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Conserved domains on  [gi|767919377|ref|XP_011509985|]
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POTE ankyrin domain family member J isoform X1 [Homo sapiens]

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 ...
679-1043 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: 855.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  679 AVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGCPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEKI 758
Cdd:cd10224     1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  759 WHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAMLSLYTSGRTTGIVMDSGDGVTHTVPI 838
Cdd:cd10224    81 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  839 YDGNALPHATLRLDLAGRELTDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMAMVASSSSLEKSYELPDG 918
Cdd:cd10224   161 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  919 QVITISNEWFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMM 998
Cdd:cd10224   241 QVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTM 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 767919377  999 KIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIV 1043
Cdd:cd10224   321 KIKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 365
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
102-359 4.52e-45

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 164.74  E-value: 4.52e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  102 DLDKLHRAAWWGKVARKDLIVMLRDTDVNKQDKQKRTALHLASANGNSGVVKLLLDRRCQLNVLDNKKRTALtkvcssql 181
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLL-------- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  182 yqHEAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVV 261
Cdd:COG0666    92 --HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  262 KFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYKEKQMLKI 341
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
                         250
                  ....*....|....*...
gi 767919377  342 SSENSNPEQDLKLTSEEE 359
Cdd:COG0666   250 KDGLTALLLAAAAGAALI 267
CCDC144C super family cl25942
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ...
621-674 2.31e-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: 83.88  E-value: 2.31e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767919377   621 NSMLREEIAMLRLELDTMKHQSQLRKKKYLEDIESVKKKNDNLLKALQLNELTM 674
Cdd:pfam14915    1 NCMLQDEIAMLRLEIDTIKNQNQEKEKKYLEDIEILKEKNDDLQKTLKLNEETL 54
2A1904 super family cl36772
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
343-580 1.43e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


The actual alignment was detected with superfamily member TIGR00927:

Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 42.68  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   343 SENSNPEQdlkltSEEESQRFKGSENSQPEKMSQEPEINKDGDREVEEEMKKHESNNVGLLENLSNGVTAGNGDDGLIPQ 422
Cdd:TIGR00927  655 AEGENGEE-----SGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEGTEDE 729
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   423 RKSRTPENQQFPDNESE---EYHRICELVSDYKEKQMPKYSSENSNPEQDLKLTSEEESQRLKGSEnGQPEKRSQEPEIN 499
Cdd:TIGR00927  730 GEIETGEEGEEVEDEGEgeaEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEMKGDE-GAEGKVEHEGETE 808
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   500 KDGDRELENFMAIEEMKKHGSTHVGFPE-NLTNGATAGNGDDGLIPPRKSRTPESQQFPDTENEEYHSDEQNDTQKQFCE 578
Cdd:TIGR00927  809 AGEKDEHEGQSETQADDTEVKDETGEQElNAENQGEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEE 888

                   ..
gi 767919377   579 EQ 580
Cdd:TIGR00927  889 EN 890
 
Name Accession Description Interval E-value
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
679-1043 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: 855.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  679 AVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGCPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEKI 758
Cdd:cd10224     1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  759 WHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAMLSLYTSGRTTGIVMDSGDGVTHTVPI 838
Cdd:cd10224    81 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  839 YDGNALPHATLRLDLAGRELTDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMAMVASSSSLEKSYELPDG 918
Cdd:cd10224   161 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  919 QVITISNEWFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMM 998
Cdd:cd10224   241 QVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTM 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 767919377  999 KIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIV 1043
Cdd:cd10224   321 KIKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIV 365
PTZ00281 PTZ00281
actin; Provisional
674-1048 0e+00

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 718.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  674 MDDDTAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGCPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWD 753
Cdd:PTZ00281    2 DGEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  754 DMEKIWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAMLSLYTSGRTTGIVMDSGDGVT 833
Cdd:PTZ00281   82 DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  834 HTVPIYDGNALPHATLRLDLAGRELTDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMAMVASSSSLEKSY 913
Cdd:PTZ00281  162 HTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKSY 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  914 ELPDGQVITISNEWFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAAL 993
Cdd:PTZ00281  242 ELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTAL 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767919377  994 APSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 1048
Cdd:PTZ00281  322 APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKCF 376
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
678-1048 0e+00

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 613.11  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377    678 TAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGCPRQQGMMGGMhQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEK 757
Cdd:smart00268    1 VPAIVIDNGSGTIKAGFAGEDFPQVVFPSIVGRPKDGKGMVGD-AKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEK 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377    758 IWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAMLSLYTSGRTTGIVMDSGDGVTHTVP 837
Cdd:smart00268   80 IWDYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVP 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377    838 IYDGNALPHATLRLDLAGRELTDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMAMVAS---SSSLEKSYE 914
Cdd:smart00268  160 VVDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAREsseSSKLEKTYE 239
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377    915 LPDGQVITISNEWFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALA 994
Cdd:smart00268  240 LPDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQLA 319
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|....
gi 767919377    995 PSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 1048
Cdd:smart00268  320 PKKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKCF 373
Actin pfam00022
Actin;
678-1048 1.94e-179

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 528.41  E-value: 1.94e-179
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   678 TAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGCPRQQGmmgGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEK 757
Cdd:pfam00022    1 VSALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGTK---VEAANKYYVGDEALTYRPGMEVRSPVEDGIVVDWDAMEE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   758 IWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAMLSLYTSGRTTGIVMDSGDGVTHTVP 837
Cdd:pfam00022   78 IWEHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   838 IYDGNALPHATLRLDLAGRELTDYLMKILTER------------------------------GYRFTTMAEREIVRDIKE 887
Cdd:pfam00022  158 VHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRnieitprylikskkpgdpapavtkrelpdtTYSYKTYQERRVLEEIKE 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   888 KLCYVALDFeqEMAMVASSSSLEKSYELPDGQVITISNEWFRCPEALFQPCFLGMES--------CGIHETTFNSIMKSD 959
Cdd:pfam00022  238 SVCYVSDDP--FGDETTSSSIPTRVYELPDGSTIILGAERFRVPEILFNPSLIGSESelpppqtaVGIPELIVDAINACD 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   960 VDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMMKIRIIAPPK---RKYSVWVGGSILASLSTFQQMWISKQEYD 1036
Cdd:pfam00022  316 VDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGNtveRRYSAWIGGSILASLGTFQQMWVSKQEYE 395
                          410
                   ....*....|..
gi 767919377  1037 ESGPSIVHRKCF 1048
Cdd:pfam00022  396 EHGASVVERKCK 407
COG5277 COG5277
Actin-related protein [Cytoskeleton];
680-1038 9.86e-118

