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Conserved domains on  [gi|2113274756|gb|KAH1187893|]
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hypothetical protein KIL84_017901 [Mauremys mutica]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
 15-80 5.07e-33

ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.


The actual alignment was detected with superfamily member cd13395:

Pssm-ID: 483947 [Multi-domain]  Cd Length: 413  Bit Score: 131.15  E-value: 5.07e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2113274756  15 LYGSVIVTGGNTLLQGFTDRLNRELSQKTPPvsvcSMRLKLIASNSTMERRFSPWIGGSILASLGT 80
Cdd:cd13395   337 LYGNVVLTGGNSLLPGFTDRLNRELSEKAPG----SLKLKILASGNTVERRFSSWIGGSILASLGS 398
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 440-565 1.05e-28

von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.


:

Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 111.69  E-value: 1.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113274756 440 CYVSGDPHYQTFDGRRLDFMGTCTYTLAQPCGNYTGPWFSVEGKNEARGRRGVsYLRAVHVRLPGAGLTLRKGRRVLING 519
Cdd:pfam00094   1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGTVLVNG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2113274756 520 TRVTLP-ARPTRDASVALSGQ-YVAVETSFGLALRWDGTHYLEIRAPR 565
Cdd:pfam00094  80 QKVSLPyKSDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSP 127
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 79-210 9.42e-28

von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.


:

Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 109.00  E-value: 9.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113274756  79 GTCTYVLAQPCNASLAPApFAVRAASEHRHGHSTvsYVRAVVLELPGATVGLLKNRVVQVNGSQVTLPAVPA-PGVSVRL 157
Cdd:pfam00094  21 GTCTYVLAKDCSEEPDFS-FSVTNKNCNGGASGV--CLKSVTVIVGDLEITLQKGGTVLVNGQKVSLPYKSDgGEVEILG 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2113274756 158 SG-AFAEVRTDFGLVVRYDGNHYAEVRVGQQYRGALCGLCGDYNGDPGDDFRTP 210
Cdd:pfam00094  98 SGfVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTP 151
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 249-323 7.70e-25

This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.


:

Pssm-ID: 214843  Cd Length: 76  Bit Score: 98.18  E-value: 7.70e-25
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2113274756  249 YEGPGACGILLAPDGPFAPCHGQLSPMTFFRDCVFDLCALGGDRRQLCSALGSYGAQCQTHSVSLGPWRNQTLCP 323
Cdd:smart00832   2 YYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 326-378 2.78e-11

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.


:

Pssm-ID: 460351  Cd Length: 55  Bit Score: 58.94  E-value: 2.78e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2113274756 326 CPTHSHYEPCGPPCPAACPEAGVR-GCQGPCLEGCSCDPGFLLSGGG-CVPQGGC 378
Cdd:pfam01826   1 CPANEVYSECGSACPPTCANLSPPdVCPEPCVEGCVCPPGFVRNSGGkCVPPSDC 55
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 380-433 1.06e-09

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


The actual alignment was detected with superfamily member pfam12714:

Pssm-ID: 450195  Cd Length: 54  Bit Score: 54.23  E-value: 1.06e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2113274756 380 CSYAGGYHELGEEFFGPGCGSRCRCEGGNrTHCQAWQCRPTETCGLHNGLYGCH 433
Cdd:pfam12714   2 KDAQGNYIPAGKTWFSSGCTQSCTCTGGN-IQCQPFQCPPGTVCKDNDGSSNCH 54
 
Name Accession Description Interval E-value
ASKHA_NBD_Arp4_ACTL6-like cd13395
nucleotide-binding domain (NBD) of the actin-related protein 4 (Arp4)-like subfamily; The ...
 15-80 5.07e-33

nucleotide-binding domain (NBD) of the actin-related protein 4 (Arp4)-like subfamily; The Arp4-like subfamily includes Arp4, also called actin-like protein 4, from fungi and plants. Saccharomyces cerevisiae Arp4 acts synergistically with Arp8 to depolymerize F-actin; it binds ATP, but unlike conventional actin, does not form filaments. It is a component of the NuA4 histone acetyltransferase complex, the chromatin-remodeling INO80 complex and the SWR1 chromatin remodeling complex. Arabidopsis thaliana Arp4 is involved in several developmental processes including organization of plant organs, flowering time, anther development, flower senescence and fertility, probably by regulating the chromatin structure. This family also includes human homologs of yeast and plant, which are actin-like protein 6A (encoded by the ACTL6A gene; also known as ArpNbeta, 53 kDa BRG1-associated factor A/BRG1-associated factor 53A/BAF35A, and INO80 complex subunit K/INO80K) and actin-like protein 6B (encoded by the ACTL6B gene; also known as ArpNalpha, 53 kDa BRG1-associated factor B/BRG1-associated factor 53B/BAF35B). ACTL6A and ACTL6B are involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). They are components of numerous complexes with chromatin remodeling and histone acetyltransferase activity. ACTL6A is also a putative core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Schizosaccharomyces pombe actin-related protein 42 (Arp42) is also included in this family. It is also a component of SWI/SNF and RSC complexes.


