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Conserved domains on  [gi|281485553|ref|NP_001139450|]
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protein mono-ADP-ribosyltransferase PARP4 [Mus musculus]

Protein Classification

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 ...
 244-557 1.37e-107

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: 347.72  E-value: 1.37e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  244 EEVISSGALSQEVSDLLEVIWTEALGHLENTLLKPVNSMSLNDVSKAEGILLLVKTALKNGDS-PGQLQKTMAEFYRLLP 322
Cdd:cd01437     2 SKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSqGSQLEELSNEFYTLIP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  323 HRHPASEEVNLR---LLAQKEDLCQLVRDMVNVCETNLSK---PNPPSLAKYRALRCKIEHVDQNTEEFSRVRKEVLQNN 396
Cdd:cd01437    82 HDFGMSKPPVIDneeLLKAKRELLEALRDIEIASKLLKDDeddSDDPLDANYEKLKCKIEPLDKDSEEYKIIEKYLKNTH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  397 RS--EQPVDILQIFRVGRVNEATEFL--SKLGNVRLLFHGSPVRNILGILSRGLLLPKVaedrgvqRTDVGNL--GSGIY 470
Cdd:cd01437   162 APttEYTVEVQEIFRVEREGETDRFKpfKKLGNRKLLWHGSRLTNFVGILSQGLRIAPP-------EAPVTGYmfGKGIY 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  471 FSDSLSTSIKYAHAGETDGSRLLVVCDVALGKCVNLFKKDFSLTEAPPGYDSVHGVSETTSVPTDFQDD----------- 539
Cdd:cd01437   235 FADMFSKSANYCHASASDPTGLLLLCEVALGKMNELKKADYMAKELPKGKHSVKGLGKTAPDPSEFEIDldgvvvplgkp 314

                         330       340       350
                  ....*....|....*....|....*....|..
gi 281485553  540 --------------EFVVYKTNQVKMKYIVKF 557
Cdd:cd01437   315 vpsghktdtsllynEYIVYDVAQVRLKYLLEV 346
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 616-726 7.40e-54

Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one light chain and a variable set of heavy chains. ITIs play a role in extracellular matrix (ECM) stabilization and tumour metastasis as well as in plasma protease inhibition. The vault protein inter-alpha-trypsin (VIT) domain described here is found to the N-terminus of a von Willebrand factor type A domain (pfam00092) in ITI heavy chains (ITIHs) and their precursors.


:

Pssm-ID: 462492 [Multi-domain]  Cd Length: 111  Bit Score: 183.84  E-value: 7.40e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553   616 LDSVHIKGRVIDFVAQVIVFQTYTNQSHVPIEAKYIFPLDDKAAVCGFEAFINGKHIVGEIKEKEEARQEYREAVSQGHG 695
Cdd:pfam08487    1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 281485553   696 AYLMDQDTPDVFTVSVGNLPPRAKVLIKITY 726
Cdd:pfam08487   81 AGLLEQDTPDVFTTSVGNIPPGEKVTVELTY 111
BRCT super family cl00038
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 5-88 1.42e-29

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.


The actual alignment was detected with superfamily member cd17726:

Pssm-ID: 469589 [Multi-domain]  Cd Length: 85  Bit Score: 113.54  E-value: 1.42e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553    5 IFANCIFCLKVKYLPR-QQKKKLQTDIKENGGKFSFLLNPQCTHVIVDSADVLSRCHLNSIQKNDVQIANPAFIQDSVRQ 83
Cdd:cd17726     1 VFSGCQIVLDLKTLPGfKEKKKLKKKITENGGIISYIINKKCTHVVVNNAKALSSYKCRMAQKYGIPVVSLDYIWKCVEA 80


                  ....*
gi 281485553   84 RRLLD 88
Cdd:cd17726    81 GKLLD 85
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 847-1011 1.87e-18

Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];


:

Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 87.43  E-value: 1.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  847 EACMLVFQPELADVLPDLRGknEVIICLDCSSSMEGVTFTQAKQVALYALSLLGEEQKVNIMQFGTGYKElfSYPKCITD 926
Cdd:COG2425   100 LAALLLLAAPASAAVPLLEG--PVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVE--DLPLTADD 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  927 SKM-ATEFImSAAPSMGNTDFWKVLRY-LSLL-YPSEGFRNILLISDGHLQSESL-TLQLVKRNIQHTRVFTCAVGSTAN 1002
Cdd:COG2425   176 GLEdAIEFL-SGLFAGGGTDIAPALRAaLELLeEPDYRNADIVLITDGEAGVSPEeLLREVRAKESGVRLFTVAIGDAGN 254


                  ....*....
gi 281485553 1003 RHILRTLSQ 1011
Cdd:COG2425   255 PGLLEALAD 263
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 1372-1618 1.13e-10

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


:

Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 61.81  E-value: 1.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  1372 PPHPLGGthpppplplpDGTHLPSPLFGSTHPPPPLFGGTLIPPPSSLfggthlppppplpggthipppppiPGGTLIPP 1451
Cdd:pfam06346    2 PPPPLPG----------DSSTIPLPPGACIPTPPPLPGGGGPPPPPPL------------------------PGSAAIPP 47

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  1452 SSSLFGGTHLPPPPLLSAGTHIPPPPllsagthlppppllpagthippppPITGSTHPPPPSSLfggthlppppplpggt 1531
Cdd:pfam06346   48 PPPLPGGTSIPPPPPLPGAASIPPPP------------------------PLPGSTGIPPPPPL---------------- 87

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  1532 hipppppIPGGTLIPSPSSLFGGthlppppllpAGThipppppitgsthPPPPSSLFGGTHLPPPPPAGTQFSLSPigfI 1611
Cdd:pfam06346   88 -------PGGAGIPPPPPPLPGG----------AGV-------------PPPPPPLPGGPGIPPPPPFPGGPGIPP---P 134


                   ....*..
gi 281485553  1612 PPKLGPP 1618
Cdd:pfam06346  135 PPGMGMP 141
 
Name Accession Description Interval E-value
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 244-557 1.37e-107