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 368.73  E-value: 9.86e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  680 VLVIDNGSGMCKAG-FAGDDAP-----RAVFPSIVGCPRQQGMMGGMhQKESYVGKEAQS-----KRGILTLKYPMEHGI 748
Cdd:COG5277    10 VIGIDFGTSYVKYGpIALEEKPrviqtRGLFLRIVGESKLLGPMEGL-SRGLVVGDEVSKylssvRDAIRNLKYPLRDGI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  749 IT-----NWDDMEKIWHHTFYNELRVAPEEHP--ILLTEAPLNPKANREKMTQIMFETF---NTPAMYVAIQAMLSLYTS 818
Cdd:COG5277    89 VRrddedAWRVLKELLRYTFAQFLVVDPEFHGflVVVALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVAIAE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  819 GRTTGIVMDSGDGVTHTVPIYDGnALPHATLRLDLAGRELTDYLMKILTERGYRFTTMAEReIVRDIKEKLCYVALDFEQ 898
Cdd:COG5277   169 KAVTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSDTAREEY-VVRVVKEALGLVPRDLAK 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  899 EMAMVASS-SSLEKSYELPDGQV-ITISN---EWFRCPEALFQPCFLGMESC----------------------GIHETT 951
Cdd:COG5277   247 AIQKAASNpDSFEAKVRLPNPTVeIELGNyawERFLIGEILFNPNHEGFESYiqqgrlriedavigdvvlygemGLAEAI 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  952 FNSIMKSDVDIRKDLYTNTVLSGGTTMY---PGMA-------HRMQKEIAALAPSmMKIRIIAPPKRKYSVWVGGSILAS 1021
Cdd:COG5277   327 INSIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEdvavdsvTRVQIELSELAPE-LKVNVRLVSDPQYSVWKGAIIYGY 405
                         410
                  ....*....|....*....
gi 767919377 1022 LSTFQQMW--ISKQEYDES 1038
Cdd:COG5277   406 ALPFSVKWswITKEGWYFL 424
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
102-359 4.52e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 164.74  E-value: 4.52e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  102 DLDKLHRAAWWGKVARKDLIVMLRDTDVNKQDKQKRTALHLASANGNSGVVKLLLDRRCQLNVLDNKKRTALtkvcssql 181
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLL-------- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  182 yqHEAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVV 261
Cdd:COG0666    92 --HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  262 KFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYKEKQMLKI 341
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
                         250
                  ....*....|....*...
gi 767919377  342 SSENSNPEQDLKLTSEEE 359
Cdd:COG0666   250 KDGLTALLLAAAAGAALI 267
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
976-1047 3.62e-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: 3.62e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767919377  976 TTMYPGMAHRMQKEIAALAPSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKC 1047
Cdd:NF040575   61 RVNESGFYEKLKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSIVHRKC 132
Ank_2 pfam12796
Ankyrin repeats (3 copies);
216-308 3.21e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 3.21e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   216 LHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIkKKANLNALDrYGRTALILAVCCGSASIVS 295
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 767919377   296 LLLEQNIDVSSQD 308
Cdd:pfam12796   79 LLLEKGADINVKD 91
CCDC144C pfam14915
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ...
621-674 2.31e-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: 83.88  E-value: 2.31e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767919377   621 NSMLREEIAMLRLELDTMKHQSQLRKKKYLEDIESVKKKNDNLLKALQLNELTM 674
Cdd:pfam14915    1 NCMLQDEIAMLRLEIDTIKNQNQEKEKKYLEDIEILKEKNDDLQKTLKLNEETL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
121-277 2.07e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 82.79  E-value: 2.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  121 IVMLRDTDVNKQDKQKRTALHLASAN--GNSGVVKLLLDRRCQLNVLDNKKRTALtkvcssqlyqHEAVQCQEDECAL-- 196
Cdd:PHA03100   91 LLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLL----------HLYLESNKIDLKIlk 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  197 ----------------MLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQV 260
Cdd:PHA03100  161 llidkgvdinaknrvnYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI 240
                         170
                  ....*....|....*..
gi 767919377  261 VKFLIKKKANLNALDRY 277
Cdd:PHA03100  241 FKLLLNNGPSIKTIIET 257
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
134-313 3.50e-08

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: 57.33  E-value: 3.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  134 KQKRTA---LHLASANGNSGVVK-LLLDRRCqlnvlDNKKR-----TALtkvcssqlyqHEAVQCQEDECALMLLEhgTD 204
Cdd:cd22192    12 QQKRISespLLLAAKENDVQAIKkLLKCPSC-----DLFQRgalgeTAL----------HVAALYDNLEAAVVLME--AA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  205 P---NIP---DEY-GNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLtplllgvheqkqqvvkFLIKKKANLNaldRY 277
Cdd:cd22192    75 PelvNEPmtsDLYqGETALHIAVVNQNLNLVRELIARGADVVSPRATGT----------------FFRPGPKNLI---YY 135
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 767919377  278 GRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQT 313
Cdd:cd22192   136 GEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
186-335 2.48e-07

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: 54.70  E-value: 2.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   186 AVQCQEDECALMLLEHGTDPNIpdeyGNTTLHyAIYNEDKLMAKALLLYGADIESKNK--------------HGLTPLLL 251
Cdd:TIGR00870   60 AIENENLELTELLLNLSCRGAV----GDTLLH-AISLEYVDAVEAILLHLLAAFRKSGplelandqytseftPGITALHL 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   252 GVHEQKQQVVKFLIKKKANLNA--------------LDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREY 317
Cdd:TIGR00870  135 AAHRQNYEIVKLLLERGASVPAracgdffvksqgvdSFYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHL 214
                          170
                   ....*....|....*...
gi 767919377   318 AVsshhhVICQLLSDYKE 335
Cdd:TIGR00870  215 LV-----MENEFKAEYEE 227
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
343-580 1.43e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 42.68  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   343 SENSNPEQdlkltSEEESQRFKGSENSQPEKMSQEPEINKDGDREVEEEMKKHESNNVGLLENLSNGVTAGNGDDGLIPQ 422
Cdd:TIGR00927  655 AEGENGEE-----SGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEGTEDE 729
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   423 RKSRTPENQQFPDNESE---EYHRICELVSDYKEKQMPKYSSENSNPEQDLKLTSEEESQRLKGSEnGQPEKRSQEPEIN 499
Cdd:TIGR00927  730 GEIETGEEGEEVEDEGEgeaEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEMKGDE-GAEGKVEHEGETE 808
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   500 KDGDRELENFMAIEEMKKHGSTHVGFPE-NLTNGATAGNGDDGLIPPRKSRTPESQQFPDTENEEYHSDEQNDTQKQFCE 578
Cdd:TIGR00927  809 AGEKDEHEGQSETQADDTEVKDETGEQElNAENQGEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEE 888

                   ..
gi 767919377   579 EQ 580
Cdd:TIGR00927  889 EN 890
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
135-164 4.77e-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: 35.64  E-value: 4.77e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 767919377    135 QKRTALHLASANGNSGVVKLLLDRRCQLNV 164
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
264-494 7.16e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 40.24  E-value: 7.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  264 LIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYkekqmlkisS 343
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF---------A 614
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  344 ENSNPEQ--DLKLTSEEesqrfKGSENSQPEKMSQEPEI---NKDGDREVEEEMKKHESNNVGLLenLSNG--VTAGNGD 416
Cdd:PLN03192  615 SISDPHAagDLLCTAAK-----RNDLTAMKELLKQGLNVdseDHQGATALQVAMAEDHVDMVRLL--IMNGadVDKANTD 687
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767919377  417 DGLIPQRKSRTPEnqqfpdnESEEYHRIceLVSDYKEKQMPKYSSENSNPEQDLKLTSEEESQRLKGS-ENGQPEKRSQ 494
Cdd:PLN03192  688 DDFSPTELRELLQ-------KRELGHSI--TIVDSVPADEPDLGRDGGSRPGRLQGTSSDNQCRPRVSiYKGHPLLRNE 757
 
