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Conserved domains on  [gi|1034610912|ref|XP_016858605|]
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beta-centractin isoform X2 [Homo sapiens]

Protein Classification

acetate and sugar kinases/Hsc70/actin family protein( domain architecture ID 99298)

acetate and sugar kinases/Hsc70/actin (ASKHA) family protein catalyzes phosphoryl transfer from ATP to their respective substrates

CATH:  3.30.420.40
Gene Ontology:  GO:0000166
PubMed:  8800467|7781919
SCOP:  3000092

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
1-331 0e+00

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: 723.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912   1 MRVMAGALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMERIWQYVYSKDQLQTFSEEHPVLLTEAPLNPSKNREKA 80
Cdd:cd10216    37 VRVMAGALEGDVFVGPKAEEHRGLLKIRYPMEHGIVTDWNDMERIWQYVYSKLQLNTFSEEHPVLLTEAPLNPRKNREKA 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  81 AEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGVD 160
Cdd:cd10216   117 AEVFFETFNVPALFVSMQAVLSLYASGRTTGVVLDSGDGVTHAVPIYEGFALPHSIRRVDIAGRDVTEYLQLLLRKSGYN 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 161 FHTSAEFEVVRTIKERACYLSINPQKDEALE---TEKVQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVVAF 237
Cdd:cd10216   197 FHTSAEFEIVREIKEKACYVALNPQKEEKLEeekTEKAQYTLPDGSTIEIGPERFRAPEILFNPELIGLEYPGVHEVLVD 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 238 AIHKSDMDLRRTLFANIVLSGGSTLFKGFGDRLLSEVKKLAPKDIKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKK 317
Cdd:cd10216   277 SIQKSDLDLRKTLYSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVKIRISAPPERLYSTWIGGSILASLSTFKKMWVSKK 356
                         330
                  ....*....|....
gi 1034610912 318 EYEEDGSRAIHRKT 331
Cdd:cd10216   357 EYEEDGARILHRKT 370
 
Name Accession Description Interval E-value
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
1-331 0e+00

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: 723.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912   1 MRVMAGALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMERIWQYVYSKDQLQTFSEEHPVLLTEAPLNPSKNREKA 80
Cdd:cd10216    37 VRVMAGALEGDVFVGPKAEEHRGLLKIRYPMEHGIVTDWNDMERIWQYVYSKLQLNTFSEEHPVLLTEAPLNPRKNREKA 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  81 AEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGVD 160
Cdd:cd10216   117 AEVFFETFNVPALFVSMQAVLSLYASGRTTGVVLDSGDGVTHAVPIYEGFALPHSIRRVDIAGRDVTEYLQLLLRKSGYN 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 161 FHTSAEFEVVRTIKERACYLSINPQKDEALE---TEKVQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVVAF 237
Cdd:cd10216   197 FHTSAEFEIVREIKEKACYVALNPQKEEKLEeekTEKAQYTLPDGSTIEIGPERFRAPEILFNPELIGLEYPGVHEVLVD 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 238 AIHKSDMDLRRTLFANIVLSGGSTLFKGFGDRLLSEVKKLAPKDIKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKK 317
Cdd:cd10216   277 SIQKSDLDLRKTLYSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVKIRISAPPERLYSTWIGGSILASLSTFKKMWVSKK 356
                         330
                  ....*....|....
gi 1034610912 318 EYEEDGSRAIHRKT 331
Cdd:cd10216   357 EYEEDGARILHRKT 370
PTZ00466 PTZ00466
actin-like protein; Provisional
2-332 0e+00

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 519.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912   2 RVMAGALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMERIWQYVYSkdQLQTFSEEHPVLLTEAPLNPSKNREKAA 81
Cdd:PTZ00466   49 RVMAGAVEGNIFVGNKAEEYRGLLKVTYPINHGIIENWNDMENIWIHVYN--SMKINSEEHPVLLTEAPLNPQKNKEKIA 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  82 EVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGVDF 161
Cdd:PTZ00466  127 EVFFETFNVPALFISIQAILSLYSCGKTNGTVLDCGDGVCHCVSIYEGYSITNTITRTDVAGRDITTYLGYLLRKNGHLF 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 162 HTSAEFEVVRTIKERACYLSINPQKDEAlETEK----VQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVVAF 237
Cdd:PTZ00466  207 NTSAEMEVVKNMKENCCYVSFNMNKEKN-SSEKalttLPYILPDGSQILIGSERYRAPEVLFNPSILGLEYLGLSELIVT 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 238 AIHKSDMDLRRTLFANIVLSGGSTLFKGFGDRLLSEVKKLAPKDIKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKK 317
Cdd:PTZ00466  286 SITRADMDLRRTLYSHIVLSGGTTMFHGFGDRLLNEIRKFAPKDITIRISAPPERKFSTFIGGSILASLATFKKIWISKQ 365
                         330
                  ....*....|....*
gi 1034610912 318 EYEEDGSRAIHRKTF 332
Cdd:PTZ00466  366 EFDEYGSVILHRKTF 380
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
5-332 5.78e-174

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 487.15  E-value: 5.78e-174
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912    5 AGALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMERIWQYVYSKdQLQTFSEEHPVLLTEAPLNPSKNREKAAEVF 84
Cdd:smart00268  40 MVGDAKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEKIWDYTFFN-ELRVEPEEHPVLLTEPPMNPKSNREKILEIM 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912   85 FETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGVDFHTS 164
Cdd:smart00268 119 FETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVPVVDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSS 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  165 AEFEVVRTIKERACYLSINPQKDEALE-------TEKVQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVVAF 237
Cdd:smart00268 199 AEFEIVREIKEKLCYVAEDFEKEMKLAressessKLEKTYELPDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYE 278
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  238 AIHKSDMDLRRTLFANIVLSGGSTLFKGFGDRLLSEVKKLAPKDIKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKK 317
Cdd:smart00268 279 SIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQLAPKKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKK 358
                          330
                   ....*....|....*
gi 1034610912  318 EYEEDGSRAIHRKTF 332
Cdd:smart00268 359 EYEESGSQIVERKCF 373
Actin pfam00022
Actin;
6-332 2.10e-167