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: 347.72  E-value: 1.37e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  244 EEVISSGALSQEVSDLLEVIWTEALGHLENTLLKPVNSMSLNDVSKAEGILLLVKTALKNGDS-PGQLQKTMAEFYRLLP 322
Cdd:cd01437     2 SKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSqGSQLEELSNEFYTLIP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  323 HRHPASEEVNLR---LLAQKEDLCQLVRDMVNVCETNLSK---PNPPSLAKYRALRCKIEHVDQNTEEFSRVRKEVLQNN 396
Cdd:cd01437    82 HDFGMSKPPVIDneeLLKAKRELLEALRDIEIASKLLKDDeddSDDPLDANYEKLKCKIEPLDKDSEEYKIIEKYLKNTH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  397 RS--EQPVDILQIFRVGRVNEATEFL--SKLGNVRLLFHGSPVRNILGILSRGLLLPKVaedrgvqRTDVGNL--GSGIY 470
Cdd:cd01437   162 APttEYTVEVQEIFRVEREGETDRFKpfKKLGNRKLLWHGSRLTNFVGILSQGLRIAPP-------EAPVTGYmfGKGIY 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  471 FSDSLSTSIKYAHAGETDGSRLLVVCDVALGKCVNLFKKDFSLTEAPPGYDSVHGVSETTSVPTDFQDD----------- 539
Cdd:cd01437   235 FADMFSKSANYCHASASDPTGLLLLCEVALGKMNELKKADYMAKELPKGKHSVKGLGKTAPDPSEFEIDldgvvvplgkp 314

                         330       340       350
                  ....*....|....*....|....*....|..
gi 281485553  540 --------------EFVVYKTNQVKMKYIVKF 557
Cdd:cd01437   315 vpsghktdtsllynEYIVYDVAQVRLKYLLEV 346
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 616-726 7.40e-54

Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one light chain and a variable set of heavy chains. ITIs play a role in extracellular matrix (ECM) stabilization and tumour metastasis as well as in plasma protease inhibition. The vault protein inter-alpha-trypsin (VIT) domain described here is found to the N-terminus of a von Willebrand factor type A domain (pfam00092) in ITI heavy chains (ITIHs) and their precursors.


Pssm-ID: 462492 [Multi-domain]  Cd Length: 111  Bit Score: 183.84  E-value: 7.40e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553   616 LDSVHIKGRVIDFVAQVIVFQTYTNQSHVPIEAKYIFPLDDKAAVCGFEAFINGKHIVGEIKEKEEARQEYREAVSQGHG 695
Cdd:pfam08487    1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 281485553   696 AYLMDQDTPDVFTVSVGNLPPRAKVLIKITY 726
Cdd:pfam08487   81 AGLLEQDTPDVFTTSVGNIPPGEKVTVELTY 111
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 382-559 7.42e-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: 181.38  E-value: 7.42e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553   382 TEEFSRVRKEVLQNNRSEQ--PVDILQIFRVGRVNEATEFLS--KLGNVRLLFHGSPVRNILGILSRGLLLPKVAEDRGV 457
Cdd:pfam00644    1 SEEYQIIEKYFLSTHDPTHgyPLFILEIFRVQRDGEWERFQPkkKLRNRRLLWHGSRLTNFLGILSQGLRIAPPEAPVTG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553   458 QRtdvgnLGSGIYFSDSLSTSIKYAHAGETDGSRLLVVCDVALGKCVNLFKKDFsLTEAPPGYDSVHGVSETTS------ 531
Cdd:pfam00644   81 YM-----FGKGIYFADDASKSANYCPPSEAHGNGLMLLSEVALGDMNELKKADY-AEKLPPGKHSVKGLGKTAPesfvdl 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 281485553   532 --VPT-----------DFQDDEFVVYKTNQVKMKYIVKFCT 559
Cdd:pfam00644  155 dgVPLgklvatgydssVLLYNEYVVYNVNQVRPKYLLEVKF 195
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
603-728 1.17e-45

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 160.99  E-value: 1.17e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553    603 KAGLQDASANPVPLDSVHIKGRVIDFVAQVIVFQTYTNQShVPIEAKYIFPLDDKAAVCGFEAF-INGKHIVGEIKEKEE 681
Cdd:smart00609    4 KRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRA-VPAQEVTFDVELPKTAFISNFAMtIDGKTYVGEIKEKEV 82

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 281485553    682 ARQEYREAVSQGHGAYLMDQDTP--DVFTVSVgNLPPRAKVLIKITYIT 728
Cdd:smart00609   83 AQKQYEKAVSQGKTAGLVRASGRsmEQFTVSV-NVAPGSKVTFELTYEE 130
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 278-558 6.65e-31

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 131.50  E-value: 6.65e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  278 PVNSMSLNDVSKAEGILLLVKTALKNGDsPGQLQKTMAEFYRLLPH----RHPASEEVNlrllaQKEDL-CQLvrDMV-- 350
Cdd:PLN03124  326 PLGKLSKSTILKGYEVLKRIAEVISRSD-RETLEELSGEFYTVIPHdfgfKKMRQFTID-----TPQKLkHKL--EMVea 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  351 --------NVCETNLSKPNPPSLAKYRALRCKIEHVDQNTEEFSRVrKEVLQNNRSEQ----PVDILQIFRVGRVNEATE 418
Cdd:PLN03124  398 lgeieiatKLLKDDIGEQDDPLYAHYKRLNCELEPLDTDSEEFSMI-AKYLENTHGQThsgyTLEIVQIFKVSREGEDER 476

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  419 F--LSKLGNVRLLFHGSPVRNILGILSRGL-LLPKVAEDRGVQrtdvgnLGSGIYFSDSLSTSIKYAHAGETDGSRLLVV 495
Cdd:PLN03124  477 FqkFSSTKNRMLLWHGSRLTNWTGILSQGLrIAPPEAPSTGYM------FGKGVYFADMFSKSANYCYASAANPDGVLLL 550

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  496 CDVALGKCVNLFKKDFSLTEAPPGYDSVHGVSETTSVPTDFQ--DD----------------------EFVVYKTNQVKM 551
Cdd:PLN03124  551 CEVALGDMNELLQADYNANKLPPGKLSTKGVGRTVPDPSEAKtlEDgvvvplgkpvespyskgsleynEYIVYNVDQIRM 630


                  ....*....
gi 281485553  552 KYI--VKFC 558
Cdd:PLN03124  631 RYVlqVKFN 639
BRCT_PARP4_like cd17726
BRCT domain of poly [ADP-ribose] polymerase 4 (PARP-4) and similar proteins; PARP-4, also ...
 5-88 1.42e-29

BRCT domain of poly [ADP-ribose] polymerase 4 (PARP-4) and similar proteins; PARP-4, also termed 193 kDa vault protein, or ADP-ribosyltransferase diphtheria toxin-like 4 (ARTD4), or PARP-related/IalphaI-related H5/proline-rich (PH5P), or vault poly(ADP-ribose) polymerase (VPARP), shows poly(ADP-ribosyl)ation activity that catalyzes the formation of ADP-ribose polymers in response to DNA damage. PARP-4 is a component of the vault ribonucleoprotein particle, at least composed of MVP, PARP4 and one or more vault RNAs (vRNAs). The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this group.