Name Accession Description Interval E-value
ASKHA_NBD_actin cd10224
nucleotide-binding domain (NBD) of actin and similar proteins; Actin is a ubiquitous protein ...
679-1043 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: 855.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  679 AVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGCPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEKI 758
Cdd:cd10224     1 AALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  759 WHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAMLSLYTSGRTTGIVMDSGDGVTHTVPI 838
Cdd:cd10224    81 WHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  839 YDGNALPHATLRLDLAGRELTDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMAMVASSSSLEKSYELPDG 918
Cdd:cd10224   161 YEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  919 QVITISNEWFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMM 998
Cdd:cd10224   241 QVITIGNERFRCPEALFQPSFLGMEAAGIHETTYNSIMKCDVDIRKDLYANIVLSGGTTMFPGIADRMQKEITALAPSTM 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 767919377  999 KIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIV 1043
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 ...
679-1039 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: 727.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  679 AVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGCPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEKI 758
Cdd:cd13397     1 PAVVIDNGSGLIKAGFAGEDLPRAVFPSVVGRPKYKAVMLGAGQKEVYVGDEAQEKRGVLTLSYPIEHGIVTNWDDMEKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  759 WHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAMLSLYTSGRTTGIVMDSGDGVTHTVPI 838
Cdd:cd13397    81 WHHTFENELRVKPEEHPVLLTEAPLNPKQNREKMAEIMFETFGVPAFYVAIQAVLSLYSSGRTTGLVLDSGDGVTHTVPI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  839 YDGNALPHATLRLDLAGRELTDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMAmvASSSSLEKSYELPDG 918
Cdd:cd13397   161 YEGYALPHAVQRLDLAGRDLTEYLMKLLKERGHSFTTTAEREIVRDIKEKLCYVALDYEEELK--KKSEELEKEYTLPDG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  919 QVITISNEWFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMM 998
Cdd:cd13397   239 QVIKIGSERFRCPEALFRPSLIGREAPGIHKLVYNSIMKCDIDIRKDLYSNIVLSGGSTMFPGLPERLQKELEALAPSST 318
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 767919377  999 KIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESG 1039
Cdd:cd13397   319 KVKVIAPPERKYSVWIGGSILASLSTFKSMWITRAEYDEFG 359
PTZ00281 PTZ00281
actin; Provisional
674-1048 0e+00

actin; Provisional


Pssm-ID: 173506 [Multi-domain]  Cd Length: 376  Bit Score: 718.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  674 MDDDTAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGCPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWD 753
Cdd:PTZ00281    2 DGEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  754 DMEKIWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAMLSLYTSGRTTGIVMDSGDGVT 833
Cdd:PTZ00281   82 DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  834 HTVPIYDGNALPHATLRLDLAGRELTDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMAMVASSSSLEKSY 913
Cdd:PTZ00281  162 HTVPIYEGYALPHAILRLDLAGRDLTDYMMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEAEMQTAASSSALEKSY 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  914 ELPDGQVITISNEWFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAAL 993
Cdd:PTZ00281  242 ELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMNKELTAL 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767919377  994 APSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 1048
Cdd:PTZ00281  322 APSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKCF 376
PTZ00004 PTZ00004
actin-2; Provisional
674-1048 0e+00

actin-2; Provisional


Pssm-ID: 240225 [Multi-domain]  Cd Length: 378  Bit Score: 658.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  674 MDDDTAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGCPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWD 753
Cdd:PTZ00004    2 SVEETNAAVVDNGSGMVKAGFAGDDAPRCVFPSIVGRPKNPGIMVGMEEKDCYVGDEAQDKRGILTLKYPIEHGIVTNWD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  754 DMEKIWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAMLSLYTSGRTTGIVMDSGDGVT 833
Cdd:PTZ00004   82 DMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETHNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  834 HTVPIYDGNALPHATLRLDLAGRELTDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMAMVASSSSL-EKS 912
Cdd:PTZ00004  162 HTVPIYEGYSLPHAIHRLDVAGRDLTEYMMKILHERGTTFTTTAEKEIVRDIKEKLCYIALDFDEEMGNSAGSSDKyEES 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  913 YELPDGQVITISNEWFRCPEALFQPCFLGMESC-GIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIA 991
Cdd:PTZ00004  242 YELPDGTIITVGSERFRCPEALFQPSLIGKEEPpGIHELTFQSINKCDIDIRKDLYGNIVLSGGTTMYRGLPERLTKELT 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767919377  992 ALAPSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 1048
Cdd:PTZ00004  322 TLAPSTMKIKVVAPPERKYSVWIGGSILSSLPTFQQMWVTKEEYDESGPSIVHRKCF 378
ACTIN smart00268
Actin; ACTIN subfamily of ACTIN/mreB/sugarkinase/Hsp70 superfamily
678-1048 0e+00

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


Pssm-ID: 214592 [Multi-domain]  Cd Length: 373  Bit Score: 613.11  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377    678 TAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGCPRQQGMMGGMhQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEK 757
Cdd:smart00268    1 VPAIVIDNGSGTIKAGFAGEDFPQVVFPSIVGRPKDGKGMVGD-AKDIFVGDEAQEKRGGLELKYPIENGIVENWDDMEK 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377    758 IWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAMLSLYTSGRTTGIVMDSGDGVTHTVP 837
Cdd:smart00268   80 IWDYTFFNELRVEPEEHPVLLTEPPMNPKSNREKILEIMFETFNFPALYIAIQAVLSLYASGRTTGLVIDSGDGVTHVVP 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377    838 IYDGNALPHATLRLDLAGRELTDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMAMVAS---SSSLEKSYE 914
Cdd:smart00268  160 VVDGYVLPHAIKRIDIAGRDITDYLKELLSERGYQFNSSAEFEIVREIKEKLCYVAEDFEKEMKLAREsseSSKLEKTYE 239
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377    915 LPDGQVITISNEWFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALA 994
Cdd:smart00268  240 LPDGNTIKVGNERFRIPEILFSPELIGLEQKGIHELVYESIQKCDIDVRKDLYENIVLSGGSTLIPGFGERLEKELKQLA 319
                           330       340       350       360       370
                    ....*....|....*....|....*....|....*....|....*....|....
gi 767919377    995 PSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 1048
Cdd:smart00268  320 PKKLKVKVIAPPERKYSVWLGGSILASLSTFEDMWITKKEYEESGSQIVERKCF 373
ASKHA_NBD_Arp1 cd10216
nucleotide-binding domain (NBD) of actin-related protein 1 (Arp1) and similar proteins; Arp1, ...
681-1047 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: 585.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  681 LVIDNGSGMCKAGFAGDDAPRAVFPSIVGCPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEKIWH 760
Cdd:cd10216     4 VVIDNGSGVIKAGFAGDDIPKVVFPSYVGRPKHVRVMAGALEGDVFVGPKAEEHRGLLKIRYPMEHGIVTDWNDMERIWQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  761 HTFYNE-LRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAMLSLYTSGRTTGIVMDSGDGVTHTVPIY 839
Cdd:cd10216    84 YVYSKLqLNTFSEEHPVLLTEAPLNPRKNREKAAEVFFETFNVPALFVSMQAVLSLYASGRTTGVVLDSGDGVTHAVPIY 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  840 DGNALPHATLRLDLAGRELTDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMAMvASSSSLEKSYELPDGQ 919
Cdd:cd10216   164 EGFALPHSIRRVDIAGRDVTEYLQLLLRKSGYNFHTSAEFEIVREIKEKACYVALNPQKEEKL-EEEKTEKAQYTLPDGS 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  920 VITISNEWFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMMK 999
Cdd:cd10216   243 TIEIGPERFRAPEILFNPELIGLEYPGVHEVLVDSIQKSDLDLRKTLYSNIVLSGGSTLFKGFGDRLLSEVKKLAPKDVK 322
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 767919377 1000 IRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKC 1047
Cdd:cd10216   323 IRISAPPERLYSTWIGGSILASLSTFKKMWVSKKEYEEDGARILHRKT 370
Actin pfam00022
Actin;
678-1048 1.94e-179

