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Conserved domains on  [gi|1443062733|ref|XP_025879375|]
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protein ADP-ribosyltransferase PARP3 isoform X3 [Oryza sativa Japonica Group]

Protein Classification

PLN03122 family protein( domain architecture ID 11477447)

PLN03122 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03122 PLN03122
Poly [ADP-ribose] polymerase; Provisional
 1-836 0e+00

Poly [ADP-ribose] polymerase; Provisional


:

Pssm-ID: 178669 [Multi-domain]  Cd Length: 815  Bit Score: 1436.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733   1 MVHETRSRTLAASQEEGKAAPKKQKteskeqeggqqapsknkktADNEEHDGEQEPSKNKKLKAEESDLNGKA----TAV 76
Cdd:PLN03122    1 KVHETRSQAHAPAAEEGKGGTRKQK-------------------AENKEHEGEQSPKKAKKEKKQDDSGNGNGksaeDAV 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733  77 KEFSEFCKAIREHLTIEDMRKILQGNEQDASGSEDAVVPRCEDVMFYGPLDKCPVCGGQLECKGLKYNCTGTHSEWACCS 156
Cdd:PLN03122   62 KEFEEFCKAIEEHLSIEQMREILEENGQDSSGSDDAVLPRCQDQLFYGPLEKCPLCGGALECDGHRYTCTGFISEWSSCT 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 157 FSTNNPSRRGGPIKVPDDVKNDFVRKWLKQ-QEGNKYPKRNL-DDEGIFSGMMIALSGRMSRSHGYFKEQIMKHGGKVNN 234
Cdd:PLN03122  142 FSTKNPPRKEEPLKIPDSVKNSFITKLLKKhQDPSKRPKRELgAPGKPFSGMMISLSGRLSRTHQYWKKDIEKHGGKVAN 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 235 SVIGVTCVVASPAERHQGGSGGFAEALERGTPVVSENWIIDSVQKKEKQPLAAYDIASDVVPEGRGLPLGNLDPTEEAIE 314
Cdd:PLN03122  222 SVEGVTCLVVSPAERERGGSSKIAEAMERGIPVVREAWLIDSIEKQEAQPLEAYDVVSDLSVEGRGIPWDKQDPSEEAIE 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 315 TLAAELKLAGKRAVHKDSKLEKDGGHIYEKDGIIYNCAFSVCDLGGDINQLCIMQLIMVPENHLHLYYKKGPIGHDQMAE 394
Cdd:PLN03122  302 SLSAELKLYGKRGVYKDSKLQEEGGKIFEKDGILYNCAFSICDLGRGLNEYCIMQLITVPDSNLHLYYKKGRVGDDPNAE 381

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 395 ERVEDFGSrFNDAIKEFVRLFEEVTGNEFEPWEREKKFKKKCMKMYPLDMDDGVDVRHGGVALRQLGAAAAHCKLDPSVT 474
Cdd:PLN03122  382 ERLEEWED-VDAAIKEFVRLFEEITGNEFEPWEREKKFEKKRLKFYPIDMDDGVDVRAGGLGLRQLGVAAAHCKLDPKVA 460

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 475 FIMKQLCSQEIYRaschrYALTEMGHDVPDLPIGMLTDLHLKRGEETLLEWKQDVESAPESGPAADAFWMEISNKWFTLF 554
Cdd:PLN03122  461 NFMKVLCSQEIYR-----YAMMEMGLDSPDLPMGMLSDFHLKRCEEVLLEFAEFVKSEKETGQKAEAMWLDFSNKWFSLV 535

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 555 PTTRPYTMKGYEQIADNVASGLETVRDINVASRLIGDVFGSTLDDPLSQCYKKLGCSINRVVEDSEDYKMILKYLEKTYE 634
Cdd:PLN03122  536 HSTRPFVIRDIDELADHAASALETVRDINVASRLIGDMTGSTLDDPLSDRYKKLGCSISPVDKESDDYKMIVKYLEKTYE 615

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 635 PVKVGDVVYSATVERIYAVESSALPSYDEIKKLPNKVLLWCGTRSSNLLRHLRDGFVPAVCHIPVPGYMFGKAIVCSDAA 714
Cdd:PLN03122  616 PVKVGDVSYSVSVENIFAVESSAGPSLDEIKKLPNKVLLWCGTRSSNLLRHLAKGFLPAVCSLPVPGYMFGKAIVCSDAA 695

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 715 AEAALYGFTAVDRPEGYLVLAVASLGKEIQEITGTPgsEDVKRMEEKKMGVKGVGRKTTDPSEHFTWRDGVTVPCGKLVP 794
Cdd:PLN03122  696 AEAARYGFTAVDRPEGFLVLAVASLGDEVLELTKPP--EDVKSYEEKKVGVKGLGRKKTDESEHFKWRDDITVPCGRLIP 773