Pssm-ID: 466846 [Multi-domain]  Cd Length: 413  Bit Score: 131.15  E-value: 5.07e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2113274756  15 LYGSVIVTGGNTLLQGFTDRLNRELSQKTPPvsvcSMRLKLIASNSTMERRFSPWIGGSILASLGT 80
Cdd:cd13395   337 LYGNVVLTGGNSLLPGFTDRLNRELSEKAPG----SLKLKILASGNTVERRFSSWIGGSILASLGS 398
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 440-565 1.05e-28

von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 111.69  E-value: 1.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113274756 440 CYVSGDPHYQTFDGRRLDFMGTCTYTLAQPCGNYTGPWFSVEGKNEARGRRGVsYLRAVHVRLPGAGLTLRKGRRVLING 519
Cdd:pfam00094   1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGTVLVNG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2113274756 520 TRVTLP-ARPTRDASVALSGQ-YVAVETSFGLALRWDGTHYLEIRAPR 565
Cdd:pfam00094  80 QKVSLPyKSDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSP 127
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 79-210 9.42e-28

von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 109.00  E-value: 9.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113274756  79 GTCTYVLAQPCNASLAPApFAVRAASEHRHGHSTvsYVRAVVLELPGATVGLLKNRVVQVNGSQVTLPAVPA-PGVSVRL 157
Cdd:pfam00094  21 GTCTYVLAKDCSEEPDFS-FSVTNKNCNGGASGV--CLKSVTVIVGDLEITLQKGGTVLVNGQKVSLPYKSDgGEVEILG 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2113274756 158 SG-AFAEVRTDFGLVVRYDGNHYAEVRVGQQYRGALCGLCGDYNGDPGDDFRTP 210
Cdd:pfam00094  98 SGfVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTP 151
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 72-210 2.41e-26

von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 105.18  E-value: 2.41e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113274756   72 GSILASLGTCTYVLAQPCNASLapaPFAVRAASEHRHGhsTVSYVRAVVLELPGATVGLLK-NRVVQVNGSQVTLPAVPA 150
Cdd:smart00216  25 GVAYTFPGNCYYVLAQDCSSEP---TFSVLLKNVPCGG--GATCLKSVKVELNGDEIELKDdNGKVTVNGQQVSLPYKTS 99

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2113274756  151 PG-VSVRLSGAFAEVRTDFGLV-VRYDGNHYAEVRVGQQYRGALCGLCGDYNGDPGDDFRTP 210
Cdd:smart00216 100 DGsIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTP 161
Actin pfam00022
Actin;
15-80 1.36e-25

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 109.32  E-value: 1.36e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2113274756  15 LYGSVIVTGGNTLLQGFTDRLNRELSQKTPPvsvcSMRLKLIASNSTMERRFSPWIGGSILASLGT 80
Cdd:pfam00022 322 LLANIVVTGGNSLFPGFTERLEKELAQLAPP----GVKVKIIAPGNTVERRYSAWIGGSILASLGT 383
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 249-323 7.70e-25

This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 98.18  E-value: 7.70e-25
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2113274756  249 YEGPGACGILLAPDGPFAPCHGQLSPMTFFRDCVFDLCALGGDRRQLCSALGSYGAQCQTHSVSLGPWRNQTLCP 323
Cdd:smart00832   2 YYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 432-564 1.39e-23

von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 97.47  E-value: 1.39e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113274756  432 CHPTASAPCYVSGDPHYQTFDGRRLDFMGTCTYTLAQPCGnyTGPWFSVEGKNEARGrRGVSYLRAVHVRLPGAGLTLRK 511
Cdd:smart00216   4 TQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCS--SEPTFSVLLKNVPCG-GGATCLKSVKVELNGDEIELKD 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2113274756  512 GRR-VLINGTRVTLPA-RPTRDASVALSGQYVAVETSFGLA-LRWDGTHYLEIRAP 564
Cdd:smart00216  81 DNGkVTVNGQQVSLPYkTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLP 136
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 255-322 7.34e-21

