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Conserved domains on  [gi|767977296|ref|XP_011533233|]
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protein mono-ADP-ribosyltransferase PARP4 isoform X1 [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 ...
 298-612 5.45e-111

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: 356.97  E-value: 5.45e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  298 EEVMNSSTLSQEVSDLVEMIWAEALGHLEHMLLKPVNRISLNDVSKAEGILLLVKAALKNGE-TAEQLQKMMTEFYRLIP 376
Cdd:cd01437     2 SKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSsQGSQLEELSNEFYTLIP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  377 HKGTMPKEVNLG---LLAKKADLCQLIRDMVNVCETNLSK---PNPPSLAKYRALRCKIEHVEQNTEEFLRVRKEVLQNH 450
Cdd:cd01437    82 HDFGMSKPPVIDneeLLKAKRELLEALRDIEIASKLLKDDeddSDDPLDANYEKLKCKIEPLDKDSEEYKIIEKYLKNTH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  451 HS--KSPVDVLQIFRVGRVNETTEFL--SKLGNVRPLLHGSPVQNIVGILCRGLLLPKVvedrgvqRTDVGNL--GSGIY 524
Cdd:cd01437   162 APttEYTVEVQEIFRVEREGETDRFKpfKKLGNRKLLWHGSRLTNFVGILSQGLRIAPP-------EAPVTGYmfGKGIY 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  525 FSDSLSTSIKYSHPGETDGTRLLLICDVALGKCMDLHEKDFSLTEAPPGYDSVHGVSQTASVTTDFEDD----------- 593
Cdd:cd01437   235 FADMFSKSANYCHASASDPTGLLLLCEVALGKMNELKKADYMAKELPKGKHSVKGLGKTAPDPSEFEIDldgvvvplgkp 314

                         330       340       350
                  ....*....|....*....|....*....|...
gi 767977296  594 --------------EFVVYKTNQVKMKYIIKFS 612
Cdd:cd01437   315 vpsghktdtsllynEYIVYDVAQVRLKYLLEVK 347
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 670-780 2.97e-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: 2.97e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296   670 LEDVHIKGRIIDTVAQVIVFQTYTNKSHVPIEAKYIFPLDDKAAVCGFEAFINGKHIVGEIKEKEEAQQEYLEAVTQGHG 749
Cdd:pfam08487    1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 767977296   750 AYLMSQDAPDVFTVSVGNLPPKAKVLIKITY 780
Cdd:pfam08487   81 AGLLEQDTPDVFTTSVGNIPPGEKVTVELTY 111
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 924-1080 1.83e-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: 1.83e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296    924 VIICLDCSSSMEGVTFLQAKQIA---LHALSLVGEKQKVNIIQFGTGYKELFSYPKHiTSNTMAAEFIMSATPTM-GNTD 999
Cdd:smart00327    2 VVFLLDGSGSMGGNRFELAKEFVlklVEQLDIGPDGDRVGLVTFSDDARVLFPLNDS-RSKDALLEALASLSYKLgGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296   1000 FWKTLRYLS--LLYPARGSRN-----ILLVSDGHLQDESL-TLQLVKR-SRPHTRLFACGIGSTANRHVLRILSQCGAGV 1070
Cdd:smart00327   81 LGAALQYALenLFSKSAGSRRgapkvVILITDGESNDGPKdLLKAAKElKRSGVKVFVVGVGNDVDEEELKKLASAPGGV 160

                           170
                    ....*....|
gi 767977296   1071 FEYFNAKSKH 1080
Cdd:smart00327  161 YVFLPELLDL 170
BRCT super family cl00038
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 91-135 1.12e-16

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: 76.56  E-value: 1.12e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 767977296   91 QCTHIILDNADVLSQYQLNSIQKNHVHIANPDFIWKSIREKRLLD 135
Cdd:cd17726    41 KCTHVVVNNAKALSSYKCRMAQKYGIPVVSLDYIWKCVEAGKLLD 85
KLF1_2_4_N super family cl41729
N-terminal domain of Kruppel-like factor (KLF) 1, KLF2, KLF4, and similar proteins; Kruppel ...
 1364-1532 2.21e-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: 42.37  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296 1364 PILAPAvgsYLPPTArAHSP----ASLSFASYRQVASFGSAAPPRqfDASQFSQGPVPGTCADwIPQSA--SCPTGPP-- 1435
Cdd:cd21582   152 PDLDPA---YLQPTS-LHGKfvvkTTMDMGDYSQSINVSKSAPMT--KSSVAPSSSLPFMCPR-IKQENpsTCTISRPmd 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296 1436 QNPPSSPYCGivfsgsslsSAQSAPLQHPGGFTTRPSAGTFPELDSPQLHFSLPTDPDPIR-----GFGsYHPSAS-SPF 1509
Cdd:cd21582   225 GHLGGNSQHG---------FSQRAPLPSRTTPSGGPGGGNSSTAESLMSRDHHPSSQVLSHpplplPQG-YHPSPGyPPF 294