                         810       820       830       840
                  ....*....|....*....|....*....|....*....|..
gi 1443062733 795 STNKDGPLEYNEYAVYDPKQVSIAFLVGVKYEEQNMEVVPDE 836
Cdd:PLN03122  774 SEHKDSPLEYNEYAVYDPKQVSIRFLVGVKYEEKGAEMVTAE 815
 
Name Accession Description Interval E-value
PLN03122 PLN03122
Poly [ADP-ribose] polymerase; Provisional
 1-836 0e+00

Poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 178669 [Multi-domain]  Cd Length: 815  Bit Score: 1436.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733   1 MVHETRSRTLAASQEEGKAAPKKQKteskeqeggqqapsknkktADNEEHDGEQEPSKNKKLKAEESDLNGKA----TAV 76
Cdd:PLN03122    1 KVHETRSQAHAPAAEEGKGGTRKQK-------------------AENKEHEGEQSPKKAKKEKKQDDSGNGNGksaeDAV 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733  77 KEFSEFCKAIREHLTIEDMRKILQGNEQDASGSEDAVVPRCEDVMFYGPLDKCPVCGGQLECKGLKYNCTGTHSEWACCS 156
Cdd:PLN03122   62 KEFEEFCKAIEEHLSIEQMREILEENGQDSSGSDDAVLPRCQDQLFYGPLEKCPLCGGALECDGHRYTCTGFISEWSSCT 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 157 FSTNNPSRRGGPIKVPDDVKNDFVRKWLKQ-QEGNKYPKRNL-DDEGIFSGMMIALSGRMSRSHGYFKEQIMKHGGKVNN 234
Cdd:PLN03122  142 FSTKNPPRKEEPLKIPDSVKNSFITKLLKKhQDPSKRPKRELgAPGKPFSGMMISLSGRLSRTHQYWKKDIEKHGGKVAN 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 235 SVIGVTCVVASPAERHQGGSGGFAEALERGTPVVSENWIIDSVQKKEKQPLAAYDIASDVVPEGRGLPLGNLDPTEEAIE 314
Cdd:PLN03122  222 SVEGVTCLVVSPAERERGGSSKIAEAMERGIPVVREAWLIDSIEKQEAQPLEAYDVVSDLSVEGRGIPWDKQDPSEEAIE 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 315 TLAAELKLAGKRAVHKDSKLEKDGGHIYEKDGIIYNCAFSVCDLGGDINQLCIMQLIMVPENHLHLYYKKGPIGHDQMAE 394
Cdd:PLN03122  302 SLSAELKLYGKRGVYKDSKLQEEGGKIFEKDGILYNCAFSICDLGRGLNEYCIMQLITVPDSNLHLYYKKGRVGDDPNAE 381

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 395 ERVEDFGSrFNDAIKEFVRLFEEVTGNEFEPWEREKKFKKKCMKMYPLDMDDGVDVRHGGVALRQLGAAAAHCKLDPSVT 474
Cdd:PLN03122  382 ERLEEWED-VDAAIKEFVRLFEEITGNEFEPWEREKKFEKKRLKFYPIDMDDGVDVRAGGLGLRQLGVAAAHCKLDPKVA 460

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 475 FIMKQLCSQEIYRaschrYALTEMGHDVPDLPIGMLTDLHLKRGEETLLEWKQDVESAPESGPAADAFWMEISNKWFTLF 554
Cdd:PLN03122  461 NFMKVLCSQEIYR-----YAMMEMGLDSPDLPMGMLSDFHLKRCEEVLLEFAEFVKSEKETGQKAEAMWLDFSNKWFSLV 535

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 555 PTTRPYTMKGYEQIADNVASGLETVRDINVASRLIGDVFGSTLDDPLSQCYKKLGCSINRVVEDSEDYKMILKYLEKTYE 634
Cdd:PLN03122  536 HSTRPFVIRDIDELADHAASALETVRDINVASRLIGDMTGSTLDDPLSDRYKKLGCSISPVDKESDDYKMIVKYLEKTYE 615

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 635 PVKVGDVVYSATVERIYAVESSALPSYDEIKKLPNKVLLWCGTRSSNLLRHLRDGFVPAVCHIPVPGYMFGKAIVCSDAA 714
Cdd:PLN03122  616 PVKVGDVSYSVSVENIFAVESSAGPSLDEIKKLPNKVLLWCGTRSSNLLRHLAKGFLPAVCSLPVPGYMFGKAIVCSDAA 695

