIIEEDKGSDCYVFRKWGRVGnEKIGGNKLEEMSKSDAIHEFKRLFLEKTGnp 592

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  261 -LAWKDRLNSPKN-NKYTFIERNYeesddedeKSDNKLVKQPSNIPASKLPAPVQNVISFIFNQKYFLETMAQMSYDANK 338
Cdd:PLN03123 593 wESWEQKTNFQKQpGKFYPLDIDY--------GVNEQPKKKAASGSKSNLAPRLVELMKMLFDVETYRAAMMEFEINMSE 664

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  339 LPLGKLSKRTLMAGYETLKELAELATKPSMAmskygmqlrPAMEQL-----SNRYFTTIPHVfgrnRPPVLDNQAYIKRE 413
Cdd:PLN03123 665 MPLGKLSKANIQKGFEALTEIQNLLKENDQD---------PSIRESllvdaSNRFFTLIPSI----HPHIIRDEDDLKSK 731

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  414 IELLETLTDMEITNSILKDASKMEDanPLDSQYAGLGMqEMTPLDHASEEFRELEKYLSGTRGSTH-GVKYKVIDIFRIE 492
Cdd:PLN03123 732 VKMLEALQDIEIASRLVGFDVDEDD--SLDDKYKKLHC-DISPLPHDSEDYKLIEKYLLTTHAPTHtDWSLELEEVFSLE 808

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  493 RQGEHDRfksssYAGLKNS--NRRLLWHGSRSTNYGGILSQGLRIAPPEAPVSGYMFGKGVYFADMSSKSANYCWSHNSD 570
Cdd:PLN03123 809 REGEFDK-----YAPYKEKlkNRMLLWHGSRLTNFVGILSQGLRIAPPEAPATGYMFGKGVYFADLVSKSAQYCYTDRKN 883

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  571 HKALLLLGDVELGDpIYELYDSDYnagENAKKEGKIATLGKGRSIP-----AGWKDagcihphlkGIQVPDADSGTTDHK 645
Cdd:PLN03123 884 PVGLMLLSEVALGE-IYELKKAKY---MDKPPRGKHSTKGLGKTVPqesefVKWRD---------DVVVPCGKPVPSKVK 950

                        490       500
                 ....*....|....*....|....*..
gi 33621227  646 TDQgyLLYNEYIVYDVAQIRLRYLFFV 672
Cdd:PLN03123 951 ASE--LMYNEYIVYNTAQVKLQFLLKV 975
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 461-672 1.58e-82

Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.


Pssm-ID: 395519 [Multi-domain]  Cd Length: 195  Bit Score: 258.80  E-value: 1.58e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227   461 SEEFRELEKYLSGTRGSTHGVKYKVIDIFRIERQGEHDRFKSSSyaglKNSNRRLLWHGSRSTNYGGILSQGLRIAPPEA 540
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDPTHGYPLFILEIFRVQRDGEWERFQPKK----KLRNRRLLWHGSRLTNFLGILSQGLRIAPPEA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227   541 PVSGYMFGKGVYFADMSSKSANYCWSHNSDHKALLLLGDVELGDpIYELYDSDYnagENAKKEGKIATLGKGRSIPagwk 620
Cdd:pfam00644  77 PVTGYMFGKGIYFADDASKSANYCPPSEAHGNGLMLLSEVALGD-MNELKKADY---AEKLPPGKHSVKGLGKTAP---- 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 33621227   621 dagCIHPHLKGiqVPDADSGTTDHKTDQgyLLYNEYIVYDVAQIRLRYLFFV 672
Cdd:pfam00644 149 ---ESFVDLDG--VPLGKLVATGYDSSV--LLYNEYVVYNVNQVRPKYLLEV 193
PARP_reg pfam02877
Poly(ADP-ribose) polymerase, regulatory domain; Poly(ADP-ribose) polymerase catalyzes the ...
 306-446 1.78e-61

Poly(ADP-ribose) polymerase, regulatory domain; Poly(ADP-ribose) polymerase catalyzes the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.