                         170       180
                  ....*....|....*....|...
gi 767977296 1510 HfQPSAASLTANLRLPMASALPE 1532
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 ...
 298-612 5.45e-111

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: 356.97  E-value: 5.45e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  298 EEVMNSSTLSQEVSDLVEMIWAEALGHLEHMLLKPVNRISLNDVSKAEGILLLVKAALKNGE-TAEQLQKMMTEFYRLIP 376
Cdd:cd01437     2 SKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSsQGSQLEELSNEFYTLIP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  377 HKGTMPKEVNLG---LLAKKADLCQLIRDMVNVCETNLSK---PNPPSLAKYRALRCKIEHVEQNTEEFLRVRKEVLQNH 450
Cdd:cd01437    82 HDFGMSKPPVIDneeLLKAKRELLEALRDIEIASKLLKDDeddSDDPLDANYEKLKCKIEPLDKDSEEYKIIEKYLKNTH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  451 HS--KSPVDVLQIFRVGRVNETTEFL--SKLGNVRPLLHGSPVQNIVGILCRGLLLPKVvedrgvqRTDVGNL--GSGIY 524
Cdd:cd01437   162 APttEYTVEVQEIFRVEREGETDRFKpfKKLGNRKLLWHGSRLTNFVGILSQGLRIAPP-------EAPVTGYmfGKGIY 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  525 FSDSLSTSIKYSHPGETDGTRLLLICDVALGKCMDLHEKDFSLTEAPPGYDSVHGVSQTASVTTDFEDD----------- 593
Cdd:cd01437   235 FADMFSKSANYCHASASDPTGLLLLCEVALGKMNELKKADYMAKELPKGKHSVKGLGKTAPDPSEFEIDldgvvvplgkp 314

                         330       340       350
                  ....*....|....*....|....*....|...
gi 767977296  594 --------------EFVVYKTNQVKMKYIIKFS 612
Cdd:cd01437   315 vpsghktdtsllynEYIVYDVAQVRLKYLLEVK 347
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 670-780 2.97e-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: 2.97e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296   670 LEDVHIKGRIIDTVAQVIVFQTYTNKSHVPIEAKYIFPLDDKAAVCGFEAFINGKHIVGEIKEKEEAQQEYLEAVTQGHG 749
Cdd:pfam08487    1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 767977296   750 AYLMSQDAPDVFTVSVGNLPPKAKVLIKITY 780
Cdd:pfam08487   81 AGLLEQDTPDVFTTSVGNIPPGEKVTVELTY 111
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 436-613 2.63e-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: 174.06  E-value: 2.63e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296   436 TEEFLRVRKEVLQNHHS--KSPVDVLQIFRVGRVNETTEFLS--KLGNVRPLLHGSPVQNIVGILCRGLLLPKVVEDRGV 511
Cdd:pfam00644    1 SEEYQIIEKYFLSTHDPthGYPLFILEIFRVQRDGEWERFQPkkKLRNRRLLWHGSRLTNFLGILSQGLRIAPPEAPVTG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296   512 QRtdvgnLGSGIYFSDSLSTSIKYSHPGETDGTRLLLICDVALGKCMDLHEKDFsLTEAPPGYDSVHGVSQTASV----- 586
Cdd:pfam00644   81 YM-----FGKGIYFADDASKSANYCPPSEAHGNGLMLLSEVALGDMNELKKADY-AEKLPPGKHSVKGLGKTAPEsfvdl 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 767977296   587 --------------TTDFEDDEFVVYKTNQVKMKYIIKFSM 613
Cdd:pfam00644  155 dgvplgklvatgydSSVLLYNEYVVYNVNQVRPKYLLEVKF 195
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
654-782 1.11e-47

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 166.76  E-value: 1.11e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296    654 SSTKAGLQDASGNLVPLEDVHIKGRIIDTVAQVIVFQTYTNKShVPIEAKYIFPLDDKAAVCGFEAF-INGKHIVGEIKE 732
Cdd:smart00609    1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRA-VPAQEVTFDVELPKTAFISNFAMtIDGKTYVGEIKE 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|..
gi 767977296    733 KEEAQQEYLEAVTQGHGAYLMSQDAP--DVFTVSVgNLPPKAKVLIKITYIT 782
Cdd:smart00609   80 KEVAQKQYEKAVSQGKTAGLVRASGRsmEQFTVSV-NVAPGSKVTFELTYEE 130
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 332-609 3.19e-30