C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 86.28  E-value: 7.34e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2113274756 255 CGILLApDGPFAPCHGQLSPMTFFRDCVFDLCALGGDRRQLCSALGSYGAQCQTHSVSLGPWRNQTLC 322
Cdd:pfam08742   2 CGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
 15-80 3.96e-16

Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 80.38  E-value: 3.96e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2113274756   15 LYGSVIVTGGNTLLQGFTDRLNRELSQKTPPvsvcSMRLKLIAsnsTMERRFSPWIGGSILASLGT 80
Cdd:smart00268 291 LYENIVLSGGSTLIPGFGERLEKELKQLAPK----KLKVKVIA---PPERKYSVWLGGSILASLST 349
PTZ00004 PTZ00004
actin-2; Provisional
 15-80 1.68e-11

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 66.33  E-value: 1.68e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2113274756  15 LYGSVIVTGGNTLLQGFTDRLNRELSQKTPPvsvcSMRLKLIASnstMERRFSPWIGGSILASLGT 80
Cdd:PTZ00004  296 LYGNIVLSGGTTMYRGLPERLTKELTTLAPS----TMKIKVVAP---PERKYSVWIGGSILSSLPT 354
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 326-378 2.78e-11

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 58.94  E-value: 2.78e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2113274756 326 CPTHSHYEPCGPPCPAACPEAGVR-GCQGPCLEGCSCDPGFLLSGGG-CVPQGGC 378
Cdd:pfam01826   1 CPANEVYSECGSACPPTCANLSPPdVCPEPCVEGCVCPPGFVRNSGGkCVPPSDC 55
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 326-378 1.66e-10

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 56.56  E-value: 1.66e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2113274756 326 CPTHSHYEPCGPPCPAACPE-AGVRGCQGPCLEGCSCDPGFLLSGGG-CVPQGGC 378
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANpNAPPPCTKQCVEGCFCPEGYVRNSGGkCVPPSQC 55
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 380-433 1.06e-09

TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative.


Pssm-ID: 432736  Cd Length: 54  Bit Score: 54.23  E-value: 1.06e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2113274756 380 CSYAGGYHELGEEFFGPGCGSRCRCEGGNrTHCQAWQCRPTETCGLHNGLYGCH 433
Cdd:pfam12714   2 KDAQGNYIPAGKTWFSSGCTQSCTCTGGN-IQCQPFQCPPGTVCKDNDGSSNCH 54
 
Name Accession Description Interval E-value
ASKHA_NBD_Arp4_ACTL6-like cd13395
nucleotide-binding domain (NBD) of the actin-related protein 4 (Arp4)-like subfamily; The ...
 15-80 5.07e-33

nucleotide-binding domain (NBD) of the actin-related protein 4 (Arp4)-like subfamily; The Arp4-like subfamily includes Arp4, also called actin-like protein 4, from fungi and plants. Saccharomyces cerevisiae Arp4 acts synergistically with Arp8 to depolymerize F-actin; it binds ATP, but unlike conventional actin, does not form filaments. It is a component of the NuA4 histone acetyltransferase complex, the chromatin-remodeling INO80 complex and the SWR1 chromatin remodeling complex. Arabidopsis thaliana Arp4 is involved in several developmental processes including organization of plant organs, flowering time, anther development, flower senescence and fertility, probably by regulating the chromatin structure. This family also includes human homologs of yeast and plant, which are actin-like protein 6A (encoded by the ACTL6A gene; also known as ArpNbeta, 53 kDa BRG1-associated factor A/BRG1-associated factor 53A/BAF35A, and INO80 complex subunit K/INO80K) and actin-like protein 6B (encoded by the ACTL6B gene; also known as ArpNalpha, 53 kDa BRG1-associated factor B/BRG1-associated factor 53B/BAF35B). ACTL6A and ACTL6B are involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). They are components of numerous complexes with chromatin remodeling and histone acetyltransferase activity. ACTL6A is also a putative core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Schizosaccharomyces pombe actin-related protein 42 (Arp42) is also included in this family. It is also a component of SWI/SNF and RSC complexes.


