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Conserved domains on  [gi|112789550|ref|NP_006428|]
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protein mono-ADP-ribosyltransferase PARP4 [Homo sapiens]

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 ...
 251-565 1.37e-110

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: 355.42  E-value: 1.37e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  251 EEVMNSSTLSQEVSDLVEMIWAEALGHLEHMLLKPVNRISLNDVSKAEGILLLVKAALKNGE-TAEQLQKMMTEFYRLIP 329
Cdd:cd01437     2 SKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSsQGSQLEELSNEFYTLIP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  330 HKGTMPKEVNLG---LLAKKADLCQLIRDMVNVCETNLSK---PNPPSLAKYRALRCKIEHVEQNTEEFLRVRKEVLQNH 403
Cdd:cd01437    82 HDFGMSKPPVIDneeLLKAKRELLEALRDIEIASKLLKDDeddSDDPLDANYEKLKCKIEPLDKDSEEYKIIEKYLKNTH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  404 HS--KSPVDVLQIFRVGRVNETTEFL--SKLGNVRPLLHGSPVQNIVGILCRGLLLPKVvedrgvqRTDVGNL--GSGIY 477
Cdd:cd01437   162 APttEYTVEVQEIFRVEREGETDRFKpfKKLGNRKLLWHGSRLTNFVGILSQGLRIAPP-------EAPVTGYmfGKGIY 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  478 FSDSLSTSIKYSHPGETDGTRLLLICDVALGKCMDLHEKDFSLTEAPPGYDSVHGVSQTASVTTDFEDD----------- 546
Cdd:cd01437   235 FADMFSKSANYCHASASDPTGLLLLCEVALGKMNELKKADYMAKELPKGKHSVKGLGKTAPDPSEFEIDldgvvvplgkp 314

                         330       340       350
                  ....*....|....*....|....*....|...
gi 112789550  547 --------------EFVVYKTNQVKMKYIIKFS 565
Cdd:cd01437   315 vpsghktdtsllynEYIVYDVAQVRLKYLLEVK 347
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 623-733 2.89e-52

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: 178.83  E-value: 2.89e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550   623 LEDVHIKGRIIDTVAQVIVFQTYTNKSHVPIEAKYIFPLDDKAAVCGFEAFINGKHIVGEIKEKEEAQQEYLEAVTQGHG 702
Cdd:pfam08487    1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 112789550   703 AYLMSQDAPDVFTVSVGNLPPKAKVLIKITY 733
Cdd:pfam08487   81 AGLLEQDTPDVFTTSVGNIPPGEKVTVELTY 111
BRCT_PARP4_like cd17726
BRCT domain of poly [ADP-ribose] polymerase 4 (PARP-4) and similar proteins; PARP-4, also ...
 5-88 5.84e-37

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: 134.34  E-value: 5.84e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550    5 IFANCIFCLKVKYLP-QQQKKKLQTDIKENGGKFSFSLNPQCTHIILDNADVLSQYQLNSIQKNHVHIANPDFIWKSIRE 83
Cdd:cd17726     1 VFSGCQIVLDLKTLPgFKEKKKLKKKITENGGIISYIINKKCTHVVVNNAKALSSYKCRMAQKYGIPVVSLDYIWKCVEA 80


                  ....*
gi 112789550   84 KRLLD 88
Cdd:cd17726    81 GKLLD 85
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 877-1033 1.78e-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: 81.73  E-value: 1.78e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550    877 VIICLDCSSSMEGVTFLQAKQIA---LHALSLVGEKQKVNIIQFGTGYKELFSYPKHiTSNTMAAEFIMSATPTM-GNTD 952
Cdd:smart00327    2 VVFLLDGSGSMGGNRFELAKEFVlklVEQLDIGPDGDRVGLVTFSDDARVLFPLNDS-RSKDALLEALASLSYKLgGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550    953 FWKTLRYLS--LLYPARGSRN-----ILLVSDGHLQDESL-TLQLVKR-SRPHTRLFACGIGSTANRHVLRILSQCGAGV 1023
Cdd:smart00327   81 LGAALQYALenLFSKSAGSRRgapkvVILITDGESNDGPKdLLKAAKElKRSGVKVFVVGVGNDVDEEELKKLASAPGGV 160

                           170
                    ....*....|
gi 112789550   1024 FEYFNAKSKH 1033
Cdd:smart00327  161 YVFLPELLDL 170
KLF1_2_4_N super family cl41729
N-terminal domain of Kruppel-like factor (KLF) 1, KLF2, KLF4, and similar proteins; Kruppel ...
 1317-1485 1.14e-03

N-terminal domain of Kruppel-like factor (KLF) 1, KLF2, KLF4, and similar proteins; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specifity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the related N-terminal domains of KLF1, KLF2, KLF4, and similar proteins.


The actual alignment was detected with superfamily member cd21582:

Pssm-ID: 425360 [Multi-domain]  Cd Length: 335  Bit Score: 43.14  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550 1317 PILAPAvgsYLPPTArAHSP----ASLSFASYRQVASFGSAAPPRqfDASQFSQGPVPGTCADwIPQSA--SCPTGPP-- 1388
Cdd:cd21582   152 PDLDPA---YLQPTS-LHGKfvvkTTMDMGDYSQSINVSKSAPMT--KSSVAPSSSLPFMCPR-IKQENpsTCTISRPmd 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550 1389 QNPPSSPYCGivfsgsslsSAQSAPLQHPGGFTTRPSAGTFPELDSPQLHFSLPTDPDPIR-----GFGsYHPSAS-SPF 1462
Cdd:cd21582   225 GHLGGNSQHG---------FSQRAPLPSRTTPSGGPGGGNSSTAESLMSRDHHPSSQVLSHpplplPQG-YHPSPGyPPF 294

                         170       180
                  ....*....|....*....|...
gi 112789550 1463 HfQPSAASLTANLRLPMASALPE 1485
Cdd:cd21582   295 P-PPPSQPQQYQELMSPGSCLPE 316
 
Name Accession Description Interval E-value
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 251-565 1.37e-110