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 129.19  E-value: 3.19e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  332 PVNRISLNDVSKAEGILLLVKAALKNGETaEQLQKMMTEFYRLIPHKGTMPKEVNLGLLAKKADLCQLirDMV------- 404
Cdd:PLN03124  326 PLGKLSKSTILKGYEVLKRIAEVISRSDR-ETLEELSGEFYTVIPHDFGFKKMRQFTIDTPQKLKHKL--EMVealgeie 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  405 ---NVCETNLSKPNPPSLAKYRALRCKIEHVEQNTEEFLRVRKEVLQNH---HSKSPVDVLQIFRVGRVNETTEF--LSK 476
Cdd:PLN03124  403 iatKLLKDDIGEQDDPLYAHYKRLNCELEPLDTDSEEFSMIAKYLENTHgqtHSGYTLEIVQIFKVSREGEDERFqkFSS 482

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  477 LGNVRPLLHGSPVQNIVGILCRGL-LLPKVVEDRGVQrtdvgnLGSGIYFSDSLSTSIKYSHPGETDGTRLLLICDVALG 555
Cdd:PLN03124  483 TKNRMLLWHGSRLTNWTGILSQGLrIAPPEAPSTGYM------FGKGVYFADMFSKSANYCYASAANPDGVLLLCEVALG 556

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767977296  556 KCMDLHEKDFSLTEAPPGYDSVHGVSQTA---SVTTDFED---------------------DEFVVYKTNQVKMKYII 609
Cdd:PLN03124  557 DMNELLQADYNANKLPPGKLSTKGVGRTVpdpSEAKTLEDgvvvplgkpvespyskgsleyNEYIVYNVDQIRMRYVL 634
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 924-1080 1.83e-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: 1.83e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296    924 VIICLDCSSSMEGVTFLQAKQIA---LHALSLVGEKQKVNIIQFGTGYKELFSYPKHiTSNTMAAEFIMSATPTM-GNTD 999
Cdd:smart00327    2 VVFLLDGSGSMGGNRFELAKEFVlklVEQLDIGPDGDRVGLVTFSDDARVLFPLNDS-RSKDALLEALASLSYKLgGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296   1000 FWKTLRYLS--LLYPARGSRN-----ILLVSDGHLQDESL-TLQLVKR-SRPHTRLFACGIGSTANRHVLRILSQCGAGV 1070
Cdd:smart00327   81 LGAALQYALenLFSKSAGSRRgapkvVILITDGESNDGPKdLLKAAKElKRSGVKVFVVGVGNDVDEEELKKLASAPGGV 160

                           170
                    ....*....|
gi 767977296   1071 FEYFNAKSKH 1080
Cdd:smart00327  161 YVFLPELLDL 170
BRCT_PARP4_like cd17726
BRCT domain of poly [ADP-ribose] polymerase 4 (PARP-4) and similar proteins; PARP-4, also ...
 91-135 1.12e-16

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: 76.56  E-value: 1.12e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 767977296   91 QCTHIILDNADVLSQYQLNSIQKNHVHIANPDFIWKSIREKRLLD 135
Cdd:cd17726    41 KCTHVVVNNAKALSSYKCRMAQKYGIPVVSLDYIWKCVEAGKLLD 85
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 913-1065 1.43e-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: 1.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  913 VDLPDLASESEVIICLDCSSSMEGVTFLQAKQIALHALSLVGEKQKVNIIQFGTGYKELFSYPKHiTSNTMAAEFImSAT 992
Cdd:COG2425   110 ASAAVPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVEDLPLTAD-DGLEDAIEFL-SGL 187

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767977296  993 PTMGNTDFWKTLRY-LSLL-YPARGSRNILLVSDGHLQDESL-TLQLVKRSRPHTRLFACGIGSTANRHVLRILSQ 1065
Cdd:COG2425   188 FAGGGTDIAPALRAaLELLeEPDYRNADIVLITDGEAGVSPEeLLREVRAKESGVRLFTVAIGDAGNPGLLEALAD 263
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 923-1092 7.20e-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: 7.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  923 EVIICLDCSSSMEGVTFLQAKQIALHALSLVGEKQKVNIIQFGTGYKELFSYPKHITSNTMAA--EFI--MSAtptMGNT 998
Cdd:cd01461     4 EVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAaiEYVnrLQA---LGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  999 DFWKTL-RYLSLLYPARGS-RNILLVSDGHLQDESLTLQLVKRSRPHT-RLFACGIGSTANRHVLRILSQCGAGVFEYFN 1075
Cdd:cd01461    81 NMNDALeAALELLNSSPGSvPQIILLTDGEVTNESQILKNVREALSGRiRLFTFGIGSDVNTYLLERLAREGRGIARRIY 160

                         170
                  ....*....|....*..
gi 767977296 1076 AKSkhswrkQIEDQMTR 1092
Cdd:cd01461   161 ETD------DIESQLLR 171
VWA pfam00092
von Willebrand factor type A domain;
923-1079 1.63e-13