Pssm-ID: 466846 [Multi-domain]  Cd Length: 413  Bit Score: 131.15  E-value: 5.07e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2113274756  15 LYGSVIVTGGNTLLQGFTDRLNRELSQKTPPvsvcSMRLKLIASNSTMERRFSPWIGGSILASLGT 80
Cdd:cd13395   337 LYGNVVLTGGNSLLPGFTDRLNRELSEKAPG----SLKLKILASGNTVERRFSSWIGGSILASLGS 398
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 440-565 1.05e-28

von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 111.69  E-value: 1.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113274756 440 CYVSGDPHYQTFDGRRLDFMGTCTYTLAQPCGNYTGPWFSVEGKNEARGRRGVsYLRAVHVRLPGAGLTLRKGRRVLING 519
Cdd:pfam00094   1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDCSEEPDFSFSVTNKNCNGGASGV-CLKSVTVIVGDLEITLQKGGTVLVNG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2113274756 520 TRVTLP-ARPTRDASVALSGQ-YVAVETSFGLALRWDGTHYLEIRAPR 565
Cdd:pfam00094  80 QKVSLPyKSDGGEVEILGSGFvVVDLSPGVGLQVDGDGRGQLFVTLSP 127
VWD pfam00094
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ...
 79-210 9.42e-28

von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.


Pssm-ID: 459671 [Multi-domain]  Cd Length: 154  Bit Score: 109.00  E-value: 9.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113274756  79 GTCTYVLAQPCNASLAPApFAVRAASEHRHGHSTvsYVRAVVLELPGATVGLLKNRVVQVNGSQVTLPAVPA-PGVSVRL 157
Cdd:pfam00094  21 GTCTYVLAKDCSEEPDFS-FSVTNKNCNGGASGV--CLKSVTVIVGDLEITLQKGGTVLVNGQKVSLPYKSDgGEVEILG 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2113274756 158 SG-AFAEVRTDFGLVVRYDGNHYAEVRVGQQYRGALCGLCGDYNGDPGDDFRTP 210
Cdd:pfam00094  98 SGfVVVDLSPGVGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTP 151
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 72-210 2.41e-26

von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 105.18  E-value: 2.41e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113274756   72 GSILASLGTCTYVLAQPCNASLapaPFAVRAASEHRHGhsTVSYVRAVVLELPGATVGLLK-NRVVQVNGSQVTLPAVPA 150
Cdd:smart00216  25 GVAYTFPGNCYYVLAQDCSSEP---TFSVLLKNVPCGG--GATCLKSVKVELNGDEIELKDdNGKVTVNGQQVSLPYKTS 99

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2113274756  151 PG-VSVRLSGAFAEVRTDFGLV-VRYDGNHYAEVRVGQQYRGALCGLCGDYNGDPGDDFRTP 210
Cdd:smart00216 100 DGsIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTP 161
Actin pfam00022
Actin;
15-80 1.36e-25

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 109.32  E-value: 1.36e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2113274756  15 LYGSVIVTGGNTLLQGFTDRLNRELSQKTPPvsvcSMRLKLIASNSTMERRFSPWIGGSILASLGT 80
Cdd:pfam00022 322 LLANIVVTGGNSLFPGFTERLEKELAQLAPP----GVKVKIIAPGNTVERRYSAWIGGSILASLGT 383
C8 smart00832
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ...
 249-323 7.70e-25

This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.


Pssm-ID: 214843  Cd Length: 76  Bit Score: 98.18  E-value: 7.70e-25
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2113274756  249 YEGPGACGILLAPDGPFAPCHGQLSPMTFFRDCVFDLCALGGDRRQLCSALGSYGAQCQTHSVSLGPWRNQTLCP 323
Cdd:smart00832   2 YYACSQCGILLSPRGPFAACHSVVDPEPFFENCVYDTCACGGDCECLCDALAAYAAACAEAGVCISPWRTPTFCP 76
VWD smart00216
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ...
 432-564 1.39e-23

von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.


Pssm-ID: 214566 [Multi-domain]  Cd Length: 163  Bit Score: 97.47  E-value: 1.39e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113274756  432 CHPTASAPCYVSGDPHYQTFDGRRLDFMGTCTYTLAQPCGnyTGPWFSVEGKNEARGrRGVSYLRAVHVRLPGAGLTLRK 511
Cdd:smart00216   4 TQEECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCS--SEPTFSVLLKNVPCG-GGATCLKSVKVELNGDEIELKD 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2113274756  512 GRR-VLINGTRVTLPA-RPTRDASVALSGQYVAVETSFGLA-LRWDGTHYLEIRAP 564
Cdd:smart00216  81 DNGkVTVNGQQVSLPYkTSDGSIQIRSSGGYLVVITSLGLIqVTFDGLTLLSVQLP 136
C8 pfam08742
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ...
 255-322 7.34e-21

C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.


