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Conserved domains on  [gi|215273934|sp|A5A3E0|]
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RecName: Full=POTE ankyrin domain family member F; AltName: Full=ANKRD26-like family C member 1B; AltName: Full=Chimeric POTE-actin protein

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
706-1070 0e+00

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: 865.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  706 AVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEKI 785
Cdd:cd10224     1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  786 WHHTFYNELRVAPEEHPVLLTEATLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYTSGRTTGIVMDSGDGVTHTVPI 865
Cdd:cd10224    81 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  866 YEGNALPHATLRLDLAGRELPDYLMKILTEHGYRFTTMAEREIVRDIKEKLCYVALDFEQEMATVASSSSLEKSYELPDG 945
Cdd:cd10224   161 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  946 QVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMM 1025
Cdd:cd10224   241 QVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTM 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 215273934 1026 KIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIV 1070
Cdd:cd10224   321 KIKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 365
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
138-368 1.23e-47

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 172.06  E-value: 1.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  138 EDLDKLHRAAWWGKVPRKDLIVMLRDTDVNKQDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQ 217
Cdd:COG0666    52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  218 EDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKAN 297
Cdd:COG0666   132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215273934  298 LNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYKEKQMLKI 368
Cdd:COG0666   212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
CCDC144C super family cl25942
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ...
648-701 3.98e-17

CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.


The actual alignment was detected with superfamily member pfam14915:

Pssm-ID: 464371 [Multi-domain]  Cd Length: 304  Bit Score: 83.50  E-value: 3.98e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 215273934   648 NSTLREEIAMLRLELDTMKHQSQLREKKYLEDIESVKKRNDNLLKALQLNELTM 701
Cdd:pfam14915    1 NCMLQDEIAMLRLEIDTIKNQNQEKEKKYLEDIEILKEKNDDLQKTLKLNEETL 54
 
Name Accession Description Interval E-value
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
706-1070 0e+00

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: 865.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  706 AVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEKI 785
Cdd:cd10224     1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  786 WHHTFYNELRVAPEEHPVLLTEATLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYTSGRTTGIVMDSGDGVTHTVPI 865
Cdd:cd10224    81 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  866 YEGNALPHATLRLDLAGRELPDYLMKILTEHGYRFTTMAEREIVRDIKEKLCYVALDFEQEMATVASSSSLEKSYELPDG 945
Cdd:cd10224   161 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  946 QVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMM 1025
Cdd:cd10224   241 QVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTM 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 215273934 1026 KIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIV 1070
Cdd:cd10224   321 KIKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 365
PTZ00281 PTZ00281
actin; Provisional
701-1075 0e+00

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 723.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  701 MDDDTAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWD 780
Cdd:PTZ00281    2 DGEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  781 DMEKIWHHTFYNELRVAPEEHPVLLTEATLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYTSGRTTGIVMDSGDGVT 860
Cdd:PTZ00281   82 DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  861 HTVPIYEGNALPHATLRLDLAGRELPDYLMKILTEHGYRFTTMAEREIVRDIKEKLCYVALDFEQEMATVASSSSLEKSY 940
Cdd:PTZ00281  162 HTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKSY 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  941 ELPDGQVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAAL 1020
Cdd:PTZ00281  242 ELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTAL 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 215273934 1021 APSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKCL 1075
Cdd:PTZ00281  322 APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKCF 376
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
705-1074 0e+00

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 615.42  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934    705 TAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMhQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEK 784
Cdd:smart00268    1 VPAIVIDNGSGTIKAGFAGEDFPQVVFPSIVGRPKDGKGMVGD-AKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEK 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934    785 IWHHTFYNELRVAPEEHPVLLTEATLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYTSGRTTGIVMDSGDGVTHTVP 864
Cdd:smart00268   80 IWDYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVP 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934    865 IYEGNALPHATLRLDLAGRELPDYLMKILTEHGYRFTTMAEREIVRDIKEKLCYVALDFEQEMATVAS---SSSLEKSYE 941
Cdd:smart00268  160 VVDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAREsseSSKLEKTYE 239
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934    942 LPDGQVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALA 1021
Cdd:smart00268  240 LPDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQLA 319
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|...
gi 215273934   1022 PSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKC 1074
Cdd:smart00268  320 PKKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKC 372
Actin pfam00022
Actin;
705-1074 0e+00

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 534.19  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934   705 TAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGmmgGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEK 784
Cdd:pfam00022    1 VSALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGTK---VEAANKYYVGDEALTYRPGMEVRSPVEDGIVVDWDAMEE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934   785 IWHHTFYNELRVAPEEHPVLLTEATLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYTSGRTTGIVMDSGDGVTHTVP 864
Cdd:pfam00022   78 IWEHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934   865 IYEGNALPHATLRLDLAGRELPDYLMKILTE------------------------------HGYRFTTMAEREIVRDIKE 914
Cdd:pfam00022  158 VHDGYVLQKAIRRSDLGGDFLTDYLRELLRSrnieitprylikskkpgdpapavtkrelpdTTYSYKTYQERRVLEEIKE 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934   915 KLCYVALDFeqEMATVASSSSLEKSYELPDGQVITIGNERFRCPEALFQPCFLGMES--------CGIHETTFNSIMKSD 986
Cdd:pfam00022  238 SVCYVSDDP--FGDETTSSSIPTRVYELPDGSTIILGAERFRVPEILFNPSLIGSESelpppqtaVGIPELIVDAINACD 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934   987 VDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMMKIRIIAPPK---RKYSVWVGGSILASLSTFQQMWISKQEYD 1063
Cdd:pfam00022  316 VDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGNtveRRYSAWIGGSILASLGTFQQMWVSKQEYE 395
                          410
                   ....*....|.
gi 215273934  1064 ESGPSIVHRKC 1074
Cdd:pfam00022  396 EHGASVVERKC 406
COG5277 COG5277
Actin-related protein [Cytoskeleton];
707-1065 6.70e-120

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 375.28  E-value: 6.70e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  707 VLVIDNGSGMCKAG-FAGDDAP-----RAVFPSIVGRPRQQGMMGGMhQKESYVGKEAQS-----KRGILTLKYPMEHGI 775
Cdd:COG5277    10 VIGIDFGTSYVKYGpIALEEKPrviqtRGLFLRIVGESKLLGPMEGL-SRGLVVGDEVSKylssvRDAIRNLKYPLRDGI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  776 IT-----NWDDMEKIWHHTFYNELRVAPEEHP--VLLTEATLNPKANREKMTQIMFETF---NTPAMYVAIQAVLSLYTS 845
Cdd:COG5277    89 VRrddedAWRVLKELLRYTFAQFLVVDPEFHGflVVVALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVAIAE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  846 GRTTGIVMDSGDGVTHTVPIYEGnALPHATLRLDLAGRELPDYLMKILTEHGYRFTTMAEReIVRDIKEKLCYVALDFEQ 925
Cdd:COG5277   169 KAVTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSDTAREEY-VVRVVKEALGLVPRDLAK 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  926 EM-ATVASSSSLEKSYELPDGQV-ITIGN---ERFRCPEALFQPCFLGMESC----------------------GIHETT 978
Cdd:COG5277   247 AIqKAASNPDSFEAKVRLPNPTVeIELGNyawERFLIGEILFNPNHEGFESYiqqgrlriedavigdvvlygemGLAEAI 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  979 FNSIMKSDVDIRKDLYTNTVLSGGTTMY---PGMA-------HRMQKEIAALAPSmMKIRIIAPPKRKYSVWVGGSILAS 1048
Cdd:COG5277   327 INSIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEdvavdsvTRVQIELSELAPE-LKVNVRLVSDPQYSVWKGAIIYGY 405
                         410
                  ....*....|....*....
gi 215273934 1049 LSTFQQMW--ISKQEYDES 1065
Cdd:COG5277   406 ALPFSVKWswITKEGWYFL 424
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
138-368 1.23e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 172.06  E-value: 1.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  138 EDLDKLHRAAWWGKVPRKDLIVMLRDTDVNKQDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQ 217
Cdd:COG0666    52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  218 EDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKAN 297
Cdd:COG0666   132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215273934  298 LNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYKEKQMLKI 368
Cdd:COG0666   212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
1003-1074 3.72e-34

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: 127.40  E-value: 3.72e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215273934 1003 TTMYPGMAHRMQKEIAALAPSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKC 1074
Cdd:NF040575   61 RVNESGFYEKLKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSIVHRKC 132
PHA03100 PHA03100
ankyrin repeat protein; Provisional
158-361 1.33e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 95.89  E-value: 1.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  158 IVMLrDTDVNKQDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTAL-----IKAVQCQEDECALMLLEHGTDP 232
Cdd:PHA03100   21 IIME-DDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  233 NIPDEYGNTTLHYAIYN--EDKLMAKALLLYGADIESKNKHGLTPL--LLGVHEQKQQVVKFLIKKKANLNALDR----- 303
Cdd:PHA03100  100 NAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLhlYLESNKIDLKILKLLIDKGVDINAKNRvnyll 179
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 215273934  304 -----------YGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYK 361
Cdd:PHA03100  180 sygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248
Ank_2 pfam12796
Ankyrin repeats (3 copies);
177-269 5.02e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.55  E-value: 5.02e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934   177 LHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEHGtDPNIPDeYGNTTLHYAIYNEDKLMAK 256
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 215273934   257 ALLLYGADIESKN 269
Cdd:pfam12796   79 LLLEKGADINVKD 91
CCDC144C pfam14915
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ...
648-701 3.98e-17

CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.