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 70.38  E-value: 1.63e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296   923 EVIICLDCSSSMEGVTFLQAKQIALH---ALSLVGEKQKVNIIQFGTGYKELFSYPKHiTSNTMAAEFIMSATP-TMGNT 998
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKlveSLDIGPDGTRVGLVQYSSDVRTEFPLNDY-SSKEELLSAVDNLRYlGGGTT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296   999 DFWKTLRYL--SLLYPARGSR-----NILLVSDGHLQDESLT--LQLVKRSRphTRLFACGIGSTANRHvLRILSQCGAG 1069
Cdd:pfam00092   80 NTGKALKYAleNLFSSAAGARpgapkVVVLLTDGRSQDGDPEevARELKSAG--VTVFAVGVGNADDEE-LRKIASEPGE 156

                          170
                   ....*....|
gi 767977296  1070 VFEYFNAKSK 1079
Cdd:pfam00092  157 GHVFTVSDFE 166
KLF4_N cd21582
N-terminal domain of Kruppel-like factor 4; Kruppel-like factor 4 (KLF4; also known as ...
 1364-1532 2.21e-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: 42.37  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296 1364 PILAPAvgsYLPPTArAHSP----ASLSFASYRQVASFGSAAPPRqfDASQFSQGPVPGTCADwIPQSA--SCPTGPP-- 1435
Cdd:cd21582   152 PDLDPA---YLQPTS-LHGKfvvkTTMDMGDYSQSINVSKSAPMT--KSSVAPSSSLPFMCPR-IKQENpsTCTISRPmd 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296 1436 QNPPSSPYCGivfsgsslsSAQSAPLQHPGGFTTRPSAGTFPELDSPQLHFSLPTDPDPIR-----GFGsYHPSAS-SPF 1509
Cdd:cd21582   225 GHLGGNSQHG---------FSQRAPLPSRTTPSGGPGGGNSSTAESLMSRDHHPSSQVLSHpplplPQG-YHPSPGyPPF 294

                         170       180
                  ....*....|....*....|...
gi 767977296 1510 HfQPSAASLTANLRLPMASALPE 1532
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 ...
 298-612 5.45e-111

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: 356.97  E-value: 5.45e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  298 EEVMNSSTLSQEVSDLVEMIWAEALGHLEHMLLKPVNRISLNDVSKAEGILLLVKAALKNGE-TAEQLQKMMTEFYRLIP 376
Cdd:cd01437     2 SKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSsQGSQLEELSNEFYTLIP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  377 HKGTMPKEVNLG---LLAKKADLCQLIRDMVNVCETNLSK---PNPPSLAKYRALRCKIEHVEQNTEEFLRVRKEVLQNH 450
Cdd:cd01437    82 HDFGMSKPPVIDneeLLKAKRELLEALRDIEIASKLLKDDeddSDDPLDANYEKLKCKIEPLDKDSEEYKIIEKYLKNTH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  451 HS--KSPVDVLQIFRVGRVNETTEFL--SKLGNVRPLLHGSPVQNIVGILCRGLLLPKVvedrgvqRTDVGNL--GSGIY 524
Cdd:cd01437   162 APttEYTVEVQEIFRVEREGETDRFKpfKKLGNRKLLWHGSRLTNFVGILSQGLRIAPP-------EAPVTGYmfGKGIY 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  525 FSDSLSTSIKYSHPGETDGTRLLLICDVALGKCMDLHEKDFSLTEAPPGYDSVHGVSQTASVTTDFEDD----------- 593
Cdd:cd01437   235 FADMFSKSANYCHASASDPTGLLLLCEVALGKMNELKKADYMAKELPKGKHSVKGLGKTAPDPSEFEIDldgvvvplgkp 314

                         330       340       350
                  ....*....|....*....|....*....|...
gi 767977296  594 --------------EFVVYKTNQVKMKYIIKFS 612
Cdd:cd01437   315 vpsghktdtsllynEYIVYDVAQVRLKYLLEVK 347
VIT pfam08487
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 670-780 2.97e-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: 2.97e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296   670 LEDVHIKGRIIDTVAQVIVFQTYTNKSHVPIEAKYIFPLDDKAAVCGFEAFINGKHIVGEIKEKEEAQQEYLEAVTQGHG 749
Cdd:pfam08487    1 LKSVSVDATITGRIARTTVTQTFVNPSNEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKT 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 767977296   750 AYLMSQDAPDVFTVSVGNLPPKAKVLIKITY 780
Cdd:pfam08487   81 AGLLEQDTPDVFTTSVGNIPPGEKVTVELTY 111
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 436-613 2.63e-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: 174.06  E-value: 2.63e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296   436 TEEFLRVRKEVLQNHHS--KSPVDVLQIFRVGRVNETTEFLS--KLGNVRPLLHGSPVQNIVGILCRGLLLPKVVEDRGV 511
Cdd:pfam00644    1 SEEYQIIEKYFLSTHDPthGYPLFILEIFRVQRDGEWERFQPkkKLRNRRLLWHGSRLTNFLGILSQGLRIAPPEAPVTG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296   512 QRtdvgnLGSGIYFSDSLSTSIKYSHPGETDGTRLLLICDVALGKCMDLHEKDFsLTEAPPGYDSVHGVSQTASV----- 586
Cdd:pfam00644   81 YM-----FGKGIYFADDASKSANYCPPSEAHGNGLMLLSEVALGDMNELKKADY-AEKLPPGKHSVKGLGKTAPEsfvdl 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 767977296   587 --------------TTDFEDDEFVVYKTNQVKMKYIIKFSM 613
Cdd:pfam00644  155 dgvplgklvatgydSSVLLYNEYVVYNVNQVRPKYLLEVKF 195
VIT smart00609
Vault protein Inter-alpha-Trypsin domain;
654-782 1.11e-47