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: 355.42  E-value: 1.37e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  251 EEVMNSSTLSQEVSDLVEMIWAEALGHLEHMLLKPVNRISLNDVSKAEGILLLVKAALKNGE-TAEQLQKMMTEFYRLIP 329
Cdd:cd01437     2 SKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSsQGSQLEELSNEFYTLIP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  330 HKGTMPKEVNLG---LLAKKADLCQLIRDMVNVCETNLSK---PNPPSLAKYRALRCKIEHVEQNTEEFLRVRKEVLQNH 403
Cdd:cd01437    82 HDFGMSKPPVIDneeLLKAKRELLEALRDIEIASKLLKDDeddSDDPLDANYEKLKCKIEPLDKDSEEYKIIEKYLKNTH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  404 HS--KSPVDVLQIFRVGRVNETTEFL--SKLGNVRPLLHGSPVQNIVGILCRGLLLPKVvedrgvqRTDVGNL--GSGIY 477
Cdd:cd01437   162 APttEYTVEVQEIFRVEREGETDRFKpfKKLGNRKLLWHGSRLTNFVGILSQGLRIAPP-------EAPVTGYmfGKGIY 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  478 FSDSLSTSIKYSHPGETDGTRLLLICDVALGKCMDLHEKDFSLTEAPPGYDSVHGVSQTASVTTDFEDD----------- 546
Cdd:cd01437   235 FADMFSKSANYCHASASDPTGLLLLCEVALGKMNELKKADYMAKELPKGKHSVKGLGKTAPDPSEFEIDldgvvvplgkp 314

                         330       340       350
                  ....*....|....*....|....*....|...
gi 112789550  547 --------------EFVVYKTNQVKMKYIIKFS 565
Cdd:cd01437   315 vpsghktdtsllynEYIVYDVAQVRLKYLLEVK 347
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 623-733 2.89e-52

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: 178.83  E-value: 2.89e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550   623 LEDVHIKGRIIDTVAQVIVFQTYTNKSHVPIEAKYIFPLDDKAAVCGFEAFINGKHIVGEIKEKEEAQQEYLEAVTQGHG 702
Cdd:pfam08487    1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 112789550   703 AYLMSQDAPDVFTVSVGNLPPKAKVLIKITY 733
Cdd:pfam08487   81 AGLLEQDTPDVFTTSVGNIPPGEKVTVELTY 111
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 389-566 3.51e-49

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: 173.67  E-value: 3.51e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550   389 TEEFLRVRKEVLQNHHS--KSPVDVLQIFRVGRVNETTEFLS--KLGNVRPLLHGSPVQNIVGILCRGLLLPKVVEDRGV 464
Cdd:pfam00644    1 SEEYQIIEKYFLSTHDPthGYPLFILEIFRVQRDGEWERFQPkkKLRNRRLLWHGSRLTNFLGILSQGLRIAPPEAPVTG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550   465 QRtdvgnLGSGIYFSDSLSTSIKYSHPGETDGTRLLLICDVALGKCMDLHEKDFsLTEAPPGYDSVHGVSQTASV----- 539
Cdd:pfam00644   81 YM-----FGKGIYFADDASKSANYCPPSEAHGNGLMLLSEVALGDMNELKKADY-AEKLPPGKHSVKGLGKTAPEsfvdl 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 112789550   540 --------------TTDFEDDEFVVYKTNQVKMKYIIKFSM 566
Cdd:pfam00644  155 dgvplgklvatgydSSVLLYNEYVVYNVNQVRPKYLLEVKF 195
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
607-735 2.10e-47

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 165.99  E-value: 2.10e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550    607 SSTKAGLQDASGNLVPLEDVHIKGRIIDTVAQVIVFQTYTNKShVPIEAKYIFPLDDKAAVCGFEAF-INGKHIVGEIKE 685
Cdd:smart00609    1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRA-VPAQEVTFDVELPKTAFISNFAMtIDGKTYVGEIKE 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|..
gi 112789550    686 KEEAQQEYLEAVTQGHGAYLMSQDAP--DVFTVSVgNLPPKAKVLIKITYIT 735
Cdd:smart00609   80 KEVAQKQYEKAVSQGKTAGLVRASGRsmEQFTVSV-NVAPGSKVTFELTYEE 130
BRCT_PARP4_like cd17726
BRCT domain of poly [ADP-ribose] polymerase 4 (PARP-4) and similar proteins; PARP-4, also ...
 5-88 5.84e-37

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: 134.34  E-value: 5.84e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550    5 IFANCIFCLKVKYLP-QQQKKKLQTDIKENGGKFSFSLNPQCTHIILDNADVLSQYQLNSIQKNHVHIANPDFIWKSIRE 83
Cdd:cd17726     1 VFSGCQIVLDLKTLPgFKEKKKLKKKITENGGIISYIINKKCTHVVVNNAKALSSYKCRMAQKYGIPVVSLDYIWKCVEA 80


                  ....*
gi 112789550   84 KRLLD 88
Cdd:cd17726    81 GKLLD 85
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 285-562 3.08e-30

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 129.19  E-value: 3.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  285 PVNRISLNDVSKAEGILLLVKAALKNGETaEQLQKMMTEFYRLIPHKGTMPKEVNLGLLAKKADLCQLirDMV------- 357
Cdd:PLN03124  326 PLGKLSKSTILKGYEVLKRIAEVISRSDR-ETLEELSGEFYTVIPHDFGFKKMRQFTIDTPQKLKHKL--EMVealgeie 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  358 ---NVCETNLSKPNPPSLAKYRALRCKIEHVEQNTEEFLRVRKEVLQNH---HSKSPVDVLQIFRVGRVNETTEF--LSK 429
Cdd:PLN03124  403 iatKLLKDDIGEQDDPLYAHYKRLNCELEPLDTDSEEFSMIAKYLENTHgqtHSGYTLEIVQIFKVSREGEDERFqkFSS 482

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  430 LGNVRPLLHGSPVQNIVGILCRGL-LLPKVVEDRGVQrtdvgnLGSGIYFSDSLSTSIKYSHPGETDGTRLLLICDVALG 508
Cdd:PLN03124  483 TKNRMLLWHGSRLTNWTGILSQGLrIAPPEAPSTGYM------FGKGVYFADMFSKSANYCYASAANPDGVLLLCEVALG 556