Pssm-ID: 460732 [Multi-domain]  Cd Length: 135  Bit Score: 201.21  E-value: 1.78e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227   306 SKLPAPVQNVISFIFNQKYFLETMAQMSYDANKLPLGKLSKRTLMAGYETLKELAELATKPSMAmskygmQLRPAMEQLS 385
Cdd:pfam02877   1 SKLPPPVQELMKLIFNVEMMKKAMKEMKYDAKKMPLGKLSKRQIKKGYEVLKELSELLKKPSLA------KAKAKLEDLS 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 33621227   386 NRYFTTIPHVFGRNRPPVLDNQAYIKREIELLETLTDMEITNSILKDASKMEDANPLDSQY 446
Cdd:pfam02877  75 NRFYTLIPHDFGRNRPPVIDTEEELKEKLELLEALLDIEVASKLLKDSKSDDDEHPLDRHY 135
PLN03122 PLN03122
Poly [ADP-ribose] polymerase; Provisional
 43-669 5.01e-41

Poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 178669 [Multi-domain]  Cd Length: 815  Bit Score: 160.35  E-value: 5.01e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227   43 LTRHSYAgdLKAIVERHGATFTSSV-GTDCthLIATQKEADKKG-AKL-----------SLDWLLDSDKAKKPVSEAPYR 109
Cdd:PLN03122 201 LSRTHQY--WKKDIEKHGGKVANSVeGVTC--LVVSPAERERGGsSKIaeamergipvvREAWLIDSIEKQEAQPLEAYD 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  110 FGAShsnrnsqadpAKSEKKRSAKAVQDTDDdrsnkkpkqimEDAQMITAE--KAAKVRVRVDEyyHSNEHTWQVFIDDs 187
Cdd:PLN03122 277 VVSD----------LSVEGRGIPWDKQDPSE-----------EAIESLSAElkLYGKRGVYKDS--KLQEEGGKIFEKD- 332

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  188 GLIWDATLNLTVSAANNNKFYLIQILNSKDGSRYQTWTRwGRVGER--GQSVLLGDGTLDSAKKQFEKKFKDKSG---LA 262
Cdd:PLN03122 333 GILYNCAFSICDLGRGLNEYCIMQLITVPDSNLHLYYKK-GRVGDDpnAEERLEEWEDVDAAIKEFVRLFEEITGnefEP 411

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  263 W-KDRLNSPKNNKYTFIERNyeesDDEDEKSDNKLVKQPSNIPA-SKLPAPVQNVISFIFNQKYFLETMAQMSYDANKLP 340
Cdd:PLN03122 412 WeREKKFEKKRLKFYPIDMD----DGVDVRAGGLGLRQLGVAAAhCKLDPKVANFMKVLCSQEIYRYAMMEMGLDSPDLP 487

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  341 LGKLSKRTLMAGYETLKELAELATKPSMAMSKYgmqlrPAM-EQLSNRYFTTIPhvfgRNRPPVLDNQAYIKREI-ELLE 418
Cdd:PLN03122 488 MGMLSDFHLKRCEEVLLEFAEFVKSEKETGQKA-----EAMwLDFSNKWFSLVH----STRPFVIRDIDELADHAaSALE 558

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  419 TLTDMEITNSILKD--ASKMEDanPLDSQYAGLGMQeMTPLDHASEEFRELEKYLSGTrgsTHGVKYKVID-------IF 489
Cdd:PLN03122 559 TVRDINVASRLIGDmtGSTLDD--PLSDRYKKLGCS-ISPVDKESDDYKMIVKYLEKT---YEPVKVGDVSysvsvenIF 632

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  490 RIERQG--EHDRFKsssyaglKNSNRRLLWHGSRSTNYGGILSQGLRIAPPEAPVSGYMFGKGVYFADMSSKSANYCWSH 567
Cdd:PLN03122 633 AVESSAgpSLDEIK-------KLPNKVLLWCGTRSSNLLRHLAKGFLPAVCSLPVPGYMFGKAIVCSDAAAEAARYGFTA 705