Vault protein Inter-alpha-Trypsin domain;


Pssm-ID: 197803 [Multi-domain]  Cd Length: 130  Bit Score: 166.76  E-value: 1.11e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296    654 SSTKAGLQDASGNLVPLEDVHIKGRIIDTVAQVIVFQTYTNKShVPIEAKYIFPLDDKAAVCGFEAF-INGKHIVGEIKE 732
Cdd:smart00609    1 LSGKRGLQTAEVNGVPLYSLKVNSKVTSRFAHTVVTSRVVNRA-VPAQEVTFDVELPKTAFISNFAMtIDGKTYVGEIKE 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|..
gi 767977296    733 KEEAQQEYLEAVTQGHGAYLMSQDAP--DVFTVSVgNLPPKAKVLIKITYIT 782
Cdd:smart00609   80 KEVAQKQYEKAVSQGKTAGLVRASGRsmEQFTVSV-NVAPGSKVTFELTYEE 130
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 332-609 3.19e-30

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 129.19  E-value: 3.19e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  332 PVNRISLNDVSKAEGILLLVKAALKNGETaEQLQKMMTEFYRLIPHKGTMPKEVNLGLLAKKADLCQLirDMV------- 404
Cdd:PLN03124  326 PLGKLSKSTILKGYEVLKRIAEVISRSDR-ETLEELSGEFYTVIPHDFGFKKMRQFTIDTPQKLKHKL--EMVealgeie 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  405 ---NVCETNLSKPNPPSLAKYRALRCKIEHVEQNTEEFLRVRKEVLQNH---HSKSPVDVLQIFRVGRVNETTEF--LSK 476
Cdd:PLN03124  403 iatKLLKDDIGEQDDPLYAHYKRLNCELEPLDTDSEEFSMIAKYLENTHgqtHSGYTLEIVQIFKVSREGEDERFqkFSS 482

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  477 LGNVRPLLHGSPVQNIVGILCRGL-LLPKVVEDRGVQrtdvgnLGSGIYFSDSLSTSIKYSHPGETDGTRLLLICDVALG 555
Cdd:PLN03124  483 TKNRMLLWHGSRLTNWTGILSQGLrIAPPEAPSTGYM------FGKGVYFADMFSKSANYCYASAANPDGVLLLCEVALG 556

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767977296  556 KCMDLHEKDFSLTEAPPGYDSVHGVSQTA---SVTTDFED---------------------DEFVVYKTNQVKMKYII 609
Cdd:PLN03124  557 DMNELLQADYNANKLPPGKLSTKGVGRTVpdpSEAKTLEDgvvvplgkpvespyskgsleyNEYIVYNVDQIRMRYVL 634
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
 421-610 9.28e-18

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 89.85  E-value: 9.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  421 KYRALRCKIEHVEQNTEEFLRVRKEVLQNH---HSKSPVDVLQIFRVGRVNETTEFL---SKLGNVRPLLHGSPVQNIVG 494
Cdd:PLN03123  761 KYKKLHCDISPLPHDSEDYKLIEKYLLTTHaptHTDWSLELEEVFSLEREGEFDKYApykEKLKNRMLLWHGSRLTNFVG 840

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  495 ILCRGL-LLPKVVEDRGVQrtdvgnLGSGIYFSDSLSTSIKYSHPGETDGTRLLLICDVALGKCMDLheKDFSLTEAPP- 572
Cdd:PLN03123  841 ILSQGLrIAPPEAPATGYM------FGKGVYFADLVSKSAQYCYTDRKNPVGLMLLSEVALGEIYEL--KKAKYMDKPPr 912

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767977296  573 GYDSVHGVSQTASVTTDF---EDD---------------------EFVVYKTNQVKMKYIIK 610
Cdd:PLN03123  913 GKHSTKGLGKTVPQESEFvkwRDDvvvpcgkpvpskvkaselmynEYIVYNTAQVKLQFLLK 974
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 924-1080 1.83e-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: 1.83e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296    924 VIICLDCSSSMEGVTFLQAKQIA---LHALSLVGEKQKVNIIQFGTGYKELFSYPKHiTSNTMAAEFIMSATPTM-GNTD 999
Cdd:smart00327    2 VVFLLDGSGSMGGNRFELAKEFVlklVEQLDIGPDGDRVGLVTFSDDARVLFPLNDS-RSKDALLEALASLSYKLgGGTN 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296   1000 FWKTLRYLS--LLYPARGSRN-----ILLVSDGHLQDESL-TLQLVKR-SRPHTRLFACGIGSTANRHVLRILSQCGAGV 1070
Cdd:smart00327   81 LGAALQYALenLFSKSAGSRRgapkvVILITDGESNDGPKdLLKAAKElKRSGVKVFVVGVGNDVDEEELKKLASAPGGV 160