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 112789550  509 KCMDLHEKDFSLTEAPPGYDSVHGVSQTA---SVTTDFED---------------------DEFVVYKTNQVKMKYII 562
Cdd:PLN03124  557 DMNELLQADYNANKLPPGKLSTKGVGRTVpdpSEAKTLEDgvvvplgkpvespyskgsleyNEYIVYNVDQIRMRYVL 634
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 877-1033 1.78e-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: 81.73  E-value: 1.78e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550    877 VIICLDCSSSMEGVTFLQAKQIA---LHALSLVGEKQKVNIIQFGTGYKELFSYPKHiTSNTMAAEFIMSATPTM-GNTD 952
Cdd:smart00327    2 VVFLLDGSGSMGGNRFELAKEFVlklVEQLDIGPDGDRVGLVTFSDDARVLFPLNDS-RSKDALLEALASLSYKLgGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550    953 FWKTLRYLS--LLYPARGSRN-----ILLVSDGHLQDESL-TLQLVKR-SRPHTRLFACGIGSTANRHVLRILSQCGAGV 1023
Cdd:smart00327   81 LGAALQYALenLFSKSAGSRRgapkvVILITDGESNDGPKdLLKAAKElKRSGVKVFVVGVGNDVDEEELKKLASAPGGV 160

                           170
                    ....*....|
gi 112789550   1024 FEYFNAKSKH 1033
Cdd:smart00327  161 YVFLPELLDL 170
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 866-1018 1.39e-16

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 81.65  E-value: 1.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  866 VDLPDLASESEVIICLDCSSSMEGVTFLQAKQIALHALSLVGEKQKVNIIQFGTGYKELFSYPKHiTSNTMAAEFImSAT 945
Cdd:COG2425   110 ASAAVPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVEDLPLTAD-DGLEDAIEFL-SGL 187

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 112789550  946 PTMGNTDFWKTLRY-LSLL-YPARGSRNILLVSDGHLQDESL-TLQLVKRSRPHTRLFACGIGSTANRHVLRILSQ 1018
Cdd:COG2425   188 FAGGGTDIAPALRAaLELLeEPDYRNADIVLITDGEAGVSPEeLLREVRAKESGVRLFTVAIGDAGNPGLLEALAD 263
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 876-1045 7.00e-15

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: 74.17  E-value: 7.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  876 EVIICLDCSSSMEGVTFLQAKQIALHALSLVGEKQKVNIIQFGTGYKELFSYPKHITSNTMAA--EFI--MSAtptMGNT 951
Cdd:cd01461     4 EVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAaiEYVnrLQA---LGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  952 DFWKTL-RYLSLLYPARGS-RNILLVSDGHLQDESLTLQLVKRSRPHT-RLFACGIGSTANRHVLRILSQCGAGVFEYFN 1028
Cdd:cd01461    81 NMNDALeAALELLNSSPGSvPQIILLTDGEVTNESQILKNVREALSGRiRLFTFGIGSDVNTYLLERLAREGRGIARRIY 160

                         170
                  ....*....|....*..
gi 112789550 1029 AKSkhswrkQIEDQMTR 1045
Cdd:cd01461   161 ETD------DIESQLLR 171
VWA pfam00092
von Willebrand factor type A domain;
876-1032 1.59e-13

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 70.38  E-value: 1.59e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550   876 EVIICLDCSSSMEGVTFLQAKQIALH---ALSLVGEKQKVNIIQFGTGYKELFSYPKHiTSNTMAAEFIMSATP-TMGNT 951
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKlveSLDIGPDGTRVGLVQYSSDVRTEFPLNDY-SSKEELLSAVDNLRYlGGGTT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550   952 DFWKTLRYL--SLLYPARGSR-----NILLVSDGHLQDESLT--LQLVKRSRphTRLFACGIGSTANRHvLRILSQCGAG 1022
Cdd:pfam00092   80 NTGKALKYAleNLFSSAAGARpgapkVVVLLTDGRSQDGDPEevARELKSAG--VTVFAVGVGNADDEE-LRKIASEPGE 156

                          170
                   ....*....|
gi 112789550  1023 VFEYFNAKSK 1032
Cdd:pfam00092  157 GHVFTVSDFE 166
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 2-81 3.23e-11

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: 60.77  E-value: 3.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550     2 VMGIFANCIFCLKVkyLPQQQKKKLQTDIKENGGKFSFSLNPQCTHIILDNadvlSQYQLNSIQKNHVHIANPDFIWKSI 81
Cdd:pfam00533    2 KEKLFSGKTFVITG--LDGLERDELKELIEKLGGKVTDSLSKKTTHVIVEA----RTKKYLKAKELGIPIVTEEWLLDCI 75
BRCT smart00292
breast cancer carboxy-terminal domain;
3-81 8.92e-10

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 56.61  E-value: 8.92e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550      3 MGIFANCIFCLkVKYLPQQQKKKLQTDIKENGGKFSFSLN-PQCTHIILDNADVlSQYQLNSIQKNHVHIANPDFIWKSI 81
Cdd:smart00292    1 PKLFKGKTFYI-TGSFDKEERDELKELIEALGGKVTSSLSsKTTTHVIVGSPEG-GKLELLKAIALGIPIVKEEWLLDCL 78
KLF4_N cd21582
N-terminal domain of Kruppel-like factor 4; Kruppel-like factor 4 (KLF4; also known as ...
 1317-1485 1.14e-03

N-terminal domain of Kruppel-like factor 4; Kruppel-like factor 4 (KLF4; also known as Krueppel-like factor 4 or gut-enriched Kruppel-like factor/GKLF) is a protein that, in humans, is encoded by the KLF4 gene. Evidence also suggests that KLF4 is a tumor suppressor in certain cancers, including colorectal cancer, gastric cancer, esophageal squamous cell carcinoma, intestinal cancer, prostate cancer, bladder cancer and lung cancer. It may act as a tumor promoter where increased KLF4 expression has been reported, such as in oral squamous cell carcinoma and in primary breast ductal carcinoma. KLF4 is one of four key factors that are essential for inducing pluripotent stem cells. KLF4 is highly expressed in non-dividing cells and its overexpression induces cell cycle arrest. KLF proteins KLF1, KLF2, KLF4, KLF5, KLF6, and KLF7 are transcriptional activators. KLF4 belongs to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF4, which is related to the N-terminal domains of KLF1 and KLF2.