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  568 NSDHKALLLLGDVELGDPIYELYDSDYNAGENAKKEGKIATLGKGRSIPAG---WKDagcihphlkGIQVPDADSGTTDH 644
Cdd:PLN03122 706 VDRPEGFLVLAVASLGDEVLELTKPPEDVKSYEEKKVGVKGLGRKKTDESEhfkWRD---------DITVPCGRLIPSEH 776

                        650       660
                 ....*....|....*....|....*
gi 33621227  645 KtdQGYLLYNEYIVYDVAQIRLRYL 669
Cdd:PLN03122 777 K--DSPLEYNEYAVYDPKQVSIRFL 799
WGR_PARP cd07997
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ...
 185-282 3.91e-38

WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins and histones. Higher eukaryotes contain several PARPs and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. Poly-ADP-ribosylation was thought to be a reversible post-translational covalent modification that serves as a regulatory mechanism for protein substrates. However, it is now known that it plays important roles in many cellular processes including maintenance of genomic stability, transcriptional regulation, energy metabolism, cell death and survival, among others.


Pssm-ID: 153426  Cd Length: 102  Bit Score: 136.67  E-value: 3.91e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227 185 DDSGLIWDATLNLTVSAANNNKFYLIQILNSKDGSRYQTWTRWGRVGERGQSVLLGDGTLDSAKKQFEKKFKDKSGLAWK 264
Cdd:cd07997   4 GDIATVYDATLNQTDISNNNNKFYKIQILESKGPNTYALFTRWGRVGERGQSQLTPFGSLESAIKEFEKKFKDKTGNEWE 83

                        90
                ....*....|....*....
gi 33621227 265 DRLNSPK-NNKYTFIERNY 282
Cdd:cd07997  84 NRPLFKKqPGKYALVELDY 102
WGR_PARP2_like cd08003
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ...
 190-282 1.43e-29

WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins. Higher eukaryotes contain several PARPs and and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. This subfamily is composed of human PARP-2 and similar proteins. Similar to PARP-1, PARP-2 is ubiquitously expressed and its activity is induced by DNA strand breaks. It also plays a role in cell differentiation, cell death, and maintaining genomic stability. Studies on mice deficient with PARP-2 shows that it is important in fat storage, T cell maturation, and spermatogenesis.


Pssm-ID: 153430  Cd Length: 103  Bit Score: 112.81  E-value: 1.43e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227 190 IWDATLNLTVSAANNNKFYLIQILNSKDGSRYQTWTRWGRVGERGQSVLLGDGT-LDSAKKQFEKKFKDKSGLAWKDRLN 268
Cdd:cd08003   9 VYDAMLNQTNIQQNNNKYYIIQLLEDDAEKIYSVWFRWGRVGKKGQSSLVPCGSdLEQAKSLFEKKFLDKTKNEWEDRAN 88

                        90
                ....*....|....*
gi 33621227 269 -SPKNNKYTFIERNY 282
Cdd:cd08003  89 fEKVAGKYDLLEMDY 103
WGR_PARP3_like cd08002
WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins; The WGR domain is found in a ...
 191-282 3.16e-28

WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins. Higher eukaryotes contain several PARPs and and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. This subfamily is composed of human PARP-3 and similar proteins, including Arabidopsis thaliana PARP-2. PARP-3 displays a tissue-specific expression, with highest amounts found in the nuclei of epithelial cells of prostate ducts, salivary glands, liver, pancreas, and in the neurons of terminal ganglia. Unlike PARP-1 and PARP-2, PARP-3 activity is not induced by DNA strand breaks. However, it co-localizes with Polycomb group bodies and is part of complexes making up DNA-PKcs, DNA ligases III and IV, Ku70, and Ku80. PARP-3 is a nuclear protein that may be involved in transcriptional control and responses to DNA damage.


