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Conserved domains on  [gi|90193622|ref|NP_001035026|]
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integrator complex subunit 6 isoform b [Homo sapiens]

Protein Classification

integrator subunit 6 family protein( domain architecture ID 11219369)

integrator subunit 6 family protein similar to integrator complex subunit 6 (INTS6) is a component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing

CATH:  3.40.50.410
Gene Ontology:  GO:0034472|GO:0032039
SCOP:  3000832

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
INT_SG_DDX_CT_C pfam15300
INTS6/SAGE1/DDX26B/CT45 C-terminus; This domain is found at the C-terminus of integrator ...
794-855 6.82e-29

INTS6/SAGE1/DDX26B/CT45 C-terminus; This domain is found at the C-terminus of integrator complex subunit 6 (INTS6), sarcoma antigen 1 (SAGE1), protein DDX26B (DDX26B) and members of the cancer/testis antigen family 45.


:

Pssm-ID: 464626  Cd Length: 62  Bit Score: 109.50  E-value: 6.82e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90193622   794 EVNTELKAQIMKEIRKPGRKYERIFTLLKHVQGSLQTRLIFLQNVIKEASRFKKRMLIEQLE 855
Cdd:pfam15300   1 EHNAELKKQVFKEIRRPGRNYEKIFKLLEQVQGPLEIRKKFVEDVIKEAARFKRRVLIQQLE 62
VWA_2 pfam13519
von Willebrand factor type A domain;
1-90 5.45e-10

von Willebrand factor type A domain;


:

Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 57.30  E-value: 5.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90193622     1 MNQRShLGTTYLDTAKGAVETFMKLRardpasRGDRYMLVTFEEPPYaIKAGWKENHATFMNELKNLQAE-GLTTLGQSL 79
Cdd:pfam13519  11 MRNGD-YGPTRLEAAKDAVLALLKSL------PGDRVGLVTFGDGPE-VLIPLTKDRAKILRALRRLEPKgGGTNLAAAL 82
                          90
                  ....*....|.
gi 90193622    80 RTAFDLLNLNR 90
Cdd:pfam13519  83 QLARAALKHRR 93
 
Name Accession Description Interval E-value
INT_SG_DDX_CT_C pfam15300
INTS6/SAGE1/DDX26B/CT45 C-terminus; This domain is found at the C-terminus of integrator ...
794-855 6.82e-29

INTS6/SAGE1/DDX26B/CT45 C-terminus; This domain is found at the C-terminus of integrator complex subunit 6 (INTS6), sarcoma antigen 1 (SAGE1), protein DDX26B (DDX26B) and members of the cancer/testis antigen family 45.


Pssm-ID: 464626  Cd Length: 62  Bit Score: 109.50  E-value: 6.82e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90193622   794 EVNTELKAQIMKEIRKPGRKYERIFTLLKHVQGSLQTRLIFLQNVIKEASRFKKRMLIEQLE 855
Cdd:pfam15300   1 EHNAELKKQVFKEIRRPGRNYEKIFKLLEQVQGPLEIRKKFVEDVIKEAARFKRRVLIQQLE 62
VWA_2 pfam13519
von Willebrand factor type A domain;
1-90 5.45e-10

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 57.30  E-value: 5.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90193622     1 MNQRShLGTTYLDTAKGAVETFMKLRardpasRGDRYMLVTFEEPPYaIKAGWKENHATFMNELKNLQAE-GLTTLGQSL 79
Cdd:pfam13519  11 MRNGD-YGPTRLEAAKDAVLALLKSL------PGDRVGLVTFGDGPE-VLIPLTKDRAKILRALRRLEPKgGGTNLAAAL 82
                          90
                  ....*....|.
gi 90193622    80 RTAFDLLNLNR 90
Cdd:pfam13519  83 QLARAALKHRR 93
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
8-118 1.30e-06

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: 49.10  E-value: 1.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90193622   8 GTTYLDTAKGAVETFmkLRARDPASRGDRYMLVTFEEPPY----AIKAGWKENHATFMNELKNlQAEGLTTLGQSLRTAF 83
Cdd:cd00198  14 GGEKLDKAKEALKAL--VSSLSASPPGDRVGLVTFGSNARvvlpLTTDTDKADLLEAIDALKK-GLGGGTNIGAALRLAL 90
                        90       100       110
                ....*....|....*....|....*....|....*
gi 90193622  84 DLLNLNRLVTGidnygqgrnpfflePAIIITITDG 118
Cdd:cd00198  91 ELLKSAKRPNA--------------RRVIILLTDG 111
 
Name Accession Description Interval E-value
INT_SG_DDX_CT_C pfam15300
INTS6/SAGE1/DDX26B/CT45 C-terminus; This domain is found at the C-terminus of integrator ...
794-855 6.82e-29

INTS6/SAGE1/DDX26B/CT45 C-terminus; This domain is found at the C-terminus of integrator complex subunit 6 (INTS6), sarcoma antigen 1 (SAGE1), protein DDX26B (DDX26B) and members of the cancer/testis antigen family 45.


Pssm-ID: 464626  Cd Length: 62  Bit Score: 109.50  E-value: 6.82e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90193622   794 EVNTELKAQIMKEIRKPGRKYERIFTLLKHVQGSLQTRLIFLQNVIKEASRFKKRMLIEQLE 855
Cdd:pfam15300   1 EHNAELKKQVFKEIRRPGRNYEKIFKLLEQVQGPLEIRKKFVEDVIKEAARFKRRVLIQQLE 62
VWA_2 pfam13519
von Willebrand factor type A domain;
1-90 5.45e-10

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 57.30  E-value: 5.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90193622     1 MNQRShLGTTYLDTAKGAVETFMKLRardpasRGDRYMLVTFEEPPYaIKAGWKENHATFMNELKNLQAE-GLTTLGQSL 79
Cdd:pfam13519  11 MRNGD-YGPTRLEAAKDAVLALLKSL------PGDRVGLVTFGDGPE-VLIPLTKDRAKILRALRRLEPKgGGTNLAAAL 82
                          90
                  ....*....|.
gi 90193622    80 RTAFDLLNLNR 90
Cdd:pfam13519  83 QLARAALKHRR 93
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
8-118 1.30e-06

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: 49.10  E-value: 1.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90193622   8 GTTYLDTAKGAVETFmkLRARDPASRGDRYMLVTFEEPPY----AIKAGWKENHATFMNELKNlQAEGLTTLGQSLRTAF 83
Cdd:cd00198  14 GGEKLDKAKEALKAL--VSSLSASPPGDRVGLVTFGSNARvvlpLTTDTDKADLLEAIDALKK-GLGGGTNIGAALRLAL 90
                        90       100       110
                ....*....|....*....|....*....|....*
gi 90193622  84 DLLNLNRLVTGidnygqgrnpfflePAIIITITDG 118
Cdd:cd00198  91 ELLKSAKRPNA--------------RRVIILLTDG 111
 
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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