Pssm-ID: 464371 [Multi-domain]  Cd Length: 304  Bit Score: 83.50  E-value: 3.98e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 215273934   648 NSTLREEIAMLRLELDTMKHQSQLREKKYLEDIESVKKRNDNLLKALQLNELTM 701
Cdd:pfam14915    1 NCMLQDEIAMLRLEIDTIKNQNQEKEKKYLEDIEILKEKNDDLQKTLKLNEETL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
171-340 5.54e-09

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 60.03  E-value: 5.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  171 KQKRTA---LHLASANGNSEVVK-LLLDRRCqlnvlDNKKR-----TALIKAVQCQEDECALMLLEhgTDP---NIP--- 235
Cdd:cd22192    12 QQKRISespLLLAAKENDVQAIKkLLKCPSC-----DLFQRgalgeTALHVAALYDNLEAAVVLME--AAPelvNEPmts 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  236 DEY-GNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLtplllgvheqkqqvvkFLIKKKANLNaldRYGRTALILAVC 314
Cdd:cd22192    85 DLYqGETALHIAVVNQNLNLVRELIARGADVVSPRATGT----------------FFRPGPKNLI---YYGEHPLSFAAC 145
                         170       180
                  ....*....|....*....|....*.
gi 215273934  315 CGSASIVSLLLEQNIDVSSQDLSGQT 340
Cdd:cd22192   146 VGNEEIVRLLIEHGADIRAQDSLGNT 171
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
198-362 8.33e-09

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 59.71  E-value: 8.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934   198 QLNVLDNKKRTALIKAVQCQE-DECALMLLEHGTDPNIpdeyGNTTLHyAIYNEDKLMAKALLLYGADIESKNK------ 270
Cdd:TIGR00870   44 NINCPDRLGRSALFVAAIENEnLELTELLLNLSCRGAV----GDTLLH-AISLEYVDAVEAILLHLLAAFRKSGplelan 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934   271 --------HGLTPLLLGVHEQKQQVVKFLIKKKANLNA--------------LDRYGRTALILAVCCGSASIVSLLLEQN 328
Cdd:TIGR00870  119 dqytseftPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgvdSFYHGESPLNAAACLGSPSIVALLSEDP 198
                          170       180       190
                   ....*....|....*....|....*....|....
gi 215273934   329 IDVSSQDLSGQTAREYAVsshhhVICQLLSDYKE 362
Cdd:TIGR00870  199 ADILTADSLGNTLLHLLV-----MENEFKAEYEE 227
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
172-201 5.36e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 5.36e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 215273934    172 QKRTALHLASANGNSEVVKLLLDRRCQLNV 201
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
706-1070 0e+00

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: 865.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  706 AVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEKI 785
Cdd:cd10224     1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  786 WHHTFYNELRVAPEEHPVLLTEATLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYTSGRTTGIVMDSGDGVTHTVPI 865
Cdd:cd10224    81 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  866 YEGNALPHATLRLDLAGRELPDYLMKILTEHGYRFTTMAEREIVRDIKEKLCYVALDFEQEMATVASSSSLEKSYELPDG 945
Cdd:cd10224   161 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  946 QVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMM 1025
Cdd:cd10224   241 QVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTM 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 215273934 1026 KIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIV 1070
Cdd:cd10224   321 KIKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 365
ASKHA_NBD_actin_Arp-T1-3 cd13397
nucleotide-binding domain (NBD) of actin, actin-related proteins T1-T3 (Arp-T1-3), and similar ...
706-1066 0e+00

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


Pssm-ID: 466848 [Multi-domain]  Cd Length: 359  Bit Score: 735.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  706 AVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEKI 785
Cdd:cd13397     1 PAVVIDNGSGLIKAGFAGEDLPRAVFPSVVGRPKYKAVMLGAGQKEVYVGDEAQEKRGVLTLSYPIEHGIVTNWDDMEKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  786 WHHTFYNELRVAPEEHPVLLTEATLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYTSGRTTGIVMDSGDGVTHTVPI 865
Cdd:cd13397    81 WHHTFENELRVKPEEHPVLLTEAPLNPKQNREKMAEIMFETFGVPAFYVAIQAVLSLYSSGRTTGLVLDSGDGVTHTVPI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  866 YEGNALPHATLRLDLAGRELPDYLMKILTEHGYRFTTMAEREIVRDIKEKLCYVALDFEQEMAtvASSSSLEKSYELPDG 945
Cdd:cd13397   161 YEGYALPHAVQRLDLAGRDLTEYLMKLLKERGHSFTTTAEREIVRDIKEKLCYVALDYEEELK--KKSEELEKEYTLPDG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  946 QVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMM 1025
Cdd:cd13397   239 QVIKIGSERFRCPEALFRPSLIGREAPGIHKLVYNSIMKCDIDIRKDLYSNIVLSGGSTMFPGLPERLQKELEALAPSST 318
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 215273934 1026 KIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESG 1066
Cdd:cd13397   319 KVKVIAPPERKYSVWIGGSILASLSTFKSMWITRAEYDEFG 359
PTZ00281 PTZ00281
actin; Provisional
701-1075 0e+00

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 723.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  701 MDDDTAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWD 780
Cdd:PTZ00281    2 DGEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  781 DMEKIWHHTFYNELRVAPEEHPVLLTEATLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYTSGRTTGIVMDSGDGVT 860
Cdd:PTZ00281   82 DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  861 HTVPIYEGNALPHATLRLDLAGRELPDYLMKILTEHGYRFTTMAEREIVRDIKEKLCYVALDFEQEMATVASSSSLEKSY 940
Cdd:PTZ00281  162 HTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKSY 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  941 ELPDGQVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAAL 1020
Cdd:PTZ00281  242 ELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTAL 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 215273934 1021 APSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKCL 1075
Cdd:PTZ00281  322 APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKCF 376
PTZ00004 PTZ00004
actin-2; Provisional
701-1075 0e+00

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 664.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  701 MDDDTAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWD 780
Cdd:PTZ00004    2 SVEETNAAVVDNGSGMVKAGFAGDDAPRCVFPSIVGRPKNPGIMVGMEEKDCYVGDEAQDKRGILTLKYPIEHGIVTNWD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  781 DMEKIWHHTFYNELRVAPEEHPVLLTEATLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYTSGRTTGIVMDSGDGVT 860
Cdd:PTZ00004   82 DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  861 HTVPIYEGNALPHATLRLDLAGRELPDYLMKILTEHGYRFTTMAEREIVRDIKEKLCYVALDFEQEMATVASSSSL-EKS 939
Cdd:PTZ00004  162 HTVPIYEGYSLPHAIHRLDVAGRDLTEYMMKILHERGTTFTTTAEKEIVRDIKEKLCYIALDFDEEMGNSAGSSDKyEES 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  940 YELPDGQVITIGNERFRCPEALFQPCFLGMESC-GIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIA 1018
Cdd:PTZ00004  242 YELPDGTIITVGSERFRCPEALFQPSLIGKEEPpGIHELTFQSINKCDIDIRKDLYGNIVLSGGTTMYRGLPERLTKELT 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 215273934 1019 ALAPSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKCL 1075
Cdd:PTZ00004  322 TLAPSTMKIKVVAPPERKYSVWIGGSILSSLPTFQQMWVTKEEYDESGPSIVHRKCF 378
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
705-1074 0e+00

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 615.42  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934    705 TAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMhQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEK 784
Cdd:smart00268    1 VPAIVIDNGSGTIKAGFAGEDFPQVVFPSIVGRPKDGKGMVGD-AKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEK 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934    785 IWHHTFYNELRVAPEEHPVLLTEATLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYTSGRTTGIVMDSGDGVTHTVP 864
Cdd:smart00268   80 IWDYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVP 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934    865 IYEGNALPHATLRLDLAGRELPDYLMKILTEHGYRFTTMAEREIVRDIKEKLCYVALDFEQEMATVAS---SSSLEKSYE 941
Cdd:smart00268  160 VVDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAREsseSSKLEKTYE 239
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934    942 LPDGQVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALA 1021
Cdd:smart00268  240 LPDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQLA 319
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|...
gi 215273934   1022 PSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKC 1074
Cdd:smart00268  320 PKKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKC 372
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
708-1074 0e+00

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


Pssm-ID: 466820 [Multi-domain]  Cd Length: 370  Bit Score: 595.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  708 LVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEKIWH 787
Cdd:cd10216     4 VVIDNGSGVIKAGFAGDDIPKVVFPSYVGRPKHVRVMAGALEGDVFVGPKAEEHRGLLKIRYPMEHGIVTDWNDMERIWQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  788 HTFYNE-LRVAPEEHPVLLTEATLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYTSGRTTGIVMDSGDGVTHTVPIY 866
Cdd:cd10216    84 YVYSKLqLNTFSEEHPVLLTEAPLNPRKNREKAAEVFFETFNVPALFVSMQAVLSLYASGRTTGVVLDSGDGVTHAVPIY 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  867 EGNALPHATLRLDLAGRELPDYLMKILTEHGYRFTTMAEREIVRDIKEKLCYVALDFeQEMATVASSSSLEKSYELPDGQ 946
Cdd:cd10216   164 EGFALPHSIRRVDIAGRDVTEYLQLLLRKSGYNFHTSAEFEIVREIKEKACYVALNP-QKEEKLEEEKTEKAQYTLPDGS 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  947 VITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMMK 1026
Cdd:cd10216   243 TIEIGPERFRAPEILFNPELIGLEYPGVHEVLVDSIQKSDLDLRKTLYSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVK 322
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 215273934 1027 IRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKC 1074
Cdd:cd10216   323 IRISAPPERLYSTWIGGSILASLSTFKKMWVSKKEYEEDGARILHRKT 370
Actin pfam00022
Actin;
705-1074 0e+00

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 534.19  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934   705 TAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGmmgGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEK 784
Cdd:pfam00022    1 VSALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGTK---VEAANKYYVGDEALTYRPGMEVRSPVEDGIVVDWDAMEE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934   785 IWHHTFYNELRVAPEEHPVLLTEATLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYTSGRTTGIVMDSGDGVTHTVP 864
Cdd:pfam00022   78 IWEHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934   865 IYEGNALPHATLRLDLAGRELPDYLMKILTE------------------------------HGYRFTTMAEREIVRDIKE 914
Cdd:pfam00022  158 VHDGYVLQKAIRRSDLGGDFLTDYLRELLRSrnieitprylikskkpgdpapavtkrelpdTTYSYKTYQERRVLEEIKE 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934   915 KLCYVALDFeqEMATVASSSSLEKSYELPDGQVITIGNERFRCPEALFQPCFLGMES--------CGIHETTFNSIMKSD 986
Cdd:pfam00022  238 SVCYVSDDP--FGDETTSSSIPTRVYELPDGSTIILGAERFRVPEILFNPSLIGSESelpppqtaVGIPELIVDAINACD 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934   987 VDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMMKIRIIAPPK---RKYSVWVGGSILASLSTFQQMWISKQEYD 1063
Cdd:pfam00022  316 VDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGNtveRRYSAWIGGSILASLGTFQQMWVSKQEYE 395
                          410
                   ....*....|.
gi 215273934  1064 ESGPSIVHRKC 1074
Cdd:pfam00022  396 EHGASVVERKC 406
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
707-1070 1.11e-170