                           170
                    ....*....|
gi 767977296   1071 FEYFNAKSKH 1080
Cdd:smart00327  161 YVFLPELLDL 170
BRCT_PARP4_like cd17726
BRCT domain of poly [ADP-ribose] polymerase 4 (PARP-4) and similar proteins; PARP-4, also ...
 91-135 1.12e-16

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: 76.56  E-value: 1.12e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 767977296   91 QCTHIILDNADVLSQYQLNSIQKNHVHIANPDFIWKSIREKRLLD 135
Cdd:cd17726    41 KCTHVVVNNAKALSSYKCRMAQKYGIPVVSLDYIWKCVEAGKLLD 85
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 913-1065 1.43e-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: 1.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  913 VDLPDLASESEVIICLDCSSSMEGVTFLQAKQIALHALSLVGEKQKVNIIQFGTGYKELFSYPKHiTSNTMAAEFImSAT 992
Cdd:COG2425   110 ASAAVPLLEGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVEDLPLTAD-DGLEDAIEFL-SGL 187

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767977296  993 PTMGNTDFWKTLRY-LSLL-YPARGSRNILLVSDGHLQDESL-TLQLVKRSRPHTRLFACGIGSTANRHVLRILSQ 1065
Cdd:COG2425   188 FAGGGTDIAPALRAaLELLeEPDYRNADIVLITDGEAGVSPEeLLREVRAKESGVRLFTVAIGDAGNPGLLEALAD 263
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 923-1092 7.20e-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: 7.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  923 EVIICLDCSSSMEGVTFLQAKQIALHALSLVGEKQKVNIIQFGTGYKELFSYPKHITSNTMAA--EFI--MSAtptMGNT 998
Cdd:cd01461     4 EVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAaiEYVnrLQA---LGGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  999 DFWKTL-RYLSLLYPARGS-RNILLVSDGHLQDESLTLQLVKRSRPHT-RLFACGIGSTANRHVLRILSQCGAGVFEYFN 1075
Cdd:cd01461    81 NMNDALeAALELLNSSPGSvPQIILLTDGEVTNESQILKNVREALSGRiRLFTFGIGSDVNTYLLERLAREGRGIARRIY 160

                         170
                  ....*....|....*..
gi 767977296 1076 AKSkhswrkQIEDQMTR 1092
Cdd:cd01461   161 ETD------DIESQLLR 171
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 924-1073 1.18e-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: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  924 VIICLDCSSSMEGVTFLQAKQIA---LHALSLVGEKQKVNIIQFGTGYKELFSYPKHITSNTMAAEFIMSATPTMGNTDF 1000
Cdd:cd00198     3 IVFLLDVSGSMGGEKLDKAKEALkalVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKKGLGGGTNI 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767977296 1001 WKTLRYLSLLYPARGSRN----ILLVSDGHLQDESLTLQLVKRS--RPHTRLFACGIGSTANRHVLRILSQCGAGVFEY 1073
Cdd:cd00198    83 GAALRLALELLKSAKRPNarrvIILLTDGEPNDGPELLAEAARElrKLGITVYTIGIGDDANEDELKEIADKTTGGAVF 161
VWA pfam00092
von Willebrand factor type A domain;
923-1079 1.63e-13

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 70.38  E-value: 1.63e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296   923 EVIICLDCSSSMEGVTFLQAKQIALH---ALSLVGEKQKVNIIQFGTGYKELFSYPKHiTSNTMAAEFIMSATP-TMGNT 998
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKlveSLDIGPDGTRVGLVQYSSDVRTEFPLNDY-SSKEELLSAVDNLRYlGGGTT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296   999 DFWKTLRYL--SLLYPARGSR-----NILLVSDGHLQDESLT--LQLVKRSRphTRLFACGIGSTANRHvLRILSQCGAG 1069
Cdd:pfam00092   80 NTGKALKYAleNLFSSAAGARpgapkVVVLLTDGRSQDGDPEevARELKSAG--VTVFAVGVGNADDEE-LRKIASEPGE 156

                          170
                   ....*....|
gi 767977296  1070 VFEYFNAKSK 1079
Cdd:pfam00092  157 GHVFTVSDFE 166
VWA_3 pfam13768
von Willebrand factor type A domain;
922-1072 5.15e-13