Actin;


Pssm-ID: 394979 [Multi-domain]  Cd Length: 407  Bit Score: 528.41  E-value: 1.94e-179
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   678 TAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGCPRQQGmmgGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEK 757
Cdd:pfam00022    1 VSALVIDNGSHTTRAGFAGEDAPKAVIPSCVGKPRGTK---VEAANKYYVGDEALTYRPGMEVRSPVEDGIVVDWDAMEE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   758 IWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAMLSLYTSGRTTGIVMDSGDGVTHTVP 837
Cdd:pfam00022   78 IWEHVLKEELQVDPEEHPLLLTEPPWNPPANREKAAEIMFEKFGVPALYLAKNPVLSAFASGRTTGLVVDSGAGVTSVVP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   838 IYDGNALPHATLRLDLAGRELTDYLMKILTER------------------------------GYRFTTMAEREIVRDIKE 887
Cdd:pfam00022  158 VHDGYVLQKAIRRSDLGGDFLTDYLRELLRSRnieitprylikskkpgdpapavtkrelpdtTYSYKTYQERRVLEEIKE 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   888 KLCYVALDFeqEMAMVASSSSLEKSYELPDGQVITISNEWFRCPEALFQPCFLGMES--------CGIHETTFNSIMKSD 959
Cdd:pfam00022  238 SVCYVSDDP--FGDETTSSSIPTRVYELPDGSTIILGAERFRVPEILFNPSLIGSESelpppqtaVGIPELIVDAINACD 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   960 VDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMMKIRIIAPPK---RKYSVWVGGSILASLSTFQQMWISKQEYD 1036
Cdd:pfam00022  316 VDLRPSLLANIVVTGGNSLFPGFTERLEKELAQLAPPGVKVKIIAPGNtveRRYSAWIGGSILASLGTFQQMWVSKQEYE 395
                          410
                   ....*....|..
gi 767919377  1037 ESGPSIVHRKCF 1048
Cdd:pfam00022  396 EHGASVVERKCK 407
ASKHA_NBD_Arp2 cd10220
nucleotide-binding domain (NBD) of actin-related protein2 (Arp2) and similar proteins; Arp2, ...
680-1043 1.85e-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: 504.41  E-value: 1.85e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  680 VLVIDNGSGMCKAGFAGDDAPRAVFPSIVGCP--RQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEK 757
Cdd:cd10220     2 VVVCDNGTGFVKCGFAGSNFPEHVFPSLVGRPilRAEEKVGDIEIKDIMVGDEASELRSMLEVTYPMENGIVRNWDDMEH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  758 IWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAMLSLYTSGRTTGIVMDSGDGVTHTVP 837
Cdd:cd10220    82 LWDYTFGEKLKIDPRECKILLTEPPMNPTKNREKMVEVMFEKYGFAGVYVAIQAVLTLYAQGLLTGVVVDSGDGVTHIVP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  838 IYDGNALPHATLRLDLAGRELTDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMAMVASSSSLEKSYELPD 917
Cdd:cd10220   162 VYEGFSLPHLTRRLDVAGRDITRYLIKLLLLRGYAFNRTADFETVREIKEKLCYVAYDIELEQKLALETTVLVESYTLPD 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  918 GQVITISNEWFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAAL---- 993
Cdd:cd10220   242 GRVIKVGGERFEAPEALFQPHLIDVEGPGIAELLFNTIQAADIDTRPELYKHIVLSGGSTMYPGLPSRLEKEIKQLyler 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767919377  994 -------APSMMKIRIIAPPKRKYSVWVGGSILASLSTFQ-QMWISKQEYDESGPSIV 1043
Cdd:cd10220   322 vlkgdteRLSKFKIRIEDPPRRKHMVFLGGAVLADIMKDKdEFWITRQEYEEQGVRVL 379
PTZ00452 PTZ00452
actin; Provisional
674-1048 1.47e-157

actin; Provisional


Pssm-ID: 185631  Cd Length: 375  Bit Score: 470.78  E-value: 1.47e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  674 MDDDTAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGCPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWD 753
Cdd:PTZ00452    1 MQAQYPAVVIDNGSGYCKIGIAGDDAPTSCFPAIVGRSKQNDGIFSTFNKEYYVGEEAQAKRGVLAIKEPIQNGIINSWD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  754 DMEKIWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAMLSLYTSGRTTGIVMDSGDGVT 833
Cdd:PTZ00452   81 DIEIIWHHAFYNELCMSPEDQPVFMTDAPMNSKFNRERMTQIMFETFNTPCLYISNEAVLSLYTSGKTIGLVVDSGEGVT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  834 HTVPIYDGNALPHATLRLDLAGRELTDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMAMVASSSSLEKSY 913
Cdd:PTZ00452  161 HCVPVFEGHQIPQAITKINLAGRLCTDYLTQILQELGYSLTEPHQRIIVKNIKERLCYTALDPQDEKRIYKESNSQDSPY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  914 ELPDGQVITISNEWFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAAL 993
Cdd:PTZ00452  241 KLPDGNILTIKSQKFRCSEILFQPKLIGLEVAGIHHLAYSSIKKCDLDLRQELCRNIVLSGGTTLFPGIANRLSNELTNL 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767919377  994 APSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 1048
Cdd:PTZ00452  321 VPSQLKIQVAAPPDRRFSAWIGGSIQCTLSTQQPQWIKRQEYDEQGPSIVHRKCF 375
ASKHA_NBD_ACTL7 cd10214
nucleotide-binding domain (NBD) of the actin-like protein 7 (ACTL7)-like family; The ...
678-1047 1.33e-155