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: 505.56  E-value: 1.11e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  707 VLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRP--RQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEK 784
Cdd:cd10220     2 VVVCDNGTGFVKCGFAGSNFPEHVFPSLVGRPilRAEEKVGDIEIKDIMVGDEASELRSMLEVTYPMENGIVRNWDDMEH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  785 IWHHTFYNELRVAPEEHPVLLTEATLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYTSGRTTGIVMDSGDGVTHTVP 864
Cdd:cd10220    82 LWDYTFGEKLKIDPRECKILLTEPPMNPTKNREKMVEVMFEKYGFAGVYVAIQAVLTLYAQGLLTGVVVDSGDGVTHIVP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  865 IYEGNALPHATLRLDLAGRELPDYLMKILTEHGYRFTTMAEREIVRDIKEKLCYVALDFEQEMATVASSSSLEKSYELPD 944
Cdd:cd10220   162 VYEGFSLPHLTRRLDVAGRDITRYLIKLLLLRGYAFNRTADFETVREIKEKLCYVAYDIELEQKLALETTVLVESYTLPD 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  945 GQVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAAL---- 1020
Cdd:cd10220   242 GRVIKVGGERFEAPEALFQPHLIDVEGPGIAELLFNTIQAADIDTRPELYKHIVLSGGSTMYPGLPSRLEKEIKQLyler 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 215273934 1021 -------APSMMKIRIIAPPKRKYSVWVGGSILASLSTFQ-QMWISKQEYDESGPSIV 1070
Cdd:cd10220   322 vlkgdteRLSKFKIRIEDPPRRKHMVFLGGAVLADIMKDKdEFWITRQEYEEQGVRVL 379
PTZ00452 PTZ00452
actin; Provisional
701-1075 5.75e-157

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 470.01  E-value: 5.75e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  701 MDDDTAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWD 780
Cdd:PTZ00452    1 MQAQYPAVVIDNGSGYCKIGIAGDDAPTSCFPAIVGRSKQNDGIFSTFNKEYYVGEEAQAKRGVLAIKEPIQNGIINSWD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  781 DMEKIWHHTFYNELRVAPEEHPVLLTEATLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYTSGRTTGIVMDSGDGVT 860
Cdd:PTZ00452   81 DIEIIWHHAFYNELCMSPEDQPVFMTDAPMNSKFNRERMTQIMFETFNTPCLYISNEAVLSLYTSGKTIGLVVDSGEGVT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  861 HTVPIYEGNALPHATLRLDLAGRELPDYLMKILTEHGYRFTTMAEREIVRDIKEKLCYVALDFEQEMATVASSSSLEKSY 940
Cdd:PTZ00452  161 HCVPVFEGHQIPQAITKINLAGRLCTDYLTQILQELGYSLTEPHQRIIVKNIKERLCYTALDPQDEKRIYKESNSQDSPY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  941 ELPDGQVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAAL 1020
Cdd:PTZ00452  241 KLPDGNILTIKSQKFRCSEILFQPKLIGLEVAGIHHLAYSSIKKCDLDLRQELCRNIVLSGGTTLFPGIANRLSNELTNL 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 215273934 1021 APSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKCL 1075
Cdd:PTZ00452  321 VPSQLKIQVAAPPDRRFSAWIGGSIQCTLSTQQPQWIKRQEYDEQGPSIVHRKCF 375
PTZ00466 PTZ00466
actin-like protein; Provisional
708-1075 1.97e-156

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 469.04  E-value: 1.97e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  708 LVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEKIWH 787
Cdd:PTZ00466   15 IIIDNGTGYIKAGFAGEDVPNLVFPSYVGRPKYKRVMAGAVEGNIFVGNKAEEYRGLLKVTYPINHGIIENWNDMENIWI 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  788 HTfYNELRVAPEEHPVLLTEATLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYTSGRTTGIVMDSGDGVTHTVPIYE 867
Cdd:PTZ00466   95 HV-YNSMKINSEEHPVLLTEAPLNPQKNKEKIAEVFFETFNVPALFISIQAILSLYSCGKTNGTVLDCGDGVCHCVSIYE 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  868 GNALPHATLRLDLAGRELPDYLMKILTEHGYRFTTMAEREIVRDIKEKLCYVALDFEQEMATvASSSSLEKSYELPDGQV 947
Cdd:PTZ00466  174 GYSITNTITRTDVAGRDITTYLGYLLRKNGHLFNTSAEMEVVKNMKENCCYVSFNMNKEKNS-SEKALTTLPYILPDGSQ 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  948 ITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMMKI 1027
Cdd:PTZ00466  253 ILIGSERYRAPEVLFNPSILGLEYLGLSELIVTSITRADMDLRRTLYSHIVLSGGTTMFHGFGDRLLNEIRKFAPKDITI 332
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 215273934 1028 RIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKCL 1075
Cdd:PTZ00466  333 RISAPPERKFSTFIGGSILASLATFKKIWISKQEFDEYGSVILHRKTF 380
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
705-1074 7.28e-156

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: 466.90  E-value: 7.28e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  705 TAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEK 784
Cdd:cd10214     3 TKAVIIDLGTGYCKAGFAGQPRPSYVISSTVGKPPQESAKTGDNRKETFVGKELANVEPPLKLVNPLRHGIVVDWDCVQD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  785 IWHHTFYNELRVAPEEHPVLLTEATLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYTSGRTTGIVMDSGDGVTHTVP 864
Cdd:cd10214    83 IWEYIFEKEMKILPEEHAVLVSDPPLSPTTNREKYAELMFETFSIPAMHIAYQSRLSLYSYGRTSGLVVESGHGVSYVVP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  865 IYEGNALPHATLRLDLAGRELPDYLMKILTEHGYRFTTmAEREIVRDIKEKLCYVALDFEQEMATVASSSSLEksYELPD 944
Cdd:cd10214   163 IHEGYNLPHITGRADYAGSDLTAYLMKLLNEAGNKFTD-DQLHIVEDIKKKCCYVALDFEEEMGLPPQEYTVD--YELPD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  945 GQVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSM 1024
Cdd:cd10214   240 GHLITIGKERFRCPEMLFNPSLIGSKQPGLHTLTMNSLNKCDANLKKDLAKNILLCGGSTMFDGFPDRFQKELSKLCPND 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 215273934 1025 MKIrIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKC 1074
Cdd:cd10214   320 NPI-VAASPERKYSVWTGGSILASLKSFQQLWVRRREYEERGPFVIYRKC 368
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
708-1066 7.73e-143

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: 428.45  E-value: 7.73e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  708 LVIDNGSGMCKAGFAGDDAPRAVFPsivgrprqqgmmggmhqkesyvgkeaqskrgiltlkypmehgiitnWDDMEKIWH 787
Cdd:cd10169     1 IVIDNGSGTIKAGFAGEDAPRLIFP----------------------------------------------WDDMEKIWE 34
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  788 HTFYNELRVAPEEHPVLLTEATLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYTSGRTTGIVMDSGDGVTHTVPIYE 867
Cdd:cd10169    35 HVFYNLLRVDPEEHPVLLTEPPLNPKANREKLAEILFETFNVPSLYIANQAVLSLYASGRTTGLVVDSGEGVTHIVPVYE 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  868 GNALPHATLRLDLAGRELPDYLMKILTEHGYRFTTMAEREIVRDIKEKLcyvaldfeqematvassssleksyelpdgqv 947
Cdd:cd10169   115 GYVLPHAVRRLDIGGRDLTDYLAKLLREKGYSFSTSAEREIVRDIKEKL------------------------------- 163
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  948 itignerfrcpealfqpcflgmesCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMMKI 1027
Cdd:cd10169   164 ------------------------CGLHELIYDSIMKCDIDLRKELYSNIVLSGGTTLFPGFAERLQKELSKLAPSSVKV 219
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 215273934 1028 RIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESG 1066
Cdd:cd10169   220 KVIAPPERKYSAWIGGSILASLSTFQQMWITKEEYEEHG 258
ASKHA_NBD_Arp4_ACTL6-like cd13395
nucleotide-binding domain (NBD) of the actin-related protein 4 (Arp4)-like subfamily; The ...
703-1066 1.90e-134

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: 412.73  E-value: 1.90e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  703 DDTAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRP--RQQGMMGGMHQKES----YVGKEA-QSKRGILTLKYPMEHGI 775
Cdd:cd13395     2 DEVGALVLDIGSYSTRAGYAGEDTPKAVFPSVVGVVtdDDDAEDYVGGSGEKkrkyYIGTNSiGVPRPNMEVISPLKDGL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  776 ITNWDDMEKIWHHTFYNELRVAPEEHPVLLTEATLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYTSGRTTGIVMDS 855
Cdd:cd13395    82 IEDWDAFEKLWDHALKNRLRVDPSEHPLLLTEPSWNTRANREKLTELMFEKYNVPAFFLAKNAVLSAFANGRSTALVVDS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  856 GDGVTHTVPIYEGNALPHATLRLDLAGRELPDYLMKILTEHG------YRF---------------------TT-----M 903
Cdd:cd13395   162 GATSTSVVPVHDGYVLQKAIVRSPLGGDFLTDQLLKLLESKNieiiprYMIkskepveggapakytkkdlpnTTssyhrY 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  904 AEREIVRDIKEKLCYVALDFEQEmatVASSSSLEKSYELPDGQVITIGNERFRCPEALFQPCFL---------GMESCGI 974
Cdd:cd13395   242 MVRRVLQDFKESVCQVSDSPFDE---SEAASIPTVSYELPDGYNIEFGAERFKIPELLFDPSLVkgipappseGNELLGL 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  975 HETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMMKIRIIAPPK---RKYSVWVGGSILASLST 1051
Cdd:cd13395   319 PQLVYTSIGSCDVDIRPELYGNVVLTGGNSLLPGFTDRLNRELSEKAPGSLKLKILASGNtveRRFSSWIGGSILASLGS 398
                         410
                  ....*....|....*
gi 215273934 1052 FQQMWISKQEYDESG 1066
Cdd:cd13395   399 FQQMWISKQEYEEHG 413
COG5277 COG5277
Actin-related protein [Cytoskeleton];
707-1065 6.70e-120