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 68.58  E-value: 5.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296   922 SEVIICLDCSSSMEGVTFLQAKQI--ALHALSlvgEKQKVNIIQFGTGYKELFSYPKHITSNTM--AAEFIMSATPTMGN 997
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEPKLQKDALsvALRQLP---TGDKFAVLGFGTLPRPLFPGWRVVSPRSLqeAFQFIKTLQPPLGG 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767977296   998 TDFWKTLRYLSLLYPARGS-RNILLVSDGH-LQDESLTLQLVKRSRPHTRLFACGIGSTANRHVLRILSQCGAGVFE 1072
Cdd:pfam13768   78 SDLLGALKEAVRAPASPGYiRHVLLLTDGSpMQGETRVSDLISRAPGKIRFFAYGLGASISAPMLQLLAEASNGTYE 154
VIT_2 pfam13757
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ...
 663-734 3.46e-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: 3.46e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767977296   663 ASGNLVPLEDVHIKGRIIDTVAQVIVFQTYTNKSHVPIEAKYIFPLDDKAAVCGFEAFINGKHIVGEIKEKE 734
Cdd:pfam13757    7 STRTPLPLKASRVSACVNGYSLGVTASLTYYNPQPYPVEGVFVYPLDEGTTVVGFEAEIAGRVISVQLKERE 78
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 922-1073 8.05e-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: 8.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  922 SEVIICLDCSSSMEGVTFLQAKQIALHALSLVGEKQKVNIIQFGTGYKELFSyPKHITSNTMAAEFIMSATPTmGNTDFW 1001
Cdd:COG2304    92 LNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLP-PTPATDRAKILAAIDRLQAG-GGTALG 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296 1002 KTLRY-LSLL---YPARGSRNILLVSDGH----LQDESLTLQLVKRSRP-HTRLFACGIGSTANRHVLRILSQCGAGVFE 1072
Cdd:COG2304   170 AGLELaYELArkhFIPGRVNRVILLTDGDanvgITDPEELLKLAEEAREeGITLTTLGVGSDYNEDLLERLADAGGGNYY 249


                  .
gi 767977296 1073 Y 1073
Cdd:COG2304   250 Y 250
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 483-607 3.42e-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: 3.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  483 LLHGSPVQNIVGILCRGLLLPKVvedrGVQRTDvGNLGSGIYFSDSLSTSIKYSH-PGETDGT---------------RL 546
Cdd:cd01341     2 LFHGSPPGNVISILKLGLRPASY----GVLLNG-GMFGKGIYSAPNISKSNGYSVgCDGQHVFqngkpkvcgrelcvfGF 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767977296  547 LLICDVALGKCMDLHEKDFSLTEAPPGYDSVHGVSQTASVTTdFEDDEFVVY-KTNQVKMKY 607
Cdd:cd01341    77 LTLGVMSGATEESSRVLFPRNFRGATGAEVVDLLVAMCRDAL-LLPREYIIFePYSQVSIRY 137
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 466-613 3.02e-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: 3.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  466 RVNETTEFLSKLGNVRPLLHGSPVQNivGILCRGLllpkvvEDRGVQRTdvGNLGSGIYFSDSLSTSIKYSH-------- 537
Cdd:cd01438    75 RQKEIAEENHNHHNERMLFHGSPFIN--AIIHKGF------DERHAYIG--GMFGAGIYFAENSSKSNQYVYgigggtgc 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  538 PGETDGT-----RLLLICDVALGKCMdLHEKDFSLTEAPPGYDSVHGVSQTASVTTdfedDEFVVYKTNQVKMKYIIKFS 612
Cdd:cd01438   145 PTHKDRScyvchRQMLFCRVTLGKSF-LQFSAMKMAHAPPGHHSVIGRPSVNGLAY----AEYVIYRGEQAYPEYLITYQ 219


                  .
gi 767977296  613 M 613
Cdd:cd01438   220 I 220
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 867-1076 2.38e-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: 2.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  867 EGSSLDSSGFSLHIGLSAAYLPRMWVEKHPEKESEACMLVFQPDLDVDLPDLASESEVIICLDCSSSMEGVTFL-QAKQI 945
Cdd:COG1240    38 LLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENRLeAAKGA 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  946 ALHALSLVGEKQKVNIIQFGTGYKELFSypkhITSNTMAAEFIMSATPTMGNTDFW----KTLRYLSLLYPARgSRNILL 1021
Cdd:COG1240   118 LLDFLDDYRPRDRVGLVAFGGEAEVLLP----LTRDREALKRALDELPPGGGTPLGdalaLALELLKRADPAR-RKVIVL 192

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767977296 1022 VSDGHLQDESLTLQLVKR--SRPHTRLFACGIGSTA-NRHVLRILSQCGAGvfEYFNA 1076
Cdd:COG1240   193 LTDGRDNAGRIDPLEAAElaAAAGIRIYTIGVGTEAvDEGLLREIAEATGG--RYFRA 248
VWA_2 pfam13519
von Willebrand factor type A domain;
924-1022 2.91e-06