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 471.79  E-value: 2.10e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912   6 GALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMERIWQYVYsKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFF 85
Cdd:pfam00022  39 VEAANKYYVGDEALTYRPGMEVRSPVEDGIVVDWDAMEEIWEHVL-KEELQVDPEEHPLLLTEPPWNPPANREKAAEIMF 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  86 ETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGVD----- 160
Cdd:pfam00022 118 EKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVPVHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRNIEitpry 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 161 -------------------------FHTSAEFEVVRTIKERACYLSINPQKDEALETE--KVQYTLPDGSTLDVGPARFR 213
Cdd:pfam00022 198 likskkpgdpapavtkrelpdttysYKTYQERRVLEEIKESVCYVSDDPFGDETTSSSipTRVYELPDGSTIILGAERFR 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 214 APELLFQPDLVGDESE--------GLHEVVAFAIHKSDMDLRRTLFANIVLSGGSTLFKGFGDRLLSEVKKLAPKDIKIK 285
Cdd:pfam00022 278 VPEILFNPSLIGSESElpppqtavGIPELIVDAINACDVDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVK 357
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034610912 286 ISAPQ---ERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRKTF 332
Cdd:pfam00022 358 IIAPGntvERRYSAWIGGSILASLGTFQQMWVSKQEYEEHGASVVERKCK 407
COG5277 COG5277
Actin-related protein [Cytoskeleton];
1-321 1.39e-66

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 215.04  E-value: 1.39e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912   1 MRVMAGALEGDLFIGPKAEEH-----RGLLTIRYPMEHGVVR-----DWNDMERIWQYVYSKdQLQTFSEEHP--VLLTE 68
Cdd:COG5277    49 LLGPMEGLSRGLVVGDEVSKYlssvrDAIRNLKYPLRDGIVRrddedAWRVLKELLRYTFAQ-FLVVDPEFHGflVVVAL 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  69 APLNPSKNREKAAEVFFETF---NVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGfAMPHSIMRVDIAGRD 145
Cdd:COG5277   128 SALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVAIAEKAVTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAE 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 146 VSRYLRLLLRKEGVDFhTSAEFEVVRTIKERACYL------SINPQKDEALETEKVqYTLPDGSTL----DVGPARFRAP 215
Cdd:COG5277   207 ANAITREILKDRGYSD-TAREEYVVRVVKEALGLVprdlakAIQKAASNPDSFEAK-VRLPNPTVEielgNYAWERFLIG 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 216 ELLFQPDLVGDESE----------------------GLHEVVAFAIHKSDMDLRRTLFANIVLSGGSTLF---KGFGD-- 268
Cdd:COG5277   285 EILFNPNHEGFESYiqqgrlriedavigdvvlygemGLAEAIINSIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEDva 364
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 269 -----RLLSEVKKLAPkDIKIKISAPQERLYSTWIGGSILASLDTFKKMW--VSKKEYEE 321
Cdd:COG5277   365 vdsvtRVQIELSELAP-ELKVNVRLVSDPQYSVWKGAIIYGYALPFSVKWswITKEGWYF 423
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
265-330 4.21e-16

syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in the plant pathogen Pseudomonas syringae and related species. This model was created, in part, to clarify that the family is real and distinct, rather than an artifact of eukaryotic contamination of bacterial genomic sequence data. As of the creation of this HMM, the family is uncharacterized.


Pssm-ID: 468549 [Multi-domain]  Cd Length: 132  Bit Score: 73.86  E-value: 4.21e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034610912 265 GFGDRLLSEVKKLAPKDIKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRK 330
Cdd:NF040575   66 GFYEKLKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSIVHRK 131
 
Name Accession Description Interval E-value
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
1-331 0e+00

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: 723.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912   1 MRVMAGALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMERIWQYVYSKDQLQTFSEEHPVLLTEAPLNPSKNREKA 80
Cdd:cd10216    37 VRVMAGALEGDVFVGPKAEEHRGLLKIRYPMEHGIVTDWNDMERIWQYVYSKLQLNTFSEEHPVLLTEAPLNPRKNREKA 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  81 AEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGVD 160
Cdd:cd10216   117 AEVFFETFNVPALFVSMQAVLSLYASGRTTGVVLDSGDGVTHAVPIYEGFALPHSIRRVDIAGRDVTEYLQLLLRKSGYN 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 161 FHTSAEFEVVRTIKERACYLSINPQKDEALE---TEKVQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVVAF 237
Cdd:cd10216   197 FHTSAEFEIVREIKEKACYVALNPQKEEKLEeekTEKAQYTLPDGSTIEIGPERFRAPEILFNPELIGLEYPGVHEVLVD 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 238 AIHKSDMDLRRTLFANIVLSGGSTLFKGFGDRLLSEVKKLAPKDIKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKK 317
Cdd:cd10216   277 SIQKSDLDLRKTLYSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVKIRISAPPERLYSTWIGGSILASLSTFKKMWVSKK 356
                         330
                  ....*....|....
gi 1034610912 318 EYEEDGSRAIHRKT 331
Cdd:cd10216   357 EYEEDGARILHRKT 370
PTZ00466 PTZ00466
actin-like protein; Provisional
2-332 0e+00

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 519.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912   2 RVMAGALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMERIWQYVYSkdQLQTFSEEHPVLLTEAPLNPSKNREKAA 81
Cdd:PTZ00466   49 RVMAGAVEGNIFVGNKAEEYRGLLKVTYPINHGIIENWNDMENIWIHVYN--SMKINSEEHPVLLTEAPLNPQKNKEKIA 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  82 EVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGVDF 161
Cdd:PTZ00466  127 EVFFETFNVPALFISIQAILSLYSCGKTNGTVLDCGDGVCHCVSIYEGYSITNTITRTDVAGRDITTYLGYLLRKNGHLF 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 162 HTSAEFEVVRTIKERACYLSINPQKDEAlETEK----VQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVVAF 237
Cdd:PTZ00466  207 NTSAEMEVVKNMKENCCYVSFNMNKEKN-SSEKalttLPYILPDGSQILIGSERYRAPEVLFNPSILGLEYLGLSELIVT 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 238 AIHKSDMDLRRTLFANIVLSGGSTLFKGFGDRLLSEVKKLAPKDIKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKK 317
Cdd:PTZ00466  286 SITRADMDLRRTLYSHIVLSGGTTMFHGFGDRLLNEIRKFAPKDITIRISAPPERKFSTFIGGSILASLATFKKIWISKQ 365
                         330
                  ....*....|....*
gi 1034610912 318 EYEEDGSRAIHRKTF 332
Cdd:PTZ00466  366 EFDEYGSVILHRKTF 380
ASKHA_NBD_actin_Arp-T1-3 cd13397
nucleotide-binding domain (NBD) of actin, actin-related proteins T1-T3 (Arp-T1-3), and similar ...
1-323 0e+00