Pssm-ID: 409228 [Multi-domain]  Cd Length: 335  Bit Score: 43.14  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550 1317 PILAPAvgsYLPPTArAHSP----ASLSFASYRQVASFGSAAPPRqfDASQFSQGPVPGTCADwIPQSA--SCPTGPP-- 1388
Cdd:cd21582   152 PDLDPA---YLQPTS-LHGKfvvkTTMDMGDYSQSINVSKSAPMT--KSSVAPSSSLPFMCPR-IKQENpsTCTISRPmd 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550 1389 QNPPSSPYCGivfsgsslsSAQSAPLQHPGGFTTRPSAGTFPELDSPQLHFSLPTDPDPIR-----GFGsYHPSAS-SPF 1462
Cdd:cd21582   225 GHLGGNSQHG---------FSQRAPLPSRTTPSGGPGGGNSSTAESLMSRDHHPSSQVLSHpplplPQG-YHPSPGyPPF 294

                         170       180
                  ....*....|....*....|...
gi 112789550 1463 HfQPSAASLTANLRLPMASALPE 1485
Cdd:cd21582   295 P-PPPSQPQQYQELMSPGSCLPE 316
 
Name Accession Description Interval E-value
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 251-565 1.37e-110

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: 355.42  E-value: 1.37e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  251 EEVMNSSTLSQEVSDLVEMIWAEALGHLEHMLLKPVNRISLNDVSKAEGILLLVKAALKNGE-TAEQLQKMMTEFYRLIP 329
Cdd:cd01437     2 SKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSsQGSQLEELSNEFYTLIP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  330 HKGTMPKEVNLG---LLAKKADLCQLIRDMVNVCETNLSK---PNPPSLAKYRALRCKIEHVEQNTEEFLRVRKEVLQNH 403
Cdd:cd01437    82 HDFGMSKPPVIDneeLLKAKRELLEALRDIEIASKLLKDDeddSDDPLDANYEKLKCKIEPLDKDSEEYKIIEKYLKNTH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  404 HS--KSPVDVLQIFRVGRVNETTEFL--SKLGNVRPLLHGSPVQNIVGILCRGLLLPKVvedrgvqRTDVGNL--GSGIY 477
Cdd:cd01437   162 APttEYTVEVQEIFRVEREGETDRFKpfKKLGNRKLLWHGSRLTNFVGILSQGLRIAPP-------EAPVTGYmfGKGIY 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  478 FSDSLSTSIKYSHPGETDGTRLLLICDVALGKCMDLHEKDFSLTEAPPGYDSVHGVSQTASVTTDFEDD----------- 546
Cdd:cd01437   235 FADMFSKSANYCHASASDPTGLLLLCEVALGKMNELKKADYMAKELPKGKHSVKGLGKTAPDPSEFEIDldgvvvplgkp 314

                         330       340       350
                  ....*....|....*....|....*....|...
gi 112789550  547 --------------EFVVYKTNQVKMKYIIKFS 565
Cdd:cd01437   315 vpsghktdtsllynEYIVYDVAQVRLKYLLEVK 347
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 623-733 2.89e-52

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: 178.83  E-value: 2.89e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550   623 LEDVHIKGRIIDTVAQVIVFQTYTNKSHVPIEAKYIFPLDDKAAVCGFEAFINGKHIVGEIKEKEEAQQEYLEAVTQGHG 702
Cdd:pfam08487    1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 112789550   703 AYLMSQDAPDVFTVSVGNLPPKAKVLIKITY 733
Cdd:pfam08487   81 AGLLEQDTPDVFTTSVGNIPPGEKVTVELTY 111
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 389-566 3.51e-49

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: 173.67  E-value: 3.51e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550   389 TEEFLRVRKEVLQNHHS--KSPVDVLQIFRVGRVNETTEFLS--KLGNVRPLLHGSPVQNIVGILCRGLLLPKVVEDRGV 464
Cdd:pfam00644    1 SEEYQIIEKYFLSTHDPthGYPLFILEIFRVQRDGEWERFQPkkKLRNRRLLWHGSRLTNFLGILSQGLRIAPPEAPVTG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550   465 QRtdvgnLGSGIYFSDSLSTSIKYSHPGETDGTRLLLICDVALGKCMDLHEKDFsLTEAPPGYDSVHGVSQTASV----- 539
Cdd:pfam00644   81 YM-----FGKGIYFADDASKSANYCPPSEAHGNGLMLLSEVALGDMNELKKADY-AEKLPPGKHSVKGLGKTAPEsfvdl 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 112789550   540 --------------TTDFEDDEFVVYKTNQVKMKYIIKFSM 566
Cdd:pfam00644  155 dgvplgklvatgydSSVLLYNEYVVYNVNQVRPKYLLEVKF 195
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
607-735 2.10e-47

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 165.99  E-value: 2.10e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550    607 SSTKAGLQDASGNLVPLEDVHIKGRIIDTVAQVIVFQTYTNKShVPIEAKYIFPLDDKAAVCGFEAF-INGKHIVGEIKE 685
Cdd:smart00609    1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRA-VPAQEVTFDVELPKTAFISNFAMtIDGKTYVGEIKE 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|..
gi 112789550    686 KEEAQQEYLEAVTQGHGAYLMSQDAP--DVFTVSVgNLPPKAKVLIKITYIT 735
Cdd:smart00609   80 KEVAQKQYEKAVSQGKTAGLVRASGRsmEQFTVSV-NVAPGSKVTFELTYEE 130
BRCT_PARP4_like cd17726
BRCT domain of poly [ADP-ribose] polymerase 4 (PARP-4) and similar proteins; PARP-4, also ...
 5-88 5.84e-37

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: 134.34  E-value: 5.84e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550    5 IFANCIFCLKVKYLP-QQQKKKLQTDIKENGGKFSFSLNPQCTHIILDNADVLSQYQLNSIQKNHVHIANPDFIWKSIRE 83
Cdd:cd17726     1 VFSGCQIVLDLKTLPgFKEKKKLKKKITENGGIISYIINKKCTHVVVNNAKALSSYKCRMAQKYGIPVVSLDYIWKCVEA 80


                  ....*
gi 112789550   84 KRLLD 88
Cdd:cd17726    81 GKLLD 85
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 285-562 3.08e-30