Pssm-ID: 349358 [Multi-domain]  Cd Length: 85  Bit Score: 113.54  E-value: 1.42e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553    5 IFANCIFCLKVKYLPR-QQKKKLQTDIKENGGKFSFLLNPQCTHVIVDSADVLSRCHLNSIQKNDVQIANPAFIQDSVRQ 83
Cdd:cd17726     1 VFSGCQIVLDLKTLPGfKEKKKLKKKITENGGIISYIINKKCTHVVVNNAKALSSYKCRMAQKYGIPVVSLDYIWKCVEA 80


                  ....*
gi 281485553   84 RRLLD 88
Cdd:cd17726    81 GKLLD 85
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 847-1011 1.87e-18

Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 87.43  E-value: 1.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  847 EACMLVFQPELADVLPDLRGknEVIICLDCSSSMEGVTFTQAKQVALYALSLLGEEQKVNIMQFGTGYKElfSYPKCITD 926
Cdd:COG2425   100 LAALLLLAAPASAAVPLLEG--PVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVE--DLPLTADD 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  927 SKM-ATEFImSAAPSMGNTDFWKVLRY-LSLL-YPSEGFRNILLISDGHLQSESL-TLQLVKRNIQHTRVFTCAVGSTAN 1002
Cdd:COG2425   176 GLEdAIEFL-SGLFAGGGTDIAPALRAaLELLeEPDYRNADIVLITDGEAGVSPEeLLREVRAKESGVRLFTVAIGDAGN 254


                  ....*....
gi 281485553 1003 RHILRTLSQ 1011
Cdd:COG2425   255 PGLLEALAD 263
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 870-1026 3.11e-17

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 81.35  E-value: 3.11e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553    870 VIICLDCSSSMEGVTFTQAKQVALYALSLLGEEQK---VNIMQFGTGYKELFSYPKCiTDSKMATEFIMSAAPSM-GNTD 945
Cdd:smart00327    2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDgdrVGLVTFSDDARVLFPLNDS-RSKDALLEALASLSYKLgGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553    946 FWKVLRYLS--LLYPSEGFRN-----ILLISDGHLQSESLTLQLVKRNIQHTRV--FTCAVGSTANRHILRTLSQCGAGV 1016
Cdd:smart00327   81 LGAALQYALenLFSKSAGSRRgapkvVILITDGESNDGPKDLLKAAKELKRSGVkvFVVGVGNDVDEEELKKLASAPGGV 160

                           170
                    ....*....|
gi 281485553   1017 FEYFNSKSKH 1026
Cdd:smart00327  161 YVFLPELLDL 170
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 870-1019 4.90e-15

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 74.52  E-value: 4.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  870 VIICLDCSSSMEGVTFTQAKQVALYALSLLGEEQ---KVNIMQFGTGYKELFSYPKCITDSKMATEFIMSAAPSMGNTDF 946
Cdd:cd00198     3 IVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPpgdRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGTNI 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281485553  947 WKVLRYLSLLYPSEGFRN----ILLISDGHLQSESLTLQLVKRNIQ--HTRVFTCAVGSTANRHILRTLSQCGAGVFEY 1019
Cdd:cd00198    83 GAALRLALELLKSAKRPNarrvIILLTDGEPNDGPELLAEAARELRklGITVYTIGIGDDANEDELKEIADKTTGGAVF 161
VWA_3 pfam13768
von Willebrand factor type A domain;
868-1018 5.76e-13

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 68.58  E-value: 5.76e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553   868 NEVIICLDCSSSMEGVTFTQAKqvalyALSL----LGEEQKVNIMQFGTGYKELFSYPKCITDSKM--ATEFIMSAAPSM 941
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEPKLQKD-----ALSValrqLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLqeAFQFIKTLQPPL 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281485553   942 GNTDFWKVLRY-LSLLYPSEGFRNILLISDGH-LQSESLTLQLVKRNIQHTRVFTCAVGSTANRHILRTLSQCGAGVFE 1018
Cdd:pfam13768   76 GGSDLLGALKEaVRAPASPGYIRHVLLLTDGSpMQGETRVSDLISRAPGKIRFFAYGLGASISAPMLQLLAEASNGTYE 154
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 4-92 4.70e-11

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: 60.46  E-value: 4.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553     4 GIFANCIFCLKVKylPRQQKKKLQTDIKENGGKFSFLLNPQCTHVIVDSADVLSrchlnSIQKNDVQIANPAFIQDSVRQ 83
Cdd:pfam16589    3 NLFEPLRFYINAI--PSPSRSKLKRLIEANGGTVVDNINPAVYIVIAPYNKTDK-----LAENTKLGVVSPQWIFDCVKK 75


                   ....*....
gi 281485553    84 RRLLDVRNY 92
Cdd:pfam16589   76 GKLLPLENY 84
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 1372-1618 1.13e-10

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 61.81  E-value: 1.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  1372 PPHPLGGthpppplplpDGTHLPSPLFGSTHPPPPLFGGTLIPPPSSLfggthlppppplpggthipppppiPGGTLIPP 1451
Cdd:pfam06346    2 PPPPLPG----------DSSTIPLPPGACIPTPPPLPGGGGPPPPPPL------------------------PGSAAIPP 47

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  1452 SSSLFGGTHLPPPPLLSAGTHIPPPPllsagthlppppllpagthippppPITGSTHPPPPSSLfggthlppppplpggt 1531
Cdd:pfam06346   48 PPPLPGGTSIPPPPPLPGAASIPPPP------------------------PLPGSTGIPPPPPL---------------- 87

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  1532 hipppppIPGGTLIPSPSSLFGGthlppppllpAGThipppppitgsthPPPPSSLFGGTHLPPPPPAGTQFSLSPigfI 1611
Cdd:pfam06346   88 -------PGGAGIPPPPPPLPGG----------AGV-------------PPPPPPLPGGPGIPPPPPFPGGPGIPP---P 134


                   ....*..
gi 281485553  1612 PPKLGPP 1618
Cdd:pfam06346  135 PPGMGMP 141
BRCT smart00292
breast cancer carboxy-terminal domain;
4-81 3.18e-08

