NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|24580804|ref|NP_608579|]
View 

integrator 14 [Drosophila melanogaster]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
IntS14_b-barrel super family cl44853
Integrator complex subunit 14, beta-barrel domain; This entry represents the central ...
 228-426 1.31e-46

Integrator complex subunit 14, beta-barrel domain; This entry represents the central beta-barrel domain of Integrator complex subunit 14 (IntS14), a component of the integrator complex which is involved in the transcription of small nuclear RNAs (snRNA) and their 3'-box-dependent processing. This complex is also involved in the 3'-end processing of the U7 snRNA, and the spliceosomal snRNAs U1 and U5. IntS14 interacts with IntS13, both of them consist of an N-terminal von-Willebrand type A like domain (VWA), followed by a central beta-barrel domain and a C-terminal alpha-helical domain connected through a linker. The interface involves all domains of both proteins, both beta-barrel domains form the centre of the complex and contribute to the major contact between Ints13-IntS14.


The actual alignment was detected with superfamily member pfam19435:

Pssm-ID: 466081  Cd Length: 147  Bit Score: 160.51  E-value: 1.31e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580804   228 YKSSEVTLKCGSyfrMEASVLLWPPTAPYEQKSHIFGREPTIRHTdqkIEVCGFLSLSDIGSPATLSRHWVLP-KVEREK 306
Cdd:pfam19435   1 YSPFHGTLKCGN---LSSPVQLFPPPEPYTKDTDFEPITRTISDD---IEICGFIDIADVASPPVISRHLVLPlSTKKEK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580804   307 SGSsrrsgnlsaaakppklnldtsnpnyelekleadikefyaKDSKDTEESGDDDVTIvlkpgpqtEQQKENLCVLLHGA 386
Cdd:pfam19435  75 DES---------------------------------------GKGGKAGEDEDESNTD--------EGKIPSFCVLLHGS 107

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 24580804   387 LKMENMAALVRVGDKWYGFIYAFTDSKKKSNLMLNILPPG 426
Cdd:pfam19435 108 LKVENMVALVQVGEDWYGMLYSWADSKKKSNLMLSIFEPG 147
IntS14_C super family cl48658
Integrator complex subunit 14, alpha-helical domain; This entry represents the C-terminal ...
 468-566 8.12e-42

Integrator complex subunit 14, alpha-helical domain; This entry represents the C-terminal alpha-helical domain of Integrator complex subunit 14 (IntS14), a component of the integrator complex which is involved in the transcription of small nuclear RNAs (snRNA) and their 3'-box dependent processing. This complex is also involved in the 3'-end processing of the U7 snRNA, and the spliceosomal snRNAs U1 and U5. IntS14 interacts with IntS13; both of them consist of an N-terminal VWA domain followed by a central beta-barrel domain and a C-terminal alpha-helical domain, which are connected through a linker devoid of secondary structure elements. This domain contribute to binding by packing against the beta-barrel of IntS13.


The actual alignment was detected with superfamily member pfam20504:

Pssm-ID: 466653  Cd Length: 103  Bit Score: 145.93  E-value: 8.12e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580804   468 VWIRQASLQSDVQKVLRHAKKMPDKTQHFYKELNRIRRAALALGFVELLEALAMLLEKECAHLSlNGASNDCTLQLQHAA 547
Cdd:pfam20504   1 VWIKPGGLQSDIQKILRHARKLPEKTQQFYKELNRLRRAALSFGFLELLEGLAAMLERECTLLP-GTAHPDAALQLTHAA 79

                          90
                  ....*....|....*....
gi 24580804   548 TELRKTSNRDMKSMIVPLQ 566
Cdd:pfam20504  80 NQLRKSQSRDYKYNITPLQ 98
ChlD super family cl34203
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 4-173 1.14e-07

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


The actual alignment was detected with superfamily member COG1240:

Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 53.40  E-value: 1.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580804   4 LIALDASLSMLRPvpGRNEhtyqslATKG-IQHLLDNLTAAGKlehVALLSYSTTAELKVDFTRDYDQVRQAVKKVEPVD 82
Cdd:COG1240  96 VLVVDASGSMAAE--NRLE------AAKGaLLDFLDDYRPRDR---VGLVAFGGEAEVLLPLTRDREALKRALDELPPGG 164

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580804  83 KACLMSMLKAVVSIMSPWGNQNILQVVVFTDcglGFGNTSITGFLEAYAE-------------KESEPEFGFLKTLANYn 149
Cdd:COG1240 165 GTPLGDALALALELLKRADPARRKVIVLLTD---GRDNAGRIDPLEAAELaaaagiriytigvGTEAVDEGLLREIAEA- 240

                       170       180
                ....*....|....*....|....*...
gi 24580804 150 lnficlgLHGDYYFTRGL----AVYQQL 173
Cdd:COG1240 241 -------TGGRYFRADDLselaAIYREI 261
 