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 129.19  E-value: 3.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  285 PVNRISLNDVSKAEGILLLVKAALKNGETaEQLQKMMTEFYRLIPHKGTMPKEVNLGLLAKKADLCQLirDMV------- 357
Cdd:PLN03124  326 PLGKLSKSTILKGYEVLKRIAEVISRSDR-ETLEELSGEFYTVIPHDFGFKKMRQFTIDTPQKLKHKL--EMVealgeie 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  358 ---NVCETNLSKPNPPSLAKYRALRCKIEHVEQNTEEFLRVRKEVLQNH---HSKSPVDVLQIFRVGRVNETTEF--LSK 429
Cdd:PLN03124  403 iatKLLKDDIGEQDDPLYAHYKRLNCELEPLDTDSEEFSMIAKYLENTHgqtHSGYTLEIVQIFKVSREGEDERFqkFSS 482

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  430 LGNVRPLLHGSPVQNIVGILCRGL-LLPKVVEDRGVQrtdvgnLGSGIYFSDSLSTSIKYSHPGETDGTRLLLICDVALG 508
Cdd:PLN03124  483 TKNRMLLWHGSRLTNWTGILSQGLrIAPPEAPSTGYM------FGKGVYFADMFSKSANYCYASAANPDGVLLLCEVALG 556

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 112789550  509 KCMDLHEKDFSLTEAPPGYDSVHGVSQTA---SVTTDFED---------------------DEFVVYKTNQVKMKYII 562
Cdd:PLN03124  557 DMNELLQADYNANKLPPGKLSTKGVGRTVpdpSEAKTLEDgvvvplgkpvespyskgsleyNEYIVYNVDQIRMRYVL 634
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
 374-563 8.89e-18

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 89.85  E-value: 8.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  374 KYRALRCKIEHVEQNTEEFLRVRKEVLQNH---HSKSPVDVLQIFRVGRVNETTEFL---SKLGNVRPLLHGSPVQNIVG 447
Cdd:PLN03123  761 KYKKLHCDISPLPHDSEDYKLIEKYLLTTHaptHTDWSLELEEVFSLEREGEFDKYApykEKLKNRMLLWHGSRLTNFVG 840

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  448 ILCRGL-LLPKVVEDRGVQrtdvgnLGSGIYFSDSLSTSIKYSHPGETDGTRLLLICDVALGKCMDLheKDFSLTEAPP- 525
Cdd:PLN03123  841 ILSQGLrIAPPEAPATGYM------FGKGVYFADLVSKSAQYCYTDRKNPVGLMLLSEVALGEIYEL--KKAKYMDKPPr 912

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 112789550  526 GYDSVHGVSQTASVTTDF---EDD---------------------EFVVYKTNQVKMKYIIK 563
Cdd:PLN03123  913 GKHSTKGLGKTVPQESEFvkwRDDvvvpcgkpvpskvkaselmynEYIVYNTAQVKLQFLLK 974
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 877-1033 1.78e-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: 81.73  E-value: 1.78e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550    877 VIICLDCSSSMEGVTFLQAKQIA---LHALSLVGEKQKVNIIQFGTGYKELFSYPKHiTSNTMAAEFIMSATPTM-GNTD 952
Cdd:smart00327    2 VVFLLDGSGSMGGNRFELAKEFVlklVEQLDIGPDGDRVGLVTFSDDARVLFPLNDS-RSKDALLEALASLSYKLgGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550    953 FWKTLRYLS--LLYPARGSRN-----ILLVSDGHLQDESL-TLQLVKR-SRPHTRLFACGIGSTANRHVLRILSQCGAGV 1023
Cdd:smart00327   81 LGAALQYALenLFSKSAGSRRgapkvVILITDGESNDGPKdLLKAAKElKRSGVKVFVVGVGNDVDEEELKKLASAPGGV 160

                           170
                    ....*....|
gi 112789550   1024 FEYFNAKSKH 1033
Cdd:smart00327  161 YVFLPELLDL 170
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 866-1018 1.39e-16

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


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 81.65  E-value: 1.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  866 VDLPDLASESEVIICLDCSSSMEGVTFLQAKQIALHALSLVGEKQKVNIIQFGTGYKELFSYPKHiTSNTMAAEFImSAT 945
Cdd:COG2425   110 ASAAVPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVEDLPLTAD-DGLEDAIEFL-SGL 187

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 112789550  946 PTMGNTDFWKTLRY-LSLL-YPARGSRNILLVSDGHLQDESL-TLQLVKRSRPHTRLFACGIGSTANRHVLRILSQ 1018
Cdd:COG2425   188 FAGGGTDIAPALRAaLELLeEPDYRNADIVLITDGEAGVSPEeLLREVRAKESGVRLFTVAIGDAGNPGLLEALAD 263
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 876-1045 7.00e-15

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: 74.17  E-value: 7.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  876 EVIICLDCSSSMEGVTFLQAKQIALHALSLVGEKQKVNIIQFGTGYKELFSYPKHITSNTMAA--EFI--MSAtptMGNT 951
Cdd:cd01461     4 EVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAaiEYVnrLQA---LGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  952 DFWKTL-RYLSLLYPARGS-RNILLVSDGHLQDESLTLQLVKRSRPHT-RLFACGIGSTANRHVLRILSQCGAGVFEYFN 1028
Cdd:cd01461    81 NMNDALeAALELLNSSPGSvPQIILLTDGEVTNESQILKNVREALSGRiRLFTFGIGSDVNTYLLERLAREGRGIARRIY 160

                         170
                  ....*....|....*..
gi 112789550 1029 AKSkhswrkQIEDQMTR 1045
Cdd:cd01461   161 ETD------DIESQLLR 171
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 877-1026 1.15e-14

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: 73.37  E-value: 1.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  877 VIICLDCSSSMEGVTFLQAKQIA---LHALSLVGEKQKVNIIQFGTGYKELFSYPKHITSNTMAAEFIMSATPTMGNTDF 953
Cdd:cd00198     3 IVFLLDVSGSMGGEKLDKAKEALkalVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGTNI 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 112789550  954 WKTLRYLSLLYPARGSRN----ILLVSDGHLQDESLTLQLVKRS--RPHTRLFACGIGSTANRHVLRILSQCGAGVFEY 1026
Cdd:cd00198    83 GAALRLALELLKSAKRPNarrvIILLTDGEPNDGPELLAEAARElrKLGITVYTIGIGDDANEDELKEIADKTTGGAVF 161
VWA pfam00092
von Willebrand factor type A domain;
876-1032 1.59e-13

