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Conserved domains on  [gi|440216457|gb|AGB95105|]
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integrator 6, isoform C [Drosophila melanogaster]

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
PubMed:  12579041|10830113|12388743
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 ...
 1196-1256 4.30e-26

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: 102.19  E-value: 4.30e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 440216457  1196 HNVELRLQIFRDIRRPGRDYSQLLEHLNLVKGDQDMQSDFVDMCIVESLRFRRHRMASSIQ 1256
Cdd:pfam15300    2 HNAELKKQVFKEIRRPGRNYEKIFKLLEQVQGPLEIRKKFVEDVIKEAARFKRRVLIQQLE 62
VWA_2 pfam13519
von Willebrand factor type A domain;
4-131 1.08e-14

von Willebrand factor type A domain;


:

Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 71.17  E-value: 1.08e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216457     4 ILFLVDTSSSMCQKAYvngvQKTYLDIAKGAVETFLKYRQrtqdclGDRYMLLTFEEPPaNVKAGWKENHATFMNELKNL 83
Cdd:pfam13519    1 LVFVLDTSGSMRNGDY----GPTRLEAAKDAVLALLKSLP------GDRVGLVTFGDGP-EVLIPLTKDRAKILRALRRL 69

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 440216457    84 Q-SHGLTSMGESLRNAFDLLNLNRMQsgidtygqgrcpfylEPSVIIVI 131
Cdd:pfam13519   70 EpKGGGTNLAAALQLARAALKHRRKN---------------QPRRIVLI 103
 
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 ...
 1196-1256 4.30e-26

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: 102.19  E-value: 4.30e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 440216457  1196 HNVELRLQIFRDIRRPGRDYSQLLEHLNLVKGDQDMQSDFVDMCIVESLRFRRHRMASSIQ 1256
Cdd:pfam15300    2 HNAELKKQVFKEIRRPGRNYEKIFKLLEQVQGPLEIRKKFVEDVIKEAARFKRRVLIQQLE 62
VWA_2 pfam13519
von Willebrand factor type A domain;
4-131 1.08e-14

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 71.17  E-value: 1.08e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216457     4 ILFLVDTSSSMCQKAYvngvQKTYLDIAKGAVETFLKYRQrtqdclGDRYMLLTFEEPPaNVKAGWKENHATFMNELKNL 83
Cdd:pfam13519    1 LVFVLDTSGSMRNGDY----GPTRLEAAKDAVLALLKSLP------GDRVGLVTFGDGP-EVLIPLTKDRAKILRALRRL 69

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 440216457    84 Q-SHGLTSMGESLRNAFDLLNLNRMQsgidtygqgrcpfylEPSVIIVI 131
Cdd:pfam13519   70 EpKGGGTNLAAALQLARAALKHRRKN---------------QPRRIVLI 103
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 4-147 5.59e-12

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: 65.28  E-value: 5.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216457    4 ILFLVDTSSSMcqkayvngvQKTYLDIAKGAVETFLKyrQRTQDCLGDRYMLLTFEEPPANV----KAGWKENHATFMNE 79
Cdd:cd00198     3 IVFLLDVSGSM---------GGEKLDKAKEALKALVS--SLSASPPGDRVGLVTFGSNARVVlpltTDTDKADLLEAIDA 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 440216457   80 LKNlQSHGLTSMGESLRNAFDLLNLNRMQSGidtygqgrcpfylePSVIIVITDGGRYSYRNGVHQEI 147
Cdd:cd00198    72 LKK-GLGGGTNIGAALRLALELLKSAKRPNA--------------RRVIILLTDGEPNDGPELLAEAA 124
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 4-134 2.38e-09

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: 59.57  E-value: 2.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216457    4 ILFLVDTSSSMcqkayvngVQKTYLDIAKGAVETFLK-YRQRtqdclgDRYMLLTFEEpPANVKAGWKENHATFMNELKN 82
Cdd:COG1240    95 VVLVVDASGSM--------AAENRLEAAKGALLDFLDdYRPR------DRVGLVAFGG-EAEVLLPLTRDREALKRALDE 159