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 52.38  E-value: 3.18e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281485553      4 GIFANCIFCLkVKYLPRQQKKKLQTDIKENGGKFSFLLN-PQCTHVIVDSADVlSRCHLNSIQKNDVQIANPAFIQDSV 81
Cdd:smart00292    2 KLFKGKTFYI-TGSFDKEERDELKELIEALGGKVTSSLSsKTTTHVIVGSPEG-GKLELLKAIALGIPIVKEEWLLDCL 78
 
Name Accession Description Interval E-value
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 244-557 1.37e-107

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: 347.72  E-value: 1.37e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  244 EEVISSGALSQEVSDLLEVIWTEALGHLENTLLKPVNSMSLNDVSKAEGILLLVKTALKNGDS-PGQLQKTMAEFYRLLP 322
Cdd:cd01437     2 SKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSqGSQLEELSNEFYTLIP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  323 HRHPASEEVNLR---LLAQKEDLCQLVRDMVNVCETNLSK---PNPPSLAKYRALRCKIEHVDQNTEEFSRVRKEVLQNN 396
Cdd:cd01437    82 HDFGMSKPPVIDneeLLKAKRELLEALRDIEIASKLLKDDeddSDDPLDANYEKLKCKIEPLDKDSEEYKIIEKYLKNTH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  397 RS--EQPVDILQIFRVGRVNEATEFL--SKLGNVRLLFHGSPVRNILGILSRGLLLPKVaedrgvqRTDVGNL--GSGIY 470
Cdd:cd01437   162 APttEYTVEVQEIFRVEREGETDRFKpfKKLGNRKLLWHGSRLTNFVGILSQGLRIAPP-------EAPVTGYmfGKGIY 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  471 FSDSLSTSIKYAHAGETDGSRLLVVCDVALGKCVNLFKKDFSLTEAPPGYDSVHGVSETTSVPTDFQDD----------- 539
Cdd:cd01437   235 FADMFSKSANYCHASASDPTGLLLLCEVALGKMNELKKADYMAKELPKGKHSVKGLGKTAPDPSEFEIDldgvvvplgkp 314

                         330       340       350
                  ....*....|....*....|....*....|..
gi 281485553  540 --------------EFVVYKTNQVKMKYIVKF 557
Cdd:cd01437   315 vpsghktdtsllynEYIVYDVAQVRLKYLLEV 346
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 616-726 7.40e-54

Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one light chain and a variable set of heavy chains. ITIs play a role in extracellular matrix (ECM) stabilization and tumour metastasis as well as in plasma protease inhibition. The vault protein inter-alpha-trypsin (VIT) domain described here is found to the N-terminus of a von Willebrand factor type A domain (pfam00092) in ITI heavy chains (ITIHs) and their precursors.


Pssm-ID: 462492 [Multi-domain]  Cd Length: 111  Bit Score: 183.84  E-value: 7.40e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553   616 LDSVHIKGRVIDFVAQVIVFQTYTNQSHVPIEAKYIFPLDDKAAVCGFEAFINGKHIVGEIKEKEEARQEYREAVSQGHG 695
Cdd:pfam08487    1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 281485553   696 AYLMDQDTPDVFTVSVGNLPPRAKVLIKITY 726
Cdd:pfam08487   81 AGLLEQDTPDVFTTSVGNIPPGEKVTVELTY 111
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 382-559 7.42e-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: 181.38  E-value: 7.42e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553   382 TEEFSRVRKEVLQNNRSEQ--PVDILQIFRVGRVNEATEFLS--KLGNVRLLFHGSPVRNILGILSRGLLLPKVAEDRGV 457
Cdd:pfam00644    1 SEEYQIIEKYFLSTHDPTHgyPLFILEIFRVQRDGEWERFQPkkKLRNRRLLWHGSRLTNFLGILSQGLRIAPPEAPVTG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553   458 QRtdvgnLGSGIYFSDSLSTSIKYAHAGETDGSRLLVVCDVALGKCVNLFKKDFsLTEAPPGYDSVHGVSETTS------ 531
Cdd:pfam00644   81 YM-----FGKGIYFADDASKSANYCPPSEAHGNGLMLLSEVALGDMNELKKADY-AEKLPPGKHSVKGLGKTAPesfvdl 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 281485553   532 --VPT-----------DFQDDEFVVYKTNQVKMKYIVKFCT 559
Cdd:pfam00644  155 dgVPLgklvatgydssVLLYNEYVVYNVNQVRPKYLLEVKF 195
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
603-728 1.17e-45

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 160.99  E-value: 1.17e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553    603 KAGLQDASANPVPLDSVHIKGRVIDFVAQVIVFQTYTNQShVPIEAKYIFPLDDKAAVCGFEAF-INGKHIVGEIKEKEE 681
Cdd:smart00609    4 KRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRA-VPAQEVTFDVELPKTAFISNFAMtIDGKTYVGEIKEKEV 82

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 281485553    682 ARQEYREAVSQGHGAYLMDQDTP--DVFTVSVgNLPPRAKVLIKITYIT 728
Cdd:smart00609   83 AQKQYEKAVSQGKTAGLVRASGRsmEQFTVSV-NVAPGSKVTFELTYEE 130
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 278-558 6.65e-31

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 131.50  E-value: 6.65e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  278 PVNSMSLNDVSKAEGILLLVKTALKNGDsPGQLQKTMAEFYRLLPH----RHPASEEVNlrllaQKEDL-CQLvrDMV-- 350
Cdd:PLN03124  326 PLGKLSKSTILKGYEVLKRIAEVISRSD-RETLEELSGEFYTVIPHdfgfKKMRQFTID-----TPQKLkHKL--EMVea 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  351 --------NVCETNLSKPNPPSLAKYRALRCKIEHVDQNTEEFSRVrKEVLQNNRSEQ----PVDILQIFRVGRVNEATE 418
Cdd:PLN03124  398 lgeieiatKLLKDDIGEQDDPLYAHYKRLNCELEPLDTDSEEFSMI-AKYLENTHGQThsgyTLEIVQIFKVSREGEDER 476

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  419 F--LSKLGNVRLLFHGSPVRNILGILSRGL-LLPKVAEDRGVQrtdvgnLGSGIYFSDSLSTSIKYAHAGETDGSRLLVV 495
Cdd:PLN03124  477 FqkFSSTKNRMLLWHGSRLTNWTGILSQGLrIAPPEAPSTGYM------FGKGVYFADMFSKSANYCYASAANPDGVLLL 550

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  496 CDVALGKCVNLFKKDFSLTEAPPGYDSVHGVSETTSVPTDFQ--DD----------------------EFVVYKTNQVKM 551
Cdd:PLN03124  551 CEVALGDMNELLQADYNANKLPPGKLSTKGVGRTVPDPSEAKtlEDgvvvplgkpvespyskgsleynEYIVYNVDQIRM 630