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 70.38  E-value: 1.59e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550   876 EVIICLDCSSSMEGVTFLQAKQIALH---ALSLVGEKQKVNIIQFGTGYKELFSYPKHiTSNTMAAEFIMSATP-TMGNT 951
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKlveSLDIGPDGTRVGLVQYSSDVRTEFPLNDY-SSKEELLSAVDNLRYlGGGTT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550   952 DFWKTLRYL--SLLYPARGSR-----NILLVSDGHLQDESLT--LQLVKRSRphTRLFACGIGSTANRHvLRILSQCGAG 1022
Cdd:pfam00092   80 NTGKALKYAleNLFSSAAGARpgapkVVVLLTDGRSQDGDPEevARELKSAG--VTVFAVGVGNADDEE-LRKIASEPGE 156

                          170
                   ....*....|
gi 112789550  1023 VFEYFNAKSK 1032
Cdd:pfam00092  157 GHVFTVSDFE 166
VWA_3 pfam13768
von Willebrand factor type A domain;
875-1025 5.01e-13

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 68.58  E-value: 5.01e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550   875 SEVIICLDCSSSMEGVTFLQAKQI--ALHALSlvgEKQKVNIIQFGTGYKELFSYPKHITSNTM--AAEFIMSATPTMGN 950
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEPKLQKDALsvALRQLP---TGDKFAVLGFGTLPRPLFPGWRVVSPRSLqeAFQFIKTLQPPLGG 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 112789550   951 TDFWKTLRYLSLLYPARGS-RNILLVSDGH-LQDESLTLQLVKRSRPHTRLFACGIGSTANRHVLRILSQCGAGVFE 1025
Cdd:pfam13768   78 SDLLGALKEAVRAPASPGYiRHVLLLTDGSpMQGETRVSDLISRAPGKIRFFAYGLGASISAPMLQLLAEASNGTYE 154
VIT_2 pfam13757
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 616-687 3.37e-12

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: 63.64  E-value: 3.37e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 112789550   616 ASGNLVPLEDVHIKGRIIDTVAQVIVFQTYTNKSHVPIEAKYIFPLDDKAAVCGFEAFINGKHIVGEIKEKE 687
Cdd:pfam13757    7 STRTPLPLKASRVSACVNGYSLGVTASLTYYNPQPYPVEGVFVYPLDEGTTVVGFEAEIAGRVISVQLKERE 78
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 875-1026 7.81e-12

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 68.20  E-value: 7.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  875 SEVIICLDCSSSMEGVTFLQAKQIALHALSLVGEKQKVNIIQFGTGYKELFSyPKHITSNTMAAEFIMSATPTmGNTDFW 954
Cdd:COG2304    92 LNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLP-PTPATDRAKILAAIDRLQAG-GGTALG 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  955 KTLRY-LSLL---YPARGSRNILLVSDGH----LQDESLTLQLVKRSRP-HTRLFACGIGSTANRHVLRILSQCGAGVFE 1025
Cdd:COG2304   170 AGLELaYELArkhFIPGRVNRVILLTDGDanvgITDPEELLKLAEEAREeGITLTTLGVGSDYNEDLLERLADAGGGNYY 249


                  .
gi 112789550 1026 Y 1026
Cdd:COG2304   250 Y 250
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 2-81 3.23e-11

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: 60.77  E-value: 3.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550     2 VMGIFANCIFCLKVkyLPQQQKKKLQTDIKENGGKFSFSLNPQCTHIILDNadvlSQYQLNSIQKNHVHIANPDFIWKSI 81
Cdd:pfam00533    2 KEKLFSGKTFVITG--LDGLERDELKELIEKLGGKVTDSLSKKTTHVIVEA----RTKKYLKAKELGIPIVTEEWLLDCI 75
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 4-92 7.51e-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: 60.07  E-value: 7.51e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550     4 GIFANCIFCLKVKylPQQQKKKLQTDIKENGGKFSFSLNPQCTHIILDNADVLSQyqlnsIQKNHVHIANPDFIWKSIRE 83
Cdd:pfam16589    3 NLFEPLRFYINAI--PSPSRSKLKRLIEANGGTVVDNINPAVYIVIAPYNKTDKL-----AENTKLGVVSPQWIFDCVKK 75


                   ....*....
gi 112789550    84 KRLLDVKNY 92
Cdd:pfam16589   76 GKLLPLENY 84
BRCT_TopBP1_rpt2_like cd17731
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 4-82 5.57e-10

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: 57.16  E-value: 5.57e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 112789550    4 GIFANCIFClkVKYLPQQQKKKLQTDIKENGGKFSFSLNPQCTHIILDNADvlSQYQLNSIQKNHVHIANPDFIWKSIR 82
Cdd:cd17731     1 PPFKGLVIC--VTGFDSEERKEIQQLVEQNGGSYSPDLSKNCTHLIAGSPS--GQKYEFARKWNSIHIVTPEWLYDSIE 75
BRCT smart00292
breast cancer carboxy-terminal domain;
3-81 8.92e-10

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 56.61  E-value: 8.92e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550      3 MGIFANCIFCLkVKYLPQQQKKKLQTDIKENGGKFSFSLN-PQCTHIILDNADVlSQYQLNSIQKNHVHIANPDFIWKSI 81
Cdd:smart00292    1 PKLFKGKTFYI-TGSFDKEERDELKELIEALGGKVTSSLSsKTTTHVIVGSPEG-GKLELLKAIALGIPIVKEEWLLDCL 78
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 436-560 3.33e-09

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: 56.80  E-value: 3.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  436 LLHGSPVQNIVGILCRGLLLPKVvedrGVQRTDvGNLGSGIYFSDSLSTSIKYSH-PGETDGT---------------RL 499
Cdd:cd01341     2 LFHGSPPGNVISILKLGLRPASY----GVLLNG-GMFGKGIYSAPNISKSNGYSVgCDGQHVFqngkpkvcgrelcvfGF 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 112789550  500 LLICDVALGKCMDLHEKDFSLTEAPPGYDSVHGVSQTASVTTdFEDDEFVVY-KTNQVKMKY 560
Cdd:cd01341    77 LTLGVMSGATEESSRVLFPRNFRGATGAEVVDLLVAMCRDAL-LLPREYIIFePYSQVSIRY 137
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 419-566 2.93e-07