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: 515.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912   1 MRVMAGALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMERIWQYVYsKDQLQTFSEEHPVLLTEAPLNPSKNREKA 80
Cdd:cd13397    36 KAVMLGAGQKEVYVGDEAQEKRGVLTLSYPIEHGIVTNWDDMEKIWHHTF-ENELRVKPEEHPVLLTEAPLNPKQNREKM 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  81 AEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGVD 160
Cdd:cd13397   115 AEIMFETFGVPAFYVAIQAVLSLYSSGRTTGLVLDSGDGVTHTVPIYEGYALPHAVQRLDLAGRDLTEYLMKLLKERGHS 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 161 FHTSAEFEVVRTIKERACYLSINPQKDEALETEKVQ--YTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVVAFA 238
Cdd:cd13397   195 FTTTAEREIVRDIKEKLCYVALDYEEELKKKSEELEkeYTLPDGQVIKIGSERFRCPEALFRPSLIGREAPGIHKLVYNS 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 239 IHKSDMDLRRTLFANIVLSGGSTLFKGFGDRLLSEVKKLAPKDIKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKE 318
Cdd:cd13397   275 IMKCDIDIRKDLYSNIVLSGGSTMFPGLPERLQKELEALAPSSTKVKVIAPPERKYSVWIGGSILASLSTFKSMWITRAE 354

                  ....*
gi 1034610912 319 YEEDG 323
Cdd:cd13397   355 YDEFG 359
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
5-332 5.78e-174

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 487.15  E-value: 5.78e-174
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912    5 AGALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMERIWQYVYSKdQLQTFSEEHPVLLTEAPLNPSKNREKAAEVF 84
Cdd:smart00268  40 MVGDAKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEKIWDYTFFN-ELRVEPEEHPVLLTEPPMNPKSNREKILEIM 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912   85 FETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGVDFHTS 164
Cdd:smart00268 119 FETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVPVVDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSS 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  165 AEFEVVRTIKERACYLSINPQKDEALE-------TEKVQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVVAF 237
Cdd:smart00268 199 AEFEIVREIKEKLCYVAEDFEKEMKLAressessKLEKTYELPDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYE 278
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  238 AIHKSDMDLRRTLFANIVLSGGSTLFKGFGDRLLSEVKKLAPKDIKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKK 317
Cdd:smart00268 279 SIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQLAPKKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKK 358
                          330
                   ....*....|....*
gi 1034610912  318 EYEEDGSRAIHRKTF 332
Cdd:smart00268 359 EYEESGSQIVERKCF 373
Actin pfam00022
Actin;
6-332 2.10e-167

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 471.79  E-value: 2.10e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912   6 GALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMERIWQYVYsKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFF 85
Cdd:pfam00022  39 VEAANKYYVGDEALTYRPGMEVRSPVEDGIVVDWDAMEEIWEHVL-KEELQVDPEEHPLLLTEPPWNPPANREKAAEIMF 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  86 ETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGVD----- 160
Cdd:pfam00022 118 EKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVPVHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRNIEitpry 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 161 -------------------------FHTSAEFEVVRTIKERACYLSINPQKDEALETE--KVQYTLPDGSTLDVGPARFR 213
Cdd:pfam00022 198 likskkpgdpapavtkrelpdttysYKTYQERRVLEEIKESVCYVSDDPFGDETTSSSipTRVYELPDGSTIILGAERFR 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 214 APELLFQPDLVGDESE--------GLHEVVAFAIHKSDMDLRRTLFANIVLSGGSTLFKGFGDRLLSEVKKLAPKDIKIK 285
Cdd:pfam00022 278 VPEILFNPSLIGSESElpppqtavGIPELIVDAINACDVDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVK 357
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034610912 286 ISAPQ---ERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRKTF 332
Cdd:pfam00022 358 IIAPGntvERRYSAWIGGSILASLGTFQQMWVSKQEYEEHGASVVERKCK 407
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
3-323 2.76e-167

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: 469.92  E-value: 2.76e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912   3 VMAGALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMERIWQYVYSkDQLQTFSEEHPVLLTEAPLNPSKNREKAAE 82
Cdd:cd10224    38 VMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFY-NELRVAPEEHPVLLTEAPLNPKANREKMTQ 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  83 VFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGVDFH 162
Cdd:cd10224   117 IMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFT 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 163 TSAEFEVVRTIKERACYLSINpqKDEALET-------EKvQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVV 235
Cdd:cd10224   197 TTAEREIVRDIKEKLCYVALD--FEQEMQTaasssslEK-SYELPDGQVITIGNERFRCPEALFQPSFLGMEAAGIHETT 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 236 AFAIHKSDMDLRRTLFANIVLSGGSTLFKGFGDRLLSEVKKLAPKDIKIKISAPQERLYSTWIGGSILASLDTFKKMWVS 315
Cdd:cd10224   274 YNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTMKIKIVAPPERKYSVWIGGSILASLSTFQQMWIS 353

                  ....*...
gi 1034610912 316 KKEYEEDG 323
Cdd:cd10224   354 KQEYDESG 361
PTZ00004 PTZ00004
actin-2; Provisional
1-332 2.04e-149

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 424.95  E-value: 2.04e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912   1 MRVMAGALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMERIWQYVYSkDQLQTFSEEHPVLLTEAPLNPSKNREKA 80
Cdd:PTZ00004   42 PGIMVGMEEKDCYVGDEAQDKRGILTLKYPIEHGIVTNWDDMEKIWHHTFY-NELRVAPEEHPVLLTEAPLNPKANREKM 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  81 AEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGVD 160
Cdd:PTZ00004  121 TQIMFETHNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYSLPHAIHRLDVAGRDLTEYMMKILHERGTT 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 161 FHTSAEFEVVRTIKERACYLSINPQK-----DEALETEKVQYTLPDGSTLDVGPARFRAPELLFQPDLVG-DESEGLHEV 234
Cdd:PTZ00004  201 FTTTAEKEIVRDIKEKLCYIALDFDEemgnsAGSSDKYEESYELPDGTIITVGSERFRCPEALFQPSLIGkEEPPGIHEL 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 235 VAFAIHKSDMDLRRTLFANIVLSGGSTLFKGFGDRLLSEVKKLAPKDIKIKISAPQERLYSTWIGGSILASLDTFKKMWV 314
Cdd:PTZ00004  281 TFQSINKCDIDIRKDLYGNIVLSGGTTMYRGLPERLTKELTTLAPSTMKIKVVAPPERKYSVWIGGSILSSLPTFQQMWV 360
                         330
                  ....*....|....*...
gi 1034610912 315 SKKEYEEDGSRAIHRKTF 332
Cdd:PTZ00004  361 TKEEYDESGPSIVHRKCF 378
PTZ00281 PTZ00281
actin; Provisional
3-332 1.32e-139