                  ....*....
gi 281485553  552 KYI--VKFC 558
Cdd:PLN03124  631 RYVlqVKFN 639
BRCT_PARP4_like cd17726
BRCT domain of poly [ADP-ribose] polymerase 4 (PARP-4) and similar proteins; PARP-4, also ...
 5-88 1.42e-29

BRCT domain of poly [ADP-ribose] polymerase 4 (PARP-4) and similar proteins; PARP-4, also termed 193 kDa vault protein, or ADP-ribosyltransferase diphtheria toxin-like 4 (ARTD4), or PARP-related/IalphaI-related H5/proline-rich (PH5P), or vault poly(ADP-ribose) polymerase (VPARP), shows poly(ADP-ribosyl)ation activity that catalyzes the formation of ADP-ribose polymers in response to DNA damage. PARP-4 is a component of the vault ribonucleoprotein particle, at least composed of MVP, PARP4 and one or more vault RNAs (vRNAs). The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this group.


Pssm-ID: 349358 [Multi-domain]  Cd Length: 85  Bit Score: 113.54  E-value: 1.42e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553    5 IFANCIFCLKVKYLPR-QQKKKLQTDIKENGGKFSFLLNPQCTHVIVDSADVLSRCHLNSIQKNDVQIANPAFIQDSVRQ 83
Cdd:cd17726     1 VFSGCQIVLDLKTLPGfKEKKKLKKKITENGGIISYIINKKCTHVVVNNAKALSSYKCRMAQKYGIPVVSLDYIWKCVEA 80


                  ....*
gi 281485553   84 RRLLD 88
Cdd:cd17726    81 GKLLD 85
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
 367-556 9.98e-20

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 96.78  E-value: 9.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  367 KYRALRCKIEHVDQNTEEFSRVRKEVLQNN---RSEQPVDILQIFRVGRVNEATEFL---SKLGNVRLLFHGSPVRNILG 440
Cdd:PLN03123  761 KYKKLHCDISPLPHDSEDYKLIEKYLLTTHaptHTDWSLELEEVFSLEREGEFDKYApykEKLKNRMLLWHGSRLTNFVG 840

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  441 ILSRGL-LLPKVAEDRGVQrtdvgnLGSGIYFSDSLSTSIKYAHAGETDGSRLLVVCDVALGKcVNLFKKDFSLTEAPPG 519
Cdd:PLN03123  841 ILSQGLrIAPPEAPATGYM------FGKGVYFADLVSKSAQYCYTDRKNPVGLMLLSEVALGE-IYELKKAKYMDKPPRG 913

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281485553  520 YDSVHGVSETTSVPTDF---QDD---------------------EFVVYKTNQVKMKYIVK 556
Cdd:PLN03123  914 KHSTKGLGKTVPQESEFvkwRDDvvvpcgkpvpskvkaselmynEYIVYNTAQVKLQFLLK 974
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 847-1011 1.87e-18

Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 87.43  E-value: 1.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  847 EACMLVFQPELADVLPDLRGknEVIICLDCSSSMEGVTFTQAKQVALYALSLLGEEQKVNIMQFGTGYKElfSYPKCITD 926
Cdd:COG2425   100 LAALLLLAAPASAAVPLLEG--PVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVE--DLPLTADD 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  927 SKM-ATEFImSAAPSMGNTDFWKVLRY-LSLL-YPSEGFRNILLISDGHLQSESL-TLQLVKRNIQHTRVFTCAVGSTAN 1002
Cdd:COG2425   176 GLEdAIEFL-SGLFAGGGTDIAPALRAaLELLeEPDYRNADIVLITDGEAGVSPEeLLREVRAKESGVRLFTVAIGDAGN 254


                  ....*....
gi 281485553 1003 RHILRTLSQ 1011
Cdd:COG2425   255 PGLLEALAD 263
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 870-1026 3.11e-17

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 81.35  E-value: 3.11e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553    870 VIICLDCSSSMEGVTFTQAKQVALYALSLLGEEQK---VNIMQFGTGYKELFSYPKCiTDSKMATEFIMSAAPSM-GNTD 945
Cdd:smart00327    2 VVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGPDgdrVGLVTFSDDARVLFPLNDS-RSKDALLEALASLSYKLgGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553    946 FWKVLRYLS--LLYPSEGFRN-----ILLISDGHLQSESLTLQLVKRNIQHTRV--FTCAVGSTANRHILRTLSQCGAGV 1016
Cdd:smart00327   81 LGAALQYALenLFSKSAGSRRgapkvVILITDGESNDGPKDLLKAAKELKRSGVkvFVVGVGNDVDEEELKKLASAPGGV 160

                           170
                    ....*....|
gi 281485553   1017 FEYFNSKSKH 1026
Cdd:smart00327  161 YVFLPELLDL 170
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 870-1019 4.90e-15

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 74.52  E-value: 4.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  870 VIICLDCSSSMEGVTFTQAKQVALYALSLLGEEQ---KVNIMQFGTGYKELFSYPKCITDSKMATEFIMSAAPSMGNTDF 946
Cdd:cd00198     3 IVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPpgdRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGTNI 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281485553  947 WKVLRYLSLLYPSEGFRN----ILLISDGHLQSESLTLQLVKRNIQ--HTRVFTCAVGSTANRHILRTLSQCGAGVFEY 1019
Cdd:cd00198    83 GAALRLALELLKSAKRPNarrvIILLTDGEPNDGPELLAEAARELRklGITVYTIGIGDDANEDELKEIADKTTGGAVF 161
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 869-1038 3.41e-14

vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- two heavy chains and one light chain (bikunin). Bikunin confers the protease-inhibitor function while the heavy chains are involved in rendering stability to the extracellular matrix by binding to hyaluronic acid. The heavy chains carry the VWA domain with a conserved MIDAS motif. Although the exact role of the VWA domains remains unknown, it has been speculated to be involved in mediating protein-protein interactions with the components of the extracellular matrix.