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: 53.37  E-value: 2.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  419 RVNETTEFLSKLGNVRPLLHGSPVQNivGILCRGLllpkvvEDRGVQRTdvGNLGSGIYFSDSLSTSIKYSH-------- 490
Cdd:cd01438    75 RQKEIAEENHNHHNERMLFHGSPFIN--AIIHKGF------DERHAYIG--GMFGAGIYFAENSSKSNQYVYgigggtgc 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  491 PGETDGT-----RLLLICDVALGKCMdLHEKDFSLTEAPPGYDSVHGVSQTASVTTdfedDEFVVYKTNQVKMKYIIKFS 565
Cdd:cd01438   145 PTHKDRScyvchRQMLFCRVTLGKSF-LQFSAMKMAHAPPGHHSVIGRPSVNGLAY----AEYVIYRGEQAYPEYLITYQ 219


                  .
gi 112789550  566 M 566
Cdd:cd01438   220 I 220
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 18-80 1.07e-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: 47.74  E-value: 1.07e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 112789550   18 LPQQQKKKLQTDIKENGGKFSFSLNPQCTHIILDNADVlSQYQLNSIqKNHVHIANPDFIWKS 80
Cdd:cd00027     8 LDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSPSG-EKYYLAAL-AWGIPIVSPEWLLDC 68
BRCT_PAXIP1_rpt2 cd17710
second BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 5-88 2.15e-06

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


Pssm-ID: 349342 [Multi-domain]  Cd Length: 81  Bit Score: 47.23  E-value: 2.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550    5 IFANCIFCLKvkYLPQQQKKKLQTDIKENGGKFSFSLNPQCTHIILDNAdVLSQYQLnSIQKNHVHIANPDFIWKSIREK 84
Cdd:cd17710     1 LFSGVVVCPS--QISAEDRLKLWAMVTFHGGKCQLNLDKKCTHLVTGKA-SGAKYEC-ALKHEGIKIVTPDWVTDCIKAK 76


                  ....
gi 112789550   85 RLLD 88
Cdd:cd17710    77 TLLD 80
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 820-1029 2.31e-06

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: 51.09  E-value: 2.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  820 EGSSLDSSGFSLHIGLSAAYLPRMWVEKHPEKESEACMLVFQPDLDVDLPDLASESEVIICLDCSSSMEGVTFL-QAKQI 898
Cdd:COG1240    38 LLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENRLeAAKGA 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  899 ALHALSLVGEKQKVNIIQFGTGYKELFSypkhITSNTMAAEFIMSATPTMGNTDFW----KTLRYLSLLYPARgSRNILL 974
Cdd:COG1240   118 LLDFLDDYRPRDRVGLVAFGGEAEVLLP----LTRDREALKRALDELPPGGGTPLGdalaLALELLKRADPAR-RKVIVL 192

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 112789550  975 VSDGHLQDESLTLQLVKR--SRPHTRLFACGIGSTA-NRHVLRILSQCGAGvfEYFNA 1029
Cdd:COG1240   193 LTDGRDNAGRIDPLEAAElaAAAGIRIYTIGVGTEAvDEGLLREIAEATGG--RYFRA 248
VWA_2 pfam13519
von Willebrand factor type A domain;
877-975 2.83e-06

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 47.67  E-value: 2.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550   877 VIICLDCSSSMEGVTFLQAK-QIALHALSLVGEK---QKVNIIQFGTGYkELFSYPKhiTSNTMAAEFIMSATPTMGNTD 952
Cdd:pfam13519    1 LVFVLDTSGSMRNGDYGPTRlEAAKDAVLALLKSlpgDRVGLVTFGDGP-EVLIPLT--KDRAKILRALRRLEPKGGGTN 77

                           90       100
                   ....*....|....*....|....*
gi 112789550   953 FWKTLRYLSLLYPAR--GSRNILLV 975
Cdd:pfam13519   78 LAAALQLARAALKHRrkNQPRRIVL 102
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
876-1014 2.54e-05

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 46.84  E-value: 2.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  876 EVIICLDCSSSMEGV----------TFLQakqiALHALSLVGEKQKVNIIQFGTGYKELFSYpkhitsnTMAAEFIMSAT 945
Cdd:COG4245     7 PVYLLLDTSGSMSGEpiealneglqALID----ELRQDPYALETVEVSVITFDGEAKVLLPL-------TDLEDFQPPDL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  946 PTMGNTDFWKTLRYL-------SLLYPARGSRN----ILLVSDGHLQDESLT--LQLVKR--SRPHTRLFACGIGSTANR 1010
Cdd:COG4245    76 SASGGTPLGAALELLldlierrVQKYTAEGKGDwrpvVFLITDGEPTDSDWEaaLQRLKDgeAAKKANIFAIGVGPDADT 155


                  ....
gi 112789550 1011 HVLR 1014
Cdd:COG4245   156 EVLK 159
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 ...
 5-97 2.65e-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: 44.21  E-value: 2.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550    5 IFANCIFCLKVKYLPQQQKKKLQTDIKENGGKFSFSLNPQCTHIILD---NADVLSQyqlnsIQKNHVHIANPDFIWKSI 81
Cdd:cd17722     1 IFEGVEFCVMSDMSSPKSKAELEKLIKENGGKVVQNPGAPDTICVIAgreVVKVKNL-----IKSGGHDVVKPSWLLDCI 75

                          90
                  ....*....|....*.
gi 112789550   82 REKRLLdvknydPYKP 97
Cdd:cd17722    76 ARKELL------PLEP 85
PARP_reg pfam02877
Poly(ADP-ribose) polymerase, regulatory domain; Poly(ADP-ribose) polymerase catalyzes the ...
 257-356 3.76e-05

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: 45.21  E-value: 3.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550   257 STLSQEVSDLVEMI-----WAEALGHLEHMLLK-PVNRISLNDVSKAEGILLLVKAALKNGETA---EQLQKMMTEFYRL 327
Cdd:pfam02877    1 SKLPPPVQELMKLIfnvemMKKAMKEMKYDAKKmPLGKLSKRQIKKGYEVLKELSELLKKPSLAkakAKLEDLSNRFYTL 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 112789550   328 IPHK-GTMPKEV--NLGLLAKKADLCQLIRDM 356
Cdd:pfam02877   81 IPHDfGRNRPPVidTEEELKEKLELLEALLDI 112
BRCT_BRC1_like_rpt1 cd18435
first (N-terminal) BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) ...
 22-97 6.60e-05

first (N-terminal) BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) and similar proteins; Schizosaccharomyces pombe BRC1 is required for mitotic fidelity, specifically in the G2 phase of the cell cycle. It plays a role in chromatin organization. Members in this family contains six BRCT domains. This family corresponds to the fourth repeat.