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 375.28  E-value: 6.70e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  707 VLVIDNGSGMCKAG-FAGDDAP-----RAVFPSIVGRPRQQGMMGGMhQKESYVGKEAQS-----KRGILTLKYPMEHGI 775
Cdd:COG5277    10 VIGIDFGTSYVKYGpIALEEKPrviqtRGLFLRIVGESKLLGPMEGL-SRGLVVGDEVSKylssvRDAIRNLKYPLRDGI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  776 IT-----NWDDMEKIWHHTFYNELRVAPEEHP--VLLTEATLNPKANREKMTQIMFETF---NTPAMYVAIQAVLSLYTS 845
Cdd:COG5277    89 VRrddedAWRVLKELLRYTFAQFLVVDPEFHGflVVVALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVAIAE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  846 GRTTGIVMDSGDGVTHTVPIYEGnALPHATLRLDLAGRELPDYLMKILTEHGYRFTTMAEReIVRDIKEKLCYVALDFEQ 925
Cdd:COG5277   169 KAVTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSDTAREEY-VVRVVKEALGLVPRDLAK 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  926 EM-ATVASSSSLEKSYELPDGQV-ITIGN---ERFRCPEALFQPCFLGMESC----------------------GIHETT 978
Cdd:COG5277   247 AIqKAASNPDSFEAKVRLPNPTVeIELGNyawERFLIGEILFNPNHEGFESYiqqgrlriedavigdvvlygemGLAEAI 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  979 FNSIMKSDVDIRKDLYTNTVLSGGTTMY---PGMA-------HRMQKEIAALAPSmMKIRIIAPPKRKYSVWVGGSILAS 1048
Cdd:COG5277   327 INSIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEdvavdsvTRVQIELSELAPE-LKVNVRLVSDPQYSVWKGAIIYGY 405
                         410
                  ....*....|....*....
gi 215273934 1049 LSTFQQMW--ISKQEYDES 1065
Cdd:COG5277   406 ALPFSVKWswITKEGWYFL 424
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
707-1072 1.52e-103

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 331.31  E-value: 1.52e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  707 VLVIDNGSGMCKAGFAGDDAPRAVFPSIVG-RPRQQGMMG--GMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDME 783
Cdd:PTZ00280    6 VVVIDNGTGYTKMGYAGNTEPTYIIPTLIAdNSKQSRRRSkkGFEDLDFYIGDEALAASKSYTLTYPMKHGIVEDWDLME 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  784 KIWHHTFYNELRVAPEEHPVLLTEATLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYTS----------GRTTGIVM 853
Cdd:PTZ00280   86 KFWEQCIFKYLRCEPEEHYFILTEPPMNPPENREYTAEIMFETFNVKGLYIAVQAVLALRASwtskkakelgGTLTGTVI 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  854 DSGDGVTHTVPIYEGNALPHATLRLDLAGRELPDYLMKILTEHGYRFTTMAEREIVRDIKEKLCYVALDFEQEMATV--- 930
Cdd:PTZ00280  166 DSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGEPIPAEDILLLAQRIKEKYCYVAPDIAKEFEKYdsd 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  931 ---------ASSSSLEKSYElpdgqvITIGNERFRCPEALFQPCFLGME-SCGIHETTFNSIMKSDVDIRKDLYTNTVLS 1000
Cdd:PTZ00280  246 pknhfkkytAVNSVTKKPYT------VDVGYERFLGPEMFFHPEIFSSEwTTPLPEVVDDAIQSCPIDCRRPLYKNIVLS 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934 1001 GGTTMYPGMAHRMQKEI----------------AALAPSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDE 1064
Cdd:PTZ00280  320 GGSTMFKGFDKRLQRDVrkrvdrrlkkaeelsgGKLKPIPIDVNVVSHPRQRYAVWYGGSMLASSPEFEKVCHTKAEYDE 399

                  ....*...
gi 215273934 1065 SGPSIVHR 1072
Cdd:PTZ00280  400 YGPSICRY 407
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
707-1070 4.04e-103

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


Pssm-ID: 466822  Cd Length: 404  Bit Score: 329.91  E-value: 4.04e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  707 VLVIDNGSGMCKAGFAGDDAPRAVFPSIVGrPRQQGMMGGMHQKES--------YVGKEAQSKRGILTLKYPMEHGIITN 778
Cdd:cd10221     1 AVVIDNGTGYTKMGYAGNTEPQFIIPTVIA-IKESAKVGDGQRRSKkgiedldfYIGDEALANSPTYALKYPIRHGIVED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  779 WDDMEKIWHHTFYNELRVAPEEHPVLLTEATLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYTSGRT--------TG 850
Cdd:cd10221    80 WDLMERFWEQCIFKYLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALAASWTSrkvgertlTG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  851 IVMDSGDGVTHTVPIYEGNALPHATLRLDLAGRELPDYLMKILTEHGyrFTTMAE--REIVRDIKEKLCYVALDFEQEMA 928
Cdd:cd10221   160 TVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLRERE--EGIPPEdsLEVAKRIKERYCYVCPDIVKEFA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  929 TVASS-SSLEKSYELPD---GQ--VITIGNERFRCPEALFQPCFLGMESC-GIHETTFNSIMKSDVDIRKDLYTNTVLSG 1001
Cdd:cd10221   238 KYDSDpAKYIKQYTGINsvtGKpyTVDVGYERFLAPEIFFNPEIASSDFTtPLPEVVDQVIQSCPIDTRRGLYKNIVLSG 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934 1002 GTTMYPGMAHRMQKEI----------------AALAPSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDES 1065
Cdd:cd10221   318 GSTMFKDFGRRLQRDVkrivdarlkaseelsgGKLKPKPIDVNVISHPMQRYAVWFGGSMLASTPEFYTVCHTKAEYEEY 397

                  ....*
gi 215273934 1066 GPSIV 1070
Cdd:cd10221   398 GPSIC 402
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
707-1066 1.32e-85

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: 282.13  E-value: 1.32e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  707 VLVIDNGSGMCKAGFAGDDAPRaVFPSIVGRPRqqgmmggmHQKESYVGKEAQSK---RGILTLKYPMEHGIITNWDDME 783
Cdd:cd10210     1 TLVLDNGAYTIKAGFASDDPPR-VIPNCIAKPK--------SERRRLFGDDQLDEckdLSGLFYRRPFERGYLVNWDLQR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  784 KIWHHTFYNE-LRVAPEEHPVLLTEATLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLY----------TSGRTTGIV 852
Cdd:cd10210    72 QIWDHLFGKLlLNVDPSDTALVLTEPPFNPPSIQEAMDEIVFEEYGFQSLYRTTAAALSAFayladseqssSSSSQCCLV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  853 MDSGDGVTHTVPIYEGNALPHATLRLDLAGRELPDYLMKILTehgYR-FTTMAEREIVRDIKEKLCYVALDFEQEMATVA 931
Cdd:cd10210   152 VDSGFSFTHIVPFFDGKPVKRAVRRIDVGGKLLTNYLKEIIS---YRqLNVMDETYLVNQIKEDLCFVSTDFYEDLEIAK 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  932 S---SSSLEKSYELPDG-----------------------QVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKS 985
Cdd:cd10210   229 KkgkENTIRRDYVLPDYttskrgyvrdpeepnrgklkedeQVLRLNNERFTVPELLFHPSDIGIQQAGIAEAIVQSINAC 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  986 DVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDES 1065
Cdd:cd10210   309 PEELQPLLYANIVLTGGNALFPGFRERLEAELRSLAPDDYDVNVTLPEDPITYAWEGGSLLAQSPEFEELAVTRAEYEEH 388

                  .
gi 215273934 1066 G 1066
Cdd:cd10210   389 G 389
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
708-1071 4.83e-76

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: 254.62  E-value: 4.83e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  708 LVIDNGSGMCKAGFAGDDApravFPSIVGRPRQQGMM-GGMHQKESYVGKEAQskrgiltlkyPMEHGIITNWDDMEKIW 786
Cdd:cd10209     1 VVIDAGSRLLKAGYAYPDR----EPSVVEPTRVTPAVeDGEESDTVVEGNTVS----------PIRRGRIEDWDALEALL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  787 HHTFYNELR-VAPEEHPVLLTEATLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYTSGRTTGIVMDSGDGVTHTVPI 865
Cdd:cd10209    67 RYVFYTGLGwEEGNEGQVLIAEPLLTSKAERERLTQLMFETFNVSGLYASEQAVLSLYAVGRISGCVVDVGHGKIDIAPV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  866 YEGNALPHATLRLDLAGRELPDYLMKILTEHGyRFTTmAEREIVRDIKEKLCYVAldfEQEMATVASSSSLEK-SYELPD 944
Cdd:cd10209   147 WEGAIQHNAVRRFEIGGRDLTELLAAELGKSN-PKVK-LDRSIVERLKEAVAWSA---DDEEAYEKKVLTCSPeTYTLPD 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  945 GQVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSM 1024
Cdd:cd10209   222 GRVISVGKERYCVGEALFRPSILGIEEYGIVEQLVRAVSTSPSENRRQLLENIVLCGGTSSVPGLEARLQKEIRLLSSPS 301
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 215273934 1025 MKIRIIAPPK------RKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVH 1071
Cdd:cd10209   302 SRPALVKPPEympentLRYSAWIGGAILAKVVFPQNQHVTKADYDETGPSVVH 354
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
707-1067 5.00e-65

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: 223.60  E-value: 5.00e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  707 VLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMHQKESYVGKEAQSKrgiLTLKYPMEHGIITNWDDMEKIW 786
Cdd:cd10211     1 PIVIDNGSYQCRAGWAGDKEPRLVFRNLVAKPRDRKKGITVTLVGNDILNDEAVR---SHLRSPFDRNVVTNFDLQEQIL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  787 HHTFyNELRVAPE---EHPVLLTEATLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLY----TSGRTTGIVMDSGDGV 859
Cdd:cd10211    78 DYIF-SHLGINSEgsvDHPIVLTEALCNPNYSRQLMSELLFECYGVPSVAYGIDSLFSYYhnqpQGDPSDGLVISSGYST 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  860 THTVPIYEGNALPHATLRLDLAGRELPDYLMKILT----EHGYRFTTmaEReiVRDIKEKLCYVALDFEQEMATVASSSS 935
Cdd:cd10211   157 THVIPVLNGRLDLSQCKRINLGGFHATDYLQRLLQlkypTHPSAITL--SR--AEELVHEHCYVAEDYDEELKKWEDPEY 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  936 LEKSyelpdgqvitigNERFRCPealFqpcflgmescGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQK 1015
Cdd:cd10211   233 YEEN------------VRKIQLP---F----------GLVETIEFVLKRYPAEQQDRLVQNVFLTGGNALFPGLKERLEK 287
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 215273934 1016 EIAALAPSMMKIRII--APPkrKYSVWVGGSILASLSTFQQMWISKQEYDESGP 1067
Cdd:cd10211   288 ELRAIRPFGSPFNVVraKDP--VLDAWRGAAKWALDSTFEKVWITKQEYEEKGG 339
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
707-1073 7.37e-49