Pssm-ID: 462584  Cd Length: 68  Bit Score: 86.28  E-value: 7.34e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2113274756 255 CGILLApDGPFAPCHGQLSPMTFFRDCVFDLCALGGDRRQLCSALGSYGAQCQTHSVSLGPWRNQTLC 322
Cdd:pfam08742   2 CGLLSD-SGPFAPCHSVVDPEPYFEACVYDMCSCGGDDECLCAALAAYARACQAAGVCIGDWRTPTFC 68
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
 15-80 9.89e-17

nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ubiquitous in eukaryotes, and the major component of the actin cytoskeleton; monomeric globular protein (G-actin) reversibly polymerizes to form filaments (F-actin). Each actin protomer binds one molecule of ATP and either calcium or magnesium ions. F-actin filaments form with the consequent hydrolysis of ATP. Some actin-related proteins (Arps) have roles in cytoskeletal functions, such as actin polymerization (Arp2/3) and dynein motor activity (Arp1). Both conventional actin and specific Arps have been implicated in chromatin remodeling and/or transcription regulation. The actin/ARP family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466810 [Multi-domain]  Cd Length: 258  Bit Score: 80.23  E-value: 9.89e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2113274756  15 LYGSVIVTGGNTLLQGFTDRLNRELSQKTPPvsvcSMRLKLIASnstMERRFSPWIGGSILASLGT 80
Cdd:cd10169   185 LYSNIVLSGGTTLFPGFAERLQKELSKLAPS----SVKVKVIAP---PERKYSAWIGGSILASLST 243
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
 15-80 3.96e-16

Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 80.38  E-value: 3.96e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2113274756   15 LYGSVIVTGGNTLLQGFTDRLNRELSQKTPPvsvcSMRLKLIAsnsTMERRFSPWIGGSILASLGT 80
Cdd:smart00268 291 LYENIVLSGGSTLIPGFGERLEKELKQLAPK----KLKVKVIA---PPERKYSVWLGGSILASLST 349
ASKHA_NBD_actin_Arp-T1-3 cd13397
nucleotide-binding domain (NBD) of actin, actin-related proteins T1-T3 (Arp-T1-3), and similar ...
 15-80 1.25e-15

nucleotide-binding domain (NBD) of actin, actin-related proteins T1-T3 (Arp-T1-3), and similar proteins; The family includes actin and human actin-related proteins T1, T2, and T3. Actin is a ubiquitous protein involved in the formation of filaments that are major components of the cytoskeleton. It is a highly dynamic structural protein network involved in processes such as cell contraction, cell motility, vesicle trafficking, intracellular organization, cytokinesis, endocytosis and apoptosis. Arp-T1, encoded by ACTRT1/ARPT1 gene expressed in testis, negatively regulates the Hedgehog (SHH) signaling, binds to the promoter of the SHH signaling mediator, GLI1, and inhibits its expression. Arp-T2 (also called actin-related protein M2; encoded by ACTRT2/ARPM2 gene expressed in testis and various other cell types) and Arp-T3 (also called actin-related protein M1; encoded by ACTRT3/ARPM1 gene expressed in all tested human tissues) play general roles in the organization of the cytoskeleton like other cytoplasmic actin-related proteins.


Pssm-ID: 466848 [Multi-domain]  Cd Length: 359  Bit Score: 78.77  E-value: 1.25e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2113274756  15 LYGSVIVTGGNTLLQGFTDRLNRELSQKTPPvsvcSMRLKLIASNstmERRFSPWIGGSILASLGT 80
Cdd:cd13397   286 LYSNIVLSGGSTMFPGLPERLQKELEALAPS----STKVKVIAPP---ERKYSVWIGGSILASLST 344
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
 15-80 1.27e-13

nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, also called centractin, actin-like protein, alpha-centractin, actin-RPV, or centrosome-associated actin homolog, may be a component of a multi-subunit centrosomal complex involved in microtubule-based vesicle motility. In yeast, actin-related protein is essential for viability and is associated with the centrosome. In vertebrates, Arp1 is a core component of the dynactin complex which assists cytoplasmic dynein by increasing its processivity and by regulation of its cargo binding. The dynactin complex is required for the spindle translocation late in anaphase and is involved in a cell wall synthesis checkpoint. ARP1 forms the backbone filament of the dynactin rod structure and serves as the scaffold for the remaining subunits. It is required for proper orientation of the mitotic spindle. Arp1 is the only actin-related protein known to form actin-like filaments. Human Arp1/centractin is encoded by the ACTR1A gene.