Pssm-ID: 349388  Cd Length: 107  Bit Score: 43.85  E-value: 6.60e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 112789550   22 QKKKLqtdIKENGGK-FSFSLNPQCTHIILDNAD--VLSQYQLNSIQKNHVHIANPDFIWKSIREKRLLDvknYDPYKP 97
Cdd:cd18435    35 EVEKL---FIDNGGKiLDLPYDPKLTHVILDDFDspRVVELMKRTGKPRRLHLVKTKWIEDCVDENTLLD---EEEYSP 107
BRCT_Rev1 cd17719
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ...
 5-92 8.76e-05

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: 42.94  E-value: 8.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550    5 IFANC-IFCLKVKYLPQQQKKKLqtdIKENGGKFSFSLNPQ-CTHIIldnADVLSQYQLNSIQK-NHVHIANPDFIWKSI 81
Cdd:cd17719     1 IFKGVvIYVNGYTDPSADELKRL---ILLHGGQYEHYYSRSrVTHII---ATNLPGSKIKKLKKaRNYKVVRPEWIVDSI 74

                          90
                  ....*....|.
gi 112789550   82 REKRLLDVKNY 92
Cdd:cd17719    75 KAGRLLPEAPY 85
BRCT_Ect2_rpt2 cd17732
second BRCT domain of epithelial cell-transforming sequence 2 protein (ECT2) and similar ...
 5-81 7.77e-04

second BRCT domain of epithelial cell-transforming sequence 2 protein (ECT2) and similar proteins; ECT2 is a guanine nucleotide exchange factor (GEF) for Rho GTPases, phosphorylated in G2/M phases, and is involved in the regulation of cytokinesis. It contains two tandem BRCT domains. The family corresponds to the second BRCT domain.


Pssm-ID: 349364  Cd Length: 80  Bit Score: 39.95  E-value: 7.77e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 112789550    5 IFANCIFCLkVKYlPQQQKKKLQTDIKENGGKFSFSLNPQCTHIILDNADVLsqyQLNSIQKNHVHIANPDFIWKSI 81
Cdd:cd17732     1 PFEGCTLSF-LGF-SDEEKTHMEELTEENGGKVTPLGDPSCTHLVVDESTVK---ELPFEPSSKLHVVKQEWFWASI 72
KLF4_N cd21582
N-terminal domain of Kruppel-like factor 4; Kruppel-like factor 4 (KLF4; also known as ...
 1317-1485 1.14e-03

N-terminal domain of Kruppel-like factor 4; Kruppel-like factor 4 (KLF4; also known as Krueppel-like factor 4 or gut-enriched Kruppel-like factor/GKLF) is a protein that, in humans, is encoded by the KLF4 gene. Evidence also suggests that KLF4 is a tumor suppressor in certain cancers, including colorectal cancer, gastric cancer, esophageal squamous cell carcinoma, intestinal cancer, prostate cancer, bladder cancer and lung cancer. It may act as a tumor promoter where increased KLF4 expression has been reported, such as in oral squamous cell carcinoma and in primary breast ductal carcinoma. KLF4 is one of four key factors that are essential for inducing pluripotent stem cells. KLF4 is highly expressed in non-dividing cells and its overexpression induces cell cycle arrest. KLF proteins KLF1, KLF2, KLF4, KLF5, KLF6, and KLF7 are transcriptional activators. KLF4 belongs to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF4, which is related to the N-terminal domains of KLF1 and KLF2.


Pssm-ID: 409228 [Multi-domain]  Cd Length: 335  Bit Score: 43.14  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550 1317 PILAPAvgsYLPPTArAHSP----ASLSFASYRQVASFGSAAPPRqfDASQFSQGPVPGTCADwIPQSA--SCPTGPP-- 1388
Cdd:cd21582   152 PDLDPA---YLQPTS-LHGKfvvkTTMDMGDYSQSINVSKSAPMT--KSSVAPSSSLPFMCPR-IKQENpsTCTISRPmd 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550 1389 QNPPSSPYCGivfsgsslsSAQSAPLQHPGGFTTRPSAGTFPELDSPQLHFSLPTDPDPIR-----GFGsYHPSAS-SPF 1462
Cdd:cd21582   225 GHLGGNSQHG---------FSQRAPLPSRTTPSGGPGGGNSSTAESLMSRDHHPSSQVLSHpplplPQG-YHPSPGyPPF 294

                         170       180
                  ....*....|....*....|...
gi 112789550 1463 HfQPSAASLTANLRLPMASALPE 1485
Cdd:cd21582   295 P-PPPSQPQQYQELMSPGSCLPE 316
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 876-1019 2.18e-03

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: 40.41  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  876 EVIICLDCSSSMEGVTFLQAKQIALHALSLVGEKQK-VNIIQFGTGY-KELFSYPKHItsntmaAEFI--MSATPTMGNT 951
Cdd:cd01462     2 PVILLVDQSGSMYGAPEEVAKAVALALLRIALAENRdTYLILFDSEFqTKIVDKTDDL------EEPVefLSGVQLGGGT 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 112789550  952 DFWKTLRY----LSLLYPARGsrNILLVSDGH---LQDESLTLQLVKRSRPHtRLFACGIGSTANRHVLRILSQC 1019
Cdd:cd01462    76 DINKALRYalelIERRDPRKA--DIVLITDGYeggVSDELLREVELKRSRVA-RFVALALGDHGNPGYDRISAED 147
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 877-1020 2.21e-03

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: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 40.74  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112789550  877 VIICLDCSSSMEGVTFLQAKQIA---LHALSLVGEKQKVNIIQFGTGYKELFSYPKHITSNTMAAEF----IMSATPTMG 949
Cdd:cd01450     3 IVFLLDGSESVGPENFEKVKDFIeklVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVknlkYLGGGGTNT 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 112789550  950 NTDFWKTLRYLSLLYPARGSRN--ILLVSDGHLQDESLTLQLVKRSRPH-TRLFACGIGStANRHVLRILSQCG 1020
Cdd:cd01450    83 GKALQYALEQLFSESNARENVPkvIIVLTDGRSDDGGDPKEAAAKLKDEgIKVFVVGVGP-ADEEELREIASCP 155
 
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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