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: 465.36  E-value: 1.33e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  678 TAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGCPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEK 757
Cdd:cd10214     3 TKAVIIDLGTGYCKAGFAGQPRPSYVISSTVGKPPQESAKTGDNRKETFVGKELANVEPPLKLVNPLRHGIVVDWDCVQD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  758 IWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAMLSLYTSGRTTGIVMDSGDGVTHTVP 837
Cdd:cd10214    83 IWEYIFEKEMKILPEEHAVLVSDPPLSPTTNREKYAELMFETFSIPAMHIAYQSRLSLYSYGRTSGLVVESGHGVSYVVP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  838 IYDGNALPHATLRLDLAGRELTDYLMKILTERGYRFTTmAEREIVRDIKEKLCYVALDFEQEMAMVASSSSLEksYELPD 917
Cdd:cd10214   163 IHEGYNLPHITGRADYAGSDLTAYLMKLLNEAGNKFTD-DQLHIVEDIKKKCCYVALDFEEEMGLPPQEYTVD--YELPD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  918 GQVITISNEWFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSM 997
Cdd:cd10214   240 GHLITIGKERFRCPEMLFNPSLIGSKQPGLHTLTMNSLNKCDANLKKDLAKNILLCGGSTMFDGFPDRFQKELSKLCPND 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 767919377  998 MKIrIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKC 1047
Cdd:cd10214   320 NPI-VAASPERKYSVWTGGSILASLKSFQQLWVRRREYEERGPFVIYRKC 368
PTZ00466 PTZ00466
actin-like protein; Provisional
681-1048 2.00e-154

actin-like protein; Provisional


Pssm-ID: 240426 [Multi-domain]  Cd Length: 380  Bit Score: 462.88  E-value: 2.00e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  681 LVIDNGSGMCKAGFAGDDAPRAVFPSIVGCPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEKIWH 760
Cdd:PTZ00466   15 IIIDNGTGYIKAGFAGEDVPNLVFPSYVGRPKYKRVMAGAVEGNIFVGNKAEEYRGLLKVTYPINHGIIENWNDMENIWI 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  761 HTfYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAMLSLYTSGRTTGIVMDSGDGVTHTVPIYD 840
Cdd:PTZ00466   95 HV-YNSMKINSEEHPVLLTEAPLNPQKNKEKIAEVFFETFNVPALFISIQAILSLYSCGKTNGTVLDCGDGVCHCVSIYE 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  841 GNALPHATLRLDLAGRELTDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEmamvasSSSLEKS-----YEL 915
Cdd:PTZ00466  174 GYSITNTITRTDVAGRDITTYLGYLLRKNGHLFNTSAEMEVVKNMKENCCYVSFNMNKE------KNSSEKAlttlpYIL 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  916 PDGQVITISNEWFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAP 995
Cdd:PTZ00466  248 PDGSQILIGSERYRAPEVLFNPSILGLEYLGLSELIVTSITRADMDLRRTLYSHIVLSGGTTMFHGFGDRLLNEIRKFAP 327
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767919377  996 SMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF 1048
Cdd:PTZ00466  328 KDITIRISAPPERKFSTFIGGSILASLATFKKIWISKQEFDEYGSVILHRKTF 380
ASKHA_NBD_actin-like cd10169
nucleotide-binding domain (NBD) of actin and actin-related proteins (ARPs); Actin is ...
681-1039 2.08e-145

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: 434.61  E-value: 2.08e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  681 LVIDNGSGMCKAGFAGDDAPRAVFPsivgcprqqgmmggmhqkesyvgkeaqskrgiltlkypmehgiitnWDDMEKIWH 760
Cdd:cd10169     1 IVIDNGSGTIKAGFAGEDAPRLIFP----------------------------------------------WDDMEKIWE 34
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  761 HTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAMLSLYTSGRTTGIVMDSGDGVTHTVPIYD 840
Cdd:cd10169    35 HVFYNLLRVDPEEHPVLLTEPPLNPKANREKLAEILFETFNVPSLYIANQAVLSLYASGRTTGLVVDSGEGVTHIVPVYE 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  841 GNALPHATLRLDLAGRELTDYLMKILTERGYRFTTMAEREIVRDIKEKLcyvaldfeqemamvassssleksyelpdgqv 920
Cdd:cd10169   115 GYVLPHAVRRLDIGGRDLTDYLAKLLREKGYSFSTSAEREIVRDIKEKL------------------------------- 163
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  921 itisnewfrcpealfqpcflgmesCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMMKI 1000
Cdd:cd10169   164 ------------------------CGLHELIYDSIMKCDIDLRKELYSNIVLSGGTTLFPGFAERLQKELSKLAPSSVKV 219
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 767919377 1001 RIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESG 1039
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 ...
676-1039 5.91e-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: 410.80  E-value: 5.91e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  676 DDTAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGCP--RQQGMMGGMHQKES----YVGKEA-QSKRGILTLKYPMEHGI 748
Cdd:cd13395     2 DEVGALVLDIGSYSTRAGYAGEDTPKAVFPSVVGVVtdDDDAEDYVGGSGEKkrkyYIGTNSiGVPRPNMEVISPLKDGL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  749 ITNWDDMEKIWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAMLSLYTSGRTTGIVMDS 828
Cdd:cd13395    82 IEDWDAFEKLWDHALKNRLRVDPSEHPLLLTEPSWNTRANREKLTELMFEKYNVPAFFLAKNAVLSAFANGRSTALVVDS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  829 GDGVTHTVPIYDGNALPHATLRLDLAGRELTDYLMKILTERG------YRF---------------------TT-----M 876
Cdd:cd13395   162 GATSTSVVPVHDGYVLQKAIVRSPLGGDFLTDQLLKLLESKNieiiprYMIkskepveggapakytkkdlpnTTssyhrY 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  877 AEREIVRDIKEKLCYVALDFEQEmamVASSSSLEKSYELPDGQVITISNEWFRCPEALFQPCFL---------GMESCGI 947
Cdd:cd13395   242 MVRRVLQDFKESVCQVSDSPFDE---SEAASIPTVSYELPDGYNIEFGAERFKIPELLFDPSLVkgipappseGNELLGL 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  948 HETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMMKIRIIAPPK---RKYSVWVGGSILASLST 1024
Cdd:cd13395   319 PQLVYTSIGSCDVDIRPELYGNVVLTGGNSLLPGFTDRLNRELSEKAPGSLKLKILASGNtveRRFSSWIGGSILASLGS 398
                         410
                  ....*....|....*
gi 767919377 1025 FQQMWISKQEYDESG 1039
Cdd:cd13395   399 FQQMWISKQEYEEHG 413
COG5277 COG5277
Actin-related protein [Cytoskeleton];
680-1038 9.86e-118

Actin-related protein [Cytoskeleton];