Pssm-ID: 466820 [Multi-domain]  Cd Length: 370  Bit Score: 72.58  E-value: 1.27e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2113274756  15 LYGSVIVTGGNTLLQGFTDRLNRELSQKTPPvsvcSMRLKLIASNstmERRFSPWIGGSILASLGT 80
Cdd:cd10216   289 LYSNIVLSGGSTLFKGFGDRLLSEVKKLAPK----DVKIRISAPP---ERLYSTWIGGSILASLST 347
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
 15-80 1.95e-13

nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein involved in the formation of filaments that are major components of the cytoskeleton. It is a highly dynamic structural protein network involved in processes such as cell contraction, cell motility, vesicle trafficking, intracellular organization, cytokinesis, endocytosis and apoptosis. Actin is a monomeric globular protein (G-actin) that reversibly polymerizes to form filaments (F-actin). Each actin protomer binds one molecule of ATP and either calcium or magnesium ions. At low salt concentrations, actin exists as a monomer, and as the salt concentration rises F-actin forms, with the consequent hydrolysis of ATP. F-actin assembly is in constant flux with G-actin association occurring at the barbed end (+) and its disassociation at the pointed end (-). Actin monomers that have been released from the pointed end can be reused, if the ADP is exchanged for ATP. F-actin filaments can assemble into higher order structures, for example branched F-actin, and stress fibers. Actin binding proteins regulate actin filament dynamics by a range of functions including actin severing, depolymerizing, capping, stabilizing and de novo actin polymerization. Actins interaction with myosin is the basis of muscular contraction and many aspects of cell motility. In vertebrates there are three main groups of actin isoforms, alpha, beta and gamma. The alpha actins found in muscle tissues are a major constituent of the contractile apparatus. The beta and gamma actins co-exist in most cell types as components of the cytoskeleton and as mediators of internal cell motility. In plants there are many isoforms which are probably involved in a variety of functions such as cytoplasmic streaming, cell shape determination, tip growth, graviperception, cell wall deposition, etc.


Pssm-ID: 466823  Cd Length: 365  Bit Score: 72.01  E-value: 1.95e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2113274756  15 LYGSVIVTGGNTLLQGFTDRLNRELSQKTPPvsvcSMRLKLIASNstmERRFSPWIGGSILASLGT 80
Cdd:cd10224   288 LYANIVLSGGTTMFPGIADRMQKEITALAPS----TMKIKIVAPP---ERKYSVWIGGSILASLST 346
PTZ00004 PTZ00004
actin-2; Provisional
 15-80 1.68e-11

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 66.33  E-value: 1.68e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2113274756  15 LYGSVIVTGGNTLLQGFTDRLNRELSQKTPPvsvcSMRLKLIASnstMERRFSPWIGGSILASLGT 80
Cdd:PTZ00004  296 LYGNIVLSGGTTMYRGLPERLTKELTTLAPS----TMKIKVVAP---PERKYSVWIGGSILSSLPT 354
TIL pfam01826
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ...
 326-378 2.78e-11

Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.


Pssm-ID: 460351  Cd Length: 55  Bit Score: 58.94  E-value: 2.78e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2113274756 326 CPTHSHYEPCGPPCPAACPEAGVR-GCQGPCLEGCSCDPGFLLSGGG-CVPQGGC 378
Cdd:pfam01826   1 CPANEVYSECGSACPPTCANLSPPdVCPEPCVEGCVCPPGFVRNSGGkCVPPSDC 55
PTZ00281 PTZ00281
actin; Provisional
 15-80 6.44e-11

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 64.34  E-value: 6.44e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2113274756  15 LYGSVIVTGGNTLLQGFTDRLNRELSQKTPPvsvcSMRLKLIASNstmERRFSPWIGGSILASLGT 80
Cdd:PTZ00281  294 LYGNVVLSGGTTMFPGIADRMNKELTALAPS----TMKIKIIAPP---ERKYSVWIGGSILASLST 352
TIL cd19941
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ...
 326-378 1.66e-10

trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.


Pssm-ID: 410995  Cd Length: 55  Bit Score: 56.56  E-value: 1.66e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2113274756 326 CPTHSHYEPCGPPCPAACPE-AGVRGCQGPCLEGCSCDPGFLLSGGG-CVPQGGC 378
Cdd:cd19941     1 CPPNEVYSECGSACPPTCANpNAPPPCTKQCVEGCFCPEGYVRNSGGkCVPPSQC 55
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
 15-78 8.03e-10

nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ACTL7-like family includes ACTL7A, ACTL7B and ACTL9 (also known as ACTL7C). In mammalian, ACTL7A is expressed in a wide variety of adult tissues, while the ACTL7B is expressed in spermatids through the elongation phase of spermatid development. ACTL7A, also called actin-like-7-alpha, or T-ACTIN-2 in mouse, may play an important role in formation and fusion of Golgi-derived vesicles during acrosome biogenesis. ACTL7B, also called actin-like-7-beta, acts as a key regulator of spermiogenesis that is required for male fertility. ACTL9 is a testis-specific protein that plays an important role in fusion of proacrosomal vesicles and perinuclear theca formation.