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 400.23  E-value: 1.32e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912   3 VMAGALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMERIWQYVYSkDQLQTFSEEHPVLLTEAPLNPSKNREKAAE 82
Cdd:PTZ00281   44 VMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFY-NELRVAPEEHPVLLTEAPLNPKANREKMTQ 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  83 VFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGVDFH 162
Cdd:PTZ00281  123 IMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFT 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 163 TSAEFEVVRTIKERACYLSINPQKD-------EALETekvQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVV 235
Cdd:PTZ00281  203 TTAEREIVRDIKEKLAYVALDFEAEmqtaassSALEK---SYELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETT 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 236 AFAIHKSDMDLRRTLFANIVLSGGSTLFKGFGDRLLSEVKKLAPKDIKIKISAPQERLYSTWIGGSILASLDTFKKMWVS 315
Cdd:PTZ00281  280 YNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIS 359
                         330
                  ....*....|....*..
gi 1034610912 316 KKEYEEDGSRAIHRKTF 332
Cdd:PTZ00281  360 KEEYDESGPSIVHRKCF 376
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
11-327 3.71e-135

nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, also called actin-like protein 2, 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 Arp2 is encoded by the ACTR2 gene.


Pssm-ID: 466821  Cd Length: 381  Bit Score: 388.85  E-value: 3.71e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  11 DLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMERIWQYVYsKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNV 90
Cdd:cd10220    48 DIMVGDEASELRSMLEVTYPMENGIVRNWDDMEHLWDYTF-GEKLKIDPRECKILLTEPPMNPTKNREKMVEVMFEKYGF 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  91 PALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYL-RLLLRKeGVDFHTSAEFEV 169
Cdd:cd10220   127 AGVYVAIQAVLTLYAQGLLTGVVVDSGDGVTHIVPVYEGFSLPHLTRRLDVAGRDITRYLiKLLLLR-GYAFNRTADFET 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 170 VRTIKERACYLSINPQKDE--ALETEKV--QYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVVAFAIHKSDMD 245
Cdd:cd10220   206 VREIKEKLCYVAYDIELEQklALETTVLveSYTLPDGRVIKVGGERFEAPEALFQPHLIDVEGPGIAELLFNTIQAADID 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 246 LRRTLFANIVLSGGSTLFKGFGDRLLSEVKKL-----------APKDIKIKISAPQERLYSTWIGGSILASLDTFKK-MW 313
Cdd:cd10220   286 TRPELYKHIVLSGGSTMYPGLPSRLEKEIKQLylervlkgdteRLSKFKIRIEDPPRRKHMVFLGGAVLADIMKDKDeFW 365
                         330
                  ....*....|....
gi 1034610912 314 VSKKEYEEDGSRAI 327
Cdd:cd10220   366 ITRQEYEEQGVRVL 379
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
39-323 8.35e-126

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: 360.65  E-value: 8.35e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  39 WNDMERIWQYVYSKdQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGD 118
Cdd:cd10169    26 WDDMEKIWEHVFYN-LLRVDPEEHPVLLTEPPLNPKANREKLAEILFETFNVPSLYIANQAVLSLYASGRTTGLVVDSGE 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 119 GVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGVDFHTSAEFEVVRTIKERACylsinpqkdealetekvqyt 198
Cdd:cd10169   105 GVTHIVPVYEGYVLPHAVRRLDIGGRDLTDYLAKLLREKGYSFSTSAEREIVRDIKEKLC-------------------- 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 199 lpdgstldvgparfrapellfqpdlvgdeseGLHEVVAFAIHKSDMDLRRTLFANIVLSGGSTLFKGFGDRLLSEVKKLA 278
Cdd:cd10169   165 -------------------------------GLHELIYDSIMKCDIDLRKELYSNIVLSGGTTLFPGFAERLQKELSKLA 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1034610912 279 PKDIKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDG 323
Cdd:cd10169   214 PSSVKVKVIAPPERKYSAWIGGSILASLSTFQQMWITKEEYEEHG 258
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
13-330 1.64e-120

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: 351.34  E-value: 1.64e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  13 FIGPKAEEHRGLLTIRYPMEHGVVRDWNDMERIWQYVYSKDqLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPA 92
Cdd:cd10214    51 FVGKELANVEPPLKLVNPLRHGIVVDWDCVQDIWEYIFEKE-MKILPEEHAVLVSDPPLSPTTNREKYAELMFETFSIPA 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  93 LFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGVDFhTSAEFEVVRT 172
Cdd:cd10214   130 MHIAYQSRLSLYSYGRTSGLVVESGHGVSYVVPIHEGYNLPHITGRADYAGSDLTAYLMKLLNEAGNKF-TDDQLHIVED 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 173 IKERACYLSINPQKDEALETE--KVQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVVAFAIHKSDMDLRRTL 250
Cdd:cd10214   209 IKKKCCYVALDFEEEMGLPPQeyTVDYELPDGHLITIGKERFRCPEMLFNPSLIGSKQPGLHTLTMNSLNKCDANLKKDL 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 251 FANIVLSGGSTLFKGFGDRLLSEVKKLAPKDIKIKISAPqERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRK 330
Cdd:cd10214   289 AKNILLCGGSTMFDGFPDRFQKELSKLCPNDNPIVAASP-ERKYSVWTGGSILASLKSFQQLWVRRREYEERGPFVIYRK 367
ASKHA_NBD_Arp4_ACTL6-like cd13395
nucleotide-binding domain (NBD) of the actin-related protein 4 (Arp4)-like subfamily; The ...
27-323 6.37e-116