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: 177.88  E-value: 7.37e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  707 VLVIDNGSGMCKAGFAGDDA---PRAVFPSIVGRPrqqgmmggmhqkesyvgkeaqskrgiltlkYPMEHGIITNWDDME 783
Cdd:cd10208     2 ILVIDPGSQTTRAGLGLGELltpPTIEIPTRVEII------------------------------WPIQDGRVVDWDALE 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  784 KIWHHTFYNEL--RVAPEEHPVLLTEATLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYTSGRTTGIVMDSGDGVTH 861
Cdd:cd10208    52 ALWRHILFSLLsiPRPTNNSPVLLSVPPSWSKSDLELLTQLFFERLNVPAFAILEAPLAALYAAGATSGIVVDIGHEKTD 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  862 TVPIYEGNALPHATLRLDLAGRELPDYLMKILT--EHGYRFTTMAEREIVRDIKEKLcyvaldFEQEMATVASSSSleks 939
Cdd:cd10208   132 ITPIVDSQVVPHALVSIPIGGQDCTAHLAQLLKsdEPELKSQAESGEEATLDLAEAL------KKSPICEVLSDGA---- 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  940 yELPDGQVITIGNERFRCPEALFQP----CFLGMESCGIHETTFNSimkSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQK 1015
Cdd:cd10208   202 -DLASGTEITVGKERFRACEPLFKPsslrVDLLIAAIAGALVLNAS---DEPDKRPALWENIIIVGGGSRIRGLKEALLS 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934 1016 EIAA--LAPSM----MKIRIIAPPK--------RK----YSVWVGGSILASLsTF----QQMWISKQEYDESGPSIVHRK 1073
Cdd:cd10208   278 ELQQfhLISETsaspQQPRIIRLAKipdyfpewKKsgyeEAAFLGASIVAKL-VFndpsSKHYISKVDYNEKGPAAIHTK 356
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
138-368 1.23e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 172.06  E-value: 1.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  138 EDLDKLHRAAWWGKVPRKDLIVMLRDTDVNKQDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQ 217
Cdd:COG0666    52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  218 EDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKAN 297
Cdd:COG0666   132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215273934  298 LNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYKEKQMLKI 368
Cdd:COG0666   212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
139-386 3.95e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 170.52  E-value: 3.95e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  139 DLDKLHRAAWWGKVPRKDLIVMLRDTDVNKQDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQE 218
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  219 DECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANL 298
Cdd:COG0666   100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  299 NALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYKEKQMLKISSENSNPEQD 378
Cdd:COG0666   180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259

                  ....*...
gi 215273934  379 LKLTSEEE 386
Cdd:COG0666   260 AAAGAALI 267
ASKHA_NBD_Arp10 cd10207
nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; ...
709-1066 9.45e-44

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: 163.58  E-value: 9.45e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  709 VIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQgmmggmhqKESYVGKeaqsKRGILTLKypmehgiitnWDDM-EKIWH 787
Cdd:cd10207     2 VLDIGSAYTKCGFAGESAPRCIIPSEVKLPGGK--------KVIRVVD----QRSGNEEE----------LYEAlKEFLH 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  788 HTFYNELRVAPEEHPVLLTEATLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYTSGRTTGIVMDSGDGVTHTVPIYE 867
Cdd:cd10207    60 ELYFKHLLVNPKDRRVVVVESVLCPTPFRETLAKVLFKHFEVPSVLFAPSHLLSLLTLGIRTALVVDCGYRETRVLPVYE 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  868 GNALPHATLRLDLAGRELPDYLMKILTEHGYRFTTMAER------------EIVRDIKEKLCYVA-LDFEQEMATVASSS 934
Cdd:cd10207   140 GVPLLSAWQSTPLGGKALHKRLKKLLLEHATVVTGDNKGqllssvdsllseEVLEDIKVRACFVTsLERGKTLQSATEEG 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  935 SLEKS-------YELPDGQVITIGNERFRCPEALFqpcFLGMESC-GIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMY 1006
Cdd:cd10207   220 STEEPsppppvdYPLDGEKILIVPGSIRESAEELL---FEGDNEEkSLPTLILDSLLKCPIDVRKQLAENIVVIGGTSML 296
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215273934 1007 PGMAHRMQKEIAAL--------APSMMKIRIIAPP---KRKYSVWVGGSILASLSTFQQMWISKQEYDESG 1066
Cdd:cd10207   297 PGFKHRLLEELRALlrkpkyfeELAPKTFRFHTPPsvfKPNYLAWLGGSIFGALESILGRSLSREAYLQTG 367
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
143-341 6.36e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.50  E-value: 6.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  143 LHRAAWWGkvpRKDLIVML--RDTDVNKQDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDE 220
Cdd:COG0666    91 LHAAARNG---DLEIVKLLleAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLE 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  221 CALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNA 300
Cdd:COG0666   168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 215273934  301 LDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTA 341
Cdd:COG0666   248 KDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ASKHA_NBD_AtArp8-like cd13396
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ...
789-1066 1.12e-41

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: 156.17  E-value: 1.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  789 TFYNELRVAPEEHPVLLTEA------TLNPKANREKMTQIMFETF---NTPAMYVAIQAVLSLYTSGRTTGIVMDSGDGV 859
Cdd:cd13396    47 TIMTRMQVKPSRQPVVVSLPlchsddTESAAASRRQLRGTIFNVLfdmNVPAVCAVDQAVLALYAANRTSGIVVNIGFRV 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  860 THTVPIYEGNALPH-ATLRLDLAGRELPDYLMKILTEHGYRFTTMAereIVRDIKEKLCYVALDFEQEMAtvassSSLEK 938
Cdd:cd13396   127 TTIVPVYRGRVMHDiGVEVVGQGALRLTGFLKELMQQNGIRFPSLY---TVRTIKEKLCYVAEDYEAELA-----KDTQA 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  939 SYELPDGQVITIGNERFRCPEALFQPCFLGMESCGIH-------ETTFNSIMKSDvdirKDLYTNTVLSGGTTMYPGMAH 1011
Cdd:cd13396   199 SCEVAGEGWFTLSNERFKTGEILFQPGLGGMRAMGLHqavalcmDHCALVHSQGD----DGWFKTIVLSGGSACLPGLSE 274
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 215273934 1012 RMQKEIAALAPSMMK--IRIIAPPKRKYSVWVGGSILASLSTFQQMW-ISKQEYDESG 1066
Cdd:cd13396   275 RLERELRKLLPKSLSegIRIIPPPLGPDSAWQGAKLISNLSNFPDGWcITKKQFRNKP 332
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
157-357 6.71e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.16  E-value: 6.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  157 LIVMLRDTDVNKQDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEHGTDPNIPD 236
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  237 EYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCG 316
Cdd:COG0666    85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 215273934  317 SASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLL 357
Cdd:COG0666   165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
1003-1074 3.72e-34

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: 127.40  E-value: 3.72e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215273934 1003 TTMYPGMAHRMQKEIAALAPSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKC 1074
Cdd:NF040575   61 RVNESGFYEKLKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSIVHRKC 132
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
143-309 2.78e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.46  E-value: 2.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  143 LHRAAWWGKVprkDLIVML--RDTDVNKQDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDE 220
Cdd:COG0666   124 LHLAAYNGNL---EIVKLLleAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  221 CALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNA 300
Cdd:COG0666   201 IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280

                  ....*....
gi 215273934  301 LDRYGRTAL 309
Cdd:COG0666   281 ALLDLLTLL 289
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
748-1069 3.08e-25

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: 110.41  E-value: 3.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  748 HQKESYVGKEAQ--SKRGILTLKYPMEHGIItNW-----------DDMEKIWHHTFYNELRVAPEEHP----VLLTEATL 810
Cdd:cd10206   118 DYPDFLVGEEALrlPPSEEYNLHWPIRRGRL-NVhsdggsltavlDDLEDIWSHALEEKLEIPRKDLKnyraVLVIPDLF 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  811 NpKANREKMTQIMFETFNTPAMYVAIQAVLSLYTSGRTTGIVMDSGDGVTHTVPIYEGNALPHATLRLDLAGRELPDYLM 890
Cdd:cd10206   197 D-RRHVKELVDLLLRRLGFSSVFVHQESVCATFGAGLSSACVVDIGAQKTSVACVEDGLSIPNSRIRLPYGGDDITRCFL 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  891 KILTEHG--YRFTTMAER---EIVRDIKEKLCYvaldFEQEMATVASSSSLEKSyelPDGqvitignerfrcPEALFQpc 965
Cdd:cd10206   276 WLLRRSGfpYRECNLNSPldfLLLERLKETYCT----LDQDDIGVQLHEFYVRE---PGQ------------PTLKYQ-- 334
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  966 flgMESCGIHETTFNSI-MKSDVDIRKDLYTNTVLSGGTTMYPGMA----HRMQKEIAALAPSMMKIRIIAPPKRK---Y 1037
Cdd:cd10206   335 ---FKLLPLDEAIVQSIlSCASDELKRKMYSSILLVGGGAKIPGLAealeDRLLIKIPSLFEAVETVEVLPPPKDMdpsL 411
                         330       340       350
                  ....*....|....*....|....*....|..
gi 215273934 1038 SVWVGGSILASLSTFQQMWISKQEYDESGPSI 1069
Cdd:cd10206   412 LAWKGGAVLACLDSAQELWITRKEWQRLGVRA 443
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
187-357 1.13e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.64  E-value: 1.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  187 EVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIE 266
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  267 SKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAV 346
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                         170
                  ....*....|.
gi 215273934  347 SSHHHVICQLL 357
Cdd:COG0666   162 ANGNLEIVKLL 172
PHA03100 PHA03100
ankyrin repeat protein; Provisional
158-361 1.33e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 95.89  E-value: 1.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  158 IVMLrDTDVNKQDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTAL-----IKAVQCQEDECALMLLEHGTDP 232
Cdd:PHA03100   21 IIME-DDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  233 NIPDEYGNTTLHYAIYN--EDKLMAKALLLYGADIESKNKHGLTPL--LLGVHEQKQQVVKFLIKKKANLNALDR----- 303
Cdd:PHA03100  100 NAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLhlYLESNKIDLKILKLLIDKGVDINAKNRvnyll 179
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 215273934  304 -----------YGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYK 361
Cdd:PHA03100  180 sygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248
Ank_2 pfam12796
Ankyrin repeats (3 copies);
177-269 5.02e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.55  E-value: 5.02e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934   177 LHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEHGtDPNIPDeYGNTTLHYAIYNEDKLMAK 256
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 215273934   257 ALLLYGADIESKN 269
Cdd:pfam12796   79 LLLEKGADINVKD 91
ASKHA_NBD_ScArp7-like cd10212
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and ...
708-1063 9.75e-20