Pssm-ID: 444088  Cd Length: 424  Bit Score: 368.73  E-value: 9.86e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  680 VLVIDNGSGMCKAG-FAGDDAP-----RAVFPSIVGCPRQQGMMGGMhQKESYVGKEAQS-----KRGILTLKYPMEHGI 748
Cdd:COG5277    10 VIGIDFGTSYVKYGpIALEEKPrviqtRGLFLRIVGESKLLGPMEGL-SRGLVVGDEVSKylssvRDAIRNLKYPLRDGI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  749 IT-----NWDDMEKIWHHTFYNELRVAPEEHP--ILLTEAPLNPKANREKMTQIMFETF---NTPAMYVAIQAMLSLYTS 818
Cdd:COG5277    89 VRrddedAWRVLKELLRYTFAQFLVVDPEFHGflVVVALSALAPDYMRERLFDIHFEVFseeGAPAVTIIPQPLAVAIAE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  819 GRTTGIVMDSGDGVTHTVPIYDGnALPHATLRLDLAGRELTDYLMKILTERGYRFTTMAEReIVRDIKEKLCYVALDFEQ 898
Cdd:COG5277   169 KAVTCVVVEAGHGNSQVAPISRG-PIREGLVALNRGGAEANAITREILKDRGYSDTAREEY-VVRVVKEALGLVPRDLAK 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  899 EMAMVASS-SSLEKSYELPDGQV-ITISN---EWFRCPEALFQPCFLGMESC----------------------GIHETT 951
Cdd:COG5277   247 AIQKAASNpDSFEAKVRLPNPTVeIELGNyawERFLIGEILFNPNHEGFESYiqqgrlriedavigdvvlygemGLAEAI 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  952 FNSIMKSDVDIRKDLYTNTVLSGGTTMY---PGMA-------HRMQKEIAALAPSmMKIRIIAPPKRKYSVWVGGSILAS 1021
Cdd:COG5277   327 INSIMKCDVEIQDELYSNIILSGGAFNWsvpPGLEdvavdsvTRVQIELSELAPE-LKVNVRLVSDPQYSVWKGAIIYGY 405
                         410
                  ....*....|....*....
gi 767919377 1022 LSTFQQMW--ISKQEYDES 1038
Cdd:COG5277   406 ALPFSVKWswITKEGWYFL 424
PTZ00280 PTZ00280
Actin-related protein 3; Provisional
680-1045 1.95e-103

Actin-related protein 3; Provisional


Pssm-ID: 240343 [Multi-domain]  Cd Length: 414  Bit Score: 330.54  E-value: 1.95e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  680 VLVIDNGSGMCKAGFAGDDAPRAVFPSIVGCPRQQGMM---GGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDME 756
Cdd:PTZ00280    6 VVVIDNGTGYTKMGYAGNTEPTYIIPTLIADNSKQSRRrskKGFEDLDFYIGDEALAASKSYTLTYPMKHGIVEDWDLME 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  757 KIWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAMLSLYTS----------GRTTGIVM 826
Cdd:PTZ00280   86 KFWEQCIFKYLRCEPEEHYFILTEPPMNPPENREYTAEIMFETFNVKGLYIAVQAVLALRASwtskkakelgGTLTGTVI 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  827 DSGDGVTHTVPIYDGNALPHATLRLDLAGRELTDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMAMV--- 903
Cdd:PTZ00280  166 DSGDGVTHVIPVVDGYVIGSSIKHIPLAGRDITNFIQQMLRERGEPIPAEDILLLAQRIKEKYCYVAPDIAKEFEKYdsd 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  904 ---------ASSSSLEKSYElpdgqvITISNEWFRCPEALFQPCFLGME-SCGIHETTFNSIMKSDVDIRKDLYTNTVLS 973
Cdd:PTZ00280  246 pknhfkkytAVNSVTKKPYT------VDVGYERFLGPEMFFHPEIFSSEwTTPLPEVVDDAIQSCPIDCRRPLYKNIVLS 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  974 GGTTMYPGMAHRMQKEI----------------AALAPSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDE 1037
Cdd:PTZ00280  320 GGSTMFKGFDKRLQRDVrkrvdrrlkkaeelsgGKLKPIPIDVNVVSHPRQRYAVWYGGSMLASSPEFEKVCHTKAEYDE 399

                  ....*...
gi 767919377 1038 SGPSIVHR 1045
Cdd:PTZ00280  400 YGPSICRY 407
ASKHA_NBD_Arp3-like cd10221
nucleotide-binding domain (NBD) of actin-related protein3 (Arp3) and similar proteins; Arp3, ...
680-1043 4.06e-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: 329.14  E-value: 4.06e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  680 VLVIDNGSGMCKAGFAGDDAPRAVFPSIVGcPRQQGMMGGMHQKES--------YVGKEAQSKRGILTLKYPMEHGIITN 751
Cdd:cd10221     1 AVVIDNGTGYTKMGYAGNTEPQFIIPTVIA-IKESAKVGDGQRRSKkgiedldfYIGDEALANSPTYALKYPIRHGIVED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  752 WDDMEKIWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAMLSLYTSGRT--------TG 823
Cdd:cd10221    80 WDLMERFWEQCIFKYLRCEPEDHYFLLTEPPLNPPENREYTAEIMFETFNVPGLYIAVQAVLALAASWTSrkvgertlTG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  824 IVMDSGDGVTHTVPIYDGNALPHATLRLDLAGRELTDYLMKILTERGyrFTTMAE--REIVRDIKEKLCYVALDFEQEMA 901
Cdd:cd10221   160 TVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLRERE--EGIPPEdsLEVAKRIKERYCYVCPDIVKEFA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  902 MVASS-SSLEKSYELPD---GQ--VITISNEWFRCPEALFQPCFLGMESC-GIHETTFNSIMKSDVDIRKDLYTNTVLSG 974
Cdd:cd10221   238 KYDSDpAKYIKQYTGINsvtGKpyTVDVGYERFLAPEIFFNPEIASSDFTtPLPEVVDQVIQSCPIDTRRGLYKNIVLSG 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  975 GTTMYPGMAHRMQKEI----------------AALAPSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDES 1038
Cdd:cd10221   318 GSTMFKDFGRRLQRDVkrivdarlkaseelsgGKLKPKPIDVNVISHPMQRYAVWFGGSMLASTPEFYTVCHTKAEYEEY 397

                  ....*
gi 767919377 1039 GPSIV 1043
Cdd:cd10221   398 GPSIC 402
ASKHA_NBD_Arp6 cd10210
nucleotide-binding domain (NBD) of actin-related protein6 (Arp6) and similar proteins; Arp6, ...
680-1039 7.99e-86

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: 7.99e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  680 VLVIDNGSGMCKAGFAGDDAPRaVFPSIVGCPRqqgmmggmHQKESYVGKEAQSK---RGILTLKYPMEHGIITNWDDME 756
Cdd:cd10210     1 TLVLDNGAYTIKAGFASDDPPR-VIPNCIAKPK--------SERRRLFGDDQLDEckdLSGLFYRRPFERGYLVNWDLQR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  757 KIWHHTFYNE-LRVAPEEHPILLTEAPLNPKANREKMTQIMFETFN-------TPAMYVAIQAMLSLYTSGRTTG---IV 825
Cdd:cd10210    72 QIWDHLFGKLlLNVDPSDTALVLTEPPFNPPSIQEAMDEIVFEEYGfqslyrtTAAALSAFAYLADSEQSSSSSSqccLV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  826 MDSGDGVTHTVPIYDGNALPHATLRLDLAGRELTDYLMKILTergYR-FTTMAEREIVRDIKEKLCYVALDFEQEMAmVA 904
Cdd:cd10210   152 VDSGFSFTHIVPFFDGKPVKRAVRRIDVGGKLLTNYLKEIIS---YRqLNVMDETYLVNQIKEDLCFVSTDFYEDLE-IA 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  905 S----SSSLEKSYELPDG-----------------------QVITISNEWFRCPEALFQPCFLGMESCGIHETTFNSIMK 957
Cdd:cd10210   228 KkkgkENTIRRDYVLPDYttskrgyvrdpeepnrgklkedeQVLRLNNERFTVPELLFHPSDIGIQQAGIAEAIVQSINA 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  958 SDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDE 1037
Cdd:cd10210   308 CPEELQPLLYANIVLTGGNALFPGFRERLEAELRSLAPDDYDVNVTLPEDPITYAWEGGSLLAQSPEFEELAVTRAEYEE 387