Pssm-ID: 238738 [Multi-domain]  Cd Length: 171  Bit Score: 72.25  E-value: 3.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  869 EVIICLDCSSSMEGVTFTQAKQVALYALSLLGEEQKVNIMQFGTGYKELFSYPKCITDSKM--ATEFI--MSAapsMGNT 944
Cdd:cd01461     4 EVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVaaAIEYVnrLQA---LGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  945 DFWKVL-RYLSLLYPSEG-FRNILLISDGHLQSESLTLQLVKRNIQHT-RVFTCAVGSTANRHILRTLSQCGAGVFEYFN 1021
Cdd:cd01461    81 NMNDALeAALELLNSSPGsVPQIILLTDGEVTNESQILKNVREALSGRiRLFTFGIGSDVNTYLLERLAREGRGIARRIY 160

                         170
                  ....*....|....*..
gi 281485553 1022 SKSkhswkkQIEAQMTR 1038
Cdd:cd01461   161 ETD------DIESQLLR 171
VIT_2 pfam13757
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 609-680 4.78e-13

Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one light chain and a variable set of heavy chains. ITIs play a role in extracellular matrix (ECM) stabilization and tumour metastasis as well as in plasma protease inhibition. The vault protein inter-alpha-trypsin (VIT) domain described here is found to the N-terminus of a von Willebrand factor type A domain (pfam00092) in ITI heavy chains (ITIHs) and their precursors.


Pssm-ID: 404621  Cd Length: 78  Bit Score: 65.95  E-value: 4.78e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281485553   609 ASANPVPLDSVHIKGRVIDFVAQVIVFQTYTNQSHVPIEAKYIFPLDDKAAVCGFEAFINGKHIVGEIKEKE 680
Cdd:pfam13757    7 STRTPLPLKASRVSACVNGYSLGVTASLTYYNPQPYPVEGVFVYPLDEGTTVVGFEAEIAGRVISVQLKERE 78
VWA_3 pfam13768
von Willebrand factor type A domain;
868-1018 5.76e-13

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 68.58  E-value: 5.76e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553   868 NEVIICLDCSSSMEGVTFTQAKqvalyALSL----LGEEQKVNIMQFGTGYKELFSYPKCITDSKM--ATEFIMSAAPSM 941
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEPKLQKD-----ALSValrqLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLqeAFQFIKTLQPPL 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281485553   942 GNTDFWKVLRY-LSLLYPSEGFRNILLISDGH-LQSESLTLQLVKRNIQHTRVFTCAVGSTANRHILRTLSQCGAGVFE 1018
Cdd:pfam13768   76 GGSDLLGALKEaVRAPASPGYIRHVLLLTDGSpMQGETRVSDLISRAPGKIRFFAYGLGASISAPMLQLLAEASNGTYE 154
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 869-1041 1.03e-11

Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only];


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 67.82  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  869 EVIICLDCSSSMEGVTFTQAKQVALYALSLLGEEQKVNIMQFGTGYKELFSyPKCITDSKMATEFIMSAAPSmGNTDFWK 948
Cdd:COG2304    93 NLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLP-PTPATDRAKILAAIDRLQAG-GGTALGA 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  949 VLRY-LSLL--YPSEGFRN-ILLISDGH----LQSESLTLQLVKRNIQ-HTRVFTCAVGSTANRHILRTLSQCGAGVFEY 1019
Cdd:COG2304   171 GLELaYELArkHFIPGRVNrVILLTDGDanvgITDPEELLKLAEEAREeGITLTTLGVGSDYNEDLLERLADAGGGNYYY 250

                         170       180
                  ....*....|....*....|..
gi 281485553 1020 FNSKSkhswkkQIEAQMTRIRS 1041
Cdd:COG2304   251 IDDPE------EAEKVFVREFS 266
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 4-92 4.70e-11

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: 60.46  E-value: 4.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553     4 GIFANCIFCLKVKylPRQQKKKLQTDIKENGGKFSFLLNPQCTHVIVDSADVLSrchlnSIQKNDVQIANPAFIQDSVRQ 83
Cdd:pfam16589    3 NLFEPLRFYINAI--PSPSRSKLKRLIEANGGTVVDNINPAVYIVIAPYNKTDK-----LAENTKLGVVSPQWIFDCVKK 75


                   ....*....
gi 281485553    84 RRLLDVRNY 92
Cdd:pfam16589   76 GKLLPLENY 84
VWA pfam00092
von Willebrand factor type A domain;
869-1025 5.41e-11

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 63.45  E-value: 5.41e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553   869 EVIICLDCSSSMEGVTFTQAKQVALYALSLLGEEQK---VNIMQFGTGYKELFSYPKcITDSKMATEFIMSAAPSMGNTD 945
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIGPDgtrVGLVQYSSDVRTEFPLND-YSSKEELLSAVDNLRYLGGGTT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553   946 F-WKVLRYL--SLLYPSEGFR-----NILLISDGHLQSESLT--LQLVKRniQHTRVFTCAVGSTANRHiLRTLSQCGAG 1015
Cdd:pfam00092   80 NtGKALKYAleNLFSSAAGARpgapkVVVLLTDGRSQDGDPEevARELKS--AGVTVFAVGVGNADDEE-LRKIASEPGE 156

                          170
                   ....*....|
gi 281485553  1016 VFEYFNSKSK 1025
Cdd:pfam00092  157 GHVFTVSDFE 166
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 1372-1618 1.13e-10

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 61.81  E-value: 1.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  1372 PPHPLGGthpppplplpDGTHLPSPLFGSTHPPPPLFGGTLIPPPSSLfggthlppppplpggthipppppiPGGTLIPP 1451
Cdd:pfam06346    2 PPPPLPG----------DSSTIPLPPGACIPTPPPLPGGGGPPPPPPL------------------------PGSAAIPP 47

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  1452 SSSLFGGTHLPPPPLLSAGTHIPPPPllsagthlppppllpagthippppPITGSTHPPPPSSLfggthlppppplpggt 1531
Cdd:pfam06346   48 PPPLPGGTSIPPPPPLPGAASIPPPP------------------------PLPGSTGIPPPPPL---------------- 87

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  1532 hipppppIPGGTLIPSPSSLFGGthlppppllpAGThipppppitgsthPPPPSSLFGGTHLPPPPPAGTQFSLSPigfI 1611
Cdd:pfam06346   88 -------PGGAGIPPPPPPLPGG----------AGV-------------PPPPPPLPGGPGIPPPPPFPGGPGIPP---P 134


                   ....*..
gi 281485553  1612 PPKLGPP 1618
Cdd:pfam06346  135 PPGMGMP 141
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 429-553 9.34e-10