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


Pssm-ID: 466818 [Multi-domain]  Cd Length: 424  Bit Score: 93.24  E-value: 9.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  708 LVIDNGSGMCKAGFAGDDAPRAVFPS-IVGRPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEKIW 786
Cdd:cd10212     6 VVIHNGSHRTVAGFSNVELPQCIIPSsYIKRTDEGGEAEFIFGTYNMIDAAAEKRNGDEVYTLVDSQGLPYNWDALEMQW 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  787 HHTFYNELRVAPEEHPVLLTEATLNPKANR---EKMTQIMFETFNTPAMYVAIQAVLSLYTSGRTTGIVMDSGDGVTHTV 863
Cdd:cd10212    86 RYLYDTQLKVSPEELPLVITMPATNGKPDMailERYYELAFDKLNVPVFQIVIEPLAIALSMGKSSAFVIDIGASGCNVT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  864 PIYEGNALPHATLRLDLAGR----ELPDYLMKILTEHG----------------YRFTT--------------------- 902
Cdd:cd10212   166 PIIDGIVVKNAVVRSKFGGDfldfQVHERLAPLIKEENdmenmadeqkrstdvwYEASTwiqqfkstmlqvsekdlfele 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  903 ----------MAEREIVRDIKEKLCYVALDFEQEMATVASSSSLEKsyelPDGQVITIG-NERFRCPEALFQPCFLGMES 971
Cdd:cd10212   246 ryykeqadiyAKQQEQLKQMDQQLQYTALTGSPNNPLVQKKNFLFK----PLNKTLTLDlKECYQFAEYLFKPQLISDKF 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  972 C---GIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSmMKIRIIAPP---KRKYSVWVGGSI 1045
Cdd:cd10212   322 SpedGLGPLMAKSVKKAPEQVYSLLLTNVIITGSTSLIEGMEQRIIKELSIRFPQ-YKLTTFANQvmmDRKIQGWLGALT 400
                         410
                  ....*....|....*....
gi 215273934 1046 LASLSTFQ-QMWISKQEYD 1063
Cdd:cd10212   401 MANLPSWSlGKWYSKEDYE 419
Ank_2 pfam12796
Ankyrin repeats (3 copies);
243-335 3.29e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 3.29e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934   243 LHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIkKKANLNALDrYGRTALILAVCCGSASIVS 322
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 215273934   323 LLLEQNIDVSSQD 335
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
158-304 1.55e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 86.26  E-value: 1.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  158 IVMLRDTDVNKQDKQKRTALHLASAN--GNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECAL------------ 223
Cdd:PHA03100   91 LLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKIlkllidkgvdin 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  224 ------MLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKAN 297
Cdd:PHA03100  171 aknrvnYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250

                  ....*..
gi 215273934  298 LNALDRY 304
Cdd:PHA03100  251 IKTIIET 257
Ank_2 pfam12796
Ankyrin repeats (3 copies);
143-236 1.76e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 1.76e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934   143 LHRAAWWGKVprkDLIVML--RDTDVNKQDKQKRTALHLASANGNSEVVKLLLDrRCQLNVlDNKKRTALIKAVQCQEDE 220
Cdd:pfam12796    1 LHLAAKNGNL---ELVKLLleNGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNL-KDNGRTALHYAARSGHLE 75
                           90
                   ....*....|....*.
gi 215273934   221 CALMLLEHGTDPNIPD 236
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
CCDC144C pfam14915
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ...
648-701 3.98e-17

CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.


Pssm-ID: 464371 [Multi-domain]  Cd Length: 304  Bit Score: 83.50  E-value: 3.98e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 215273934   648 NSTLREEIAMLRLELDTMKHQSQLREKKYLEDIESVKKRNDNLLKALQLNELTM 701
Cdd:pfam14915    1 NCMLQDEIAMLRLEIDTIKNQNQEKEKKYLEDIEILKEKNDDLQKTLKLNEETL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
154-332 6.99e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 84.33  E-value: 6.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  154 RKDLIVMLRDT--DVNKQDKQKRTALHLAS-----ANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALM-- 224
Cdd:PHA03100   47 NIDVVKILLDNgaDINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIVey 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  225 LLEHGTDPNIPDEYGNTTLH-YAIYNEDKL-MAKALLL----------------YGADIESKNKHGLTPLLLGVHEQKQQ 286
Cdd:PHA03100  127 LLDNGANVNIKNSDGENLLHlYLESNKIDLkILKLLIDkgvdinaknrvnyllsYGVPINIKDVYGFTPLHYAVYNNNPE 206
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 215273934  287 VVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVS 332
Cdd:PHA03100  207 FVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02878 PHA02878
ankyrin repeat protein; Provisional
151-361 2.06e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 83.39  E-value: 2.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  151 KVPRKDLIVMLRDTDVNKQDKQKRTALHlasaNGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEHGT 230
Cdd:PHA02878   83 KLGMKEMIRSINKCSVFYTLVAIKDAFN----NRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGA 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  231 DPNIPDEY-GNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTAL 309
Cdd:PHA02878  159 DINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 215273934  310 ILAVC-CGSASIVSLLLEQNIDVSSQD-LSGQTAREYAVSSHHhvICQLLSDYK 361
Cdd:PHA02878  239 HISVGyCKDYDILKLLLEHGVDVNAKSyILGLTALHSSIKSER--KLKLLLEYG 290
PHA03095 PHA03095
ankyrin-like protein; Provisional
224-349 3.80e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 82.38  E-value: 3.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  224 MLLEHGTDPNIPDEYGNTTLHYAIYN---EDKLMAKALLLYGADIESKNKHGLTPL-LLGVHEQKQQVVKFLIKKKANLN 299
Cdd:PHA03095   32 RLLAAGADVNFRGEYGKTPLHLYLHYsseKVKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGADVN 111
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 215273934  300 ALDRYGRTalILAVCCGSASI----VSLLLEQNIDVSSQDLSGQTAREYAVSSH 349
Cdd:PHA03095  112 AKDKVGRT--PLHVYLSGFNInpkvIRLLLRKGADVNALDLYGMTPLAVLLKSR 163
PHA02876 PHA02876
ankyrin repeat protein; Provisional
165-360 7.85e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 82.42  E-value: 7.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  165 DVNKQDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLD-----------------------------NKKRTALIKAVQ 215
Cdd:PHA02876  170 DVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIAlddlsvlecavdsknidtikaiidnrsniNKNDLSLLKAIR 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  216 CQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNE--DKLMAKaLLLYGADIESKNKHGLTPL-LLGVHEQKQQVVKFLI 292
Cdd:PHA02876  250 NEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPslSRLVPK-LLERGADVNAKNIKGETPLyLMAKNGYDTENIRTLI 328
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 215273934  293 KKKANLNALDRYGRTALILAVCCG-SASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDY 360
Cdd:PHA02876  329 MLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDY 397
PHA03095 PHA03095
ankyrin-like protein; Provisional
165-328 3.00e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 79.68  E-value: 3.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  165 DVNKQDKQKRTALH--LASANGNSEVVKLLLDRRCQLNVLDNKKRTAL-IKAVQCQEDECAL-MLLEHGTDPNIPDEYGN 240
Cdd:PHA03095  144 DVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLhHHLQSFKPRARIVrELIRAGCDPAATDMLGN 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  241 TTLHY-AIYNEDK--LMAKaLLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGS 317
Cdd:PHA03095  224 TPLHSmATGSSCKrsLVLP-LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNN 302
                         170
                  ....*....|.
gi 215273934  318 ASIVSLLLEQN 328
Cdd:PHA03095  303 GRAVRAALAKN 313
PHA03095 PHA03095
ankyrin-like protein; Provisional
165-354 5.09e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.91  E-value: 5.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  165 DVNKQDKQKRTALHLASANGNS---EVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECAL-MLLEHGTDPNIPDEYGN 240
Cdd:PHA03095   39 DVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIkLLIKAGADVNAKDKVGR 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  241 TTLHyaIY----NEDKLMAKALLLYGADIESKNKHGLTPL--LLGVHEQKQQVVKFLIKKKANLNALDRYGRTAL----- 309
Cdd:PHA03095  119 TPLH--VYlsgfNINPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLhhhlq 196
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 215273934  310 ------------ILAVCCGSA--------------------SIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVIC 354
Cdd:PHA03095  197 sfkprarivrelIRAGCDPAAtdmlgntplhsmatgssckrSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRAC 273
PHA03095 PHA03095
ankyrin-like protein; Provisional
165-353 2.63e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.60  E-value: 2.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  165 DVNKQDKQKRTALH--LASANGNSEVVKLLLDRRCQLNVLDNKKRT---ALIKAVQCqEDECALMLLEHGTDPNIPDEYG 239
Cdd:PHA03095  109 DVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTplaVLLKSRNA-NVELLRLLIDAGADVYAVDDRF 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  240 NTTLHY-AIY---NEDKLmaKALLLYGADIESKNKHGLTPL--LLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAV 313
Cdd:PHA03095  188 RSLLHHhLQSfkpRARIV--RELIRAGCDPAATDMLGNTPLhsMATGSSCKRSLVLPLLIAGISINARNRYGQTPLHYAA 265
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 215273934  314 CCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVI 353
Cdd:PHA03095  266 VFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRA 305
PHA02874 PHA02874
ankyrin repeat protein; Provisional
165-359 2.62e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.46  E-value: 2.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  165 DVNKQDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLdnkkrtalikAVQCQEDECALMLLEHGTDPNIPDEYGNTTLH 244
Cdd:PHA02874   60 DINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIL----------PIPCIEKDMIKTILDCGIDVNIKDAELKTFLH 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  245 YAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLL 324
Cdd:PHA02874  130 YAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLL 209
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 215273934  325 LEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSD 359
Cdd:PHA02874  210 IDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINN 244
PHA02874 PHA02874
ankyrin repeat protein; Provisional
185-346 7.65e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.84  E-value: 7.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  185 NSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGAD 264
Cdd:PHA02874  103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  265 IESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVcCGSASIVSLLLeQNIDVSSQDLSGQTAREY 344
Cdd:PHA02874  183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLI-NNASINDQDIDGSTPLHH 260