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: 341.08  E-value: 6.37e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  27 IRYPMEHGVVRDWNDMERIWQYVYsKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYAT 106
Cdd:cd13395    73 VISPLKDGLIEDWDAFEKLWDHAL-KNRLRVDPSEHPLLLTEPSWNTRANREKLTELMFEKYNVPAFFLAKNAVLSAFAN 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 107 GRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGVD-------------------------- 160
Cdd:cd13395   152 GRSTALVVDSGATSTSVVPVHDGYVLQKAIVRSPLGGDFLTDQLLKLLESKNIEiiprymikskepveggapakytkkdl 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 161 ------FHTSAEFEVVRTIKERACYLSINP-QKDEALETEKVQYTLPDGSTLDVGPARFRAPELLFQPDLV--------- 224
Cdd:cd13395   232 pnttssYHRYMVRRVLQDFKESVCQVSDSPfDESEAASIPTVSYELPDGYNIEFGAERFKIPELLFDPSLVkgipappse 311
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 225 GDESEGLHEVVAFAIHKSDMDLRRTLFANIVLSGGSTLFKGFGDRLLSEVKKLAPKDIKIKISAPQ---ERLYSTWIGGS 301
Cdd:cd13395   312 GNELLGLPQLVYTSIGSCDVDIRPELYGNVVLTGGNSLLPGFTDRLNRELSEKAPGSLKLKILASGntvERRFSSWIGGS 391
                         330       340
                  ....*....|....*....|..
gi 1034610912 302 ILASLDTFKKMWVSKKEYEEDG 323
Cdd:cd13395   392 ILASLGSFQQMWISKQEYEEHG 413
PTZ00452 PTZ00452
actin; Provisional
5-332 1.20e-105

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 314.00  E-value: 1.20e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912   5 AGALEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMERIWQYVYSkDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVF 84
Cdd:PTZ00452   45 FSTFNKEYYVGEEAQAKRGVLAIKEPIQNGIINSWDDIEIIWHHAFY-NELCMSPEDQPVFMTDAPMNSKFNRERMTQIM 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  85 FETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGVDFHTS 164
Cdd:PTZ00452  124 FETFNTPCLYISNEAVLSLYTSGKTIGLVVDSGEGVTHCVPVFEGHQIPQAITKINLAGRLCTDYLTQILQELGYSLTEP 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 165 AEFEVVRTIKERACYLSINPQKDEAL----ETEKVQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVVAFAIH 240
Cdd:PTZ00452  204 HQRIIVKNIKERLCYTALDPQDEKRIykesNSQDSPYKLPDGNILTIKSQKFRCSEILFQPKLIGLEVAGIHHLAYSSIK 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 241 KSDMDLRRTLFANIVLSGGSTLFKGFGDRLLSEVKKLAPKDIKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYE 320
Cdd:PTZ00452  284 KCDLDLRQELCRNIVLSGGTTLFPGIANRLSNELTNLVPSQLKIQVAAPPDRRFSAWIGGSIQCTLSTQQPQWIKRQEYD 363
                         330
                  ....*....|..
gi 1034610912 321 EDGSRAIHRKTF 332
Cdd:PTZ00452  364 EQGPSIVHRKCF 375
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
11-323 3.14e-103

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: 308.73  E-value: 3.14e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  11 DLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMERIWQYVYSKdQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNV 90
Cdd:cd10221    52 DFYIGDEALANSPTYALKYPIRHGIVEDWDLMERFWEQCIFK-YLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNV 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  91 PALFISMQAVLSLYA-------TGRT-TGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGVDFH 162
Cdd:cd10221   131 PGLYIAVQAVLALAAswtsrkvGERTlTGTVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREEGIP 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 163 TSAEFEVVRTIKERACYLSinpqKDEALETEK---------VQYTLPDGST-----LDVGPARFRAPELLFQPDLV-GDE 227
Cdd:cd10221   211 PEDSLEVAKRIKERYCYVC----PDIVKEFAKydsdpakyiKQYTGINSVTgkpytVDVGYERFLAPEIFFNPEIAsSDF 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 228 SEGLHEVVAFAIHKSDMDLRRTLFANIVLSGGSTLFKGFGDRLLSEVK----------------KLAPKDIKIK-ISAPQ 290
Cdd:cd10221   287 TTPLPEVVDQVIQSCPIDTRRGLYKNIVLSGGSTMFKDFGRRLQRDVKrivdarlkaseelsggKLKPKPIDVNvISHPM 366
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1034610912 291 ERlYSTWIGGSILASLDTFKKMWVSKKEYEEDG 323
Cdd:cd10221   367 QR-YAVWFGGSMLASTPEFYTVCHTKAEYEEYG 398
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
11-323 2.76e-96

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 291.25  E-value: 2.76e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  11 DLFIGPKAEEHRGLLTIRYPMEHGVVRDWNDMERIWQYVYSKdQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNV 90
Cdd:PTZ00280   53 DFYIGDEALAASKSYTLTYPMKHGIVEDWDLMEKFWEQCIFK-YLRCEPEEHYFILTEPPMNPPENREYTAEIMFETFNV 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  91 PALFISMQAVLSLYAT----------GRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGVD 160
Cdd:PTZ00280  132 KGLYIAVQAVLALRASwtskkakelgGTLTGTVIDSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGEP 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 161 FHTSAEFEVVRTIKERACYLSINPQK-----DEALETEKVQYTLPDGST-----LDVGPARFRAPELLFQPDLV-GDESE 229
Cdd:PTZ00280  212 IPAEDILLLAQRIKEKYCYVAPDIAKefekyDSDPKNHFKKYTAVNSVTkkpytVDVGYERFLGPEMFFHPEIFsSEWTT 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 230 GLHEVVAFAIHKSDMDLRRTLFANIVLSGGSTLFKGFGDRLLSEVKK----------------LAPKDIKIK-ISAPQER 292
Cdd:PTZ00280  292 PLPEVVDDAIQSCPIDCRRPLYKNIVLSGGSTMFKGFDKRLQRDVRKrvdrrlkkaeelsggkLKPIPIDVNvVSHPRQR 371
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1034610912 293 lYSTWIGGSILASLDTFKKMWVSKKEYEEDG 323
Cdd:PTZ00280  372 -YAVWYGGSMLASSPEFEKVCHTKAEYDEYG 401
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
12-323 1.62e-78