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: 58.73  E-value: 9.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  429 LFHGSPVRNILGILSRGLLLPKVaedrGVQRTDvGNLGSGIYFSDSLSTSIKYAHAG----------------ETDGSRL 492
Cdd:cd01341     2 LFHGSPPGNVISILKLGLRPASY----GVLLNG-GMFGKGIYSAPNISKSNGYSVGCdgqhvfqngkpkvcgrELCVFGF 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281485553  493 LVVCDVALGKCVNLFKKDFSLTEAPPGYDSVHGVSETTSVpTDFQDDEFVVY-KTNQVKMKY 553
Cdd:cd01341    77 LTLGVMSGATEESSRVLFPRNFRGATGAEVVDLLVAMCRD-ALLLPREYIIFePYSQVSIRY 137
BRCT_TopBP1_rpt2_like cd17731
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 4-84 3.42e-09

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: 55.24  E-value: 3.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553    4 GIFANCIFClkVKYLPRQQKKKLQTDIKENGGKFSFLLNPQCTHVIVDSADvlSRCHLNSIQKNDVQIANPAFIQDSVRQ 83
Cdd:cd17731     1 PPFKGLVIC--VTGFDSEERKEIQQLVEQNGGSYSPDLSKNCTHLIAGSPS--GQKYEFARKWNSIHIVTPEWLYDSIEA 76


                  .
gi 281485553   84 R 84
Cdd:cd17731    77 G 77
BRCT smart00292
breast cancer carboxy-terminal domain;
4-81 3.18e-08

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 52.38  E-value: 3.18e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281485553      4 GIFANCIFCLkVKYLPRQQKKKLQTDIKENGGKFSFLLN-PQCTHVIVDSADVlSRCHLNSIQKNDVQIANPAFIQDSV 81
Cdd:smart00292    2 KLFKGKTFYI-TGSFDKEERDELKELIEALGGKVTSSLSsKTTTHVIVGSPEG-GKLELLKAIALGIPIVKEEWLLDCL 78
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 376-557 9.83e-08

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: 54.91  E-value: 9.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  376 EHVD--QNTEEFSRvrkevlQNNRSEQPVDILQIFRVG--RVNEATEFLSKLGNVRLLFHGSPVRNilGILSRGLllpkv 451
Cdd:cd01438    41 EHRDggNAGGIFNR------YNIIRIQKVVNKKLRERYchRQKEIAEENHNHHNERMLFHGSPFIN--AIIHKGF----- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  452 aEDRGVQRTdvGNLGSGIYFSDSLSTSIKYAH--AGET------DGS-----RLLVVCDVALGKCVNLFKKdFSLTEAPP 518
Cdd:cd01438   108 -DERHAYIG--GMFGAGIYFAENSSKSNQYVYgiGGGTgcpthkDRScyvchRQMLFCRVTLGKSFLQFSA-MKMAHAPP 183

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 281485553  519 GYDSVHGVSETTSVPTdfqdDEFVVYKTNQVKMKYIVKF 557
Cdd:cd01438   184 GHHSVIGRPSVNGLAY----AEYVIYRGEQAYPEYLITY 218
BRCT_PAXIP1_rpt2 cd17710
second BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 5-88 2.07e-07

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: 50.31  E-value: 2.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553    5 IFANCIFCLKvkYLPRQQKKKLQTDIKENGGKFSFLLNPQCTHVIV-DSADVLSRCHLnsiQKNDVQIANPAFIQDSVRQ 83
Cdd:cd17710     1 LFSGVVVCPS--QISAEDRLKLWAMVTFHGGKCQLNLDKKCTHLVTgKASGAKYECAL---KHEGIKIVTPDWVTDCIKA 75


                  ....*
gi 281485553   84 RRLLD 88
Cdd:cd17710    76 KTLLD 80
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 5-81 2.57e-07

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: 49.60  E-value: 2.57e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281485553     5 IFANCIFCLKVkyLPRQQKKKLQTDIKENGGKFSFLLNPQCTHVIVDsadvlSRCH-LNSIQKNDVQIANPAFIQDSV 81
Cdd:pfam00533    5 LFSGKTFVITG--LDGLERDELKELIEKLGGKVTDSLSKKTTHVIVE-----ARTKkYLKAKELGIPIVTEEWLLDCI 75
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 813-1021 5.87e-07

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 53.02  E-value: 5.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  813 EGSSLDSGGFSLHIGLRDAYLPRMWVEKHPEKESEACMLVFQPELADVLPDLRGKNEVIICLDCSSSMEGVT-FTQAKQV 891
Cdd:COG1240    38 LLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENrLEAAKGA 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  892 ALYALSLLGEEQKVNIMQFGTGYKELFSYPkciTDSKMATEFIMSAAPSmGNTDFWKVLRY-LSLL--YPSEGFRNILLI 968
Cdd:COG1240   118 LLDFLDDYRPRDRVGLVAFGGEAEVLLPLT---RDREALKRALDELPPG-GGTPLGDALALaLELLkrADPARRKVIVLL 193

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 281485553  969 SDGHLQSESLTLQLVKRNIQ--HTRVFTCAVGSTA-NRHILRTLSQCGAGvfEYFN 1021
Cdd:COG1240   194 TDGRDNAGRIDPLEAAELAAaaGIRIYTIGVGTEAvDEGLLREIAEATGG--RYFR 247
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
869-1010 5.98e-06

Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 49.15  E-value: 5.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  869 EVIICLDCSSSMEGVTFTQAKQV------ALYALSLLGEEQKVNIMQFGTGYKELfsYPkcITDskmATEFIMSAAPSMG 942
Cdd:COG4245     7 PVYLLLDTSGSMSGEPIEALNEGlqalidELRQDPYALETVEVSVITFDGEAKVL--LP--LTD---LEDFQPPDLSASG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  943 NTDFWKVLRYL-------SLLYPSEGFRN----ILLISDGHLQSESLT--LQLVKRNIQHTRV--FTCAVGSTANRHILR 1007
Cdd:COG4245    80 GTPLGAALELLldlierrVQKYTAEGKGDwrpvVFLITDGEPTDSDWEaaLQRLKDGEAAKKAniFAIGVGPDADTEVLK 159


                  ...
gi 281485553 1008 TLS 1010
Cdd:COG4245   160 QLT 162
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 18-80 6.27e-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: 6.27e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281485553   18 LPRQQKKKLQTDIKENGGKFSFLLNPQCTHVIVDSADVlSRCHLNSIQKNdVQIANPAFIQDS 80
Cdd:cd00027     8 LDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSPSG-EKYYLAALAWG-IPIVSPEWLLDC 68
BRCT_DNA_ligase_IV_rpt1 cd17722
first BRCT domain of DNA ligase 4 (LIG4) and similar proteins; LIG4 (EC 6.5.1.1), also termed ...
 5-87 1.93e-05

first BRCT domain of DNA ligase 4 (LIG4) and similar proteins; LIG4 (EC 6.5.1.1), also termed DNA ligase IV, or polydeoxyribonucleotide synthase [ATP] 4, is involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. It is a component of the LIG4-XRCC4 complex that is responsible for the NHEJ ligation step. LIG4 contains two BRCT domains. The family corresponds to the first one.