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 715 AEAALYGFTAVDRPEGYLVLAVASLGKEIQEITGTPgsEDVKRMEEKKMGVKGVGRKTTDPSEHFTWRDGVTVPCGKLVP 794
Cdd:PLN03122  696 AEAARYGFTAVDRPEGFLVLAVASLGDEVLELTKPP--EDVKSYEEKKVGVKGLGRKKTDESEHFKWRDDITVPCGRLIP 773

                         810       820       830       840
                  ....*....|....*....|....*....|....*....|..
gi 1443062733 795 STNKDGPLEYNEYAVYDPKQVSIAFLVGVKYEEQNMEVVPDE 836
Cdd:PLN03122  774 SEHKDSPLEYNEYAVYDPKQVSIRFLVGVKYEEKGAEMVTAE 815
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 466-824 1.55e-94

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: 299.96  E-value: 1.55e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 466 HCKLDPSVTFIMKQLCSQEIYRAschryALTEMGHDVPDLPIGMLTDLHLKRGEETLLEwkqdVESAPESGPAADAFWME 545
Cdd:cd01437     1 KSKLDKPVQELIKLIFDVEMMKK-----AMTELKIDASKMPLGKLSKNQIQKGYEVLKE----IEEALKRGSSQGSQLEE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 546 ISNKWFTLFPTTrpYTMKGYEQIADNV-----ASGLETVRDINVASRLIGDVfGSTLDDPLSQCYKKLGCSINRVVEDSE 620
Cdd:cd01437    72 LSNEFYTLIPHD--FGMSKPPVIDNEEllkakRELLEALRDIEIASKLLKDD-EDDSDDPLDANYEKLKCKIEPLDKDSE 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 621 DYKMILKYLEKTYEPVKVgdvvYSATVERIYAVESSALPS-YDEIKKLPNKVLLWCGTRSSNLLRHLRDGFVPAVCHIPV 699
Cdd:cd01437   149 EYKIIEKYLKNTHAPTTE----YTVEVQEIFRVEREGETDrFKPFKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEAPV 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 700 PGYMFGKAIVCSDAAAEAALYGFTAVDRPEGYLVLAVASLGKEiQEITGTPGSEdvKRMEEKKMGVKGVGRKTTDPSEHF 779
Cdd:cd01437   225 TGYMFGKGIYFADMFSKSANYCHASASDPTGLLLLCEVALGKM-NELKKADYMA--KELPKGKHSVKGLGKTAPDPSEFE 301

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1443062733 780 TWRDGVTVPCGKLVPST-NKDGPLEYNEYAVYDPKQVSIAFLVGVK 824
Cdd:cd01437   302 IDLDGVVVPLGKPVPSGhKTDTSLLYNEYIVYDVAQVRLKYLLEVK 347
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 619-825 3.48e-52

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: 180.61  E-value: 3.48e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 619 SEDYKMILKYLEKTYEPVKVgdvvYSATVERIYAVESSAL-PSYDEIKKLPNKVLLWCGTRSSNLLRHLRDGFVPAVCHI 697
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDPTHG----YPLFILEIFRVQRDGEwERFQPKKKLRNRRLLWHGSRLTNFLGILSQGLRIAPPEA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 698 PVPGYMFGKAIVCSDAAAEAALYGFTAVDRPEGYLVLAVASLGKEIQEITGTPGSEDvkrmEEKKMGVKGVGRKTTdpsE 777
Cdd:pfam00644  77 PVTGYMFGKGIYFADDASKSANYCPPSEAHGNGLMLLSEVALGDMNELKKADYAEKL----PPGKHSVKGLGKTAP---E 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1443062733 778 HFTWRDGvtVPCGKLVPSTNKDGPLEYNEYAVYDPKQVSIAFLVGVKY 825
Cdd:pfam00644 150 SFVDLDG--VPLGKLVATGYDSSVLLYNEYVVYNVNQVRPKYLLEVKF 195
WGR smart00773
Proposed nucleic acid binding domain; This domain is named after its most conserved central ...
 344-425 4.91e-21

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: 88.11  E-value: 4.91e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733  344 KDGIIYNCAFSVCDLGGDINQLCIMQLIMVPENHLHLYYKKGPIGHDqmAEERVEDFGSRfNDAIKEFVRLFEEVTGNEF 423
Cdd:smart00773   1 EGGEIYDVYLNFTDLASNNNKFYIIQLLEDDFGGYSVYRRWGRIGTK--GQTKLKTFDSL-EDAIKEFEKLFKEKTKNGY 77


                   ..
gi 1443062733  424 EP 425
Cdd:smart00773  78 EE 79
 
Name Accession Description Interval E-value
PLN03122 PLN03122
Poly [ADP-ribose] polymerase; Provisional
 1-836 0e+00

Poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 178669 [Multi-domain]  Cd Length: 815  Bit Score: 1436.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733   1 MVHETRSRTLAASQEEGKAAPKKQKteskeqeggqqapsknkktADNEEHDGEQEPSKNKKLKAEESDLNGKA----TAV 76
Cdd:PLN03122    1 KVHETRSQAHAPAAEEGKGGTRKQK-------------------AENKEHEGEQSPKKAKKEKKQDDSGNGNGksaeDAV 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733  77 KEFSEFCKAIREHLTIEDMRKILQGNEQDASGSEDAVVPRCEDVMFYGPLDKCPVCGGQLECKGLKYNCTGTHSEWACCS 156
Cdd:PLN03122   62 KEFEEFCKAIEEHLSIEQMREILEENGQDSSGSDDAVLPRCQDQLFYGPLEKCPLCGGALECDGHRYTCTGFISEWSSCT 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 157 FSTNNPSRRGGPIKVPDDVKNDFVRKWLKQ-QEGNKYPKRNL-DDEGIFSGMMIALSGRMSRSHGYFKEQIMKHGGKVNN 234
Cdd:PLN03122  142 FSTKNPPRKEEPLKIPDSVKNSFITKLLKKhQDPSKRPKRELgAPGKPFSGMMISLSGRLSRTHQYWKKDIEKHGGKVAN 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 235 SVIGVTCVVASPAERHQGGSGGFAEALERGTPVVSENWIIDSVQKKEKQPLAAYDIASDVVPEGRGLPLGNLDPTEEAIE 314
Cdd:PLN03122  222 SVEGVTCLVVSPAERERGGSSKIAEAMERGIPVVREAWLIDSIEKQEAQPLEAYDVVSDLSVEGRGIPWDKQDPSEEAIE 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 315 TLAAELKLAGKRAVHKDSKLEKDGGHIYEKDGIIYNCAFSVCDLGGDINQLCIMQLIMVPENHLHLYYKKGPIGHDQMAE 394
Cdd:PLN03122  302 SLSAELKLYGKRGVYKDSKLQEEGGKIFEKDGILYNCAFSICDLGRGLNEYCIMQLITVPDSNLHLYYKKGRVGDDPNAE 381

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 395 ERVEDFGSrFNDAIKEFVRLFEEVTGNEFEPWEREKKFKKKCMKMYPLDMDDGVDVRHGGVALRQLGAAAAHCKLDPSVT 474
Cdd:PLN03122  382 ERLEEWED-VDAAIKEFVRLFEEITGNEFEPWEREKKFEKKRLKFYPIDMDDGVDVRAGGLGLRQLGVAAAHCKLDPKVA 460

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 475 FIMKQLCSQEIYRaschrYALTEMGHDVPDLPIGMLTDLHLKRGEETLLEWKQDVESAPESGPAADAFWMEISNKWFTLF 554
Cdd:PLN03122  461 NFMKVLCSQEIYR-----YAMMEMGLDSPDLPMGMLSDFHLKRCEEVLLEFAEFVKSEKETGQKAEAMWLDFSNKWFSLV 535

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 555 PTTRPYTMKGYEQIADNVASGLETVRDINVASRLIGDVFGSTLDDPLSQCYKKLGCSINRVVEDSEDYKMILKYLEKTYE 634
Cdd:PLN03122  536 HSTRPFVIRDIDELADHAASALETVRDINVASRLIGDMTGSTLDDPLSDRYKKLGCSISPVDKESDDYKMIVKYLEKTYE 615

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 635 PVKVGDVVYSATVERIYAVESSALPSYDEIKKLPNKVLLWCGTRSSNLLRHLRDGFVPAVCHIPVPGYMFGKAIVCSDAA 714
Cdd:PLN03122  616 PVKVGDVSYSVSVENIFAVESSAGPSLDEIKKLPNKVLLWCGTRSSNLLRHLAKGFLPAVCSLPVPGYMFGKAIVCSDAA 695

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 715 AEAALYGFTAVDRPEGYLVLAVASLGKEIQEITGTPgsEDVKRMEEKKMGVKGVGRKTTDPSEHFTWRDGVTVPCGKLVP 794
Cdd:PLN03122  696 AEAARYGFTAVDRPEGFLVLAVASLGDEVLELTKPP--EDVKSYEEKKVGVKGLGRKKTDESEHFKWRDDITVPCGRLIP 773

                         810       820       830       840
                  ....*....|....*....|....*....|....*....|..
gi 1443062733 795 STNKDGPLEYNEYAVYDPKQVSIAFLVGVKYEEQNMEVVPDE 836
Cdd:PLN03122  774 SEHKDSPLEYNEYAVYDPKQVSIRFLVGVKYEEKGAEMVTAE 815
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
 1-825 5.75e-138