Pssm-ID: 466819 [Multi-domain]  Cd Length: 368  Bit Score: 60.90  E-value: 8.03e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2113274756  15 LYGSVIVTGGNTLLQGFTDRLNRELSQ----KTPPVSVCSmrlkliasnstmERRFSPWIGGSILASL 78
Cdd:cd10214   288 LAKNILLCGGSTMFDGFPDRFQKELSKlcpnDNPIVAASP------------ERKYSVWTGGSILASL 343
TILa pfam12714
TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is ...
 380-433 1.06e-09

TILa domain; This cysteine rich domain occurs along side the TIL pfam01826 domain and is likely to be a distantly related relative.


Pssm-ID: 432736  Cd Length: 54  Bit Score: 54.23  E-value: 1.06e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2113274756 380 CSYAGGYHELGEEFFGPGCGSRCRCEGGNrTHCQAWQCRPTETCGLHNGLYGCH 433
Cdd:pfam12714   2 KDAQGNYIPAGKTWFSSGCTQSCTCTGGN-IQCQPFQCPPGTVCKDNDGSSNCH 54
PTZ00466 PTZ00466
actin-like protein; Provisional
 15-80 6.13e-09

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 58.03  E-value: 6.13e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2113274756  15 LYGSVIVTGGNTLLQGFTDRLNRELSQKTPPvsvcSMRLKLIASNstmERRFSPWIGGSILASLGT 80
Cdd:PTZ00466  298 LYSHIVLSGGTTMFHGFGDRLLNEIRKFAPK----DITIRISAPP---ERKFSTFIGGSILASLAT 356
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
 15-77 7.85e-06

nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, also called actin-like protein 6, is required for formation and/or maintenance of proper nucleolar structure and function, plays a dual role in the regulation of ribosomal DNA (rDNA) transcription. In the presence of high glucose, Arp6 maintains active rDNA transcription through H2A.Z deposition and under glucose starvation, it is required for the repression of rDNA transcription, and this function may be independent of H2A.Z. Arp6 is also required for telomere silencing in both fission and budding yeast. It is a component of the budding yeast and Arabidopsis SWR1 complex (SWR1C) and the human SWI2/SNF2-related CBP activator protein (SRCAP) chromatin remodeling complexes which catalyze the exchange of the histone H2A with the H2AZ. Drosophila Arp6 colocalizes with HP1 (heterochromatin protein 1) in the pericentric heterochromatin, and vertebrate Arp6 also interacts with HP1. Human Arp6 is encoded by the ACTR6 gene. Arabidopsis thaliana ACTIN RELATED PROTEIN 6/EARLY IN SHORT DAYS 1/SUPPRESSOR OF FRIGIDA 3 (encoded by ARP6/ESD1/SUF3) participates in regulating several leaf and flower development stages. It is needed for Flowering locus C (FLC, the master repressor of flowering) and FLC-like gene expression in the shoot and root apex, and for the activity of the floral repressor pathway.


Pssm-ID: 466816 [Multi-domain]  Cd Length: 389  Bit Score: 48.32  E-value: 7.85e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2113274756  15 LYGSVIVTGGNTLLQGFTDRLNRELSQKTPpvsvCSMRLKLIASNSTMErrfSPWIGGSILAS 77
Cdd:cd10210   316 LYANIVLTGGNALFPGFRERLEAELRSLAP----DDYDVNVTLPEDPIT---YAWEGGSLLAQ 371
PTZ00452 PTZ00452
actin; Provisional
 18-80 2.76e-05

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 46.67  E-value: 2.76e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2113274756  18 SVIVTGGNTLLQGFTDRLNRELSQKTPPvsvcSMRLKLIASNstmERRFSPWIGGSILASLGT 80
Cdd:PTZ00452  296 NIVLSGGTTLFPGIANRLSNELTNLVPS----QLKIQVAAPP---DRRFSAWIGGSIQCTLST 351
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
 15-81 6.36e-05

nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The Arp8-like family includes Arp8, also called actin-like protein 8, from vertebrates and fungi. Human Arp8 is encoded by the ACTR8 gene and is also known as INO80 complex subunit N. It plays an important role in the functional organization of mitotic chromosomes. Arp8 exhibits low basal ATPase activity, and is unable to polymerize. It is probably a core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication, and probably DNA repair. it is required for the recruitment of INO80 (and probably the INO80 complex) to sites of DNA damage. Arp8 strongly prefers nucleosomes and H3-H4 tetramers over H2A-H2B dimers, suggesting it may act as a nucleosome recognition module within the complex. This subfamily also contains Arabidopsis thaliana Arp9.