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 440216457   83 LQSHGLTSMGESLRNAFDLLnlnrmqsgiDTYGQGRcpfylePSVIIVITDG 134
Cdd:COG1240   160 LPPGGGTPLGDALALALELL---------KRADPAR------RKVIVLLTDG 196
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 4-134 8.93e-09

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: 56.31  E-value: 8.93e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216457      4 ILFLVDTSSSMcqkayvngvQKTYLDIAKGAVETFLKyrQRTQDCLGDRYMLLTF-EEPPANVKAGWKENHATFMNELKN 82
Cdd:smart00327    2 VVFLLDGSGSM---------GGNRFELAKEFVLKLVE--QLDIGPDGDRVGLVTFsDDARVLFPLNDSRSKDALLEALAS 70

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 440216457     83 LQ--SHGLTSMGESLRNAFDLLNLNRMQSGIDtygqgrcpfylEPSVIIVITDG 134
Cdd:smart00327   71 LSykLGGGTNLGAALQYALENLFSKSAGSRRG-----------APKVVILITDG 113
 
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 ...
 1196-1256 4.30e-26

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: 102.19  E-value: 4.30e-26
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 440216457  1196 HNVELRLQIFRDIRRPGRDYSQLLEHLNLVKGDQDMQSDFVDMCIVESLRFRRHRMASSIQ 1256
Cdd:pfam15300    2 HNAELKKQVFKEIRRPGRNYEKIFKLLEQVQGPLEIRKKFVEDVIKEAARFKRRVLIQQLE 62
VWA_2 pfam13519
von Willebrand factor type A domain;
4-131 1.08e-14

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 71.17  E-value: 1.08e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216457     4 ILFLVDTSSSMCQKAYvngvQKTYLDIAKGAVETFLKYRQrtqdclGDRYMLLTFEEPPaNVKAGWKENHATFMNELKNL 83
Cdd:pfam13519    1 LVFVLDTSGSMRNGDY----GPTRLEAAKDAVLALLKSLP------GDRVGLVTFGDGP-EVLIPLTKDRAKILRALRRL 69

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 440216457    84 Q-SHGLTSMGESLRNAFDLLNLNRMQsgidtygqgrcpfylEPSVIIVI 131
Cdd:pfam13519   70 EpKGGGTNLAAALQLARAALKHRRKN---------------QPRRIVLI 103
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 4-147 5.59e-12

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: 65.28  E-value: 5.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216457    4 ILFLVDTSSSMcqkayvngvQKTYLDIAKGAVETFLKyrQRTQDCLGDRYMLLTFEEPPANV----KAGWKENHATFMNE 79
Cdd:cd00198     3 IVFLLDVSGSM---------GGEKLDKAKEALKALVS--SLSASPPGDRVGLVTFGSNARVVlpltTDTDKADLLEAIDA 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 440216457   80 LKNlQSHGLTSMGESLRNAFDLLNLNRMQSGidtygqgrcpfylePSVIIVITDGGRYSYRNGVHQEI 147
Cdd:cd00198    72 LKK-GLGGGTNIGAALRLALELLKSAKRPNA--------------RRVIILLTDGEPNDGPELLAEAA 124
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 4-134 2.38e-09

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: 59.57  E-value: 2.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216457    4 ILFLVDTSSSMcqkayvngVQKTYLDIAKGAVETFLK-YRQRtqdclgDRYMLLTFEEpPANVKAGWKENHATFMNELKN 82
Cdd:COG1240    95 VVLVVDASGSM--------AAENRLEAAKGALLDFLDdYRPR------DRVGLVAFGG-EAEVLLPLTRDREALKRALDE 159

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 440216457   83 LQSHGLTSMGESLRNAFDLLnlnrmqsgiDTYGQGRcpfylePSVIIVITDG 134
Cdd:COG1240   160 LPPGGGTPLGDALALALELL---------KRADPAR------RKVIVLLTDG 196
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 4-134 8.93e-09

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: 56.31  E-value: 8.93e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216457      4 ILFLVDTSSSMcqkayvngvQKTYLDIAKGAVETFLKyrQRTQDCLGDRYMLLTF-EEPPANVKAGWKENHATFMNELKN 82
Cdd:smart00327    2 VVFLLDGSGSM---------GGNRFELAKEFVLKLVE--QLDIGPDGDRVGLVTFsDDARVLFPLNDSRSKDALLEALAS 70