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 433.83  E-value: 5.75e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733   1 MVHETRSRTLAASQEEGKAAPKKQKTESKEQEGGQQ--APSKNKKTADNEEHDGEQEPSKNKKLKAEEsdlngkatavKE 78
Cdd:PLN03123  182 LVKKSPSEAKEEKAEERKQESKKGAKRKKDASGDDKskKAKTDRDVSTSTAASQKKSSDLESKLEAQS----------KE 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733  79 FSEFCKAIREHLTIEDMRKILQGNEQDASGSEDAVVPRCEDVMFYGPLDKCPVCGGQLECKGLKYNCTGTHSEWACCSFS 158
Cdd:PLN03123  252 LWSLKDDLKKHVSTAELREMLEANGQDTSGSELDLRDRCADGMMFGALGPCPLCSGPLLYSGGMYRCQGYLSEWSKCSYS 331

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 159 TNNPSRRGGPIKVPDDVKNDFVRKWLKQQEGNKyPKRNL--------------------DDEGIfSGMMIALSGRMSRSH 218
Cdd:PLN03123  332 TLEPERIKKKWKIPDETDNQYLRKWFKSQKSKK-PERLLppsssnessgkqaqsnssdsESEFL-GDLKVSIVGASKEKV 409

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 219 GYFKEQIMKHGGKVNNSV-IGVTCVVASPAERHQGGSggFAEALERGTPVVSENWIIDSVQKKEKQPLAAYDIasdvvpE 297
Cdd:PLN03123  410 TEWKAKIEEAGGVFHATVkKDTNCLVVCGELDDEDAE--MRKARRMKIPIVREDYLVDCFKKKKKLPFDKYKL------E 481

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 298 GRGlplgnldpTEEAIETlaaeLKLAGKRAVHKDSKLEkDGGHIYEKDGIIYNCAFSVCDLGGDINQLCIMQLIMVPE-N 376
Cdd:PLN03123  482 ASG--------TSSSMVT----VKVKGRSAVHEASGLQ-DTGHILEDGKSIYNTTLNMSDLSTGVNSYYILQIIEEDKgS 548

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 377 HLHLYYKKGPIGHDQMAEERVEDFGSrfNDAIKEFVRLFEEVTGNEFEPWEREKKFKKKCMKMYPLDMDDGVDvrhggVA 456
Cdd:PLN03123  549 DCYVFRKWGRVGNEKIGGNKLEEMSK--SDAIHEFKRLFLEKTGNPWESWEQKTNFQKQPGKFYPLDIDYGVN-----EQ 621

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 457 LRQLGAAAAHCKLDPSVTFIMKQLCSQEIYRAschryALTEMGHDVPDLPIGMLTDLHLKRGEETLLEWkQDVESAPESG 536
Cdd:PLN03123  622 PKKKAASGSKSNLAPRLVELMKMLFDVETYRA-----AMMEFEINMSEMPLGKLSKANIQKGFEALTEI-QNLLKENDQD 695

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 537 PAA-DAFWMEISNKWFTLFPTTRPYTMKGyEQIADNVASGLETVRDINVASRLIGdvFGSTLDDPLSQCYKKLGCSINRV 615
Cdd:PLN03123  696 PSIrESLLVDASNRFFTLIPSIHPHIIRD-EDDLKSKVKMLEALQDIEIASRLVG--FDVDEDDSLDDKYKKLHCDISPL 772

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 616 VEDSEDYKMILKYLEKTYEPVKVGdvvYSATVERIYAVESSA-LPSYDEIK-KLPNKVLLWCGTRSSNLLRHLRDGFVPA 693
Cdd:PLN03123  773 PHDSEDYKLIEKYLLTTHAPTHTD---WSLELEEVFSLEREGeFDKYAPYKeKLKNRMLLWHGSRLTNFVGILSQGLRIA 849

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 694 VCHIPVPGYMFGKAIVCSDAAAEAALYGFTAVDRPEGYLVLAVASLGkEIQEITgtpgseDVKRME---EKKMGVKGVGR 770
Cdd:PLN03123  850 PPEAPATGYMFGKGVYFADLVSKSAQYCYTDRKNPVGLMLLSEVALG-EIYELK------KAKYMDkppRGKHSTKGLGK 922

                         810       820       830       840       850
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1443062733 771 KTTDPSEHFTWRDGVTVPCGKLVPSTNKDGPLEYNEYAVYDPKQVSIAFLVGVKY 825
Cdd:PLN03123  923 TVPQESEFVKWRDDVVVPCGKPVPSKVKASELMYNEYIVYNTAQVKLQFLLKVRF 977
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 466-824 1.55e-94

