|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_AtARP7-like |
cd10209 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ... |
4-359 |
0e+00 |
|
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: 629.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 4 LVVDAGSKFLKAGAAIPDQSPAMIIPSQMKRMVDDGSSSADnpttVFEDVTLDPIERGLIRDWDAMEDLLRYVVYTGLGW 83
Cdd:cd10209 1 VVIDAGSRLLKAGYAYPDREPSVVEPTRVTPAVEDGEESDT----VVEGNTVSPIRRGRIEDWDALEALLRYVFYTGLGW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 84 EEGNEGNILFTDPLCTPKAIREQLVQLMFETFNVSGFYASEQAVLSLYAVGRISGCTVDIGHGKIDIAPVLEGAVQHIAS 163
Cdd:cd10209 77 EEGNEGQVLIAEPLLTSKAERERLTQLMFETFNVSGLYASEQAVLSLYAVGRISGCVVDVGHGKIDIAPVWEGAIQHNAV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 164 KRFELGGTELTKLFAQELGKTNPSMNLSMSDVEKLKEQYANCAEDEIAYKKT-QNCEIEQHTLPDGQVISIGRERYSVGE 242
Cdd:cd10209 157 RRFEIGGRDLTELLAAELGKSNPKVKLDRSIVERLKEAVAWSADDEEAYEKKvLTCSPETYTLPDGRVISVGKERYCVGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 243 ALFQPSILGLEEHGIVEQLVRIISTVSSENHRQLLENTVLCGGTTSMTGFESRFQKEANLCSSAI-RPTLVKPPEYMPEN 321
Cdd:cd10209 237 ALFRPSILGIEEYGIVEQLVRAVSTSPSENRRQLLENIVLCGGTSSVPGLEARLQKEIRLLSSPSsRPALVKPPEYMPEN 316
|
330 340 350
....*....|....*....|....*....|....*...
gi 18411737 322 LGMYSAWVGGAILAKVVFPQNQHVTKADYDETGPSVVH 359
Cdd:cd10209 317 TLRYSAWIGGAILAKVVFPQNQHVTKADYDETGPSVVH 354
|
|
| ACTIN |
smart00268 |
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily |
3-363 |
8.65e-85 |
|
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
Pssm-ID: 214592 [Multi-domain] Cd Length: 373 Bit Score: 261.42 E-value: 8.65e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 3 ALVVDAGSKFLKAGAAiPDQSPAMIIPSQMKRMVDDGSSSADNPTTVFED---------VTLDPIERGLIRDWDAMEDLL 73
Cdd:smart00268 3 AIVIDNGSGTIKAGFA-GEDFPQVVFPSIVGRPKDGKGMVGDAKDIFVGDeaqekrgglELKYPIENGIVENWDDMEKIW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 74 RYVVYTGLGWEEgNEGNILFTDPLCTPKAIREQLVQLMFETFNVSGFYASEQAVLSLYAVGRISGCTVDIGHGKIDIAPV 153
Cdd:smart00268 82 DYTFFNELRVEP-EEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 154 LEGAVQHIASKRFELGGTELTKLFAQELGKTNPSMNlSMSDVE---KLKEQYANCAED-----EIAYKKTQNC-EIEQHT 224
Cdd:smart00268 161 VDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFN-SSAEFEivrEIKEKLCYVAEDfekemKLARESSESSkLEKTYE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 225 LPDGQVISIGRERYSVGEALFQPSILGLEEHGIVEQLVRIISTVSSENHRQLLENTVLCGGTTSMTGFESRFQKEAN-LC 303
Cdd:smart00268 240 LPDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKqLA 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 304 SSAIRPTLVKPPEympenlGMYSAWVGGAILAKVVFPQNQHVTKADYDETGPSVVHRKCF 363
Cdd:smart00268 320 PKKLKVKVIAPPE------RKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKCF 373
|
|
| PTZ00004 |
PTZ00004 |
actin-2; Provisional |
3-363 |
3.93e-81 |
|
actin-2; Provisional
Pssm-ID: 240225 [Multi-domain] Cd Length: 378 Bit Score: 252.38 E-value: 3.93e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 3 ALVVDAGSKFLKAGAAiPDQSPAMIIPS------QMKRMVDDGSSS------ADNPTTVFEdvTLDPIERGLIRDWDAME 70
Cdd:PTZ00004 8 AAVVDNGSGMVKAGFA-GDDAPRCVFPSivgrpkNPGIMVGMEEKDcyvgdeAQDKRGILT--LKYPIEHGIVTNWDDME 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 71 DLLRYVVYTGLGWEEgNEGNILFTDPLCTPKAIREQLVQLMFETFNVSGFYASEQAVLSLYAVGRISGCTVDIGHGKIDI 150
Cdd:PTZ00004 85 KIWHHTFYNELRVAP-EEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 151 APVLEGAVQHIASKRFELGGTELTKLFA---QELGKT-NPSMNLSMsdVEKLKEQYANCAED----EIAYKKTQNCEIEQ 222
Cdd:PTZ00004 164 VPIYEGYSLPHAIHRLDVAGRDLTEYMMkilHERGTTfTTTAEKEI--VRDIKEKLCYIALDfdeeMGNSAGSSDKYEES 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 223 HTLPDGQVISIGRERYSVGEALFQPSILGLEE-HGIVEQLVRIISTVSSENHRQLLENTVLCGGTTSMTGFESRFQKE-A 300
Cdd:PTZ00004 242 YELPDGTIITVGSERFRCPEALFQPSLIGKEEpPGIHELTFQSINKCDIDIRKDLYGNIVLSGGTTMYRGLPERLTKElT 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18411737 301 NLCSSAIRPTLVKPPEYmpenlgMYSAWVGGAILAKVVFPQNQHVTKADYDETGPSVVHRKCF 363
Cdd:PTZ00004 322 TLAPSTMKIKVVAPPER------KYSVWIGGSILSSLPTFQQMWVTKEEYDESGPSIVHRKCF 378
|
|
| ASKHA_NBD_actin_Arp-T1-3 |
cd13397 |
nucleotide-binding domain (NBD) of actin, actin-related proteins T1-T3 (Arp-T1-3), and similar ... |
3-354 |
1.76e-76 |
|
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: 239.78 E-value: 1.76e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 3 ALVVDAGSKFLKAGAAiPDQSPAMIIPSQMKRMVDDGSSSADNPTTVF-EDVTLD---------PIERGLIRDWDAMEDL 72
Cdd:cd13397 2 AVVIDNGSGLIKAGFA-GEDLPRAVFPSVVGRPKYKAVMLGAGQKEVYvGDEAQEkrgvltlsyPIEHGIVTNWDDMEKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 73 LRYVVYTGLGWEEgNEGNILFTDPLCTPKAIREQLVQLMFETFNVSGFYASEQAVLSLYAVGRISGCTVDIGHGKIDIAP 152
Cdd:cd13397 81 WHHTFENELRVKP-EEHPVLLTEAPLNPKQNREKMAEIMFETFGVPAFYVAIQAVLSLYSSGRTTGLVLDSGDGVTHTVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 153 VLEG-AVQHiASKRFELGGTELTkLFAQELGKTNPSMNLSMSD---VEKLKEQYANCAED-EIAYKKTQNCEIEQHTLPD 227
Cdd:cd13397 160 IYEGyALPH-AVQRLDLAGRDLT-EYLMKLLKERGHSFTTTAEreiVRDIKEKLCYVALDyEEELKKKSEELEKEYTLPD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 228 GQVISIGRERYSVGEALFQPSILGLEEHGIVEQLVRIISTVSSENHRQLLENTVLCGGTTSMTGFESRFQKE-ANLCSSA 306
Cdd:cd13397 238 GQVIKIGSERFRCPEALFRPSLIGREAPGIHKLVYNSIMKCDIDIRKDLYSNIVLSGGSTMFPGLPERLQKElEALAPSS 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 18411737 307 IRPTLVKPPEYmpenlgMYSAWVGGAILAKVVFPQNQHVTKADYDETG 354
Cdd:cd13397 318 TKVKVIAPPER------KYSVWIGGSILASLSTFKSMWITRAEYDEFG 359
|
|
| ASKHA_NBD_actin |
cd10224 |
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ... |
3-358 |
3.63e-75 |
|
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: 236.49 E-value: 3.63e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 3 ALVVDAGSKFLKAGAAiPDQSPAMIIPSQMKR------MVDDGSSSA---DNPTTVFEDVTLD-PIERGLIRDWDAMEDL 72
Cdd:cd10224 2 ALVVDNGSGMCKAGFA-GDDAPRAVFPSIVGRprhqgvMVGMGQKDSyvgDEAQSKRGILTLKyPIEHGIVTNWDDMEKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 73 LRYVVYTGL--GWEEGNegnILFTDPLCTPKAIREQLVQLMFETFNVSGFYASEQAVLSLYAVGRISGCTVDIGHGKIDI 150
Cdd:cd10224 81 WHHTFYNELrvAPEEHP---VLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 151 APVLEG-AVQHiASKRFELGGTELTKLFAQELGKTNPSMNLSMSD--VEKLKEQYANCAED---EIAyKKTQNCEIEQ-H 223
Cdd:cd10224 158 VPIYEGyALPH-AILRLDLAGRDLTDYLMKILTERGYSFTTTAEReiVRDIKEKLCYVALDfeqEMQ-TAASSSSLEKsY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 224 TLPDGQVISIGRERYSVGEALFQPSILGLEEHGIVEQLVRIISTVSSENHRQLLENTVLCGGTTSMTGFESRFQKE-ANL 302
Cdd:cd10224 236 ELPDGQVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEiTAL 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 18411737 303 CSSAIRPTLVKPPEYmpenlgMYSAWVGGAILAKVVFPQNQHVTKADYDETGPSVV 358
Cdd:cd10224 316 APSTMKIKIVAPPER------KYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 365
|
|
| Actin |
pfam00022 |
Actin; |
3-363 |
2.12e-73 |
|
Actin;
Pssm-ID: 394979 [Multi-domain] Cd Length: 407 Bit Score: 233.35 E-value: 2.12e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 3 ALVVDAGSKFLKAGAAiPDQSPAMIIPSQMKRMVDDGSSSA------DNPTTVFEDVTL-DPIERGLIRDWDAMEDLLRY 75
Cdd:pfam00022 3 ALVIDNGSHTTRAGFA-GEDAPKAVIPSCVGKPRGTKVEAAnkyyvgDEALTYRPGMEVrSPVEDGIVVDWDAMEEIWEH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 76 VVYTGLGWEEgNEGNILFTDPLCTPKAIREQLVQLMFETFNVSGFYASEQAVLSLYAVGRISGCTVDIGHGKIDIAPVLE 155
Cdd:pfam00022 82 VLKEELQVDP-EEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVPVHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 156 GAVQHIASKRFELGGTELTKLFAQ------------------------------ELGKTNPSMNLSMSD--VEKLKEQYA 203
Cdd:pfam00022 161 GYVLQKAIRRSDLGGDFLTDYLREllrsrnieitprylikskkpgdpapavtkrELPDTTYSYKTYQERrvLEEIKESVC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 204 NCAEDEIAYKKTQNCEIEQH-TLPDGQVISIGRERYSVGEALFQPSILGLEE--------HGIVEQLVRIISTVSSENHR 274
Cdd:pfam00022 241 YVSDDPFGDETTSSSIPTRVyELPDGSTIILGAERFRVPEILFNPSLIGSESelpppqtaVGIPELIVDAINACDVDLRP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 275 QLLENTVLCGGTTSMTGFESRFQKE-ANLCSSAIRPTLVKPPEyMPENLgmYSAWVGGAILAKV-VFPQnQHVTKADYDE 352
Cdd:pfam00022 321 SLLANIVVTGGNSLFPGFTERLEKElAQLAPPGVKVKIIAPGN-TVERR--YSAWIGGSILASLgTFQQ-MWVSKQEYEE 396
|
410
....*....|.
gi 18411737 353 TGPSVVHRKCF 363
Cdd:pfam00022 397 HGASVVERKCK 407
|
|
| ASKHA_NBD_actin-like |
cd10169 |
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ... |
4-354 |
2.14e-72 |
|
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: 225.83 E-value: 2.14e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 4 LVVDAGSKFLKAGAAIPDqSPAMIIPsqmkrmvddgsssadnpttvfedvtldpierglirdWDAMEDLLRYVVYTGLGW 83
Cdd:cd10169 1 IVIDNGSGTIKAGFAGED-APRLIFP------------------------------------WDDMEKIWEHVFYNLLRV 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 84 EeGNEGNILFTDPLCTPKAIREQLVQLMFETFNVSGFYASEQAVLSLYAVGRISGCTVDIGHGKIDIAPVLEGAVQHIAS 163
Cdd:cd10169 44 D-PEEHPVLLTEPPLNPKANREKLAEILFETFNVPSLYIANQAVLSLYASGRTTGLVVDSGEGVTHIVPVYEGYVLPHAV 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 164 KRFELGGTELTKLFAQELGKTNPSMNLS--MSDVEKLKEQYAncaedeiaykktqnceieqhtlpdgqvisigrerysvg 241
Cdd:cd10169 123 RRLDIGGRDLTDYLAKLLREKGYSFSTSaeREIVRDIKEKLC-------------------------------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 242 ealfqpsilgleehGIVEQLVRIISTVSSENHRQLLENTVLCGGTTSMTGFESRFQKE-ANLCSSAIRPTLVKPPEympe 320
Cdd:cd10169 165 --------------GLHELIYDSIMKCDIDLRKELYSNIVLSGGTTLFPGFAERLQKElSKLAPSSVKVKVIAPPE---- 226
|
330 340 350
....*....|....*....|....*....|....
gi 18411737 321 nlGMYSAWVGGAILAKVVFPQNQHVTKADYDETG 354
Cdd:cd10169 227 --RKYSAWIGGSILASLSTFQQMWITKEEYEEHG 258
|
|
| ASKHA_NBD_ACTL7 |
cd10214 |
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ... |
3-362 |
5.24e-70 |
|
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: 223.45 E-value: 5.24e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 3 ALVVDAGSKFLKAG-AAIPdqSPAMIIPSQMKRMVDDGSSSADNPTTVF---------EDVTL-DPIERGLIRDWDAMED 71
Cdd:cd10214 5 AVIIDLGTGYCKAGfAGQP--RPSYVISSTVGKPPQESAKTGDNRKETFvgkelanvePPLKLvNPLRHGIVVDWDCVQD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 72 LLRYVVYTGLGWEEgNEGNILFTDPLCTPKAIREQLVQLMFETFNVSGFYASEQAVLSLYAVGRISGCTVDIGHGKIDIA 151
Cdd:cd10214 83 IWEYIFEKEMKILP-EEHAVLVSDPPLSPTTNREKYAELMFETFSIPAMHIAYQSRLSLYSYGRTSGLVVESGHGVSYVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 152 PVLEGAVQHIASKRFELGGTELTKLFAQELGKT-NPSMNLSMSDVEKLKEQYANCAEDeiaYKKTQNCEIEQHT----LP 226
Cdd:cd10214 162 PIHEGYNLPHITGRADYAGSDLTAYLMKLLNEAgNKFTDDQLHIVEDIKKKCCYVALD---FEEEMGLPPQEYTvdyeLP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 227 DGQVISIGRERYSVGEALFQPSILGLEEHGIVEQLVRIISTVSSENHRQLLENTVLCGGTTSMTGFESRFQKEANLCSSA 306
Cdd:cd10214 239 DGHLITIGKERFRCPEMLFNPSLIGSKQPGLHTLTMNSLNKCDANLKKDLAKNILLCGGSTMFDGFPDRFQKELSKLCPN 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 18411737 307 IRPTLVKPPEYmpenlgMYSAWVGGAILAKVVFPQNQHVTKADYDETGPSVVHRKC 362
Cdd:cd10214 319 DNPIVAASPER------KYSVWTGGSILASLKSFQQLWVRRREYEERGPFVIYRKC 368
|
|
| PTZ00281 |
PTZ00281 |
actin; Provisional |
1-363 |
5.70e-70 |
|
actin; Provisional
Pssm-ID: 173506 [Multi-domain] Cd Length: 376 Bit Score: 223.81 E-value: 5.70e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 1 MEALVVDAGSKFLKAGAAiPDQSPAMIIPSQMKR---------MVDDGSSSADNPTTVFEDVTLD-PIERGLIRDWDAME 70
Cdd:PTZ00281 6 VQALVIDNGSGMCKAGFA-GDDAPRAVFPSIVGRprhtgvmvgMGQKDSYVGDEAQSKRGILTLKyPIEHGIVTNWDDME 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 71 DLLRYVVYTGLGWEEgNEGNILFTDPLCTPKAIREQLVQLMFETFNVSGFYASEQAVLSLYAVGRISGCTVDIGHGKIDI 150
Cdd:PTZ00281 85 KIWHHTFYNELRVAP-EEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVSHT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 151 APVLEGAVQHIASKRFELGGTELTKLFAQELGKTNPSMNLSMSD--VEKLKEQYANCA---EDEIAYKKTQNCEIEQHTL 225
Cdd:PTZ00281 164 VPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEReiVRDIKEKLAYVAldfEAEMQTAASSSALEKSYEL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 226 PDGQVISIGRERYSVGEALFQPSILGLEEHGIVEQLVRIISTVSSENHRQLLENTVLCGGTTSMTGFESRFQKEAN-LCS 304
Cdd:PTZ00281 244 PDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTaLAP 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 18411737 305 SAIRPTLVKPPEYmpenlgMYSAWVGGAILAKVVFPQNQHVTKADYDETGPSVVHRKCF 363
Cdd:PTZ00281 324 STMKIKIIAPPER------KYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKCF 376
|
|
| ASKHA_NBD_Arp1 |
cd10216 |
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ... |
4-362 |
3.23e-64 |
|
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: 208.55 E-value: 3.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 4 LVVDAGSKFLKAGAAiPDQSPAMIIPS-----QMKRMVddgsssadnPTTVFEDVTLD--------------PIERGLIR 64
Cdd:cd10216 4 VVIDNGSGVIKAGFA-GDDIPKVVFPSyvgrpKHVRVM---------AGALEGDVFVGpkaeehrgllkiryPMEHGIVT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 65 DWDAMEDLLRYVvYTGLGWEEGNEGN-ILFTDPLCTPKAIREQLVQLMFETFNVSGFYASEQAVLSLYAVGRISGCTVDI 143
Cdd:cd10216 74 DWNDMERIWQYV-YSKLQLNTFSEEHpVLLTEAPLNPRKNREKAAEVFFETFNVPALFVSMQAVLSLYASGRTTGVVLDS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 144 GHGKIDIAPVLEG-AVQHiASKRFELGGTELTKLFAQELGKTNPSMNLS--MSDVEKLKEQYANCAEDEIAYKKTQN--C 218
Cdd:cd10216 153 GDGVTHAVPIYEGfALPH-SIRRVDIAGRDVTEYLQLLLRKSGYNFHTSaeFEIVREIKEKACYVALNPQKEEKLEEekT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 219 EIEQHTLPDGQVISIGRERYSVGEALFQPSILGLEEHGIVEQLVRIISTVSSENHRQLLENTVLCGGTTSMTGFESRFQK 298
Cdd:cd10216 232 EKAQYTLPDGSTIEIGPERFRAPEILFNPELIGLEYPGVHEVLVDSIQKSDLDLRKTLYSNIVLSGGSTLFKGFGDRLLS 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18411737 299 EANlcssAIRPTLVK-----PPEYmpenlgMYSAWVGGAILAKVVFPQNQHVTKADYDETGPSVVHRKC 362
Cdd:cd10216 312 EVK----KLAPKDVKirisaPPER------LYSTWIGGSILASLSTFKKMWVSKKEYEEDGARILHRKT 370
|
|
| ASKHA_NBD_ScArp9-like |
cd10208 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ... |
4-361 |
5.87e-60 |
|
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: 197.14 E-value: 5.87e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 4 LVVDAGSKFLKAGAAIPD--QSPAMIIPSQMKRMVddgsssadnpttvfedvtldPIERGLIRDWDAMEDLLRYVVYTGL 81
Cdd:cd10208 3 LVIDPGSQTTRAGLGLGEllTPPTIEIPTRVEIIW--------------------PIQDGRVVDWDALEALWRHILFSLL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 82 G-WEEGNEGNILFTDPLCTPKAIREQLVQLMFETFNVSGFYASEQAVLSLYAVGRISGCTVDIGHGKIDIAPVLEGAVQH 160
Cdd:cd10208 63 SiPRPTNNSPVLLSVPPSWSKSDLELLTQLFFERLNVPAFAILEAPLAALYAAGATSGIVVDIGHEKTDITPIVDSQVVP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 161 IASKRFELGGTELTKLFAQELGKTNPSMNLSMSDVEKlkeqyancAEDEIA--YKKTQNCEI--EQHTLPDGQVISIGRE 236
Cdd:cd10208 143 HALVSIPIGGQDCTAHLAQLLKSDEPELKSQAESGEE--------ATLDLAeaLKKSPICEVlsDGADLASGTEITVGKE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 237 RYSVGEALFQPSILGLEEHGIVEQLVRIISTVSSENHRQLL-ENTVLCGGTTSMTGFESRFQKEA---NLCSSAI----R 308
Cdd:cd10208 215 RFRACEPLFKPSSLRVDLLIAAIAGALVLNASDEPDKRPALwENIIIVGGGSRIRGLKEALLSELqqfHLISETSaspqQ 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18411737 309 PT---LVKPPEYMPE---NLGMYSAWVGGAILAKVVFPQNQ---HVTKADYDETGPSVVHRK 361
Cdd:cd10208 295 PRiirLAKIPDYFPEwkkSGYEEAAFLGASIVAKLVFNDPSskhYISKVDYNEKGPAAIHTK 356
|
|
| PTZ00452 |
PTZ00452 |
actin; Provisional |
3-363 |
3.49e-55 |
|
actin; Provisional
Pssm-ID: 185631 Cd Length: 375 Bit Score: 185.34 E-value: 3.49e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 3 ALVVDAGSKFLKAGAAiPDQSPAMIIPSQMKR--MVDDGSSSADNPTTVFEDVTL--------DPIERGLIRDWDAMEDL 72
Cdd:PTZ00452 7 AVVIDNGSGYCKIGIA-GDDAPTSCFPAIVGRskQNDGIFSTFNKEYYVGEEAQAkrgvlaikEPIQNGIINSWDDIEII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 73 LRYVVYTGLGWEEGNEgNILFTDPLCTPKAIREQLVQLMFETFNVSGFYASEQAVLSLYAVGRISGCTVDIGHGKIDIAP 152
Cdd:PTZ00452 86 WHHAFYNELCMSPEDQ-PVFMTDAPMNSKFNRERMTQIMFETFNTPCLYISNEAVLSLYTSGKTIGLVVDSGEGVTHCVP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 153 VLEGAVQHIASKRFELGG---TELTKLFAQELGK--TNPSMNLSMSDVEKLKEQYANCAEDEIAYKKTQNCEIEQHTLPD 227
Cdd:PTZ00452 165 VFEGHQIPQAITKINLAGrlcTDYLTQILQELGYslTEPHQRIIVKNIKERLCYTALDPQDEKRIYKESNSQDSPYKLPD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 228 GQVISIGRERYSVGEALFQPSILGLEEHGIVEQLVRIISTVSSENHRQLLENTVLCGGTTSMTGFESRFQKE-ANLCSSA 306
Cdd:PTZ00452 245 GNILTIKSQKFRCSEILFQPKLIGLEVAGIHHLAYSSIKKCDLDLRQELCRNIVLSGGTTLFPGIANRLSNElTNLVPSQ 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 18411737 307 IRPTLVKPPEYmpenlgMYSAWVGGAILAKVVFPQNQHVTKADYDETGPSVVHRKCF 363
Cdd:PTZ00452 325 LKIQVAAPPDR------RFSAWIGGSIQCTLSTQQPQWIKRQEYDEQGPSIVHRKCF 375
|
|
| ASKHA_NBD_Arp4_ACTL6-like |
cd13395 |
nucleotide-binding domain (NBD) of the actin-related protein 4 (Arp4)-like subfamily; The ... |
3-354 |
7.12e-53 |
|
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: 180.07 E-value: 7.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 3 ALVVDAGSKFLKAGAAIPDqSPAMIIPS------QMKRMVDDGSSSADNPTTVFEDVT-----------LDPIERGLIRD 65
Cdd:cd13395 6 ALVLDIGSYSTRAGYAGED-TPKAVFPSvvgvvtDDDDAEDYVGGSGEKKRKYYIGTNsigvprpnmevISPLKDGLIED 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 66 WDAMEDLLRYVVYTGLGwEEGNEGNILFTDPLCTPKAIREQLVQLMFETFNVSGFYASEQAVLSLYAVGRISGCTVDIGH 145
Cdd:cd13395 85 WDAFEKLWDHALKNRLR-VDPSEHPLLLTEPSWNTRANREKLTELMFEKYNVPAFFLAKNAVLSAFANGRSTALVVDSGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 146 GKIDIAPVLEGAVQHIASKRFELGGTELTKLFAQ-------------ELGKTNPSM--------------------NLSM 192
Cdd:cd13395 164 TSTSVVPVHDGYVLQKAIVRSPLGGDFLTDQLLKllesknieiipryMIKSKEPVEggapakytkkdlpnttssyhRYMV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 193 SDV-EKLKE---QYANCAEDEIAYKKTQNCEIEqhtLPDGQVISIGRERYSVGEALFQPSIL---------GLEEHGIVE 259
Cdd:cd13395 244 RRVlQDFKEsvcQVSDSPFDESEAASIPTVSYE---LPDGYNIEFGAERFKIPELLFDPSLVkgipappseGNELLGLPQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 260 QLVRIISTVSSENHRQLLENTVLCGGTTSMTGFESRFQKE-ANLCSSAIRPTLVKPPEYMpENlgMYSAWVGGAILAKV- 337
Cdd:cd13395 321 LVYTSIGSCDVDIRPELYGNVVLTGGNSLLPGFTDRLNRElSEKAPGSLKLKILASGNTV-ER--RFSSWIGGSILASLg 397
|
410
....*....|....*..
gi 18411737 338 VFpQNQHVTKADYDETG 354
Cdd:cd13395 398 SF-QQMWISKQEYEEHG 413
|
|
| ASKHA_NBD_Arp2 |
cd10220 |
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ... |
4-358 |
2.04e-51 |
|
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: 175.44 E-value: 2.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 4 LVVDAGSKFLKAGAAiPDQSPAMIIPSQMKRMVDDGSSSADNPTtvFEDVT-----------LD---PIERGLIRDWDAM 69
Cdd:cd10220 3 VVCDNGTGFVKCGFA-GSNFPEHVFPSLVGRPILRAEEKVGDIE--IKDIMvgdeaselrsmLEvtyPMENGIVRNWDDM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 70 EDLLRYVVYTGLGWEEgNEGNILFTDPLCTPKAIREQLVQLMFETFNVSGFYASEQAVLSLYAVGRISGCTVDIGHGKID 149
Cdd:cd10220 80 EHLWDYTFGEKLKIDP-RECKILLTEPPMNPTKNREKMVEVMFEKYGFAGVYVAIQAVLTLYAQGLLTGVVVDSGDGVTH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 150 IAPVLEG-AVQHIAsKRFELGGTELTKLFAQELGKTNPSMNLSmSD---VEKLKEQYANCA-----EDEIAYKKTqnCEI 220
Cdd:cd10220 159 IVPVYEGfSLPHLT-RRLDVAGRDITRYLIKLLLLRGYAFNRT-ADfetVREIKEKLCYVAydielEQKLALETT--VLV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 221 EQHTLPDGQVISIGRERYSVGEALFQPSILGLEEHGIVEQLVRIISTVSSENHRQLLENTVLCGGTTSMTGFESRFQKE- 299
Cdd:cd10220 235 ESYTLPDGRVIKVGGERFEAPEALFQPHLIDVEGPGIAELLFNTIQAADIDTRPELYKHIVLSGGSTMYPGLPSRLEKEi 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18411737 300 -------------ANLCSSAIRptLVKPP--EYMpenlgmysAWVGGAILAKVVfpQNQH---VTKADYDETGPSVV 358
Cdd:cd10220 315 kqlylervlkgdtERLSKFKIR--IEDPPrrKHM--------VFLGGAVLADIM--KDKDefwITRQEYEEQGVRVL 379
|
|
| PTZ00466 |
PTZ00466 |
actin-like protein; Provisional |
2-363 |
4.68e-50 |
|
actin-like protein; Provisional
Pssm-ID: 240426 [Multi-domain] Cd Length: 380 Bit Score: 172.05 E-value: 4.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 2 EALVVDAGSKFLKAGAAiPDQSPAMIIPS-----QMKRMVD---DGSSSADNPTTVFE---DVTLdPIERGLIRDWDAME 70
Cdd:PTZ00466 13 QPIIIDNGTGYIKAGFA-GEDVPNLVFPSyvgrpKYKRVMAgavEGNIFVGNKAEEYRgllKVTY-PINHGIIENWNDME 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 71 DLLRYVvYTGLGWEEgNEGNILFTDPLCTPKAIREQLVQLMFETFNVSGFYASEQAVLSLYAVGRISGCTVDIGHGKIDI 150
Cdd:PTZ00466 91 NIWIHV-YNSMKINS-EEHPVLLTEAPLNPQKNKEKIAEVFFETFNVPALFISIQAILSLYSCGKTNGTVLDCGDGVCHC 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 151 APVLEGAVQHIASKRFELGGTELTKLFAQELGKTNPSMNLSmSDVEKLKEQYANCAEDEIAYKKTQNCEIEQHT-----L 225
Cdd:PTZ00466 169 VSIYEGYSITNTITRTDVAGRDITTYLGYLLRKNGHLFNTS-AEMEVVKNMKENCCYVSFNMNKEKNSSEKALTtlpyiL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 226 PDGQVISIGRERYSVGEALFQPSILGLEEHGIVEQLVRIISTVSSENHRQLLENTVLCGGTTSMTGFESRFQKEA-NLCS 304
Cdd:PTZ00466 248 PDGSQILIGSERYRAPEVLFNPSILGLEYLGLSELIVTSITRADMDLRRTLYSHIVLSGGTTMFHGFGDRLLNEIrKFAP 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 18411737 305 SAIRPTLVKPPEYmpenlgMYSAWVGGAILAKVVFPQNQHVTKADYDETGPSVVHRKCF 363
Cdd:PTZ00466 328 KDITIRISAPPER------KFSTFIGGSILASLATFKKIWISKQEFDEYGSVILHRKTF 380
|
|
| ASKHA_NBD_Arp6 |
cd10210 |
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ... |
4-354 |
1.39e-47 |
|
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: 165.42 E-value: 1.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 4 LVVDAGSKFLKAGAAipDQSPAMIIPSQMKR--------MVDDGSSSADNPTTVFedvTLDPIERGLIRDWDAMEDLLRY 75
Cdd:cd10210 2 LVLDNGAYTIKAGFA--SDDPPRVIPNCIAKpkserrrlFGDDQLDECKDLSGLF---YRRPFERGYLVNWDLQRQIWDH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 76 VVYTGLGWEEGNEGNILFTDPLCTPKAIREQLVQLMFETFNVSGFYASEQAVLSLYA--------VGRISGCT--VDIGH 145
Cdd:cd10210 77 LFGKLLLNVDPSDTALVLTEPPFNPPSIQEAMDEIVFEEYGFQSLYRTTAAALSAFAyladseqsSSSSSQCClvVDSGF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 146 GKIDIAPVLEGAVQHIASKRFELGGTELTKLFaQELgktnpsmnLS-----MSD----VEKLKEQYANCAED-----EIA 211
Cdd:cd10210 157 SFTHIVPFFDGKPVKRAVRRIDVGGKLLTNYL-KEI--------ISyrqlnVMDetylVNQIKEDLCFVSTDfyedlEIA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 212 YKKTQNCEIEQH-TLPDG-----------------------QVISIGRERYSVGEALFQPSILGLEEHGIVEQLVRIIST 267
Cdd:cd10210 228 KKKGKENTIRRDyVLPDYttskrgyvrdpeepnrgklkedeQVLRLNNERFTVPELLFHPSDIGIQQAGIAEAIVQSINA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 268 VSSENHRQLLENTVLCGGTTSMTGFESRFQKEanlcssaIRPtLVkPPEY-----MPENlGMYSAWVGGAILAKVVFPQN 342
Cdd:cd10210 308 CPEELQPLLYANIVLTGGNALFPGFRERLEAE-------LRS-LA-PDDYdvnvtLPED-PITYAWEGGSLLAQSPEFEE 377
|
410
....*....|..
gi 18411737 343 QHVTKADYDETG 354
Cdd:cd10210 378 LAVTRAEYEEHG 389
|
|
| PTZ00280 |
PTZ00280 |
Actin-related protein 3; Provisional |
1-360 |
2.12e-43 |
|
Actin-related protein 3; Provisional
Pssm-ID: 240343 [Multi-domain] Cd Length: 414 Bit Score: 155.28 E-value: 2.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 1 MEALVVDAGSKFLKAGAAIPDQsPAMIIPSQMkrmVDDGSSSADNPTTVFEDvtLD------------------PIERGL 62
Cdd:PTZ00280 4 LPVVVIDNGTGYTKMGYAGNTE-PTYIIPTLI---ADNSKQSRRRSKKGFED--LDfyigdealaasksytltyPMKHGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 63 IRDWDAMEDLLRYVVYTGLGWEEGNEGNILfTDPLCTPKAIREQLVQLMFETFNVSGFYASEQAVLSLYA---------- 132
Cdd:PTZ00280 78 VEDWDLMEKFWEQCIFKYLRCEPEEHYFIL-TEPPMNPPENREYTAEIMFETFNVKGLYIAVQAVLALRAswtskkakel 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 133 VGRISGCTVDIGHGKIDIAPVLEGAVQHIASKRFELGGTELTKLFAQ---ELGKTNPSMNlSMSDVEKLKEQYANCAEDE 209
Cdd:PTZ00280 157 GGTLTGTVIDSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQmlrERGEPIPAED-ILLLAQRIKEKYCYVAPDI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 210 I----AYKKTQNCEIEQHTLPD---GQ--VISIGRERYSVGEALFQPSILGLEEHGIVEQLV-RIISTVSSENHRQLLEN 279
Cdd:PTZ00280 236 AkefeKYDSDPKNHFKKYTAVNsvtKKpyTVDVGYERFLGPEMFFHPEIFSSEWTTPLPEVVdDAIQSCPIDCRRPLYKN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 280 TVLCGGTTSMTGF------------ESRFQKEANLCSSAIRPTLVKPpEYMPENLGMYSAWVGGAILA-KVVFPQNQHvT 346
Cdd:PTZ00280 316 IVLSGGSTMFKGFdkrlqrdvrkrvDRRLKKAEELSGGKLKPIPIDV-NVVSHPRQRYAVWYGGSMLAsSPEFEKVCH-T 393
|
410
....*....|....
gi 18411737 347 KADYDETGPSVVHR 360
Cdd:PTZ00280 394 KAEYDEYGPSICRY 407
|
|
| ASKHA_NBD_Arp3-like |
cd10221 |
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ... |
3-358 |
1.98e-34 |
|
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: 130.77 E-value: 1.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 3 ALVVDAGSKFLKAGAAIPDQsPAMIIPSQMKrmVDDGSSSADNP---TTVFEDvtLD------------------PIERG 61
Cdd:cd10221 1 AVVIDNGTGYTKMGYAGNTE-PQFIIPTVIA--IKESAKVGDGQrrsKKGIED--LDfyigdealansptyalkyPIRHG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 62 LIRDWDAMEDLLRYVVYTGLGWEEGNEGNILFTDPLCTPKAiREQLVQLMFETFNVSGFYASEQAVLSLYAV-------- 133
Cdd:cd10221 76 IVEDWDLMERFWEQCIFKYLRCEPEDHYFLLTEPPLNPPEN-REYTAEIMFETFNVPGLYIAVQAVLALAASwtsrkvge 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 134 GRISGCTVDIGHGKIDIAPVLEGAVQHIASKRFELGGTELTKlFAQEL----GKTNPSmNLSMSDVEKLKEQYANCAEDe 209
Cdd:cd10221 155 RTLTGTVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITY-FIQQLlrerEEGIPP-EDSLEVAKRIKERYCYVCPD- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 210 IA-----YKKTQNCEIEQHTLPD---GQ--VISIGRERYSVGEALFQPSILGLEEHGIVEQLV-RIISTVSSENHRQLLE 278
Cdd:cd10221 232 IVkefakYDSDPAKYIKQYTGINsvtGKpyTVDVGYERFLAPEIFFNPEIASSDFTTPLPEVVdQVIQSCPIDTRRGLYK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 279 NTVLCGGTTSMTGFESRFQKE------ANLCSSAIRPTLVKPPEYMPENL---GM--YSAWVGGAILAKV-VFPQNQHvT 346
Cdd:cd10221 312 NIVLSGGSTMFKDFGRRLQRDvkrivdARLKASEELSGGKLKPKPIDVNVishPMqrYAVWFGGSMLASTpEFYTVCH-T 390
|
410
....*....|..
gi 18411737 347 KADYDETGPSVV 358
Cdd:cd10221 391 KAEYEEYGPSIC 402
|
|
| ASKHA_NBD_Arp5 |
cd10211 |
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ... |
3-355 |
2.52e-34 |
|
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: 129.23 E-value: 2.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 3 ALVVDAGSKFLKAGAAIpDQSPAMIIPSQMKRMVDdgSSSADNPTTVFEDVTLD---------PIERGLIRDWDAMEDLL 73
Cdd:cd10211 1 PIVIDNGSYQCRAGWAG-DKEPRLVFRNLVAKPRD--RKKGITVTLVGNDILNDeavrshlrsPFDRNVVTNFDLQEQIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 74 RYVvYTGLGWEEGNEGN--ILFTDPLCTPKAIREQLVQLMFETFNVSGFYASEQAVLSLYAVGRI----SGCTVDIGHGK 147
Cdd:cd10211 78 DYI-FSHLGINSEGSVDhpIVLTEALCNPNYSRQLMSELLFECYGVPSVAYGIDSLFSYYHNQPQgdpsDGLVISSGYST 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 148 IDIAPVLEGAVQHIASKRFELGGTELTKLFAQELGKTNPS--MNLSMSDVEKLKEQYANCAEDeiaYKKtqncEIEQHTL 225
Cdd:cd10211 157 THVIPVLNGRLDLSQCKRINLGGFHATDYLQRLLQLKYPThpSAITLSRAEELVHEHCYVAED---YDE----ELKKWED 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 226 PDgqvisigrerysvgealfqpsilGLEEH--------GIVEQLVRIISTVSSENHRQLLENTVLCGGTTSMTGFESRFQ 297
Cdd:cd10211 230 PE-----------------------YYEENvrkiqlpfGLVETIEFVLKRYPAEQQDRLVQNVFLTGGNALFPGLKERLE 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18411737 298 KEAnlcsSAIRPTlvkppeYMPENLGMYS-----AWVGGAILAKVVFPQNQHVTKADYDETGP 355
Cdd:cd10211 287 KEL----RAIRPF------GSPFNVVRAKdpvldAWRGAAKWALDSTFEKVWITKQEYEEKGG 339
|
|
| COG5277 |
COG5277 |
Actin-related protein [Cytoskeleton]; |
5-335 |
3.36e-24 |
|
Actin-related protein [Cytoskeleton];
Pssm-ID: 444088 Cd Length: 424 Bit Score: 102.56 E-value: 3.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 5 VVDAGSKFLKAGAAIPDQSPAM---------IIPSQMKRMVDDGSS-------SADNPTTVFEDVTLD---PIERGLIR- 64
Cdd:COG5277 12 GIDFGTSYVKYGPIALEEKPRViqtrglflrIVGESKLLGPMEGLSrglvvgdEVSKYLSSVRDAIRNlkyPLRDGIVRr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 65 ----DWDAMEDLLRYVVYTGLGWEEGNEG-NILFTDPLCTPKAIREQLVQLMFETFNVSGFYA---SEQAVLSLYAVGRI 136
Cdd:COG5277 92 ddedAWRVLKELLRYTFAQFLVVDPEFHGfLVVVALSALAPDYMRERLFDIHFEVFSEEGAPAvtiIPQPLAVAIAEKAV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 137 SGCTVDIGHGKIDIAPVLEGAVQHiASKRFELGGTELTKLFAQELgktnpsMNLSMSD-------VEKLKEQYANCAED- 208
Cdd:COG5277 172 TCVVVEAGHGNSQVAPISRGPIRE-GLVALNRGGAEANAITREIL------KDRGYSDtareeyvVRVVKEALGLVPRDl 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 209 --EIAYKKTQNCEIE-QHTLPDGQV-ISIGR---ERYSVGEALFQPSILGLE----------------------EHGIVE 259
Cdd:COG5277 245 akAIQKAASNPDSFEaKVRLPNPTVeIELGNyawERFLIGEILFNPNHEGFEsyiqqgrlriedavigdvvlygEMGLAE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 260 QLVRIISTVSSENHRQLLENTVLCGGTTSMT---GFE-------SRFQKEAnlcsSAIRPTLVKPPEYMPENLgmYSAWV 329
Cdd:COG5277 325 AIINSIMKCDVEIQDELYSNIILSGGAFNWSvppGLEdvavdsvTRVQIEL----SELAPELKVNVRLVSDPQ--YSVWK 398
|
....*.
gi 18411737 330 GGAILA 335
Cdd:COG5277 399 GAIIYG 404
|
|
| ASKHA_NBD_AtArp8-like |
cd13396 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ... |
91-354 |
2.95e-21 |
|
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: 92.99 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 91 ILFTDPLC------TPKAIREQLVQLMFETF---NVSGFYASEQAVLSLYAVGRISGCTVDIGHGKIDIAPVLEGAVQH- 160
Cdd:cd13396 61 VVVSLPLChsddteSAAASRRQLRGTIFNVLfdmNVPAVCAVDQAVLALYAANRTSGIVVNIGFRVTTIVPVYRGRVMHd 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 161 IASKRFELGGTELTKLFAQELGKTNPSMNlSMSDVEKLKEQYANCAED---EIAYKKTQNCEIEQhtlpDGQVIsIGRER 237
Cdd:cd13396 141 IGVEVVGQGALRLTGFLKELMQQNGIRFP-SLYTVRTIKEKLCYVAEDyeaELAKDTQASCEVAG----EGWFT-LSNER 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 238 YSVGEALFQPSILGLEEHGIvEQLVRI----ISTVSSENHRQLLENTVLCGGTTSMTGFESRFQKEAN--LCSSAIRPTL 311
Cdd:cd13396 215 FKTGEILFQPGLGGMRAMGL-HQAVALcmdhCALVHSQGDDGWFKTIVLSGGSACLPGLSERLERELRklLPKSLSEGIR 293
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 18411737 312 VKPPEYmpenlGMYSAWVGGAILAKV-VFPQNQHVTKADYDETG 354
Cdd:cd13396 294 IIPPPL-----GPDSAWQGAKLISNLsNFPDGWCITKKQFRNKP 332
|
|
| ASKHA_NBD_Arp10 |
cd10207 |
nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; ... |
5-354 |
3.34e-21 |
|
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: 93.47 E-value: 3.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 5 VVDAGSKFLKAGAAiPDQSPAMIIPSQMKRMvddgsssadNPTTVFEDVTLDPIERGLIRDwdAMEDLLRYVVYtglgwE 84
Cdd:cd10207 2 VLDIGSAYTKCGFA-GESAPRCIIPSEVKLP---------GGKKVIRVVDQRSGNEEELYE--ALKEFLHELYF-----K 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 85 E----GNEGNILFTDPLCTPKAIREQLVQLMFETFNVSG--FYASeqAVLSLYAVGRISGCTVDIGHGKIDIAPVLEGAV 158
Cdd:cd10207 65 HllvnPKDRRVVVVESVLCPTPFRETLAKVLFKHFEVPSvlFAPS--HLLSLLTLGIRTALVVDCGYRETRVLPVYEGVP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 159 QHIASKRFELGGTELTKLFAQELGK--------------TNPSMNLSMSDVEKLKEQYANCAEDEIAyKKTQNCEIEQHT 224
Cdd:cd10207 143 LLSAWQSTPLGGKALHKRLKKLLLEhatvvtgdnkgqllSSVDSLLSEEVLEDIKVRACFVTSLERG-KTLQSATEEGST 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 225 LP-----------DGQ--VISIGRERYSVGEALFQPSIlglEEHGIVEQLVRIISTVSSENHRQLLENTVLCGGTTSMTG 291
Cdd:cd10207 222 EEpsppppvdyplDGEkiLIVPGSIRESAEELLFEGDN---EEKSLPTLILDSLLKCPIDVRKQLAENIVVIGGTSMLPG 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18411737 292 FESRFQKEANLC------SSAIRPTL---VKPPEYMPENLGmysAWVGGAILAKVVFPQNQHVTKADYDETG 354
Cdd:cd10207 299 FKHRLLEELRALlrkpkyFEELAPKTfrfHTPPSVFKPNYL---AWLGGSIFGALESILGRSLSREAYLQTG 367
|
|
| ASKHA_NBD_Arp8-like |
cd10206 |
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ... |
105-336 |
2.39e-14 |
|
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: 73.81 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 105 EQLVQLMFETFNVSGFYASEQAVLSLYAVGRISGCTVDIGHGKIDIAPVLEGAVqhIASKRFEL--GGTELTKLFA---- 178
Cdd:cd10206 202 KELVDLLLRRLGFSSVFVHQESVCATFGAGLSSACVVDIGAQKTSVACVEDGLS--IPNSRIRLpyGGDDITRCFLwllr 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 179 ------QELGKTNPsmnLSMSDVEKLKEQYANCAEDEIAykkTQNCEIEQHTlPDGQVisigrERYSVGealfqpsILGL 252
Cdd:cd10206 280 rsgfpyRECNLNSP---LDFLLLERLKETYCTLDQDDIG---VQLHEFYVRE-PGQPT-----LKYQFK-------LLPL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 253 EEhGIVEQlvrIISTVSSENHRQLLENTVLCGGTTSMTGF----ESRFQKEANLCSSAIRPTLV-KPPEYM-PENLgmys 326
Cdd:cd10206 341 DE-AIVQS---ILSCASDELKRKMYSSILLVGGGAKIPGLaealEDRLLIKIPSLFEAVETVEVlPPPKDMdPSLL---- 412
|
250
....*....|
gi 18411737 327 AWVGGAILAK 336
Cdd:cd10206 413 AWKGGAVLAC 422
|
|
| syringactin |
NF040575 |
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ... |
286-362 |
3.94e-10 |
|
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: 57.30 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 286 TTSMTGFESRFQKEanLCSSAIRPTLVK---PPEymPEnlgmYSAWVGGAILAKVVFPQNQHVTKADYDETGPSVVHRKC 362
Cdd:NF040575 61 RVNESGFYEKLKKS--ITEKAPKGALIGmtlDPK--PE----SAAWRGAAMYAASEGFVEMAITKQEYDESGPSIVHRKC 132
|
|
| ASKHA_NBD_ScArp7-like |
cd10212 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and ... |
24-351 |
5.74e-08 |
|
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: 53.95 E-value: 5.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 24 PAMIIPSQMKRMVDDG---------------SSSADNPTTVFEDVTldpiERGLIRDWDAMEDLLRYVVYTGLGWEEgNE 88
Cdd:cd10212 25 PQCIIPSSYIKRTDEGgeaefifgtynmidaAAEKRNGDEVYTLVD----SQGLPYNWDALEMQWRYLYDTQLKVSP-EE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 89 GNILFTDPLCTPK---AIREQLVQLMFETFNVSGFYASEQAVLSLYAVGRISGCTVDIGHGKIDIAPVLEGAVQHIASKR 165
Cdd:cd10212 100 LPLVITMPATNGKpdmAILERYYELAFDKLNVPVFQIVIEPLAIALSMGKSSAFVIDIGASGCNVTPIIDGIVVKNAVVR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 166 FELGG--------TELTKLFAQELGKTNPS------------------------MNLSMSDVEKLKEQYANCAeDEIAYK 213
Cdd:cd10212 180 SKFGGdfldfqvhERLAPLIKEENDMENMAdeqkrstdvwyeastwiqqfkstmLQVSEKDLFELERYYKEQA-DIYAKQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 214 KTQNCEIEQHTL---------------------PDGQVISIG-RERYSVGEALFQPSILGLE---EHGIVEQLVRIISTV 268
Cdd:cd10212 259 QEQLKQMDQQLQytaltgspnnplvqkknflfkPLNKTLTLDlKECYQFAEYLFKPQLISDKfspEDGLGPLMAKSVKKA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 269 SSENHRQLLENTVLCGGTTSMTGFESRFQKEANLCSSAIRPTLVKPPEYMPENLgmySAWVGGAILAKV-VFPQNQHVTK 347
Cdd:cd10212 339 PEQVYSLLLTNVIITGSTSLIEGMEQRIIKELSIRFPQYKLTTFANQVMMDRKI---QGWLGALTMANLpSWSLGKWYSK 415
|
....
gi 18411737 348 ADYD 351
Cdd:cd10212 416 EDYE 419
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
141-302 |
9.90e-07 |
|
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes type IV pilus inner membrane component PilM, cell division protein FtsA, and ethanolamine utilization protein EutJ. PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. Members in PilM-like family belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466854 [Multi-domain] Cd Length: 282 Bit Score: 49.60 E-value: 9.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 141 VDIGHGKIDIAPVLEGAVqhIASKRFELGGTELTKLFAQELgktnpsmNLSMSDVEKLKEQYANcaEDEIAYKktqncEI 220
Cdd:cd24004 119 VDIGAGTTDIALIRNGGI--EAYRMVPLGGDDFTKAIAEGF-------LISFEEAEKIKRTYGI--FLLIEAK-----DQ 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 221 EQHTLPDGQVISIGRERysvgealfqpsilgleehgiVEQLVRIISTVSSE-NHRQLLENTV-LCGGTTSMTGFESRFQK 298
Cdd:cd24004 183 LGFTINKKEVYDIIKPV--------------------LEELASGIANAIEEyNGKFKLPDAVyLVGGGSKLPGLNEALAE 242
|
....
gi 18411737 299 EANL 302
Cdd:cd24004 243 KLGL 246
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
121-298 |
4.34e-06 |
|
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. FtsA binds ATP. FtsA interacts with FtsZ. This interaction plays an essential role in cell division.
Pssm-ID: 466898 [Multi-domain] Cd Length: 372 Bit Score: 48.30 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 121 YASEQAVLSlyAVGRISGCT-VDIGHGKIDIAPVLEGAVQHIASkrFELGGTELTKLFAQELgktnpsmNLSMSDVEKLK 199
Cdd:cd24048 184 LASAEAVLT--EDEKELGVAlIDIGGGTTDIAVFKNGSLRYTAV--IPVGGNHITNDIAIGL-------NTPFEEAERLK 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 200 EQYANCAEDEIA----YKKTQNCEIEQHTLPDGQVISIGRERYsvgealfqpsilglEEhgIVEQLVRIISTVSSENHrq 275
Cdd:cd24048 253 IKYGSALSEEADedeiIEIPGVGGREPREVSRRELAEIIEARV--------------EE--ILELVKKELKESGYEDL-- 314
|
170 180
....*....|....*....|...
gi 18411737 276 LLENTVLCGGTTSMTGFESRFQK 298
Cdd:cd24048 315 LPGGIVLTGGGSQLPGLVELAEE 337
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
121-298 |
1.28e-04 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 43.58 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 121 YASEQAVLSlyAVGRISGCT-VDIGHGKIDIAPVLEGAVQHIASkrFELGGTELTKLFAQELgktnpsmNLSMSDVEKLK 199
Cdd:COG0849 186 LASAEAVLT--EDEKELGVAlVDIGGGTTDIAVFKDGALRHTAV--IPVGGDHITNDIAIGL-------RTPLEEAERLK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 200 EQYANC------AEDEIAYK---KTQNCEIEQHTLpdgqvISIGRERYsvgEALFQpSILG-LEEHGIVEQLVRIIstvs 269
Cdd:COG0849 255 IKYGSAlasladEDETIEVPgigGRPPREISRKEL-----AEIIEARV---EEIFE-LVRKeLKRSGYEEKLPAGV---- 321
|
170 180
....*....|....*....|....*....
gi 18411737 270 senhrqllentVLCGGTTSMTGFESRFQK 298
Cdd:COG0849 322 -----------VLTGGGSQLPGLVELAEE 339
|
|
| FtsA |
pfam14450 |
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ... |
141-317 |
1.82e-04 |
|
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains. The FtsA protein contains two structurally related actin-like ATPase domains which are also structurally related to the ATPase domains of HSP70 (see PF00012). FtsA has a SHS2 domain PF02491 inserted in to the RnaseH fold PF02491.
Pssm-ID: 464177 [Multi-domain] Cd Length: 167 Bit Score: 41.55 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 141 VDIGHGKIDIAPVLEGAVQHIASkrFELGGTELTKLFAQELgktnpsmNLSMSDVEKLKEQYANC-AEDEIAYKKTQNCE 219
Cdd:pfam14450 3 IDIGGGTTDIAVFEDGALRHTRV--IPVGGNGITKDIAIGL-------RTAVEEAERLKIKYGSAlASLADEDEVPGVGG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 220 IEQHTLPDGQVISIGRERysvgealfqpsilgLEEhgIVEQLVRIIS--TVSSENHRQL---LENTVLCGGTTSMTGFES 294
Cdd:pfam14450 74 REPREISRKELAEIIEAR--------------VEE--ILELVRAELEdrEVLPGEYVRLevdVHGIVLTGGGSALPGLVE 137
|
170 180
....*....|....*....|....*
gi 18411737 295 RFQKEANLCSSAIRPTLV--KPPEY 317
Cdd:pfam14450 138 LAERALGLPVRIGSPDGIggRNPAY 162
|
|
| ASKHA_NBD_MamK |
cd24009 |
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ... |
57-299 |
2.54e-04 |
|
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: 42.58 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 57 PIERGLI-----RDWDAMEDLLRYVVytglgwEEGNEGNilfTDPLC--------TPKAIREQLVQLMFETFN----VSG 119
Cdd:cd24009 63 PLEDGVIkegddRDLEAARELLQHLI------ELALPGP---DDEIYavigvparASAENKQALLEIARELVDgvmvVSE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 120 FYASEqavlslYAVGRISGC-TVDIGHGKIDIApVLEGAV----QHIASKRfelGGTELTKLFAQELGKTNPSMNLSMSD 194
Cdd:cd24009 134 PFAVA------YGLDRLDNSlIVDIGAGTTDLC-RMKGTIpteeDQITLPK---AGDYIDEELVDLIKERYPEVQLTLNM 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 195 VEKLKEQYAncaedeIAYKKTQNCEIEqhtLP-DGQV--ISIGRERYSVGEALFQPsilgleehgIVEQLVRIISTVSSE 271
Cdd:cd24009 204 ARRWKEKYG------FVGDASEPVKVE---LPvDGKPvtYDITEELRIACESLVPD---------IVEGIKKLIASFDPE 265
|
250 260
....*....|....*....|....*...
gi 18411737 272 NHRQLLENTVLCGGTTSMTGFESRFQKE 299
Cdd:cd24009 266 FQEELRNNIVLAGGGSRIRGLDTYIEKA 293
|
|
| ASKHA_NBD_PilM |
cd24049 |
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
141-302 |
6.05e-04 |
|
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar proteins; PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, PilM associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.
Pssm-ID: 466899 [Multi-domain] Cd Length: 339 Bit Score: 41.50 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 141 VDIGHGKIDIAPVLEGAVQhiASKRFELGGTELTKLFAQELGktnpsmnLSMSDVEKLKEQYancaedeiaykktqncei 220
Cdd:cd24049 181 LDIGASSTTLVIVKNGKLL--FTRSIPVGGNDITEAIAKALG-------LSFEEAEELKREY------------------ 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 221 eqhtlpdGQVISIGRERYSVGEALFQPSIlgleeHGIVEQLVRIISTVSSENHRQLLENTVLCGGTTSMTGFESRFQKEA 300
Cdd:cd24049 234 -------GLLLEGEEGELKKVAEALRPVL-----ERLVSEIRRSLDYYRSQNGGEPIDKIYLTGGGSLLPGLDEYLSERL 301
|
..
gi 18411737 301 NL 302
Cdd:cd24049 302 GI 303
|
|
| ftsA |
TIGR01174 |
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the ... |
121-291 |
8.87e-04 |
|
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the bacterial homolog of tubulin. It is an ATP-binding protein and shows structural similarities to actin and heat shock cognate protein 70. [Cellular processes, Cell division]
Pssm-ID: 273483 [Multi-domain] Cd Length: 371 Bit Score: 41.08 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 121 YASEQAVLS-----LYAvgrisgCTVDIGHGKIDIAPVLEGAVQHIASkrFELGGTELTKLFAQELgktnpsmNLSMSDV 195
Cdd:TIGR01174 182 LASAIAVLTedekeLGV------CLIDIGGGTTDIAVYTGGSIRYTKV--IPIGGNHITKDIAKAL-------RTPLEEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411737 196 EKLKEQYANCAEDEIAykKTQNCEI------EQHTLPDGQVISIGRERYsvgEALFqpsilgleehGIVEQlvRIISTVS 269
Cdd:TIGR01174 247 ERIKIKYGCASIPLEG--PDENIEIpsvgerPPRSLSRKELAEIIEARA---EEIL----------EIVKQ--KELRKSG 309
|
170 180
....*....|....*....|..
gi 18411737 270 SENHrqLLENTVLCGGTTSMTG 291
Cdd:TIGR01174 310 FKEE--LNGGIVLTGGGAQLEG 329
|
|
| |