Pssm-ID: 153429  Cd Length: 100  Bit Score: 108.65  E-value: 3.16e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227 191 WDATLNLTVSAANNNKFYLIQILNSkdGSRYQTWTRWGRVGERGQSVLLGD-GTLDSAKKQFEKKFKDKSGLAWKDRLN- 268
Cdd:cd08002   9 YDCMLNQTNIGHNNNKFYVIQLLES--GKEYYVWNRWGRVGEKGQNKLKGPwDSLEGAIKDFEKKFKDKTKNNWEDRENf 86

                        90
                ....*....|....
gi 33621227 269 SPKNNKYTFIERNY 282
Cdd:cd08002  87 VPHPGKYTLIEMDY 100
WGR smart00773
Proposed nucleic acid binding domain; This domain is named after its most conserved central ...
 186-270 1.56e-27

Proposed nucleic acid binding domain; This domain is named after its most conserved central motif. It is found in a variety of polyA polymerases as well as in molybdate metabolism regulators (e.g. in E.coli) and other proteins of unknown function. The domain is found in isolation in some proteins and is between 70 and 80 residues in length. It is proposed that it may be a nucleic acid binding domain.


Pssm-ID: 214814  Cd Length: 84  Bit Score: 106.22  E-value: 1.56e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227    186 DSGLIWDATLNLTVSAANNNKFYLIQILNSkDGSRYQTWTRWGRVGERGQSVLLGDGTLDSAKKQFEKKFKDKSGLAWKD 265
Cdd:smart00773   1 EGGEIYDVYLNFTDLASNNNKFYIIQLLED-DFGGYSVYRRWGRIGTKGQTKLKTFDSLEDAIKEFEKLFKEKTKNGYEE 79


                   ....*
gi 33621227    266 RLNSP 270
Cdd:smart00773  80 RGKFV 84
WGR pfam05406
WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli ...
 191-270 5.33e-24

WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli molybdate metabolism regulator Swiss:P33345 and other proteins of unknown function. I have called this domain WGR after the most conserved central motif of the domain. The domain is found in isolation in proteins such as Swiss:Q9JN21 and is between 70 and 80 residues in length. I propose that this may be a nucleic acid binding domain.


Pssm-ID: 398851  Cd Length: 79  Bit Score: 95.77  E-value: 5.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227   191 WDATLNLTVSAANNNKFYLIQILNsKDGSRYQTWTRWGRVGERGQSVLLGDGTLDSAKKQFEKKFKDKSGLAWKDRLNSP 270
Cdd:pfam05406   1 YDLYLEQTDAARNSNKFYEIQVED-DLFGGYSLFRRWGRIGTRGQTKLKSFDSLEEAIKEFEKLFAEKTKKGYRERGEFE 79
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 516-572 2.72e-14

ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. Bacterial toxins are cytoplasmic and catalyze the transfer of a single ADP_ribose unit to eukaryotic elongation factor 2, halting protein synthesis and killing the cell. Poly(ADP-ribose) polymerases (PARPS 1-3, VPARP, tankyrase) catalyze the addition of up to 100 ADP_ribose units from NAD+. PARPs 1 and 2 are localized in the nucleaus, bind DNA, and are activated by DNA damage. VPARP is part of the vault ribonucleoprotein complex. Tankyrases regulates telomere length in part through poy(ADP_ribosylation) of telomere repeat binding factor 1 (TRF1). Poly(ADP-ribose) polymerase catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.


Pssm-ID: 238651 [Multi-domain]  Cd Length: 137  Bit Score: 70.28  E-value: 2.72e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 33621227 516 LWHGSRSTNYGGILSQGLRIAPPEAPVSGYMFGKGVYFADMSSKSANYCWSHNSDHK 572
Cdd:cd01341   2 LFHGSPPGNVISILKLGLRPASYGVLLNGGMFGKGIYSAPNISKSNGYSVGCDGQHV 58
WGR_PARP1_like cd08001
WGR domain of poly(ADP-ribose) polymerase 1 and similar proteins; The WGR domain is found in a ...
 185-271 5.05e-10

WGR domain of poly(ADP-ribose) polymerase 1 and similar proteins; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins. Higher eukaryotes contain several PARPs and and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. This subfamily is composed of vertebrate PARP-1 and similar proteins, including Arabidopsis thaliana PARP-1 and PARP-3. PARP-1 is the best-studied among the PARPs. It is a widely expressed nuclear chromatin-associated enzyme that possesses auto-mono-ADP-ribosylation (initiation), elongation, and branching activities. PARP-1 is implicated in DNA damage and cell death pathways and is important in maintaining genomic stability and regulating cell proliferation, differentiation, neuronal function, inflammation, and aging.