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: 299.96  E-value: 1.55e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 466 HCKLDPSVTFIMKQLCSQEIYRAschryALTEMGHDVPDLPIGMLTDLHLKRGEETLLEwkqdVESAPESGPAADAFWME 545
Cdd:cd01437     1 KSKLDKPVQELIKLIFDVEMMKK-----AMTELKIDASKMPLGKLSKNQIQKGYEVLKE----IEEALKRGSSQGSQLEE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 546 ISNKWFTLFPTTrpYTMKGYEQIADNV-----ASGLETVRDINVASRLIGDVfGSTLDDPLSQCYKKLGCSINRVVEDSE 620
Cdd:cd01437    72 LSNEFYTLIPHD--FGMSKPPVIDNEEllkakRELLEALRDIEIASKLLKDD-EDDSDDPLDANYEKLKCKIEPLDKDSE 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 621 DYKMILKYLEKTYEPVKVgdvvYSATVERIYAVESSALPS-YDEIKKLPNKVLLWCGTRSSNLLRHLRDGFVPAVCHIPV 699
Cdd:cd01437   149 EYKIIEKYLKNTHAPTTE----YTVEVQEIFRVEREGETDrFKPFKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEAPV 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 700 PGYMFGKAIVCSDAAAEAALYGFTAVDRPEGYLVLAVASLGKEiQEITGTPGSEdvKRMEEKKMGVKGVGRKTTDPSEHF 779
Cdd:cd01437   225 TGYMFGKGIYFADMFSKSANYCHASASDPTGLLLLCEVALGKM-NELKKADYMA--KELPKGKHSVKGLGKTAPDPSEFE 301

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1443062733 780 TWRDGVTVPCGKLVPST-NKDGPLEYNEYAVYDPKQVSIAFLVGVK 824
Cdd:cd01437   302 IDLDGVVVPLGKPVPSGhKTDTSLLYNEYIVYDVAQVRLKYLLEVK 347
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 619-825 3.48e-52

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: 180.61  E-value: 3.48e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 619 SEDYKMILKYLEKTYEPVKVgdvvYSATVERIYAVESSAL-PSYDEIKKLPNKVLLWCGTRSSNLLRHLRDGFVPAVCHI 697
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDPTHG----YPLFILEIFRVQRDGEwERFQPKKKLRNRRLLWHGSRLTNFLGILSQGLRIAPPEA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 698 PVPGYMFGKAIVCSDAAAEAALYGFTAVDRPEGYLVLAVASLGKEIQEITGTPGSEDvkrmEEKKMGVKGVGRKTTdpsE 777
Cdd:pfam00644  77 PVTGYMFGKGIYFADDASKSANYCPPSEAHGNGLMLLSEVALGDMNELKKADYAEKL----PPGKHSVKGLGKTAP---E 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1443062733 778 HFTWRDGvtVPCGKLVPSTNKDGPLEYNEYAVYDPKQVSIAFLVGVKY 825
Cdd:pfam00644 150 SFVDLDG--VPLGKLVATGYDSSVLLYNEYVVYNVNQVRPKYLLEVKF 195
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 468-825 8.43e-40

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 156.54  E-value: 8.43e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 468 KLDPSVTFIMKQLCSqeiyrASCHRYALTEMGHDVPDLPIGMLTDLHLKRGEETLLEWKQDVE-SAPESgpaadafWMEI 546
Cdd:PLN03124  293 KLDPRVAQFISLICD-----VSMMKQQMMEIGYNARKLPLGKLSKSTILKGYEVLKRIAEVISrSDRET-------LEEL 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 547 SNKWFTLFPTTRPYTmKGYEQIADN---VASGLETVR---DINVASRLIGDVFGsTLDDPLSQCYKKLGCSINRVVEDSE 620
Cdd:PLN03124  361 SGEFYTVIPHDFGFK-KMRQFTIDTpqkLKHKLEMVEalgEIEIATKLLKDDIG-EQDDPLYAHYKRLNCELEPLDTDSE 438

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 621 DYKMILKYLEKTYEPVKVG---DVVYSATVERiyAVESSALPSYdeiKKLPNKVLLWCGTRSSNLLRHLRDGFVPAVCHI 697
Cdd:PLN03124  439 EFSMIAKYLENTHGQTHSGytlEIVQIFKVSR--EGEDERFQKF---SSTKNRMLLWHGSRLTNWTGILSQGLRIAPPEA 513

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 698 PVPGYMFGKAIVCSDAAAEAALYGFTAVDRPEGYLVLAVASLGKEIQEITGtpgSEDVKRMEEKKMGVKGVGRKTTDPSE 777
Cdd:PLN03124  514 PSTGYMFGKGVYFADMFSKSANYCYASAANPDGVLLLCEVALGDMNELLQA---DYNANKLPPGKLSTKGVGRTVPDPSE 590