                  ..
gi 215273934  345 AV 346
Cdd:PHA02874  261 AI 262
PHA02876 PHA02876
ankyrin repeat protein; Provisional
143-360 1.17e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 68.94  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  143 LHRAAWWGKVPRKDLIVMLRDTDVNKQDKQKRTALHLASANG-NSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQED-E 220
Cdd:PHA02876  277 LHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNkD 356
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  221 CALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQV-VKFLIKKKANLN 299
Cdd:PHA02876  357 IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVN 436
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 215273934  300 ALDRYGRTALILAvCCGSA--SIVSLLLEQNIDVSSQDLSGQTAREYAVSshHHVICQLLSDY 360
Cdd:PHA02876  437 SKNKDLSTPLHYA-CKKNCklDVIEMLLDNGADVNAINIQNQYPLLIALE--YHGIVNILLHY 496
PHA02875 PHA02875
ankyrin repeat protein; Provisional
174-330 1.23e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 68.09  E-value: 1.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  174 RTALHLASANGNSEVVKLLLDRRCQLN-VLDNKKRTALIKAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDK 252
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 215273934  253 LMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGR-TALILAVCCGSASIVSLLLEQNID 330
Cdd:PHA02875  149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGAD 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
287-367 1.41e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.67  E-value: 1.41e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934   287 VVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEqNIDVSSQDlSGQTAREYAVSSHHHVICQLLSDYKEKQML 366
Cdd:pfam12796   12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINV 89

                   .
gi 215273934   367 K 367
Cdd:pfam12796   90 K 90
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
156-304 1.45e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 68.74  E-value: 1.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  156 DLIVMLRDTDVNkqDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALML--LEHGTDPN 233
Cdd:PLN03192  543 ELLKAKLDPDIG--DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPH 620
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215273934  234 IpdeyGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRY 304
Cdd:PLN03192  621 A----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
PHA02878 PHA02878
ankyrin repeat protein; Provisional
165-280 4.33e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.44  E-value: 4.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  165 DVNKQDKQK-RTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEHGTDPNIPDEYGNTTL 243
Cdd:PHA02878  159 DINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215273934  244 HYA-----------------------------------IYNEDKLmaKALLLYGADIESKNKHGLTPLLLGV 280
Cdd:PHA02878  239 HISvgyckdydilklllehgvdvnaksyilgltalhssIKSERKL--KLLLEYGADINSLNSYKLTPLSSAV 308
PHA02875 PHA02875
ankyrin repeat protein; Provisional
143-299 1.09e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.01  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  143 LHRAAWWGKVPRKDLIVMLRDTDVNKQDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECA 222
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 215273934  223 LMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHG-LTPLLLGVHEQKQQVVKFLIKKKANLN 299
Cdd:PHA02875  152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02875 PHA02875
ankyrin repeat protein; Provisional
177-334 1.50e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 64.63  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  177 LHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEHGTDPN-IPDEYGNTTLHYAIYNEDKLMA 255
Cdd:PHA02875   39 IKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIM 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  256 KALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQ--NIDVSS 333
Cdd:PHA02875  119 KLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSgaNIDYFG 198

                  .
gi 215273934  334 Q 334
Cdd:PHA02875  199 K 199
PHA02875 PHA02875
ankyrin repeat protein; Provisional
174-359 1.27e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.55  E-value: 1.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  174 RTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKL 253
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  254 MAKALLLYGADIESK-NKHGLTPLLLGVHEQKQQVVKFLIKKKA--NLNALDRYgrTALILAVCCGSASIVSLLLEQNID 330
Cdd:PHA02875   83 AVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGAdpDIPNTDKF--SPLHLAVMMGDIKGIELLIDHKAC 160
                         170       180
                  ....*....|....*....|....*....
gi 215273934  331 VSSQDLSGQTAREYAVSSHHHVICQLLSD 359
Cdd:PHA02875  161 LDIEDCCGCTPLIIAMAKGDIAICKMLLD 189
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
171-340 5.54e-09

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 60.03  E-value: 5.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  171 KQKRTA---LHLASANGNSEVVK-LLLDRRCqlnvlDNKKR-----TALIKAVQCQEDECALMLLEhgTDP---NIP--- 235
Cdd:cd22192    12 QQKRISespLLLAAKENDVQAIKkLLKCPSC-----DLFQRgalgeTALHVAALYDNLEAAVVLME--AAPelvNEPmts 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  236 DEY-GNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLtplllgvheqkqqvvkFLIKKKANLNaldRYGRTALILAVC 314
Cdd:cd22192    85 DLYqGETALHIAVVNQNLNLVRELIARGADVVSPRATGT----------------FFRPGPKNLI---YYGEHPLSFAAC 145
                         170       180
                  ....*....|....*....|....*.
gi 215273934  315 CGSASIVSLLLEQNIDVSSQDLSGQT 340
Cdd:cd22192   146 VGNEEIVRLLIEHGADIRAQDSLGNT 171
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
198-362 8.33e-09

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 59.71  E-value: 8.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934   198 QLNVLDNKKRTALIKAVQCQE-DECALMLLEHGTDPNIpdeyGNTTLHyAIYNEDKLMAKALLLYGADIESKNK------ 270
Cdd:TIGR00870   44 NINCPDRLGRSALFVAAIENEnLELTELLLNLSCRGAV----GDTLLH-AISLEYVDAVEAILLHLLAAFRKSGplelan 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934   271 --------HGLTPLLLGVHEQKQQVVKFLIKKKANLNA--------------LDRYGRTALILAVCCGSASIVSLLLEQN 328
Cdd:TIGR00870  119 dqytseftPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgvdSFYHGESPLNAAACLGSPSIVALLSEDP 198
                          170       180       190
                   ....*....|....*....|....*....|....
gi 215273934   329 IDVSSQDLSGQTAREYAVsshhhVICQLLSDYKE 362
Cdd:TIGR00870  199 ADILTADSLGNTLLHLLV-----MENEFKAEYEE 227
PHA02876 PHA02876
ankyrin repeat protein; Provisional
217-340 1.11e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.31  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  217 QEDE--CALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKK 294
Cdd:PHA02876  154 QQDEllIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 215273934  295 KANL-----------------------------NALDRYGRTALILAVCCGSAS-IVSLLLEQNIDVSSQDLSGQT 340
Cdd:PHA02876  234 RSNInkndlsllkairnedletslllydagfsvNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGET 309
Ank_5 pfam13857
Ankyrin repeats (many copies);
165-213 5.81e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.04  E-value: 5.81e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 215273934   165 DVNKQDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKA 213
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
225-276 8.36e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.65  E-value: 8.36e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 215273934   225 LLEHGT-DPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPL 276
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02874 PHA02874
ankyrin repeat protein; Provisional
158-367 1.69e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.97  E-value: 1.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  158 IVMLRDTDVNKQDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEHGTDPNIpde 237
Cdd:PHA02874   20 IIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI--- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  238 ygnttlhYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGS 317
Cdd:PHA02874   97 -------LPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNF 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 215273934  318 ASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYKEKQMLK 367
Cdd:PHA02874  170 FDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK 219
Ank_4 pfam13637
Ankyrin repeats (many copies);
143-193 1.83e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 1.83e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 215273934   143 LHRAAWWGKVprkDLIVMLRDT--DVNKQDKQKRTALHLASANGNSEVVKLLL 193
Cdd:pfam13637    5 LHAAAASGHL---ELLRLLLEKgaDINAVDGNGETALHFAASNGNVEVLKLLL 54
ASKHA_NBD_MamK cd24009
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ...
715-930 3.37e-07

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: 53.37  E-value: 3.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  715 GMCKAGFAGDDAPRAVFPSIVGRPRqqGMMGGMHQKESYV-GKEAQSKRGILTLKYPMEHGIITNWDDmekiwhhtfyNE 793
Cdd:cd24009     9 GTSRSAVVTSRGKRFSFRSVVGYPK--DIIARKLLGKEVLfGDEALENRLALDLRRPLEDGVIKEGDD----------RD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  794 LRVAPE--EHpvLLTEATLNPKA---------------NREKMTQIMFETFNTPAMYVAIQAVlsLYTSGRTTG-IVMDS 855
Cdd:cd24009    77 LEAAREllQH--LIELALPGPDDeiyavigvparasaeNKQALLEIARELVDGVMVVSEPFAV--AYGLDRLDNsLIVDI 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 215273934  856 GDGVThTVPIYEGnALPHAT--LRLDLAGRELPDYLMKILTEH--GYRFTtmaeREIVRDIKEKLCYVALDFEQEMATV 930
Cdd:cd24009   153 GAGTT-DLCRMKG-TIPTEEdqITLPKAGDYIDEELVDLIKERypEVQLT----LNMARRWKEKYGFVGDASEPVKVEL 225
Ank_4 pfam13637
Ankyrin repeats (many copies);
272-325 4.20e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 4.20e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 215273934   272 GLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLL 325
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
192-246 7.81e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 7.81e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 215273934   192 LLDRR-CQLNVLDNKKRTALIKAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYA 246
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
207-259 9.87e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 9.87e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 215273934   207 RTALIKAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALL 259
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
256-341 1.53e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.95  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  256 KALLLYGADIESKNKHGLTPLLLGVH---EQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGS-ASIVSLLLEQNIDV 331
Cdd:PHA03095   31 RRLLAAGADVNFRGEYGKTPLHLYLHyssEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADV 110
                          90
                  ....*....|
gi 215273934  332 SSQDLSGQTA 341
Cdd:PHA03095  111 NAKDKVGRTP 120
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
172-295 1.89e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.94  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  172 QKRTALHLASANGNSEVVKLLLDRRCQLN------VLDNKKRTALIK--------AVQCQEDECALMLLEHGTDPNIPDE 237
Cdd:cd22192    88 QGETALHIAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLIYygehplsfAACVGNEEIVRLLIEHGADIRAQDS 167
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 215273934  238 YGNTTLHYAIYNEDKLMAKAL--LLYGADIES--------KNKHGLTPLLLGVHEQKQQVVKFLIKKK 295
Cdd:cd22192   168 LGNTVLHILVLQPNKTFACQMydLILSYDKEDdlqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
PHA02798 PHA02798
ankyrin-like protein; Provisional
157-363 2.92e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 50.99  E-value: 2.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  157 LIVMLRDTDVNKQDKQKRTALHLASANG---NSEVVKLLLDRRCQLNVLDNKKRTALIKAVQ--CQED-ECALMLLEHGT 230
Cdd:PHA02798   93 KILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFMIENGADTTLLDKDGFTMLQVYLQsnHHIDiEIIKLLLEKGV 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  231 DPN-IPDEYGNTTLH-YAIYN---------------------EDKLMAKALLLY---------------------GADIE 266
Cdd:PHA02798  173 DINtHNNKEKYDTLHcYFKYNidridadilklfvdngfiinkENKSHKKKFMEYlnsllydnkrfkknildfifsYIDIN 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  267 SKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAV 346
Cdd:PHA02798  253 QVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNKNTISYTYYKLRKHIL 332
                         250
                  ....*....|....*..
gi 215273934  347 SSHHHVICQLLSDYKEK 363
Cdd:PHA02798  333 NVEGDFINQLEFDIIKK 349
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
172-295 4.58e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 50.65  E-value: 4.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  172 QKRTALHLASANGNSEVVKLLLDRRCQLNVLDNK---KRTA----------LIKAVQCQEDECALMLLEHGTDP---NIP 235
Cdd:cd21882    72 QGQTALHIAIENRNLNLVRLLVENGADVSARATGrffRKSPgnlfyfgelpLSLAACTNQEEIVRLLLENGAQPaalEAQ 151
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 215273934  236 DEYGNTTLHYAIYNEDKL---------MAKALLLYGADI-------ESKNKHGLTPLLLGVHEQKQQVVKFLIKKK 295
Cdd:cd21882   152 DSLGNTVLHALVLQADNTpensafvcqMYNLLLSYGAHLdptqqleEIPNHQGLTPLKLAAVEGKIVMFQHILQRE 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
309-376 7.88e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.11  E-value: 7.88e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 215273934   309 LILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYKEKQM-------LKISSENSNPE 376
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLkdngrtaLHYAARSGHLE 75
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
175-295 8.29e-06