Pssm-ID: 349354 [Multi-domain]  Cd Length: 90  Bit Score: 44.98  E-value: 1.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553    5 IFANCIFCLKVKYLPRQQKKKLQTDIKENGGKFSFLLNPQCTHVIVDSADVLsRChLNSIQKNDVQIANPAFIQDSVRQR 84
Cdd:cd17722     1 IFEGVEFCVMSDMSSPKSKAELEKLIKENGGKVVQNPGAPDTICVIAGREVV-KV-KNLIKSGGHDVVKPSWLLDCIARK 78


                  ...
gi 281485553   85 RLL 87
Cdd:cd17722    79 ELL 81
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 1367-1482 4.30e-05

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 45.63  E-value: 4.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  1367 IPSSLPPHPLGGTHPPPPLPLPDGTHLPSPLFGSTH--PPPPLFGGTLIPPPSSLfggthlppppplPGGTHIPPPPPIP 1444
Cdd:pfam06346   21 IPTPPPLPGGGGPPPPPPLPGSAAIPPPPPLPGGTSipPPPPLPGAASIPPPPPL------------PGSTGIPPPPPLP 88

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 281485553  1445 GGTLI-PPSSSLFGGTHL-PPPPLLSAGTHIPPPPLLSAG 1482
Cdd:pfam06346   89 GGAGIpPPPPPLPGGAGVpPPPPPLPGGPGIPPPPPFPGG 128
VWA_2 pfam13519
von Willebrand factor type A domain;
870-968 5.84e-05

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 43.82  E-value: 5.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553   870 VIICLDCSSSMEGVT-----FTQAKQVALYALSLLGeEQKVNIMQFGTGYkELFSYPKciTDSKMATEFIMSAAPSMGNT 944
Cdd:pfam13519    1 LVFVLDTSGSMRNGDygptrLEAAKDAVLALLKSLP-GDRVGLVTFGDGP-EVLIPLT--KDRAKILRALRRLEPKGGGT 76

                           90       100
                   ....*....|....*....|....*..
gi 281485553   945 DFWKVLRYLSLLYPSEGFRN---ILLI 968
Cdd:pfam13519   77 NLAAALQLARAALKHRRKNQprrIVLI 103
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 1545-1641 9.29e-05

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 44.86  E-value: 9.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  1545 IPSPSSLFGGTHLPPPPLLPAGTHIPPPPPITGSTHPPPPSSLFGGTHLPPPPPagtqfsLSPIGFIPPklgPPKLShsh 1624
Cdd:pfam06346   21 IPTPPPLPGGGGPPPPPPLPGSAAIPPPPPLPGGTSIPPPPPLPGAASIPPPPP------LPGSTGIPP---PPPLP--- 88

                           90
                   ....*....|....*..
gi 281485553  1625 klvGDTNIHDSEPPLLG 1641
Cdd:pfam06346   89 ---GGAGIPPPPPPLPG 102
BRCT_Rev1 cd17719
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ...
 5-92 1.75e-04

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: 42.17  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553    5 IFANC-IFCLKVKYLPRQQKKKLqtdIKENGGKFSFLLNPQ-CTHVIvdsADVLSRCHLNSIQK-NDVQIANPAFIQDSV 81
Cdd:cd17719     1 IFKGVvIYVNGYTDPSADELKRL---ILLHGGQYEHYYSRSrVTHII---ATNLPGSKIKKLKKaRNYKVVRPEWIVDSI 74

                          90
                  ....*....|.
gi 281485553   82 RQRRLLDVRNY 92
Cdd:cd17719    75 KAGRLLPEAPY 85
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 869-1002 6.38e-04

VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup have a conserved MIDAS motif, however, their biochemical function is not well characterised.


Pssm-ID: 238739 [Multi-domain]  Cd Length: 152  Bit Score: 42.33  E-value: 6.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  869 EVIICLDCSSSMEGVTFTQAKQVAL-YALSLLGEEQKVNIMQFGTGYkELFSYPKCITDSKmATEFIMsAAPSMGNTDFW 947
Cdd:cd01462     2 PVILLVDQSGSMYGAPEEVAKAVALaLLRIALAENRDTYLILFDSEF-QTKIVDKTDDLEE-PVEFLS-GVQLGGGTDIN 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  948 KVLRYLSLLYPSEGFRN--ILLISDGH---LQSESLTLQLVKRNIQHtRVFTCAVGSTAN 1002
Cdd:cd01462    79 KALRYALELIERRDPRKadIVLITDGYeggVSDELLREVELKRSRVA-RFVALALGDHGN 137
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 869-1001 6.53e-04

VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The alpha 2 and delta subunits result from proteolytic processing of a single gene product and carries at its N-terminus the VWA and cache domains, The alpha 2 delta gene family has orthologues in D. melanogaster and C. elegans but none have been detected in aither A. thaliana or yeast. The exact biochemical function of the VWA domain is not known but the alpha 2 delta complex has been shown to regulate various functional properties of the channel complex.


Pssm-ID: 238740 [Multi-domain]  Cd Length: 190  Bit Score: 42.77  E-value: 6.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485553  869 EVIICLDCSSSMEGVTFTQAKQVALYALSLLGEEQKVNIMQFGtgyKELFSYPKCITDSKMA------TEFI--MSAAPS 940
Cdd:cd01463    15 DIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFS---NEVNPVVPCFNDTLVQattsnkKVLKeaLDMLEA 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281485553  941 MGNTDFWKVLRY-LSLLYP----------SEGFRNILLISDGhlQSESLTLQLVKRNIQH-----TRVFTCAVGSTA 1001
Cdd:cd01463    92 KGIANYTKALEFaFSLLLKnlqsnhsgsrSQCNQAIMLITDG--VPENYKEIFDKYNWDKnseipVRVFTYLIGREV 166
BRCT_PAXIP1_rpt3 cd17711
third BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 9-52 7.46e-03

third 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 third BRCT domain.


Pssm-ID: 349343  Cd Length: 81  Bit Score: 37.24  E-value: 7.46e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 281485553    9 CIFCLK--VKYLPRQQKKKLQTDIKENGGKFSFLLNPQCTHVIVDS 52
Cdd:cd17711     2 CVFFIAdyPEQMGDQEIATWKKVIEEHGGEVVDEYSPRVTHVICES 47
 
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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