                  ..
gi 767919377 1038 SG 1039
Cdd:cd10210   388 HG 389
ASKHA_NBD_AtARP7-like cd10209
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 7 and similar ...
681-1044 1.35e-73

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: 247.69  E-value: 1.35e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  681 LVIDNGSGMCKAGFAGDDApravFPSIVGCPRQQGMM-GGMHQKESYVGKEAQskrgiltlkyPMEHGIITNWDDMEKIW 759
Cdd:cd10209     1 VVIDAGSRLLKAGYAYPDR----EPSVVEPTRVTPAVeDGEESDTVVEGNTVS----------PIRRGRIEDWDALEALL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  760 HHTFYNELR-VAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAMLSLYTSGRTTGIVMDSGDGVTHTVPI 838
Cdd:cd10209    67 RYVFYTGLGwEEGNEGQVLIAEPLLTSKAERERLTQLMFETFNVSGLYASEQAVLSLYAVGRISGCVVDVGHGKIDIAPV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  839 YDGNALPHATLRLDLAGRELTDYLMKILTERGyRFTTmAEREIVRDIKEKLCYVAldfEQEMAMVASSSSLEK-SYELPD 917
Cdd:cd10209   147 WEGAIQHNAVRRFEIGGRDLTELLAAELGKSN-PKVK-LDRSIVERLKEAVAWSA---DDEEAYEKKVLTCSPeTYTLPD 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  918 GQVITISNEWFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSM 997
Cdd:cd10209   222 GRVISVGKERYCVGEALFRPSILGIEEYGIVEQLVRAVSTSPSENRRQLLENIVLCGGTSSVPGLEARLQKEIRLLSSPS 301
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767919377  998 MKIRIIAPPK------RKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVH 1044
Cdd:cd10209   302 SRPALVKPPEympentLRYSAWIGGAILAKVVFPQNQHVTKADYDETGPSVVH 354
ASKHA_NBD_Arp5 cd10211
nucleotide-binding domain (NBD) of actin-related protein5 (Arp5) and similar proteins; Arp5, ...
680-1040 1.84e-64

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: 221.68  E-value: 1.84e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  680 VLVIDNGSGMCKAGFAGDDAPRAVFPSIVGCPRQQGMMGGMHQKESYVGKEAQSKrgiLTLKYPMEHGIITNWDDMEKIW 759
Cdd:cd10211     1 PIVIDNGSYQCRAGWAGDKEPRLVFRNLVAKPRDRKKGITVTLVGNDILNDEAVR---SHLRSPFDRNVVTNFDLQEQIL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  760 HHTFyNELRVAPE---EHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAMLSLY----TSGRTTGIVMDSGDGV 832
Cdd:cd10211    78 DYIF-SHLGINSEgsvDHPIVLTEALCNPNYSRQLMSELLFECYGVPSVAYGIDSLFSYYhnqpQGDPSDGLVISSGYST 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  833 THTVPIYDGNALPHATLRLDLAGRELTDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMAMVASSSSLEKs 912
Cdd:cd10211   157 THVIPVLNGRLDLSQCKRINLGGFHATDYLQRLLQLKYPTHPSAITLSRAEELVHEHCYVAEDYDEELKKWEDPEYYEE- 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  913 yelpdgqvitiSNEWFRCPealFqpcflgmescGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAA 992
Cdd:cd10211   236 -----------NVRKIQLP---F----------GLVETIEFVLKRYPAEQQDRLVQNVFLTGGNALFPGLKERLEKELRA 291
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 767919377  993 LAPSMMKIRII--APPkrKYSVWVGGSILASLSTFQQMWISKQEYDESGP 1040
Cdd:cd10211   292 IRPFGSPFNVVraKDP--VLDAWRGAAKWALDSTFEKVWITKQEYEEKGG 339
ASKHA_NBD_ScArp9-like cd10208
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ...
729-1046 7.10e-47

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: 172.11  E-value: 7.10e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  729 KEAQSKRGILtlkYPMEHGIITNWDDMEKIWHHTFYNEL--RVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMY 806
Cdd:cd10208    27 IEIPTRVEII---WPIQDGRVVDWDALEALWRHILFSLLsiPRPTNNSPVLLSVPPSWSKSDLELLTQLFFERLNVPAFA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  807 VAIQAMLSLYTSGRTTGIVMDSGDGVTHTVPIYDGNALPHATLRLDLAGRELTDYLMKILTER--GYRFTTMAEREIVRD 884
Cdd:cd10208   104 ILEAPLAALYAAGATSGIVVDIGHEKTDITPIVDSQVVPHALVSIPIGGQDCTAHLAQLLKSDepELKSQAESGEEATLD 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  885 IKEKLcyvaldFEQEMAMVASSSSleksyELPDGQVITISNEWFRCPEALFQP----CFLGMESCGIHETTFNSimkSDV 960
Cdd:cd10208   184 LAEAL------KKSPICEVLSDGA-----DLASGTEITVGKERFRACEPLFKPsslrVDLLIAAIAGALVLNAS---DEP 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  961 DIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAA--LAPSM----MKIRIIAPPK--------RK----YSVWVGGSILASL 1022
Cdd:cd10208   250 DKRPALWENIIIVGGGSRIRGLKEALLSELQQfhLISETsaspQQPRIIRLAKipdyfpewKKsgyeEAAFLGASIVAKL 329
                         330       340
                  ....*....|....*....|....*...
gi 767919377 1023 sTF----QQMWISKQEYDESGPSIVHRK 1046
Cdd:cd10208   330 -VFndpsSKHYISKVDYNEKGPAAIHTK 356
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
102-359 4.52e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 164.74  E-value: 4.52e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  102 DLDKLHRAAWWGKVARKDLIVMLRDTDVNKQDKQKRTALHLASANGNSGVVKLLLDRRCQLNVLDNKKRTALtkvcssql 181
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLL-------- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  182 yqHEAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVV 261
Cdd:COG0666    92 --HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  262 KFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYKEKQMLKI 341
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
                         250
                  ....*....|....*...
gi 767919377  342 SSENSNPEQDLKLTSEEE 359
Cdd:COG0666   250 KDGLTALLLAAAAGAALI 267
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
100-341 5.17e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 164.36  E-value: 5.17e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  100 REDLDKLHRAAWWGKVARKDLIVMLRDTDVNKQDKQKRTALHLASANGNSGVVKLLLDRRCQLNVLDNKKRTALtkvcss 179
Cdd:COG0666    51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL------ 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  180 qlyqHEAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQ 259
Cdd:COG0666   125 ----HLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  260 VVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYKEKQML 339
Cdd:COG0666   201 IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280