Pssm-ID: 466812 [Multi-domain]  Cd Length: 447  Bit Score: 45.69  E-value: 6.36e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2113274756  15 LYGSVIVTGGNTLLQGFTDRLNRELSQKTPPVSVCSMRLKLIASNSTMERRFSPWIGGSILASLGTC 81
Cdd:cd10206   360 MYSSILLVGGGAKIPGLAEALEDRLLIKIPSLFEAVETVEVLPPPKDMDPSLLAWKGGAVLACLDSA 426
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
 15-78 4.65e-04

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 42.80  E-value: 4.65e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2113274756  15 LYGSVIVTGGNTLLQGFTDRLNRELS-------QKTPPVSVCSMRLKLIASN--STMERRFSPWIGGSILASL 78
Cdd:PTZ00280  312 LYKNIVLSGGSTMFKGFDKRLQRDVRkrvdrrlKKAEELSGGKLKPIPIDVNvvSHPRQRYAVWYGGSMLASS 384
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
 19-76 1.78e-03

nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar proteins; Arabidopsis thaliana ARP7 is an essential nuclear protein, ubiquitously expressed in all cell types. It is needed for normal embryogenesis, plant architecture, and floral organ abscission. It may play a role in regulating various phases of plant development through chromatin-mediated gene regulation.


Pssm-ID: 466815 [Multi-domain]  Cd Length: 354  Bit Score: 40.84  E-value: 1.78e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2113274756  19 VIVTGGNTLLQGFTDRLNRELSQKTPPvsvcSMRLKLIA-----SNSTMerRFSPWIGGSILA 76
Cdd:cd10209   274 IVLCGGTSSVPGLEARLQKEIRLLSSP----SSRPALVKppeymPENTL--RYSAWIGGAILA 330
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
 15-77 1.86e-03

nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, also called actin-like protein 3, is the ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex is comprised of 7 proteins (Arp2, Arp3, and five conserved proteins, ARPC1-5). It generates cytoplasmic branched filaments networks, by promoting nucleation of actin filaments as 70 degrees branches on the side of older filaments. It is activated, by simultaneously binding to a pre-existing filament and a nucleation promoting factor plus an actin monomer. Daughter branches subsequently detach/debranch from the mother filament. Its Arp2 and Arp3 subunits must be loaded with ATP for it to initiate the assembly of branched actin filaments. ATP hydrolysis may be required for branch initiation or debranching. The Arp2/3 complex is also found in the nucleus where it plays a role in promoting de novo actin polymerization and in RNA polymerase II-dependent transcription. This may in part be through regulating nuclear actin polymerization in a way like its function in the cytoplasm. Human Arp3 and Arp3B are encoded by the ACTR3 and ACTR3B genes respectively. Arp3B is also known as actin-related protein Arp4.


Pssm-ID: 466822  Cd Length: 404  Bit Score: 41.01  E-value: 1.86e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2113274756  15 LYGSVIVTGGNTLLQGFTDRLNREL-------SQKTPPVSVCSMRLKLIASN--STMERRFSPWIGGSILAS 77
Cdd:cd10221   309 LYKNIVLSGGSTMFKDFGRRLQRDVkrivdarLKASEELSGGKLKPKPIDVNviSHPMQRYAVWFGGSMLAS 380
ASKHA_NBD_ScArp7-like cd10212
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and ...
 15-78 3.36e-03

nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and similar proteins; Saccharomyces cerevisiae Arp7, also called actin-like protein 7, is a component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. It is also part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, which is required for the positive and negative regulation of gene expression of many genes. Arp7 forms a stable heterodimer with Arp9 protein in both the RSC and SWI/SNF chromatin-remodeling complexes. It has been suggested that this dimer functions as a module with DNA bending proteins, to achieve correct architecture and facilitate complex-complex interactions. Fission yeast SWI/SNF and RSC complexes do not contain Arp7 and Arp8, but instead contain Arp9 and Arp42.


Pssm-ID: 466818 [Multi-domain]  Cd Length: 424  Bit Score: 40.09  E-value: 3.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2113274756  15 LYGSVIVTGGNTLLQGFTDRLNRELSQKTPpvsvcSMRLKLIASNSTMERRFSPWIGGSILASL 78
Cdd:cd10212   346 LLTNVIITGSTSLIEGMEQRIIKELSIRFP-----QYKLTTFANQVMMDRKIQGWLGALTMANL 404
 
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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