Pssm-ID: 153428 [Multi-domain]  Cd Length: 104  Bit Score: 56.83  E-value: 5.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227 185 DDSGLIWDATLNLTVSAANNNKFYLIQILNSKDGSRYQTWTRWGRVG-ERGQSVLLGDGTLDSAKKQFEKKFKDKSGLAW 263
Cdd:cd08001   5 EEGGNLYSAVLGLVDIQTGTNSYYKLQLLEHDKGNRYWVFRSWGRVGtTIGGNKLEEFSSLEEAKMAFEELYEEKTGNDF 84


                ....*...
gi 33621227 264 KDRLNSPK 271
Cdd:cd08001  85 ENRKNFKK 92
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 52-96 2.61e-06

C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage.


Pssm-ID: 349339 [Multi-domain]  Cd Length: 68  Bit Score: 45.43  E-value: 2.61e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 33621227  52 LKAIVERHGATFTSSVGTDCTHLIATQKEADKKGAK--------LSLDWLLDS 96
Cdd:cd00027  16 LKKLIEALGGKVSESLSSKVTHLIAKSPSGEKYYLAalawgipiVSPEWLLDC 68
BRCT_Rev1 cd17719
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ...
 51-109 4.05e-06

BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha integrin-binding protein 80, or AIBP80, or Rev1-like terminal deoxycytidyl transferase, is a DNA template-dependent dCMP transferase required for mutagenesis induced by UV light.


Pssm-ID: 349351 [Multi-domain]  Cd Length: 87  Bit Score: 45.25  E-value: 4.05e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33621227  51 DLKAIVERHGATFTSSV-GTDCTHLIATQKeADKKGAKLSL---------DWLLDSDKAKKPVSEAPYR 109
Cdd:cd17719  19 ELKRLILLHGGQYEHYYsRSRVTHIIATNL-PGSKIKKLKKarnykvvrpEWIVDSIKAGRLLPEAPYL 86
BRCT_PAXIP1_rpt2 cd17710
second BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 52-105 4.35e-06

second BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the second BRCT domain.


Pssm-ID: 349342 [Multi-domain]  Cd Length: 81  Bit Score: 44.91  E-value: 4.35e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33621227  52 LKAIVERHGATFTSSVGTDCTHLIATQKEADK-----KGAKLSL---DWLLDSDKAKKPVSE 105
Cdd:cd17710  20 LWAMVTFHGGKCQLNLDKKCTHLVTGKASGAKyecalKHEGIKIvtpDWVTDCIKAKTLLDE 81
BRCT_TopBP1_rpt2_like cd17731
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 4-100 6.50e-06

second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the second BRCT domain.


Pssm-ID: 349363 [Multi-domain]  Cd Length: 77  Bit Score: 44.45  E-value: 6.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227   4 KLFKKLVIAVSGtfpgyrqgrnfcdvqfliefFKSTTREltrhsyagDLKAIVERHGATFTSSVGTDCTHLIATQKEADK 83
Cdd:cd17731   1 PPFKGLVICVTG--------------------FDSEERK--------EIQQLVEQNGGSYSPDLSKNCTHLIAGSPSGQK 52

                        90       100
                ....*....|....*....|....*
gi 33621227  84 -KGAK-------LSLDWLLDSDKAK 100
Cdd:cd17731  53 yEFARkwnsihiVTPEWLYDSIEAG 77
BRCT_PARP1 cd17747
BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2. ...
 50-98 1.45e-05

BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2.30), also termed ADP-ribosyltransferase diphtheria toxin-like 1 (ARTD1), or NAD(+) ADP-ribosyltransferase 1 (ADPRT 1), or poly[ADP-ribose] synthase 1, is involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism.