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 50.08  E-value: 8.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934   175 TALHLASANGNSEVVKLLLDR------RCQLNVLDNKKRTAL-------IKAVQC--QEDECALmLLEHGTDPNIPDEYG 239
Cdd:TIGR00870  130 TALHLAAHRQNYEIVKLLLERgasvpaRACGDFFVKSQGVDSfyhgespLNAAAClgSPSIVAL-LSEDPADILTADSLG 208
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215273934   240 NTTLHYAIYNED------KL---MAKALLLYGADIESK-------NKHGLTPLLLGVHEQKQQVVKFLIKKK 295
Cdd:TIGR00870  209 NTLLHLLVMENEfkaeyeELscqMYNFALSLLDKLRDSkelevilNHQGLTPLKLAAKEGRIVLFRLKLAIK 280
PHA02946 PHA02946
ankyin-like protein; Provisional
185-354 9.59e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 49.28  E-value: 9.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  185 NSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLL--YG 262
Cdd:PHA02946   51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERINLLvqYG 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  263 ADI-ESKNKHGLTPlLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGS--ASIVSLLLEQNIDVSSQDLSGQ 339
Cdd:PHA02946  131 AKInNSVDEEGCGP-LLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPDHDGN 209
                         170
                  ....*....|....*
gi 215273934  340 TAReyavsshhHVIC 354
Cdd:PHA02946  210 TPL--------HIVC 216
Ank_5 pfam13857
Ankyrin repeats (many copies);
296-345 1.02e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 1.02e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 215273934   296 ANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYA 345
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
239-292 2.17e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 2.17e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 215273934   239 GNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLI 292
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
251-338 3.71e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 3.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  251 DKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNID 330
Cdd:PTZ00322   94 DAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173

                  ....*...
gi 215273934  331 VSSQDLSG 338
Cdd:PTZ00322  174 HFELGANA 181
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
180-357 3.83e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.94  E-value: 3.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  180 ASANGNSEVVKLLLDRRCQLNVLDNKKRTAL-IKAVQCQEDeCALMLLEHGTDPNIPDEYGNTTL-------HYAIYNed 251
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLhIAASKGYED-CVLVLLKHACNVHIRDANGNTALwnaisakHHKIFR-- 608
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  252 klmakaLLLYGADIEskNKHGLTPLLLgvheqkqqvvkfLIKKKANLNALDRygrtalilavccgsasivslLLEQNIDV 331
Cdd:PLN03192  609 ------ILYHFASIS--DPHAAGDLLC------------TAAKRNDLTAMKE--------------------LLKQGLNV 648
                         170       180
                  ....*....|....*....|....*.
gi 215273934  332 SSQDLSGQTAREYAVSSHHHVICQLL 357
Cdd:PLN03192  649 DSEDHQGATALQVAMAEDHVDMVRLL 674
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
222-293 4.55e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 4.55e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215273934  222 ALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIK 293
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
207-340 8.32e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 46.41  E-value: 8.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  207 RTALIKAV---QCQEDECALMLLEHGTDPNIP---------DEY--GNTTLHYAIYNEDKLMAKALLLYGADIESKNKhg 272
Cdd:cd21882    27 KTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPkelvnapctDEFyqGQTALHIAIENRNLNLVRLLVENGADVSARAT-- 104
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215273934  273 ltplllGVHEQKQQVVKFLikkkanlnaldrYGRTALILAVCCGSASIVSLLLE---QNIDVSSQDLSGQT 340
Cdd:cd21882   105 ------GRFFRKSPGNLFY------------FGELPLSLAACTNQEEIVRLLLEngaQPAALEAQDSLGNT 157
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
174-204 1.35e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 1.35e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 215273934   174 RTALHLASA-NGNSEVVKLLLDRRCQLNVLDN 204
Cdd:pfam00023    3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA02798 PHA02798
ankyrin-like protein; Provisional
178-332 3.31e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.44  E-value: 3.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  178 HLASANGNSEVVKLLLDRRCQLNVLDNKKRTALikavqcqedeCALMllehgtdPNIPDeygnttlhyaiYNEDKLMAKA 257
Cdd:PHA02798   43 YLQRDSPSTDIVKLFINLGANVNGLDNEYSTPL----------CTIL-------SNIKD-----------YKHMLDIVKI 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  258 LLLYGADIESKNKHGLTPLLLGVHE---QKQQVVKFLIKKKANLNALDRYGRTALILAV---CCGSASIVSLLLEQNIDV 331
Cdd:PHA02798   95 LIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLqsnHHIDIEIIKLLLEKGVDI 174

                  .
gi 215273934  332 S 332
Cdd:PHA02798  175 N 175
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
288-360 3.55e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.50  E-value: 3.55e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 215273934  288 VKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDY 360
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
172-201 5.36e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 5.36e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 215273934    172 QKRTALHLASANGNSEVVKLLLDRRCQLNV 201
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
238-270 7.37e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 7.37e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 215273934   238 YGNTTLHYAIYNEDKL-MAKALLLYGADIESKNK 270
Cdd:pfam00023    1 DGNTPLHLAAGRRGNLeIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
174-201 1.09e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.09e-03
                           10        20
                   ....*....|....*....|....*...
gi 215273934   174 RTALHLASANGNSEVVKLLLDRRCQLNV 201
Cdd:pfam13606    3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
280-350 1.14e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.13  E-value: 1.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215273934  280 VHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHH 350
Cdd:PHA02876  153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN 223
PHA02946 PHA02946
ankyin-like protein; Provisional
225-378 1.34e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 42.35  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  225 LLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPL--LLGVHEQKQQVVKFLIKKKANL-NAL 301
Cdd:PHA02946   58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINLLVQYGAKInNSV 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  302 DRYGRTALiLAVCCGSASIVSLLLEQNIDVSSQDLSGQtareyavsshHHVICQLLSDYKEKQ----MLKISSENSNPEQ 377
Cdd:PHA02946  138 DEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGK----------NHIHRHLMSDNPKAStiswMMKLGISPSKPDH 206

                  .
gi 215273934  378 D 378
Cdd:PHA02946  207 D 207
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
207-340 1.52e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 42.48  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  207 RTALIKAV---QCQEDECALMLLEHGTDPNIPDEY-----------GNTTLHYAIYNEDKLMAKALLLYGADIESKNKhg 272
Cdd:cd22193    30 KTCLMKALlnlNPGTNDTIRILLDIAEKTDNLKRFinaeytdeyyeGQTALHIAIERRQGDIVALLVENGADVHAHAK-- 107
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215273934  273 ltplllGVHEQKQ-QVVKFLikkkanlnaldrYGRTALILAVCCGSASIVSLLLE---QNIDVSSQDLSGQT 340
Cdd:cd22193   108 ------GRFFQPKyQGEGFY------------FGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNT 161
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
260-340 1.89e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 42.44  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  260 LYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDR--------------YGRTALILAVCCGSASIVSLLL 325
Cdd:cd22194   129 FINAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLALAACTNQPEIVQLLM 208
                          90
                  ....*....|....*.
gi 215273934  326 EQ-NIDVSSQDLSGQT 340
Cdd:cd22194   209 EKeSTDITSQDSRGNT 224
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
304-335 2.40e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 2.40e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 215273934   304 YGRTALILAVC-CGSASIVSLLLEQNIDVSSQD 335
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02859 PHA02859
ankyrin repeat protein; Provisional
183-275 3.99e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.80  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  183 NGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVqcqeDECAL------MLLEHGTDPNIPDEYGNTTLH-YAIYNEDKLMA 255
Cdd:PHA02859  100 NVEPEILKILIDSGSSITEEDEDGKNLLHMYM----CNFNVrinvikLLIDSGVSFLNKDFDNNNILYsYILFHSDKKIF 175
                          90       100
                  ....*....|....*....|
gi 215273934  256 KALLLYGADIESKNKHGLTP 275
Cdd:PHA02859  176 DFLTSLGIDINETNKSGYNC 195
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
165-228 4.78e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.04  E-value: 4.78e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215273934  165 DVNKQDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEH 228
Cdd:PTZ00322  107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
238-266 6.77e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 6.77e-03
                            10        20
                    ....*....|....*....|....*....
gi 215273934    238 YGNTTLHYAIYNEDKLMAKALLLYGADIE 266
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02884 PHA02884
ankyrin repeat protein; Provisional
188-278 8.29e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.58  E-value: 8.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  188 VVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEHGTDPNIPDEYGNTT-LHYAIYNEDKLMAKALLLYGADIE 266
Cdd:PHA02884   52 ILKLGADPEAPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITpLYISVLHGCLKCLEILLSYGADIN 131
                          90
                  ....*....|..
gi 215273934  267 SKNKHGLTPLLL 278
Cdd:PHA02884  132 IQTNDMVTPIEL 143
PHA02791 PHA02791
ankyrin-like protein; Provisional
155-247 8.69e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 39.25  E-value: 8.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215273934  155 KDLIVMLRDTDVNKQDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKkrTALIKAVQCQEDECALMLLEHGTDPNI 234
Cdd:PHA02791   12 KQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQ 89
                          90
                  ....*....|...
gi 215273934  235 PDEYGNTTLHYAI 247
Cdd:PHA02791   90 FDDKGNTALYYAV 102
 
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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