Name Accession Description Interval E-value
IntS14_b-barrel pfam19435
Integrator complex subunit 14, beta-barrel domain; This entry represents the central ...
 228-426 1.31e-46

Integrator complex subunit 14, beta-barrel domain; This entry represents the central beta-barrel domain of Integrator complex subunit 14 (IntS14), a component of the integrator complex which is involved in the transcription of small nuclear RNAs (snRNA) and their 3'-box-dependent processing. This complex is also involved in the 3'-end processing of the U7 snRNA, and the spliceosomal snRNAs U1 and U5. IntS14 interacts with IntS13, both of them consist of an N-terminal von-Willebrand type A like domain (VWA), followed by a central beta-barrel domain and a C-terminal alpha-helical domain connected through a linker. The interface involves all domains of both proteins, both beta-barrel domains form the centre of the complex and contribute to the major contact between Ints13-IntS14.


Pssm-ID: 466081  Cd Length: 147  Bit Score: 160.51  E-value: 1.31e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580804   228 YKSSEVTLKCGSyfrMEASVLLWPPTAPYEQKSHIFGREPTIRHTdqkIEVCGFLSLSDIGSPATLSRHWVLP-KVEREK 306
Cdd:pfam19435   1 YSPFHGTLKCGN---LSSPVQLFPPPEPYTKDTDFEPITRTISDD---IEICGFIDIADVASPPVISRHLVLPlSTKKEK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580804   307 SGSsrrsgnlsaaakppklnldtsnpnyelekleadikefyaKDSKDTEESGDDDVTIvlkpgpqtEQQKENLCVLLHGA 386
Cdd:pfam19435  75 DES---------------------------------------GKGGKAGEDEDESNTD--------EGKIPSFCVLLHGS 107

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 24580804   387 LKMENMAALVRVGDKWYGFIYAFTDSKKKSNLMLNILPPG 426
Cdd:pfam19435 108 LKVENMVALVQVGEDWYGMLYSWADSKKKSNLMLSIFEPG 147
IntS14_C pfam20504
Integrator complex subunit 14, alpha-helical domain; This entry represents the C-terminal ...
 468-566 8.12e-42

Integrator complex subunit 14, alpha-helical domain; This entry represents the C-terminal alpha-helical domain of Integrator complex subunit 14 (IntS14), a component of the integrator complex which is involved in the transcription of small nuclear RNAs (snRNA) and their 3'-box dependent processing. This complex is also involved in the 3'-end processing of the U7 snRNA, and the spliceosomal snRNAs U1 and U5. IntS14 interacts with IntS13; both of them consist of an N-terminal VWA domain followed by a central beta-barrel domain and a C-terminal alpha-helical domain, which are connected through a linker devoid of secondary structure elements. This domain contribute to binding by packing against the beta-barrel of IntS13.


Pssm-ID: 466653  Cd Length: 103  Bit Score: 145.93  E-value: 8.12e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580804   468 VWIRQASLQSDVQKVLRHAKKMPDKTQHFYKELNRIRRAALALGFVELLEALAMLLEKECAHLSlNGASNDCTLQLQHAA 547
Cdd:pfam20504   1 VWIKPGGLQSDIQKILRHARKLPEKTQQFYKELNRLRRAALSFGFLELLEGLAAMLERECTLLP-GTAHPDAALQLTHAA 79

                          90
                  ....*....|....*....
gi 24580804   548 TELRKTSNRDMKSMIVPLQ 566
Cdd:pfam20504  80 NQLRKSQSRDYKYNITPLQ 98
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 4-173 1.14e-07

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 53.40  E-value: 1.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580804   4 LIALDASLSMLRPvpGRNEhtyqslATKG-IQHLLDNLTAAGKlehVALLSYSTTAELKVDFTRDYDQVRQAVKKVEPVD 82
Cdd:COG1240  96 VLVVDASGSMAAE--NRLE------AAKGaLLDFLDDYRPRDR---VGLVAFGGEAEVLLPLTRDREALKRALDELPPGG 164

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580804  83 KACLMSMLKAVVSIMSPWGNQNILQVVVFTDcglGFGNTSITGFLEAYAE-------------KESEPEFGFLKTLANYn 149
Cdd:COG1240 165 GTPLGDALALALELLKRADPARRKVIVLLTD---GRDNAGRIDPLEAAELaaaagiriytigvGTEAVDEGLLREIAEA- 240

                       170       180
                ....*....|....*....|....*...
gi 24580804 150 lnficlgLHGDYYFTRGL----AVYQQL 173
Cdd:COG1240 241 -------TGGRYFRADDLselaAIYREI 261
VWA_2 pfam13519
von Willebrand factor type A domain;
3-111 1.23e-07