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 440216457     83 LQ--SHGLTSMGESLRNAFDLLNLNRMQSGIDtygqgrcpfylEPSVIIVITDG 134
Cdd:smart00327   71 LSykLGGGTNLGAALQYALENLFSKSAGSRRG-----------APKVVILITDG 113
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 6-134 1.85e-03

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 42.01  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216457    6 FLVDTSSSMcqkayvNGvQKtyLDIAKGAVETFLKyRQRTQDCLGdrymLLTFEE------PPANVkagwkENHATFMNE 79
Cdd:COG2304    96 FVIDVSGSM------SG-DK--LELAKEAAKLLVD-QLRPGDRVS----IVTFAGdarvllPPTPA-----TDRAKILAA 156

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 440216457   80 LKNLQSHGLTSMGESLRNAFDLLNLNRMQSGIdtygqgrcpfylepSVIIVITDG 134
Cdd:COG2304   157 IDRLQAGGGTALGAGLELAYELARKHFIPGRV--------------NRVILLTDG 197
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 4-134 2.87e-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: 39.97  E-value: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216457    4 ILFLVDTSSSmcqkayvngVQKTYLDIAKGAVETFLKYRQRTQDclGDRYMLLTF-EEPPANVKAGWKENHATFMNELKN 82
Cdd:cd01450     3 IVFLLDGSES---------VGPENFEKVKDFIEKLVEKLDIGPD--KTRVGLVQYsDDVRVEFSLNDYKSKDDLLKAVKN 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 440216457   83 LQSHG--LTSMGESLRNAFDLLNLNRMqsgidtygqgrcPFYLEPSVIIVITDG 134
Cdd:cd01450    72 LKYLGggGTNTGKALQYALEQLFSESN------------ARENVPKVIIVLTDG 113
vWA_Magnesium_chelatase cd01451
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ...
 2-134 4.66e-03

Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). In chlorophyll biosynthesis, insertion of Mg2+ into protoporphyrin IX is catalysed by magnesium chelatase in an ATP-dependent reaction. Magnesium chelatase is a three sub-unit (BchI, BchD and BchH) enzyme with a novel arrangement of domains: the C-terminal helical domain is located behind the nucleotide binding site. The BchD domain contains a AAA domain at its N-terminus and a VWA domain at its C-terminus. The VWA domain has been speculated to be involved in mediating protein-protein interactions.


Pssm-ID: 238728 [Multi-domain]  Cd Length: 178  Bit Score: 39.57  E-value: 4.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216457    2 TIILFLVDTSSSMcqkAYVNGVQKtyldiAKGAVETFLK--YRQRtqdclgDRYMLLTF--EE-----PPAN--VKAGwk 70
Cdd:cd01451     1 NLVIFVVDASGSM---AARHRMAA-----AKGAVLSLLRdaYQRR------DKVALIAFrgTEaevllPPTRsvELAK-- 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 440216457   71 enhatfmNELKNLQSHGLTSMGESLRNAFDLLNLNRmqsgidtYGQGRCPfylepsVIIVITDG 134
Cdd:cd01451    65 -------RRLARLPTGGGTPLAAGLLAAYELAAEQA-------RDPGQRP------LIVVITDG 108
VWA pfam00092
von Willebrand factor type A domain;
4-134 5.45e-03

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 39.18  E-value: 5.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440216457     4 ILFLVDTSSSMCQKayvngvqktYLDIAKGAVETFLKyrQRTQDCLGDRYMLLTF-EEPPANVKAGWKENHATFMNELKN 82
Cdd:pfam00092    2 IVFLLDGSGSIGGD---------NFEKVKEFLKKLVE--SLDIGPDGTRVGLVQYsSDVRTEFPLNDYSSKEELLSAVDN 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 440216457    83 L--QSHGLTSMGESLRNAFDllNLNRMQSGidtygqGRcPFYlePSVIIVITDG 134
Cdd:pfam00092   71 LryLGGGTTNTGKALKYALE--NLFSSAAG------AR-PGA--PKVVVLLTDG 113
 
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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