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1443062733 778 HFTWRDGVTVPCGKLVPSTNKDGPLEYNEYAVYDPKQVSIAFLVGVKY 825
Cdd:PLN03124  591 AKTLEDGVVVPLGKPVESPYSKGSLEYNEYIVYNVDQIRMRYVLQVKF 638
PARP_reg pfam02877
Poly(ADP-ribose) polymerase, regulatory domain; Poly(ADP-ribose) polymerase catalyzes the ...
 467-605 1.48e-29

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: 114.16  E-value: 1.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 467 CKLDPSVTFIMKQLCSQEIYRaschrYALTEMGHDVPDLPIGMLTDLHLKRGEETLLEWKQDVESAPESgpAADAFWMEI 546
Cdd:pfam02877   1 SKLPPPVQELMKLIFNVEMMK-----KAMKEMKYDAKKMPLGKLSKRQIKKGYEVLKELSELLKKPSLA--KAKAKLEDL 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443062733 547 SNKWFTLFPTT----RPYTMKGYEQIADNVaSGLETVRDINVASRLIGDVFGSTLDDPLSQCY 605
Cdd:pfam02877  74 SNRFYTLIPHDfgrnRPPVIDTEEELKEKL-ELLEALLDIEVASKLLKDSKSDDDEHPLDRHY 135
WGR_PARP1_like cd08001
WGR domain of poly(ADP-ribose) polymerase 1 and similar proteins; The WGR domain is found in a ...
 339-446 7.58e-22

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: 91.12  E-value: 7.58e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 339 GHIYEKDGIIYNCAFSVCDLGGDINQLCIMQLIMVPE-NHLHLYYKKGPIGhDQMAEERVEDFGSRfNDAIKEFVRLFEE 417
Cdd:cd08001     1 AHVLEEGGNLYSAVLGLVDIQTGTNSYYKLQLLEHDKgNRYWVFRSWGRVG-TTIGGNKLEEFSSL-EEAKMAFEELYEE 78

                          90       100
                  ....*....|....*....|....*....
gi 1443062733 418 VTGNEFEPwerEKKFKKKCMKMYPLDMDD 446
Cdd:cd08001    79 KTGNDFEN---RKNFKKKPGKFYPLDIDY 104
BRCT_PARP1 cd17747
BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2. ...
 203-278 1.32e-21

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: 89.13  E-value: 1.32e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443062733 203 FSGMMIALSGRMSRSHGYFKEQIMKHGGKVNNSVI-GVTCVVASPAERhQGGSGGFAEALERGTPVVSENWIIDSVQ 278
Cdd:cd17747     1 LTGMKFALIGKLSKSKDELKKLIEKLGGKVASKVTkKVTLCISTKAEV-EKMSKKMKEAKEAGVPVVSEDFLEDCIK 76
WGR smart00773
Proposed nucleic acid binding domain; This domain is named after its most conserved central ...
 344-425 4.91e-21

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: 88.11  E-value: 4.91e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733  344 KDGIIYNCAFSVCDLGGDINQLCIMQLIMVPENHLHLYYKKGPIGHDqmAEERVEDFGSRfNDAIKEFVRLFEEVTGNEF 423
Cdd:smart00773   1 EGGEIYDVYLNFTDLASNNNKFYIIQLLEDDFGGYSVYRRWGRIGTK--GQTKLKTFDSL-EDAIKEFEKLFKEKTKNGY 77


                   ..
gi 1443062733  424 EP 425
Cdd:smart00773  78 EE 79
PADR1 pfam08063
PADR1 (NUC008) domain; This domain is found in poly(ADP-ribose)-synthetases. The function of ...
 114-165 3.77e-17

PADR1 (NUC008) domain; This domain is found in poly(ADP-ribose)-synthetases. The function of this domain is unknown.


Pssm-ID: 462349 [Multi-domain]  Cd Length: 53  Bit Score: 75.69  E-value: 3.77e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1443062733 114 VPRCEDVMFYGPLDKCPVCG-GQLECKGLKYNCTGTHSEWACCSFSTNNPSRR 165
Cdd:pfam08063   1 LDRCADGMLFGALEPCPECKnGQLVFNGSGYKCTGYVSEWTKCTYSTKDPKRK 53
BRCT_Rev1 cd17719
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ...
 202-288 1.40e-08

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: 52.57  E-value: 1.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 202 IFSGMMIALSGRMSRSHGYFKEQIMKHGGKVNN--SVIGVTCVVAS---PAERHQggsggFAEAleRGTPVVSENWIIDS 276
Cdd:cd17719     1 IFKGVVIYVNGYTDPSADELKRLILLHGGQYEHyySRSRVTHIIATnlpGSKIKK-----LKKA--RNYKVVRPEWIVDS 73

                          90
                  ....*....|..
gi 1443062733 277 VQKKEKQPLAAY 288
Cdd:cd17719    74 IKAGRLLPEAPY 85
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 201-288 3.28e-08