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 49.98  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580804     3 TLIALDASLSMLRPVPGRNEHTYQslatkgiQHLLDNLTAAGKLEHVALLSYSTTAELKVDFTRDYDQVRQAVKKVEPVD 82
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTRLEAA-------KDAVLALLKSLPGDRVGLVTFGDGPEVLIPLTKDRAKILRALRRLEPKG 73

                          90       100       110
                  ....*....|....*....|....*....|...
gi 24580804    83 KA-CL---MSMLKAVVSIMSPWGNQnilQVVVF 111
Cdd:pfam13519  74 GGtNLaaaLQLARAALKHRRKNQPR---RIVLI 103
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 5-164 2.37e-04

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: 42.06  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580804      5 IALDASLSMlrpvpGRNEHTYQSLAtkgIQHLLDNLTAAGKLEHVALLSYSTTAELKVDF--TRDYDQVRQAVKKVEPVD 82
Cdd:smart00327   4 FLLDGSGSM-----GGNRFELAKEF---VLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLndSRSKDALLEALASLSYKL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580804     83 K------ACLMSMLKAVVSIMSPWGNQNILQVVVFTDcglGFGNTSITGFLEAyaekesepefgfLKTLANYNLNFICLG 156
Cdd:smart00327  76 GggtnlgAALQYALENLFSKSAGSRRGAPKVVILITD---GESNDGPKDLLKA------------AKELKRSGVKVFVVG 140


                   ....*...
gi 24580804    157 LHGDYYFT 164
Cdd:smart00327 141 VGNDVDEE 148
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 4-163 1.76e-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: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 39.47  E-value: 1.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580804   4 LIALDASLSMlrpvpgrnEHTYQSLATKGIQHLLDNLTAAGKLEHVALLSYSTTAELKVDFTRDYD--QVRQAVKKVE-- 79
Cdd:cd00198   4 VFLLDVSGSM--------GGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDkaDLLEAIDALKkg 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580804  80 PVDKACLMSMLKAVVSIMSPWGNQNILQV-VVFTDcglGFGNTSITGFLEAYAE-KESEPE---FGFLKTLANYNLNFIC 154
Cdd:cd00198  76 LGGGTNIGAALRLALELLKSAKRPNARRViILLTD---GEPNDGPELLAEAARElRKLGITvytIGIGDDANEDELKEIA 152


                ....*....
gi 24580804 155 LGLHGDYYF 163
Cdd:cd00198 153 DKTTGGAVF 161
 
Name Accession Description Interval E-value
IntS14_b-barrel pfam19435
Integrator complex subunit 14, beta-barrel domain; This entry represents the central ...
 228-426 1.31e-46

Integrator complex subunit 14, beta-barrel domain; This entry represents the central beta-barrel domain of Integrator complex subunit 14 (IntS14), a component of the integrator complex which is involved in the transcription of small nuclear RNAs (snRNA) and their 3'-box-dependent processing. This complex is also involved in the 3'-end processing of the U7 snRNA, and the spliceosomal snRNAs U1 and U5. IntS14 interacts with IntS13, both of them consist of an N-terminal von-Willebrand type A like domain (VWA), followed by a central beta-barrel domain and a C-terminal alpha-helical domain connected through a linker. The interface involves all domains of both proteins, both beta-barrel domains form the centre of the complex and contribute to the major contact between Ints13-IntS14.


Pssm-ID: 466081  Cd Length: 147  Bit Score: 160.51  E-value: 1.31e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580804   228 YKSSEVTLKCGSyfrMEASVLLWPPTAPYEQKSHIFGREPTIRHTdqkIEVCGFLSLSDIGSPATLSRHWVLP-KVEREK 306
Cdd:pfam19435   1 YSPFHGTLKCGN---LSSPVQLFPPPEPYTKDTDFEPITRTISDD---IEICGFIDIADVASPPVISRHLVLPlSTKKEK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580804   307 SGSsrrsgnlsaaakppklnldtsnpnyelekleadikefyaKDSKDTEESGDDDVTIvlkpgpqtEQQKENLCVLLHGA 386
Cdd:pfam19435  75 DES---------------------------------------GKGGKAGEDEDESNTD--------EGKIPSFCVLLHGS 107

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 24580804   387 LKMENMAALVRVGDKWYGFIYAFTDSKKKSNLMLNILPPG 426
Cdd:pfam19435 108 LKVENMVALVQVGEDWYGMLYSWADSKKKSNLMLSIFEPG 147
IntS14_C pfam20504
Integrator complex subunit 14, alpha-helical domain; This entry represents the C-terminal ...
 468-566 8.12e-42

Integrator complex subunit 14, alpha-helical domain; This entry represents the C-terminal alpha-helical domain of Integrator complex subunit 14 (IntS14), a component of the integrator complex which is involved in the transcription of small nuclear RNAs (snRNA) and their 3'-box dependent processing. This complex is also involved in the 3'-end processing of the U7 snRNA, and the spliceosomal snRNAs U1 and U5. IntS14 interacts with IntS13; both of them consist of an N-terminal VWA domain followed by a central beta-barrel domain and a C-terminal alpha-helical domain, which are connected through a linker devoid of secondary structure elements. This domain contribute to binding by packing against the beta-barrel of IntS13.