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: 244.77  E-value: 1.62e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  12 LFIGPKAEEHRGL--LTIRYPMEHGVVRDWnDMER-IWQYVYSKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETF 88
Cdd:cd10210    38 LFGDDQLDECKDLsgLFYRRPFERGYLVNW-DLQRqIWDHLFGKLLLNVDPSDTALVLTEPPFNPPSIQEAMDEIVFEEY 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  89 NVPALFISMQAVLSLYA----------TGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLrlllrKEG 158
Cdd:cd10210   117 GFQSLYRTTAAALSAFAyladseqsssSSSQCCLVVDSGFSFTHIVPFFDGKPVKRAVRRIDVGGKLLTNYL-----KEI 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 159 VDFHT---SAEFEVVRTIKERACYLSIN-------PQKDEALETEKVQYTLPDGST------LDVGPA------------ 210
Cdd:cd10210   192 ISYRQlnvMDETYLVNQIKEDLCFVSTDfyedleiAKKKGKENTIRRDYVLPDYTTskrgyvRDPEEPnrgklkedeqvl 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 211 -----RFRAPELLFQPDLVGDESEGLHEVVAFAIHKSDMDLRRTLFANIVLSGGSTLFKGFGDRLLSEVKKLAPKDIKIK 285
Cdd:cd10210   272 rlnneRFTVPELLFHPSDIGIQQAGIAEAIVQSINACPEELQPLLYANIVLTGGNALFPGFRERLEAELRSLAPDDYDVN 351
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1034610912 286 ISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDG 323
Cdd:cd10210   352 VTLPEDPITYAWEGGSLLAQSPEFEELAVTRAEYEEHG 389
COG5277 COG5277
Actin-related protein [Cytoskeleton];
1-321 1.39e-66

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 215.04  E-value: 1.39e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912   1 MRVMAGALEGDLFIGPKAEEH-----RGLLTIRYPMEHGVVR-----DWNDMERIWQYVYSKdQLQTFSEEHP--VLLTE 68
Cdd:COG5277    49 LLGPMEGLSRGLVVGDEVSKYlssvrDAIRNLKYPLRDGIVRrddedAWRVLKELLRYTFAQ-FLVVDPEFHGflVVVAL 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  69 APLNPSKNREKAAEVFFETF---NVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGfAMPHSIMRVDIAGRD 145
Cdd:COG5277   128 SALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVAIAEKAVTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAE 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 146 VSRYLRLLLRKEGVDFhTSAEFEVVRTIKERACYL------SINPQKDEALETEKVqYTLPDGSTL----DVGPARFRAP 215
Cdd:COG5277   207 ANAITREILKDRGYSD-TAREEYVVRVVKEALGLVprdlakAIQKAASNPDSFEAK-VRLPNPTVEielgNYAWERFLIG 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 216 ELLFQPDLVGDESE----------------------GLHEVVAFAIHKSDMDLRRTLFANIVLSGGSTLF---KGFGD-- 268
Cdd:COG5277   285 EILFNPNHEGFESYiqqgrlriedavigdvvlygemGLAEAIINSIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEDva 364
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 269 -----RLLSEVKKLAPkDIKIKISAPQERLYSTWIGGSILASLDTFKKMW--VSKKEYEE 321
Cdd:COG5277   365 vdsvtRVQIELSELAP-ELKVNVRLVSDPQYSVWKGAIIYGYALPFSVKWswITKEGWYF 423
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
30-328 1.08e-61

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: 200.31  E-value: 1.08e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  30 PMEHGVVRDWNDMERIWQYVYSKDQLQTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRT 109
Cdd:cd10209    50 PIRRGRIEDWDALEALLRYVFYTGLGWEEGNEGQVLIAEPLLTSKAERERLTQLMFETFNVSGLYASEQAVLSLYAVGRI 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 110 TGVVLDSGDGVTHAVPIYEGfAMPHS-IMRVDIAGRDVSRYLRLLLRKEGVdfHTSAEFEVVRTIKERACYLSINPQKDE 188
Cdd:cd10209   130 SGCVVDVGHGKIDIAPVWEG-AIQHNaVRRFEIGGRDLTELLAAELGKSNP--KVKLDRSIVERLKEAVAWSADDEEAYE 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 189 A--LETEKVQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVVAFAIHKSDMDLRRTLFANIVLSGGSTLFKGF 266
Cdd:cd10209   207 KkvLTCSPETYTLPDGRVISVGKERYCVGEALFRPSILGIEEYGIVEQLVRAVSTSPSENRRQLLENIVLCGGTSSVPGL 286
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034610912 267 GDRLLSEVKKLAPKDIKIKISAPQERL------YSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIH 328
Cdd:cd10209   287 EARLQKEIRLLSSPSSRPALVKPPEYMpentlrYSAWIGGAILAKVVFPQNQHVTKADYDETGPSVVH 354
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
27-330 1.21e-50

nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and similar proteins; Saccharomyces cerevisiae Arp9, also called actin-like protein 9, chromatin structure-remodeling complex protein ARP9, or SWI/SNF complex component ARP9, 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. Arp9 forms a stable heterodimer with Arp7 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: 466814  Cd Length: 356  Bit Score: 171.72  E-value: 1.21e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  27 IRYPMEHGVVRDWNDMERIWQYVYSK---DQLQTFseEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSL 103
Cdd:cd10208    35 IIWPIQDGRVVDWDALEALWRHILFSllsIPRPTN--NSPVLLSVPPSWSKSDLELLTQLFFERLNVPAFAILEAPLAAL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 104 YATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKEGVDFHTSAE------FEVVRTIKEra 177
Cdd:cd10208   113 YAAGATSGIVVDIGHEKTDITPIVDSQVVPHALVSIPIGGQDCTAHLAQLLKSDEPELKSQAEsgeeatLDLAEALKK-- 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 178 cylsinpqkDEALETEKVQYTLPDGSTLDVGPARFRAPELLFQPDLVGDESEGLHEVVAFAIHKS-DMDLRRTLFANIVL 256
Cdd:cd10208   191 ---------SPICEVLSDGADLASGTEITVGKERFRACEPLFKPSSLRVDLLIAAIAGALVLNASdEPDKRPALWENIII 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 257 SGGSTLFKGFGDRLLSEVKKL-----------APKDIKI-KI----SAPQERLY--STWIGGSILASL---DTFKKMWVS 315
Cdd:cd10208   262 VGGGSRIRGLKEALLSELQQFhlisetsaspqQPRIIRLaKIpdyfPEWKKSGYeeAAFLGASIVAKLvfnDPSSKHYIS 341
                         330
                  ....*....|....*
gi 1034610912 316 KKEYEEDGSRAIHRK 330
Cdd:cd10208   342 KVDYNEKGPAAIHTK 356
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
26-323 2.80e-44

nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, also called actin-like protein 5, may act as a core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. It is involved in DNA double-strand break repair and UV-damage excision repair. Human Arp5 is encoded by the ACTR5 gene. Arabidopsis thaliana ARP5 (AtARp5) is a ubiquitously expressed nuclear protein involved in DNA repair and required for multicellular development of all organs. AtARp5 may be part of other chromatin remodeling machines in addition to INO80.


Pssm-ID: 466817 [Multi-domain]  Cd Length: 345  Bit Score: 154.65  E-value: 2.80e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  26 TIRYPMEHGVVRDWNDMERIWQYVYSKdqL---QTFSEEHPVLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLS 102
Cdd:cd10211    57 HLRSPFDRNVVTNFDLQEQILDYIFSH--LginSEGSVDHPIVLTEALCNPNYSRQLMSELLFECYGVPSVAYGIDSLFS 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 103 LYATGRT----TGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYL-RLLLRKegVDFHTSA-EFEVVRTIKER 176
Cdd:cd10211   135 YYHNQPQgdpsDGLVISSGYSTTHVIPVLNGRLDLSQCKRINLGGFHATDYLqRLLQLK--YPTHPSAiTLSRAEELVHE 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 177 ACYLSinPQKDEALEtekvqytlpdgstldvgpaRFRAPELLFQPDLVGDESEGLHEVVAFAIHKSDMDLRRTLFANIVL 256
Cdd:cd10211   213 HCYVA--EDYDEELK-------------------KWEDPEYYEENVRKIQLPFGLVETIEFVLKRYPAEQQDRLVQNVFL 271
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034610912 257 SGGSTLFKGFGDRLLSEVKKLAPKDIKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDG 323
Cdd:cd10211   272 TGGNALFPGLKERLEKELRAIRPFGSPFNVVRAKDPVLDAWRGAAKWALDSTFEKVWITKQEYEEKG 338
ASKHA_NBD_Arp10 cd10207
nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; ...
64-324 1.81e-43

nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; Arp10, also known as actin-related protein 11 (Arp11), is a subunit of the cargo-binding portion of the dynein activator, dynactin. It, together with dynactin4 (p62), -5(p25), and -6(p27), forms a heterotetrameric complex located at the pointed end of Arp1. Arp1 forms a mini-filament of uniform size, with proteins bound along its length and at both ends. Human Arp10 is encoded by the ACTR10 gene.


Pssm-ID: 466813 [Multi-domain]  Cd Length: 375  Bit Score: 153.56  E-value: 1.81e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  64 VLLTEAPLNPSKNREKAAEVFFETFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAG 143
Cdd:cd10207    75 VVVVESVLCPTPFRETLAKVLFKHFEVPSVLFAPSHLLSLLTLGIRTALVVDCGYRETRVLPVYEGVPLLSAWQSTPLGG 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 144 RDVSRYLRLLLRKEGVDFHTSAE------------FEVVRTIKERACYL-SINPQKDEALETEKVQYTLP---------- 200
Cdd:cd10207   155 KALHKRLKKLLLEHATVVTGDNKgqllssvdsllsEEVLEDIKVRACFVtSLERGKTLQSATEEGSTEEPsppppvdypl 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 201 DGSTLDVGPARFRAP--ELLFQPDlvgDESEGLHEVVAFAIHKSDMDLRRTLFANIVLSGGSTLFKGFGDRLLSEVKKLA 278
Cdd:cd10207   235 DGEKILIVPGSIRESaeELLFEGD---NEEKSLPTLILDSLLKCPIDVRKQLAENIVVIGGTSMLPGFKHRLLEELRALL 311
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034610912 279 PKD--------IKIKISAPQERL---YSTWIGGSILASLDTFKKMWVSKKEYEEDGS 324
Cdd:cd10207   312 RKPkyfeelapKTFRFHTPPSVFkpnYLAWLGGSIFGALESILGRSLSREAYLQTGR 368
ASKHA_NBD_AtArp8-like cd13396
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ...
55-323 1.57e-39

nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and similar proteins; Arabidopsis thaliana ARP8, also called F-box protein ARP8, is an F-Box protein localized to the nucleolus. It is ubiquitously expressed in all organs and cell types and has a cell cycle-dependent subcellular pattern of distribution: it is localized to the nucleolus in interphase cells and dispersed in the cytoplasm in mitotic cells.


Pssm-ID: 466847  Cd Length: 332  Bit Score: 141.91  E-value: 1.57e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  55 LQTFSEEHPVLLTEaPLNPSKNREKAA-----------EVFFEtFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHA 123
Cdd:cd13396    52 MQVKPSRQPVVVSL-PLCHSDDTESAAasrrqlrgtifNVLFD-MNVPAVCAVDQAVLALYAANRTSGIVVNIGFRVTTI 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 124 VPIYEGFAMpHSI--MRVDIAGRDVSRYLRLLLRKEGVDFHTsaeFEVVRTIKERACYLSINPQKDEALETEKVQYTLPD 201
Cdd:cd13396   130 VPVYRGRVM-HDIgvEVVGQGALRLTGFLKELMQQNGIRFPS---LYTVRTIKEKLCYVAEDYEAELAKDTQASCEVAGE 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 202 GSTLdVGPARFRAPELLFQPDLVGDESEGLHEVVAFAIHKSDMDLR---RTLFANIVLSGGSTLFKGFGDRLLSEVKKLA 278
Cdd:cd13396   206 GWFT-LSNERFKTGEILFQPGLGGMRAMGLHQAVALCMDHCALVHSqgdDGWFKTIVLSGGSACLPGLSERLERELRKLL 284
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1034610912 279 PKDIK--IKISAPQERLYSTWIGGSILASLDTFKKMW-VSKKEYEEDG 323
Cdd:cd13396   285 PKSLSegIRIIPPPLGPDSAWQGAKLISNLSNFPDGWcITKKQFRNKP 332
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
26-327 2.40e-28