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: 51.60  E-value: 3.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 201 GIFSGMM--IALSGRMSRSHgyFKEQIMKHGGKV-NNSVIGVTCVVASPAErhqggsgGFAEALERGTPVVSENWIIDSV 277
Cdd:pfam16589   3 NLFEPLRfyINAIPSPSRSK--LKRLIEANGGTVvDNINPAVYIVIAPYNK-------TDKLAENTKLGVVSPQWIFDCV 73

                          90
                  ....*....|.
gi 1443062733 278 QKKEKQPLAAY 288
Cdd:pfam16589  74 KKGKLLPLENY 84
BRCT smart00292
breast cancer carboxy-terminal domain;
200-277 5.47e-08

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 50.84  E-value: 5.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733  200 EGIFSGMMIALSGRMSRSH-GYFKEQIMKHGGKVNNSV--IGVTCVVASPAErhqGGSGGFAEALERGTPVVSENWIIDS 276
Cdd:smart00292   1 PKLFKGKTFYITGSFDKEErDELKELIEALGGKVTSSLssKTTTHVIVGSPE---GGKLELLKAIALGIPIVKEEWLLDC 77


                   .
gi 1443062733  277 V 277
Cdd:smart00292  78 L 78
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 200-277 8.64e-08

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: 49.98  E-value: 8.64e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443062733 200 EGIFSGMMIALSGRMSRSHGYFKEQIMKHGGKVNNSV-IGVTCVVASPaerhqgGSGGFAEALERGTPVVSENWIIDSV 277
Cdd:pfam00533   3 EKLFSGKTFVITGLDGLERDELKELIEKLGGKVTDSLsKKTTHVIVEA------RTKKYLKAKELGIPIVTEEWLLDCI 75
WGR pfam05406
WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli ...
 349-429 6.95e-06

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: 44.54  E-value: 6.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 349 YNCAFSVCDLGGDINQLCIMQLIMVPENHLHLYYKKGPIGHDqmAEERVEDFGSrFNDAIKEFVRLFEEVTGNEFEPWER 428
Cdd:pfam05406   1 YDLYLEQTDAARNSNKFYEIQVEDDLFGGYSLFRRWGRIGTR--GQTKLKSFDS-LEEAIKEFEKLFAEKTKKGYRERGE 77


                  .
gi 1443062733 429 E 429
Cdd:pfam05406  78 F 78
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 208-276 2.16e-05

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: 43.12  E-value: 2.16e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 208 IALSGRMSRSHGYFKEQIMKHGGKVNNSV-IGVTCVVASPAErhqgGSGGFAEALERGTPVVSENWIIDS 276
Cdd:cd00027     3 ICFSGLDDEEREELKKLIEALGGKVSESLsSKVTHLIAKSPS----GEKYYLAALAWGIPIVSPEWLLDC 68
BRCT_p53bp1_rpt1 cd17745
first (central) BRCT domain in p53-binding protein 1 (p53BP1) and similar proteins; p53BP1, ...
 202-281 4.77e-04

first (central) BRCT domain in p53-binding protein 1 (p53BP1) and similar proteins; p53BP1, also termed 53BP1, or TP53-binding protein 1 (TP53BP1) , is a double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis. TP53BP1 contains two tandem BRCT repeats. This family also includes Schizosaccharomyces pombe Crb2, which is a checkpoint mediator required for the cellular response to DNA damage. This model corresponds to the first BRCT domain.


Pssm-ID: 349376 [Multi-domain]  Cd Length: 99  Bit Score: 39.99  E-value: 4.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 202 IFSGMMIALSGRMSRSHGYFKEQIMK----HGGKVNNSVIGVTCVVASPAERHQGG---------SGGFA------EALE 262
Cdd:cd17745     1 IFSGCAFLLTGAEETDKPFDKERLESqieaNGGTVLEDFDEELFNDGRSSTRKSRSkdlrfvfliADSPSrtpkylQALA 80

                          90
                  ....*....|....*....
gi 1443062733 263 RGTPVVSENWIIDSVQKKE 281
Cdd:cd17745    81 LGIPCVSHKWILDCIEAGK 99
BRCT_TopBP1_rpt2_like cd17731
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 201-280 1.59e-03

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: 37.90  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443062733 201 GIFSGMMIALSGRMSRSHGYFKEQIMKHGGKVNnSVIGVTC---VVASPaerhqgGSGGFAEALERGT-PVVSENWIIDS 276
Cdd:cd17731     1 PPFKGLVICVTGFDSEERKEIQQLVEQNGGSYS-PDLSKNCthlIAGSP------SGQKYEFARKWNSiHIVTPEWLYDS 73


                  ....
gi 1443062733 277 VQKK 280
Cdd:cd17731    74 IEAG 77
 
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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