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 47.67  E-value: 2.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296   924 VIICLDCSSSMEGVTFLQAK-QIALHALSLVGEK---QKVNIIQFGTGYkELFSYPKhiTSNTMAAEFIMSATPTMGNTD 999
Cdd:pfam13519    1 LVFVLDTSGSMRNGDYGPTRlEAAKDAVLALLKSlpgDRVGLVTFGDGP-EVLIPLT--KDRAKILRALRRLEPKGGGTN 77

                           90       100
                   ....*....|....*....|....*
gi 767977296  1000 FWKTLRYLSLLYPAR--GSRNILLV 1022
Cdd:pfam13519   78 LAAALQLARAALKHRrkNQPRRIVL 102
PARP_reg pfam02877
Poly(ADP-ribose) polymerase, regulatory domain; Poly(ADP-ribose) polymerase catalyzes the ...
 304-403 2.41e-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: 45.59  E-value: 2.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296   304 STLSQEVSDLVEMI-----WAEALGHLEHMLLK-PVNRISLNDVSKAEGILLLVKAALKNGETA---EQLQKMMTEFYRL 374
Cdd:pfam02877    1 SKLPPPVQELMKLIfnvemMKKAMKEMKYDAKKmPLGKLSKRQIKKGYEVLKELSELLKKPSLAkakAKLEDLSNRFYTL 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 767977296   375 IPHK-GTMPKEV--NLGLLAKKADLCQLIRDM 403
Cdd:pfam02877   81 IPHDfGRNRPPVidTEEELKEKLELLEALLDI 112
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
923-1061 2.61e-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: 2.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  923 EVIICLDCSSSMEGV----------TFLQakqiALHALSLVGEKQKVNIIQFGTGYKELFSYpkhitsnTMAAEFIMSAT 992
Cdd:COG4245     7 PVYLLLDTSGSMSGEpiealneglqALID----ELRQDPYALETVEVSVITFDGEAKVLLPL-------TDLEDFQPPDL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  993 PTMGNTDFWKTLRYL-------SLLYPARGSRN----ILLVSDGHLQDESLT--LQLVKR--SRPHTRLFACGIGSTANR 1057
Cdd:COG4245    76 SASGGTPLGAALELLldlierrVQKYTAEGKGDwrpvVFLITDGEPTDSDWEaaLQRLKDgeAAKKANIFAIGVGPDADT 155


                  ....
gi 767977296 1058 HVLR 1061
Cdd:COG4245   156 EVLK 159
KLF4_N cd21582
N-terminal domain of Kruppel-like factor 4; Kruppel-like factor 4 (KLF4; also known as ...
 1364-1532 2.21e-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: 42.37  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296 1364 PILAPAvgsYLPPTArAHSP----ASLSFASYRQVASFGSAAPPRqfDASQFSQGPVPGTCADwIPQSA--SCPTGPP-- 1435
Cdd:cd21582   152 PDLDPA---YLQPTS-LHGKfvvkTTMDMGDYSQSINVSKSAPMT--KSSVAPSSSLPFMCPR-IKQENpsTCTISRPmd 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296 1436 QNPPSSPYCGivfsgsslsSAQSAPLQHPGGFTTRPSAGTFPELDSPQLHFSLPTDPDPIR-----GFGsYHPSAS-SPF 1509
Cdd:cd21582   225 GHLGGNSQHG---------FSQRAPLPSRTTPSGGPGGGNSSTAESLMSRDHHPSSQVLSHpplplPQG-YHPSPGyPPF 294

                         170       180
                  ....*....|....*....|...
gi 767977296 1510 HfQPSAASLTANLRLPMASALPE 1532
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 ...
 923-1066 2.24e-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: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  923 EVIICLDCSSSMEGVTFLQAKQIALHALSLVGEKQK-VNIIQFGTGY-KELFSYPKHItsntmaAEFI--MSATPTMGNT 998
Cdd:cd01462     2 PVILLVDQSGSMYGAPEEVAKAVALALLRIALAENRdTYLILFDSEFqTKIVDKTDDL------EEPVefLSGVQLGGGT 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767977296  999 DFWKTLRY----LSLLYPARGsrNILLVSDGH---LQDESLTLQLVKRSRPHtRLFACGIGSTANRHVLRILSQC 1066
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 ...
 924-1067 2.27e-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: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767977296  924 VIICLDCSSSMEGVTFLQAKQIA---LHALSLVGEKQKVNIIQFGTGYKELFSYPKHITSNTMAAEF----IMSATPTMG 996
Cdd:cd01450     3 IVFLLDGSESVGPENFEKVKDFIeklVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVknlkYLGGGGTNT 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767977296  997 NTDFWKTLRYLSLLYPARGSRN--ILLVSDGHLQDESLTLQLVKRSRPH-TRLFACGIGStANRHVLRILSQCG 1067
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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