Pssm-ID: 466653  Cd Length: 103  Bit Score: 145.93  E-value: 8.12e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580804   468 VWIRQASLQSDVQKVLRHAKKMPDKTQHFYKELNRIRRAALALGFVELLEALAMLLEKECAHLSlNGASNDCTLQLQHAA 547
Cdd:pfam20504   1 VWIKPGGLQSDIQKILRHARKLPEKTQQFYKELNRLRRAALSFGFLELLEGLAAMLERECTLLP-GTAHPDAALQLTHAA 79

                          90
                  ....*....|....*....
gi 24580804   548 TELRKTSNRDMKSMIVPLQ 566
Cdd:pfam20504  80 NQLRKSQSRDYKYNITPLQ 98
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 4-173 1.14e-07

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


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 53.40  E-value: 1.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580804   4 LIALDASLSMLRPvpGRNEhtyqslATKG-IQHLLDNLTAAGKlehVALLSYSTTAELKVDFTRDYDQVRQAVKKVEPVD 82
Cdd:COG1240  96 VLVVDASGSMAAE--NRLE------AAKGaLLDFLDDYRPRDR---VGLVAFGGEAEVLLPLTRDREALKRALDELPPGG 164

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580804  83 KACLMSMLKAVVSIMSPWGNQNILQVVVFTDcglGFGNTSITGFLEAYAE-------------KESEPEFGFLKTLANYn 149
Cdd:COG1240 165 GTPLGDALALALELLKRADPARRKVIVLLTD---GRDNAGRIDPLEAAELaaaagiriytigvGTEAVDEGLLREIAEA- 240

                       170       180
                ....*....|....*....|....*...
gi 24580804 150 lnficlgLHGDYYFTRGL----AVYQQL 173
Cdd:COG1240 241 -------TGGRYFRADDLselaAIYREI 261
VWA_2 pfam13519
von Willebrand factor type A domain;
3-111 1.23e-07

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 49.98  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580804     3 TLIALDASLSMLRPVPGRNEHTYQslatkgiQHLLDNLTAAGKLEHVALLSYSTTAELKVDFTRDYDQVRQAVKKVEPVD 82
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTRLEAA-------KDAVLALLKSLPGDRVGLVTFGDGPEVLIPLTKDRAKILRALRRLEPKG 73

                          90       100       110
                  ....*....|....*....|....*....|...
gi 24580804    83 KA-CL---MSMLKAVVSIMSPWGNQnilQVVVF 111
Cdd:pfam13519  74 GGtNLaaaLQLARAALKHRRKNQPR---RIVLI 103
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 5-164 2.37e-04

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: 42.06  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580804      5 IALDASLSMlrpvpGRNEHTYQSLAtkgIQHLLDNLTAAGKLEHVALLSYSTTAELKVDF--TRDYDQVRQAVKKVEPVD 82
Cdd:smart00327   4 FLLDGSGSM-----GGNRFELAKEF---VLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLndSRSKDALLEALASLSYKL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580804     83 K------ACLMSMLKAVVSIMSPWGNQNILQVVVFTDcglGFGNTSITGFLEAyaekesepefgfLKTLANYNLNFICLG 156
Cdd:smart00327  76 GggtnlgAALQYALENLFSKSAGSRRGAPKVVILITD---GESNDGPKDLLKA------------AKELKRSGVKVFVVG 140


                   ....*...
gi 24580804    157 LHGDYYFT 164
Cdd:smart00327 141 VGNDVDEE 148
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 4-163 1.76e-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: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 39.47  E-value: 1.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580804   4 LIALDASLSMlrpvpgrnEHTYQSLATKGIQHLLDNLTAAGKLEHVALLSYSTTAELKVDFTRDYD--QVRQAVKKVE-- 79
Cdd:cd00198   4 VFLLDVSGSM--------GGEKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDkaDLLEAIDALKkg 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580804  80 PVDKACLMSMLKAVVSIMSPWGNQNILQV-VVFTDcglGFGNTSITGFLEAYAE-KESEPE---FGFLKTLANYNLNFIC 154
Cdd:cd00198  76 LGGGTNIGAALRLALELLKSAKRPNARRViILLTD---GEPNDGPELLAEAARElRKLGITvytIGIGDDANEDELKEIA 152


                ....*....
gi 24580804 155 LGLHGDYYF 163
Cdd:cd00198 153 DKTTGGAVF 161
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH