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Conserved domains on  [gi|240132127|gb|EER31685|]
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conserved hypothetical protein [Candida tropicalis MYA-3404]

Protein Classification

COG5277 superfamily protein( domain architecture ID 1903615)

COG5277 superfamily protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
243-888 7.91e-136

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: 412.79  E-value: 7.91e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 243 DVIILQPGTRFIRIGKATDAVPMVVPNVIAVRKqtKTPKLDGNFPTRSFKEDEEDGDIIiDEEFDEQKAVMTKDFRARMR 322
Cdd:cd10206    1 KTIVIHPGSRNLRIGRASDDLPVVIPHCIARRR--KQTGSARPEDVPPAVRNGEDSVES-EEEREEALKEVERALKSRKK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 323 FYKRRVLPNsrETVSNFNRKREPEKIHDHNDPNKKEWI--KGGAKEYYVGEDALKLILNDGWILRYPMINGNFNEySYDY 400
Cdd:cd10206   78 SNGRRRIPN--QVSAKQNKPSKPENVPEDLDASSGENWtdTSDYPDFLVGEEALRLPPSEEYNLHWPIRRGRLNV-HSDG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 401 ESREEILGDLSNILGECLKQ-LGIE--NISRFKVMLLIPDLYDKSYIETWVELLFKFIGFGRVGILQEAVAATFGATAST 477
Cdd:cd10206  155 GSLTAVLDDLEDIWSHALEEkLEIPrkDLKNYRAVLVIPDLFDRRHVKELVDLLLRRLGFSSVFVHQESVCATFGAGLSS 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 478 ACIVDVGAQTTKISCVDEGMIINDSRILLNYGGDNITETFIKLILEDQFPYKDINLIDSYDWELAQELKEKFITFQDADI 557
Cdd:cd10206  235 ACVVDIGAQKTSVACVEDGLSIPNSRIRLPYGGDDITRCFLWLLRRSGFPYRECNLNSPLDFLLLERLKETYCTLDQDDI 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 558 AVQLYDFYKRNPFKQTAKYEFKVfdevmlapmglffpkifqlenkkpsipnynsssktnrltvdnlfgksldqysnkpnn 637
Cdd:cd10206  315 GVQLHEFYVREPGQPTLKYQFKL--------------------------------------------------------- 337
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 638 ptsksqeelktqvnycdltdeellmkligeeitrddkveteegderlfdVPLEKAIIESITNAGlasDMSKIKKFYDNIL 717
Cdd:cd10206  338 -------------------------------------------------LPLDEAIVQSILSCA---SDELKRKMYSSIL 365
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 718 IVGGGlAKINGYDLLLTDRLNIWRPKILstsaldvvvghlndeiksntikrqnlieeaeqkiresQPVETttdadqqqqq 797
Cdd:cd10206  366 LVGGG-AKIPGLAEALEDRLLIKIPSLF-------------------------------------EAVET---------- 397
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 798 qptgevelpeetiekinnqtelkldieyidelidkngshlpVTILPSPREFDPSMITWKGGSVYGRLKVVNEMWITQKDW 877
Cdd:cd10206  398 -----------------------------------------VEVLPPPKDMDPSLLAWKGGAVLACLDSAQELWITRKEW 436
                        650
                 ....*....|.
gi 240132127 878 DLLGSRCLYYK 888
Cdd:cd10206  437 QRLGVRALRER 447
 
Name Accession Description Interval E-value
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
243-888 7.91e-136

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: 412.79  E-value: 7.91e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 243 DVIILQPGTRFIRIGKATDAVPMVVPNVIAVRKqtKTPKLDGNFPTRSFKEDEEDGDIIiDEEFDEQKAVMTKDFRARMR 322
Cdd:cd10206    1 KTIVIHPGSRNLRIGRASDDLPVVIPHCIARRR--KQTGSARPEDVPPAVRNGEDSVES-EEEREEALKEVERALKSRKK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 323 FYKRRVLPNsrETVSNFNRKREPEKIHDHNDPNKKEWI--KGGAKEYYVGEDALKLILNDGWILRYPMINGNFNEySYDY 400
Cdd:cd10206   78 SNGRRRIPN--QVSAKQNKPSKPENVPEDLDASSGENWtdTSDYPDFLVGEEALRLPPSEEYNLHWPIRRGRLNV-HSDG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 401 ESREEILGDLSNILGECLKQ-LGIE--NISRFKVMLLIPDLYDKSYIETWVELLFKFIGFGRVGILQEAVAATFGATAST 477
Cdd:cd10206  155 GSLTAVLDDLEDIWSHALEEkLEIPrkDLKNYRAVLVIPDLFDRRHVKELVDLLLRRLGFSSVFVHQESVCATFGAGLSS 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 478 ACIVDVGAQTTKISCVDEGMIINDSRILLNYGGDNITETFIKLILEDQFPYKDINLIDSYDWELAQELKEKFITFQDADI 557
Cdd:cd10206  235 ACVVDIGAQKTSVACVEDGLSIPNSRIRLPYGGDDITRCFLWLLRRSGFPYRECNLNSPLDFLLLERLKETYCTLDQDDI 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 558 AVQLYDFYKRNPFKQTAKYEFKVfdevmlapmglffpkifqlenkkpsipnynsssktnrltvdnlfgksldqysnkpnn 637
Cdd:cd10206  315 GVQLHEFYVREPGQPTLKYQFKL--------------------------------------------------------- 337
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 638 ptsksqeelktqvnycdltdeellmkligeeitrddkveteegderlfdVPLEKAIIESITNAGlasDMSKIKKFYDNIL 717
Cdd:cd10206  338 -------------------------------------------------LPLDEAIVQSILSCA---SDELKRKMYSSIL 365
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 718 IVGGGlAKINGYDLLLTDRLNIWRPKILstsaldvvvghlndeiksntikrqnlieeaeqkiresQPVETttdadqqqqq 797
Cdd:cd10206  366 LVGGG-AKIPGLAEALEDRLLIKIPSLF-------------------------------------EAVET---------- 397
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 798 qptgevelpeetiekinnqtelkldieyidelidkngshlpVTILPSPREFDPSMITWKGGSVYGRLKVVNEMWITQKDW 877
Cdd:cd10206  398 -----------------------------------------VEVLPPPKDMDPSLLAWKGGAVLACLDSAQELWITRKEW 436
                        650
                 ....*....|.
gi 240132127 878 DLLGSRCLYYK 888
Cdd:cd10206  437 QRLGVRALRER 447
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
362-890 2.09e-20

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 94.25  E-value: 2.09e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127   362 GGAKEYYVGEDALklILNDGWILRYPMINGnfneYSYDYESREEILgdlSNILGeclKQLGIENISRfKVMLLIPDLYDK 441
Cdd:smart00268  42 GDAKDIFVGDEAQ--EKRGGLELKYPIENG----IVENWDDMEKIW---DYTFF---NELRVEPEEH-PVLLTEPPMNPK 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127   442 SYIETWVELLFKFIGFGRVGILQEAVAATFGATASTACIVDVGAQTTKISCVDEGMIINDSRILLNYGGDNITETFIKLI 521
Cdd:smart00268 109 SNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVPVVDGYVLPHAIKRIDIAGRDITDYLKELL 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127   522 LED--QFPYKDinlidsyDWELAQELKEKfitfqdadiavqlydfykrnpfkqtakyefkvfdevmLAPMGLFFPKIFQL 599
Cdd:smart00268 189 SERgyQFNSSA-------EFEIVREIKEK-------------------------------------LCYVAEDFEKEMKL 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127   600 enkkpsipnYNSSSKTNRLTVDnlfgksldqYsnkpnnptsksqeELKTQVNYCDLtdeellmkligeeitrddkVETEE 679
Cdd:smart00268 225 ---------ARESSESSKLEKT---------Y-------------ELPDGNTIKVG-------------------NERFR 254
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127   680 GDERLF---DVPLEKAII-ESITNAGLASDMSKIKKFYDNILIVGGGlAKINGYDLLLTDRLNIWRPKIlstsaldvvvg 755
Cdd:smart00268 255 IPEILFspeLIGLEQKGIhELVYESIQKCDIDVRKDLYENIVLSGGS-TLIPGFGERLEKELKQLAPKK----------- 322
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127   756 hlndeiksntikrqnlieeaeqkiresqpvetttdadqqqqqqptgevelpeetiekinnqtelkldieyidelidkngs 835
Cdd:smart00268     --------------------------------------------------------------------------------
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 240132127   836 hLPVTILPSPrefDPSMITWKGGSVYGRLKVVNEMWITQKDWDLLGSRCLYYKSI 890
Cdd:smart00268 323 -LKVKVIAPP---ERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKCF 373
Actin pfam00022
Actin;
364-538 1.26e-06

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 51.92  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127  364 AKEYYVGEDALKLilNDGWILRYPMINGnfneYSYDYESREEILgdlSNILGECLKQLGIENisrfKVMLLIPDLYDKSY 443
Cdd:pfam00022  42 ANKYYVGDEALTY--RPGMEVRSPVEDG----IVVDWDAMEEIW---EHVLKEELQVDPEEH----PLLLTEPPWNPPAN 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127  444 IETWVELLFKFIGFGRVGILQEAVAATFGATASTACIVDVGAQTTKISCVDEGMIINDSRILLNYGGDNITETFIKLILE 523
Cdd:pfam00022 109 REKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVPVHDGYVLQKAIRRSDLGGDFLTDYLRELLRS 188
                         170
                  ....*....|....*
gi 240132127  524 DQFPYKDINLIDSYD 538
Cdd:pfam00022 189 RNIEITPRYLIKSKK 203
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
477-597 3.17e-04

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 43.95  E-value: 3.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 477 TACIVDVGAQTTKISCVDEGMIINDSRILLNYGGDNITEtFIKLIL---EDQFPYKDINlidsydwELAQELKEKFiTFQ 553
Cdd:PTZ00280 161 TGTVIDSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITN-FIQQMLrerGEPIPAEDIL-------LLAQRIKEKY-CYV 231
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 240132127 554 DADIAvQLYDFYKRNP---FKQ--------TAKYEFKVFDEVMLAPMGLFFPKIF 597
Cdd:PTZ00280 232 APDIA-KEFEKYDSDPknhFKKytavnsvtKKPYTVDVGYERFLGPEMFFHPEIF 285
 
Name Accession Description Interval E-value
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
243-888 7.91e-136

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: 412.79  E-value: 7.91e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 243 DVIILQPGTRFIRIGKATDAVPMVVPNVIAVRKqtKTPKLDGNFPTRSFKEDEEDGDIIiDEEFDEQKAVMTKDFRARMR 322
Cdd:cd10206    1 KTIVIHPGSRNLRIGRASDDLPVVIPHCIARRR--KQTGSARPEDVPPAVRNGEDSVES-EEEREEALKEVERALKSRKK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 323 FYKRRVLPNsrETVSNFNRKREPEKIHDHNDPNKKEWI--KGGAKEYYVGEDALKLILNDGWILRYPMINGNFNEySYDY 400
Cdd:cd10206   78 SNGRRRIPN--QVSAKQNKPSKPENVPEDLDASSGENWtdTSDYPDFLVGEEALRLPPSEEYNLHWPIRRGRLNV-HSDG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 401 ESREEILGDLSNILGECLKQ-LGIE--NISRFKVMLLIPDLYDKSYIETWVELLFKFIGFGRVGILQEAVAATFGATAST 477
Cdd:cd10206  155 GSLTAVLDDLEDIWSHALEEkLEIPrkDLKNYRAVLVIPDLFDRRHVKELVDLLLRRLGFSSVFVHQESVCATFGAGLSS 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 478 ACIVDVGAQTTKISCVDEGMIINDSRILLNYGGDNITETFIKLILEDQFPYKDINLIDSYDWELAQELKEKFITFQDADI 557
Cdd:cd10206  235 ACVVDIGAQKTSVACVEDGLSIPNSRIRLPYGGDDITRCFLWLLRRSGFPYRECNLNSPLDFLLLERLKETYCTLDQDDI 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 558 AVQLYDFYKRNPFKQTAKYEFKVfdevmlapmglffpkifqlenkkpsipnynsssktnrltvdnlfgksldqysnkpnn 637
Cdd:cd10206  315 GVQLHEFYVREPGQPTLKYQFKL--------------------------------------------------------- 337
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 638 ptsksqeelktqvnycdltdeellmkligeeitrddkveteegderlfdVPLEKAIIESITNAGlasDMSKIKKFYDNIL 717
Cdd:cd10206  338 -------------------------------------------------LPLDEAIVQSILSCA---SDELKRKMYSSIL 365
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 718 IVGGGlAKINGYDLLLTDRLNIWRPKILstsaldvvvghlndeiksntikrqnlieeaeqkiresQPVETttdadqqqqq 797
Cdd:cd10206  366 LVGGG-AKIPGLAEALEDRLLIKIPSLF-------------------------------------EAVET---------- 397
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 798 qptgevelpeetiekinnqtelkldieyidelidkngshlpVTILPSPREFDPSMITWKGGSVYGRLKVVNEMWITQKDW 877
Cdd:cd10206  398 -----------------------------------------VEVLPPPKDMDPSLLAWKGGAVLACLDSAQELWITRKEW 436
                        650
                 ....*....|.
gi 240132127 878 DLLGSRCLYYK 888
Cdd:cd10206  437 QRLGVRALRER 447
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
362-890 2.09e-20

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 94.25  E-value: 2.09e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127   362 GGAKEYYVGEDALklILNDGWILRYPMINGnfneYSYDYESREEILgdlSNILGeclKQLGIENISRfKVMLLIPDLYDK 441
Cdd:smart00268  42 GDAKDIFVGDEAQ--EKRGGLELKYPIENG----IVENWDDMEKIW---DYTFF---NELRVEPEEH-PVLLTEPPMNPK 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127   442 SYIETWVELLFKFIGFGRVGILQEAVAATFGATASTACIVDVGAQTTKISCVDEGMIINDSRILLNYGGDNITETFIKLI 521
Cdd:smart00268 109 SNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVPVVDGYVLPHAIKRIDIAGRDITDYLKELL 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127   522 LED--QFPYKDinlidsyDWELAQELKEKfitfqdadiavqlydfykrnpfkqtakyefkvfdevmLAPMGLFFPKIFQL 599
Cdd:smart00268 189 SERgyQFNSSA-------EFEIVREIKEK-------------------------------------LCYVAEDFEKEMKL 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127   600 enkkpsipnYNSSSKTNRLTVDnlfgksldqYsnkpnnptsksqeELKTQVNYCDLtdeellmkligeeitrddkVETEE 679
Cdd:smart00268 225 ---------ARESSESSKLEKT---------Y-------------ELPDGNTIKVG-------------------NERFR 254
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127   680 GDERLF---DVPLEKAII-ESITNAGLASDMSKIKKFYDNILIVGGGlAKINGYDLLLTDRLNIWRPKIlstsaldvvvg 755
Cdd:smart00268 255 IPEILFspeLIGLEQKGIhELVYESIQKCDIDVRKDLYENIVLSGGS-TLIPGFGERLEKELKQLAPKK----------- 322
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127   756 hlndeiksntikrqnlieeaeqkiresqpvetttdadqqqqqqptgevelpeetiekinnqtelkldieyidelidkngs 835
Cdd:smart00268     --------------------------------------------------------------------------------
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 240132127   836 hLPVTILPSPrefDPSMITWKGGSVYGRLKVVNEMWITQKDWDLLGSRCLYYKSI 890
Cdd:smart00268 323 -LKVKVIAPP---ERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKCF 373
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
409-562 4.47e-20

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: 90.63  E-value: 4.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 409 DLSNILGECLKQLGIENISRFKVMLLIPDLYDKSYIETWVELLFKFIGFGRVGILQEAVAATFGATASTACIVDVGAQTT 488
Cdd:cd10169   28 DMEKIWEHVFYNLLRVDPEEHPVLLTEPPLNPKANREKLAEILFETFNVPSLYIANQAVLSLYASGRTTGLVVDSGEGVT 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 489 KISCVDEGMIINDSRILLNYGGDNITETFIKLILEdqfpyKDINLIDSYDWELAQELKEKF----------ITFQDADIA 558
Cdd:cd10169  108 HIVPVYEGYVLPHAVRRLDIGGRDLTDYLAKLLRE-----KGYSFSTSAEREIVRDIKEKLcglheliydsIMKCDIDLR 182

                 ....
gi 240132127 559 VQLY 562
Cdd:cd10169  183 KELY 186
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
431-547 7.53e-11

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: 64.64  E-value: 7.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 431 VMLLIPDLYDKSYIETWVELLFKFIGFGRVGILQEAVAATFGATASTACIVDVGAQTTKISCVDEGMIINDSRILLNYGG 510
Cdd:cd10208   73 VLLSVPPSWSKSDLELLTQLFFERLNVPAFAILEAPLAALYAAGATSGIVVDIGHEKTDITPIVDSQVVPHALVSIPIGG 152
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 240132127 511 DNITETFIKLILEDQfPYKDINLIDSYDW--ELAQELKE 547
Cdd:cd10208  153 QDCTAHLAQLLKSDE-PELKSQAESGEEAtlDLAEALKK 190
Actin pfam00022
Actin;
364-538 1.26e-06

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 51.92  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127  364 AKEYYVGEDALKLilNDGWILRYPMINGnfneYSYDYESREEILgdlSNILGECLKQLGIENisrfKVMLLIPDLYDKSY 443
Cdd:pfam00022  42 ANKYYVGDEALTY--RPGMEVRSPVEDG----IVVDWDAMEEIW---EHVLKEELQVDPEEH----PLLLTEPPWNPPAN 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127  444 IETWVELLFKFIGFGRVGILQEAVAATFGATASTACIVDVGAQTTKISCVDEGMIINDSRILLNYGGDNITETFIKLILE 523
Cdd:pfam00022 109 REKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVPVHDGYVLQKAIRRSDLGGDFLTDYLRELLRS 188
                         170
                  ....*....|....*
gi 240132127  524 DQFPYKDINLIDSYD 538
Cdd:pfam00022 189 RNIEITPRYLIKSKK 203
ASKHA_NBD_MamK cd24009
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ...
360-561 5.86e-06

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: 49.13  E-value: 5.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 360 IKGGAKEYYVGEDALK--LILNdgwiLRYPMINGNFNEYSY-DYESREEilgdlsnILGECLKQLGIENISRFKVMLLIP 436
Cdd:cd24009   38 RKLLGKEVLFGDEALEnrLALD----LRRPLEDGVIKEGDDrDLEAARE-------LLQHLIELALPGPDDEIYAVIGVP 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 437 DLYDKSYIETWVELLFKFigFGRVGILQEAVAATFGATASTAC-IVDVGAQTTKIsCVDEGMI-INDSRILLNYGGDNIT 514
Cdd:cd24009  107 ARASAENKQALLEIAREL--VDGVMVVSEPFAVAYGLDRLDNSlIVDIGAGTTDL-CRMKGTIpTEEDQITLPKAGDYID 183
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 240132127 515 ETFIKLILEdQFPYKDINLidsydwELAQELKEK--FITFQDADIAVQL 561
Cdd:cd24009  184 EELVDLIKE-RYPEVQLTL------NMARRWKEKygFVGDASEPVKVEL 225
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
365-549 9.70e-05

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: 45.63  E-value: 9.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 365 KEYYVGEDALKL--ILNdgwiLRYPMING---NFN--EYSYDYesreeILGDLSNIlgeclkqlgieNISRFKVMLLIPD 437
Cdd:cd10220   47 KDIMVGDEASELrsMLE----VTYPMENGivrNWDdmEHLWDY-----TFGEKLKI-----------DPRECKILLTEPP 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 438 LYDKSYIETWVELLFKFIGFGRVGILQEAVAATFGATASTACIVDVGAQTTKISCVDEGMIINDSRILLNYGGDNITETF 517
Cdd:cd10220  107 MNPTKNREKMVEVMFEKYGFAGVYVAIQAVLTLYAQGLLTGVVVDSGDGVTHIVPVYEGFSLPHLTRRLDVAGRDITRYL 186
                        170       180       190
                 ....*....|....*....|....*....|..
gi 240132127 518 IKLILEDQFPYKdinliDSYDWELAQELKEKF 549
Cdd:cd10220  187 IKLLLLRGYAFN-----RTADFETVREIKEKL 213
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
477-597 3.17e-04

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 43.95  E-value: 3.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 477 TACIVDVGAQTTKISCVDEGMIINDSRILLNYGGDNITEtFIKLIL---EDQFPYKDINlidsydwELAQELKEKFiTFQ 553
Cdd:PTZ00280 161 TGTVIDSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITN-FIQQMLrerGEPIPAEDIL-------LLAQRIKEKY-CYV 231
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 240132127 554 DADIAvQLYDFYKRNP---FKQ--------TAKYEFKVFDEVMLAPMGLFFPKIF 597
Cdd:PTZ00280 232 APDIA-KEFEKYDSDPknhFKKytavnsvtKKPYTVDVGYERFLGPEMFFHPEIF 285
ASKHA_NBD_ParM-like cd10227
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ...
342-522 3.27e-04

nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins 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: 466825 [Multi-domain]  Cd Length: 263  Bit Score: 43.28  E-value: 3.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 342 KREPEKIHDHNDPNKKEWIKGGAKEYYVGEDALKlilndgwilrypMINGNFNEYSYDYESREEILgdlsnILGECLKQL 421
Cdd:cd10227   27 AEARESSLDDGLLEDDIIVEYNGKRYLVGELALR------------EGGGGRSTGDDKKKSEDALL-----LLLAALALL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 422 GIENISRFKVMLLIPDLYDKSYIETWVELL------FKFIG------FGRVGILQEAVAATFGA-------TASTACIVD 482
Cdd:cd10227   90 GDDEEVDVNLVVGLPISEYKEEKKELKKKLlkglheFTFNGkerritINDVKVLPEGAGAYLDYlldddelEDGNVLVID 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 240132127 483 VGAQTTKISCVDEGMIINDSRILLNyGGDNITETFIKLIL 522
Cdd:cd10227  170 IGGGTTDILTFENGKPIEESSDTLP-GGEEALEKYADDIL 208
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
436-525 6.83e-04

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: 42.76  E-value: 6.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 436 PDLYDKSYIETWVELLF-KFigfgRVGIL---QEAVAATFGATASTACIVDVGAQTTKISCVDEGMIINDSRILLNYGGD 511
Cdd:cd10209   89 PLLTSKAERERLTQLMFeTF----NVSGLyasEQAVLSLYAVGRISGCVVDVGHGKIDIAPVWEGAIQHNAVRRFEIGGR 164
                         90
                 ....*....|....
gi 240132127 512 NITETFIKLILEDQ 525
Cdd:cd10209  165 DLTELLAAELGKSN 178
ASKHA_NBD_PilM-like cd24004
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ...
410-561 1.91e-03

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: 41.12  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 410 LSNILGECLKQLGIE-NISRFKVMLLIPDLYDkSYIETWVELlfkfiGFGRVGILQEAVAA-----TFGATASTACIVDV 483
Cdd:cd24004   48 VAESIKELLKELEEKlGSKLKDVVIAIAKVVE-SLLNVLEKA-----GLEPVGLTLEPFAAanlliPYDMRDLNIALVDI 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240132127 484 GAQTTKISCVDEGMIINDSRILLnyGGDNITETfikliledqfpykdinLIDSY--DWELAQELKEKFITFQDADIAVQL 561
Cdd:cd24004  122 GAGTTDIALIRNGGIEAYRMVPL--GGDDFTKA----------------IAEGFliSFEEAEKIKRTYGIFLLIEAKDQL 183
ASKHA_NBD_MreB-like cd10225
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ...
455-523 7.91e-03

nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and similar proteins; MreB proteins are bacterial actin homologs that may play a role in cell shape determination by positioning the cell wall synthetic machinery. MreB has also been implicated in chromosome segregation; specifically, MreB is thought to bind to and segregate the replication origin of bacterial chromosomes. The family includes three MreB isoforms, MreB (also called actin-like MreB protein or rod shape-determining protein MreB), Mbl (also called actin-like Mbl protein or rod shape-determining protein Mbl) and MreBH (also called actin-like MreBH protein or rod shape-determining protein MreBH), in cell morphogenesis of Bacillus subtilis. All isoforms can support rod-shaped cell growth normal conditions. They form membrane-associated dynamic filaments that are essential for cell shape determination. They act by regulating cell wall synthesis and cell elongation, and thus cell shape. The feedback loops between cell geometry and their localizations may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on their polymerization. They organize peptidoglycan synthesis in the lateral cell wall. MreB, Mbl and MreBH can form a complex. The MreB-like 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: 466824 [Multi-domain]  Cd Length: 317  Bit Score: 39.38  E-value: 7.91e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240132127 455 IGFGRVGILQEAVAATFGA----TASTAC-IVDVGAQTTKISCVDEGMIINdSRIlLNYGGDNITETFIKLILE 523
Cdd:cd10225  117 AGAREVYLIEEPMAAAIGAglpiEEPRGSmVVDIGGGTTEIAVISLGGIVT-SRS-VRVAGDEMDEAIINYVRR 188
 
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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