Pssm-ID: 349378 [Multi-domain]  Cd Length: 76  Bit Score: 43.29  E-value: 1.45e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227  50 GDLKAIVERHGATFTSSVGTDCTHLIATQKEADKKGAKL-----------SLDWLLDSDK 98
Cdd:cd17747  17 DELKKLIEKLGGKVASKVTKKVTLCISTKAEVEKMSKKMkeakeagvpvvSEDFLEDCIK 76
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 28-96 1.60e-05

BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 43.44  E-value: 1.60e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33621227    28 DVQFLIEFFKSTTREltrhsyagDLKAIVERHGATFTSSVGTDCTHLIATQ-----KEADKKGAK-LSLDWLLDS 96
Cdd:pfam00533   8 GKTFVITGLDGLERD--------ELKELIEKLGGKVTDSLSKKTTHVIVEArtkkyLKAKELGIPiVTEEWLLDC 74
BRCT_XRCC1_rpt1 cd17725
First (central) BRCT domain in X-ray repair cross-complementing protein 1 (XRCC1) and similar ...
 60-108 5.51e-05

First (central) BRCT domain in X-ray repair cross-complementing protein 1 (XRCC1) and similar proteins; XRCC1 is a DNA repair protein that corrects defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents. It forms homodimers and interacts with polynucleotide kinase (PNK), DNA polymerase-beta (POLB), DNA ligase III (LIG3), APTX, APLF, and APEX1. XRCC1 contains an N-terminal XRCC1-specific domain and two BRCT domains. This family corresponds to the first one.


Pssm-ID: 349357 [Multi-domain]  Cd Length: 80  Bit Score: 41.88  E-value: 5.51e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 33621227  60 GATFTSSVGTDCTHLIA----TQK--EADKKGAKL-SLDWLLDSDKAKKPVSEAPY 108
Cdd:cd17725  25 GAKYRPDWTADCTHLICafanTPKykQVKGAGGIIvSKEWILDCYKKKKRLPWKRY 80
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 26-108 2.06e-04

BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found on many RAP1 proteins, usually at the very N-terminus. The function in human at least of a BRCT is to contribute to the heterogeneity of the telomere DNA length, but that may not be its general function, which remains unknown.


Pssm-ID: 465186 [Multi-domain]  Cd Length: 84  Bit Score: 40.43  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227    26 FCDVQFLIEFFKSTTREltrhsyagDLKAIVERHGATFTSSVGTDCTHLIATQKEADKKGAK-----LSLDWLLDSDKAK 100
Cdd:pfam16589   5 FEPLRFYINAIPSPSRS--------KLKRLIEANGGTVVDNINPAVYIVIAPYNKTDKLAENtklgvVSPQWIFDCVKKG 76


                  ....*...
gi 33621227   101 KPVSEAPY 108
Cdd:pfam16589  77 KLLPLENY 84
WGR_MMR_like cd07996
WGR domain of molybdate metabolism regulator and related proteins; The WGR domain is found in ...
 201-258 2.78e-04

WGR domain of molybdate metabolism regulator and related proteins; The WGR domain is found in the putative Escherichia coli molybdate metabolism regulator and related bacterial proteins, as well as in various other bacterial proteins of unknown function. It has been called WGR after the most conserved central motif of the domain. The domain appears to occur in single-domain proteins and in a variety of domain architectures, together with ATP-dependent DNA ligase domains, WD40 repeats, leucine-rich repeats, and other domains. It has been proposed to function as a nucleic acid binding domain.


Pssm-ID: 153425  Cd Length: 74  Bit Score: 39.89  E-value: 2.78e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 33621227 201 AANNNKFYLIQIlnskDGSRYQTWT---RWGRVGERGQSVLLGDGTLDSAKKQFEKKFKDK 258
Cdd:cd07996  10 ERNSARFYEIEL----EGDLFGEWSlvrRWGRIGTKGQSRTKTFDSEEEALKAAEKLIREK 66
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 515-587 2.79e-04

Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) causes pleotropic effects in mammalian species through modulating gene expression. TCCD indicible PARP (TiPARP) is a target of TCDD that may contribute to multiple responses to TCDD by modulating protein function through poly ADP-ribosylation