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: 113.88  E-value: 2.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  26 TIRYPMEHGV------------VRDwnDMERIWQYVYSKD---QLQTFSEEHPVLLTeaplnPSK-NREKAAE---VFFE 86
Cdd:cd10206   138 NLHWPIRRGRlnvhsdggsltaVLD--DLEDIWSHALEEKleiPRKDLKNYRAVLVI-----PDLfDRRHVKElvdLLLR 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  87 TFNVPALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVSRYLRLLLRKegVDFH---- 162
Cdd:cd10206   211 RLGFSSVFVHQESVCATFGAGLSSACVVDIGAQKTSVACVEDGLSIPNSRIRLPYGGDDITRCFLWLLRR--SGFPyrec 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 163 ---TSAEFEVVRTIKERACYLS---INPQKDEALETEKVQytlpdgstldvgparfraPELLFQPDLVgdeseGLHEvva 236
Cdd:cd10206   289 nlnSPLDFLLLERLKETYCTLDqddIGVQLHEFYVREPGQ------------------PTLKYQFKLL-----PLDE--- 342
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 237 fAIHKS-----DMDLRRTLFANIVLSGGSTLFKGFG----DRLLSEVKKL--APKDIKIkISAPQER--LYSTWIGGSIL 303
Cdd:cd10206   343 -AIVQSilscaSDELKRKMYSSILLVGGGAKIPGLAealeDRLLIKIPSLfeAVETVEV-LPPPKDMdpSLLAWKGGAVL 420
                         330       340
                  ....*....|....*....|....
gi 1034610912 304 ASLDTFKKMWVSKKEYEEDGSRAI 327
Cdd:cd10206   421 ACLDSAQELWITRKEWQRLGVRAL 444
ASKHA_NBD_ScArp7-like cd10212
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and ...
14-320 7.77e-20

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: 89.39  E-value: 7.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  14 IGPKAEEHRGLLTIRYPMEHGVVRDWNDMERIWQYVYSKdQLQTFSEEHPVLLTEAPLNPSKNR---EKAAEVFFETFNV 90
Cdd:cd10212    53 IDAAAEKRNGDEVYTLVDSQGLPYNWDALEMQWRYLYDT-QLKVSPEELPLVITMPATNGKPDMailERYYELAFDKLNV 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  91 PALFISMQAVLSLYATGRTTGVVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGR--DVSRYLRLL-LRKEGVDFHTSAE- 166
Cdd:cd10212   132 PVFQIVIEPLAIALSMGKSSAFVIDIGASGCNVTPIIDGIVVKNAVVRSKFGGDflDFQVHERLApLIKEENDMENMADe 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 167 ------------------------------FEVVRTIKERAcylSINPQKDEALET--EKVQYTLPDGS----------- 203
Cdd:cd10212   212 qkrstdvwyeastwiqqfkstmlqvsekdlFELERYYKEQA---DIYAKQQEQLKQmdQQLQYTALTGSpnnplvqkknf 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 204 ---------TLDVGPArFRAPELLFQPDLVGDE---SEGLHEVVAFAIHKSDMDLRRTLFANIVLSGGSTLFKGFGDRLL 271
Cdd:cd10212   289 lfkplnktlTLDLKEC-YQFAEYLFKPQLISDKfspEDGLGPLMAKSVKKAPEQVYSLLLTNVIITGSTSLIEGMEQRII 367
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034610912 272 SEVKKLAPKdIKIKISAPQ---ERLYSTWIGGSILASLDTFK-KMWVSKKEYE 320
Cdd:cd10212   368 KELSIRFPQ-YKLTTFANQvmmDRKIQGWLGALTMANLPSWSlGKWYSKEDYE 419
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
265-330 4.21e-16

syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in the plant pathogen Pseudomonas syringae and related species. This model was created, in part, to clarify that the family is real and distinct, rather than an artifact of eukaryotic contamination of bacterial genomic sequence data. As of the creation of this HMM, the family is uncharacterized.


Pssm-ID: 468549 [Multi-domain]  Cd Length: 132  Bit Score: 73.86  E-value: 4.21e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034610912 265 GFGDRLLSEVKKLAPKDIKIKISAPQERLYSTWIGGSILASLDTFKKMWVSKKEYEEDGSRAIHRK 330
Cdd:NF040575   66 GFYEKLKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSIVHRK 131
ASKHA_NBD_MamK cd24009
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ...
8-270 6.65e-09

nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called magnetosome cytoskeleton protein MamK, is a protein with ATPase activity which forms dynamic cytoplasmic filaments (probably with paralog MamK-like) that may organize magnetosomes into long chains running parallel to the long axis of the cell. Turnover of MamK filaments is probably promoted by MamK-like (e.g.. MamJ and/or LimJ), which provides a monomer pool. MamK forms twisted filaments in the presence of ATP or GTP. It serves to close gaps between magnetosomes in the chain. Interaction with MCP10 is involved in controlling the response to magnetic fields, possibly by controlling flagellar rotation. The MamK 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: 466859 [Multi-domain]  Cd Length: 328  Bit Score: 56.45  E-value: 6.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912   8 LEGDLFIGPKAEEHRGLLTIRYPMEHGVVRDW--NDMEriwqyvYSKDQLQtfseeHPVLLTEAPLN---------PS-- 74
Cdd:cd24009    41 LGKEVLFGDEALENRLALDLRRPLEDGVIKEGddRDLE------AARELLQ-----HLIELALPGPDdeiyavigvPAra 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912  75 --KNREKAAEVFFETFN----VPALFismqAVlsLYATGRTTG-VVLDSGDGVTHAVPIYEGFAMPHSIMRVDIAGRDVS 147
Cdd:cd24009   110 saENKQALLEIARELVDgvmvVSEPF----AV--AYGLDRLDNsLIVDIGAGTTDLCRMKGTIPTEEDQITLPKAGDYID 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034610912 148 RYLRLLLRKEgvdfHTSAEF--EVVRTIKERACYLSINPqkdealetEKVQYTLP-DGS--TLDVGPARFRAPELLFqPD 222
Cdd:cd24009   184 EELVDLIKER----YPEVQLtlNMARRWKEKYGFVGDAS--------EPVKVELPvDGKpvTYDITEELRIACESLV-PD 250
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1034610912 223 LVgdesEGLHEVVAfaihKSDMDLRRTLFANIVLSGGSTLFKGFGDRL 270
Cdd:cd24009   251 IV----EGIKKLIA----SFDPEFQEELRNNIVLAGGGSRIRGLDTYI 290
 
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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