Pssm-ID: 238719 [Multi-domain]  Cd Length: 121  Bit Score: 41.15  E-value: 2.79e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33621227 515 LLWHGSRSTNYGGILSQGLRIAPpeAPVSGYMFGKGVYFADMSSKSANYCWSHNSDHK------ALLLLGDVELGDPIY 587
Cdd:cd01439   1 LLFHGTSADAVEAICRHGFDRRF--CGKHGTMYGKGSYFAKNASYSHQYSKKSPKADGlkemflARVLTGDYTQGHPGY 77
BRCT smart00292
breast cancer carboxy-terminal domain;
3-96 4.53e-04

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 39.28  E-value: 4.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227      3 PKLFKKLVIAVSGTFPGYRqgrnfcdvqflieffksttREltrhsyagDLKAIVERHGATFTSSV-GTDCTHLIATQKEA 81
Cdd:smart00292   1 PKLFKGKTFYITGSFDKEE-------------------RD--------ELKELIEALGGKVTSSLsSKTTTHVIVGSPEG 53

                           90       100
                   ....*....|....*....|....
gi 33621227     82 DKKGAKLSL---------DWLLDS 96
Cdd:smart00292  54 GKLELLKAIalgipivkeEWLLDC 77
WGR cd07994
WGR domain; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases ...
 203-260 1.41e-03

WGR domain; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs) as well as the putative Escherichia coli molybdate metabolism regulator and related bacterial proteins, a small family of bacterial DNA ligases, and various other bacterial proteins of unknown function. It has been called WGR after the most conserved central motif of the domain. The domain occurs in single-domain proteins and in a variety of domain architectures, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain.


Pssm-ID: 153424  Cd Length: 73  Bit Score: 37.64  E-value: 1.41e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 33621227 203 NNNKFYLIQILNSKDGSRYQTWTRWGRVG-ERGQSVLLGDGTLDSAKKQFEKKFKDKSG 260
Cdd:cd07994  10 GSNKYYKLQLLEDDKENRYWVFRSYGRVGtVIGSTKLEQMPSKEEAEEHFMKLYEEKTG 68
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 473-565 1.45e-03

Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 poly-ADP-ribosylates Telomere Repeat Binding Factor 1 (TRF1) while Tankyrase 2 can poly-ADP-ribosylate itself or TRF1. The tankyrases also contain multiple ankyrin repeats that mediate protein-protein interaction (binding TRF1 and insulin-responsive aminopeptidase) and may function as a complex. Overexpression of Tank1 promotes increased telomere length when overexpressed, while overexpressed Tank2 has been shown to promote PARP cleavage- independent cell death (necrosis).


Pssm-ID: 238718 [Multi-domain]  Cd Length: 223  Bit Score: 40.65  E-value: 1.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33621227 473 GTRGSTHGVKYKVIDIFRIERQGEHDRF----KSSSYAGLKNSNRRLLWHGSRSTNygGILSQGLRiaPPEAPVSGyMFG 548
Cdd:cd01438  45 GGNAGGIFNRYNIIRIQKVVNKKLRERYchrqKEIAEENHNHHNERMLFHGSPFIN--AIIHKGFD--ERHAYIGG-MFG 119

                        90
                ....*....|....*..
gi 33621227 549 KGVYFADMSSKSANYCW 565
Cdd:cd01438 120 AGIYFAENSSKSNQYVY 136
WGR COG3831
WGR domain, predicted DNA-binding domain in MolR [Transcription];
195-258 3.19e-03

WGR domain, predicted DNA-binding domain in MolR [Transcription];


Pssm-ID: 443043  Cd Length: 83  Bit Score: 36.89  E-value: 3.19e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33621227 195 LNLTVSAANNNKFYLIQILNSKDGsryqTWT---RWGRVGERGQSVLLGDGTLDSAKKQFEKKFKDK 258
Cdd:COG3831   5 LERIDPAGNSARFYELEVEPDLFG----GWSltrRWGRIGTKGQTKTKTFASEEEALAALEKLVAEK 67
 
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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