                  ..
gi 767919377  340 KI 341
Cdd:COG0666   281 AL 282
ASKHA_NBD_Arp10 cd10207
nucleotide-binding domain (NBD) of actin-related protein 10 (Arp10) and similar proteins; ...
682-1039 7.66e-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: 7.66e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  682 VIDNGSGMCKAGFAGDDAPRAVFPSIVGCPRQQgmmggmhqKESYVGKeaqsKRGILTLKypmehgiitnWDDM-EKIWH 760
Cdd:cd10207     2 VLDIGSAYTKCGFAGESAPRCIIPSEVKLPGGK--------KVIRVVD----QRSGNEEE----------LYEAlKEFLH 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  761 HTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAMLSLYTSGRTTGIVMDSGDGVTHTVPIYD 840
Cdd:cd10207    60 ELYFKHLLVNPKDRRVVVVESVLCPTPFRETLAKVLFKHFEVPSVLFAPSHLLSLLTLGIRTALVVDCGYRETRVLPVYE 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  841 GNALPHATLRLDLAGRELTDYLMKILTERGYRFTTMAER------------EIVRDIKEKLCYVA-LDFEQEMAMVASSS 907
Cdd:cd10207   140 GVPLLSAWQSTPLGGKALHKRLKKLLLEHATVVTGDNKGqllssvdsllseEVLEDIKVRACFVTsLERGKTLQSATEEG 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  908 SLEKS-------YELPDGQVITISNEWFRCPEALFqpcFLGMESC-GIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMY 979
Cdd:cd10207   220 STEEPsppppvdYPLDGEKILIVPGSIRESAEELL---FEGDNEEkSLPTLILDSLLKCPIDVRKQLAENIVVIGGTSML 296
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767919377  980 PGMAHRMQKEIAAL--------APSMMKIRIIAPP---KRKYSVWVGGSILASLSTFQQMWISKQEYDESG 1039
Cdd:cd10207   297 PGFKHRLLEELRALlrkpkyfeELAPKTFRFHTPPsvfKPNYLAWLGGSIFGALESILGRSLSREAYLQTG 367
ASKHA_NBD_AtArp8-like cd13396
nucleotide-binding domain (NBD) of Arabidopsis thaliana actin-related protein 8 (AtArp8) and ...
762-1039 8.19e-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: 153.47  E-value: 8.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  762 TFYNELRVAPEEHPILLTEaPL-------NPKANREKMTQIMFETF---NTPAMYVAIQAMLSLYTSGRTTGIVMDSGDG 831
Cdd:cd13396    47 TIMTRMQVKPSRQPVVVSL-PLchsddteSAAASRRQLRGTIFNVLfdmNVPAVCAVDQAVLALYAANRTSGIVVNIGFR 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  832 VTHTVPIYDGNALPH-ATLRLDLAGRELTDYLMKILTERGYRFTTMAereIVRDIKEKLCYVALDFEQEMAmvassSSLE 910
Cdd:cd13396   126 VTTIVPVYRGRVMHDiGVEVVGQGALRLTGFLKELMQQNGIRFPSLY---TVRTIKEKLCYVAEDYEAELA-----KDTQ 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  911 KSYELPDGQVITISNEWFRCPEALFQPCFLGMESCGIH-------ETTFNSIMKSDvdirKDLYTNTVLSGGTTMYPGMA 983
Cdd:cd13396   198 ASCEVAGEGWFTLSNERFKTGEILFQPGLGGMRAMGLHqavalcmDHCALVHSQGD----DGWFKTIVLSGGSACLPGLS 273
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767919377  984 HRMQKEIAALAPSMMK--IRIIAPPKRKYSVWVGGSILASLSTFQQMW-ISKQEYDESG 1039
Cdd:cd13396   274 ERLERELRKLLPKSLSegIRIIPPPLGPDSAWQGAKLISNLSNFPDGWcITKKQFRNKP 332
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
106-314 2.15e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.18  E-value: 2.15e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  106 LHRAAWWGKVARKDLIVmLRDTDVNKQDKQKRTALHLASANGNSGVVKLLLDRRCQLNVLDNKKRTALtkvcssqlyqHE 185
Cdd:COG0666    91 LHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL----------HL 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  186 AVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLI 265
Cdd:COG0666   160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 767919377  266 KKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTA 314
Cdd:COG0666   240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
syringactin NF040575
syringactin; Syringactin are close homologs of the normally eukaryotic protein actin, found in ...
976-1047 3.62e-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: 3.62e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767919377  976 TTMYPGMAHRMQKEIAALAPSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKC 1047
Cdd:NF040575   61 RVNESGFYEKLKKSITEKAPKGALIGMTLDPKPESAAWRGAAMYAASEGFVEMAITKQEYDESGPSIVHRKC 132
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
106-282 2.45e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.98  E-value: 2.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  106 LHRAAWWGKVarkDLIVML--RDTDVNKQDKQKRTALHLASANGNSGVVKLLLDRRCQLNVLDNKKRTALtkvcssqlyq 183
Cdd:COG0666   124 LHLAAYNGNL---EIVKLLleAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL---------- 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  184 HEAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKF 263
Cdd:COG0666   191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
                         170
                  ....*....|....*....
gi 767919377  264 LIKKKANLNALDRYGRTAL 282
Cdd:COG0666   271 LLLALLLLAAALLDLLTLL 289
ASKHA_NBD_Arp8-like cd10206
nucleotide-binding domain (NBD) of the actin-related protein 8 (Arp8)-like subfamily; The ...
721-1042 7.10e-24

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: 106.17  E-value: 7.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  721 HQKESYVGKEAQ--SKRGILTLKYPMEHGIItNW-----------DDMEKIWHHTFYNELRVAPEEHP----ILLTEAPL 783
Cdd:cd10206   118 DYPDFLVGEEALrlPPSEEYNLHWPIRRGRL-NVhsdggsltavlDDLEDIWSHALEEKLEIPRKDLKnyraVLVIPDLF 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  784 NpKANREKMTQIMFETFNTPAMYVAIQAMLSLYTSGRTTGIVMDSGDGVTHTVPIYDGNALPHATLRLDLAGRELTDYLM 863
Cdd:cd10206   197 D-RRHVKELVDLLLRRLGFSSVFVHQESVCATFGAGLSSACVVDIGAQKTSVACVEDGLSIPNSRIRLPYGGDDITRCFL 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  864 KILTERG--YRFTTMAER---EIVRDIKEKLCYVALDFeqemamvassssleksyelpDGQVITISNEWFRC-PEALFQp 937
Cdd:cd10206   276 WLLRRSGfpYRECNLNSPldfLLLERLKETYCTLDQDD--------------------IGVQLHEFYVREPGqPTLKYQ- 334
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  938 cflgMESCGIHETTFNSI-MKSDVDIRKDLYTNTVLSGGTTMYPGMA----HRMQKEIAALAPSMMKIRIIAPPKRK--- 1009
Cdd:cd10206   335 ----FKLLPLDEAIVQSIlSCASDELKRKMYSSILLVGGGAKIPGLAealeDRLLIKIPSLFEAVETVEVLPPPKDMdps 410
                         330       340       350
                  ....*....|....*....|....*....|...
gi 767919377 1010 YSVWVGGSILASLSTFQQMWISKQEYDESGPSI 1042
Cdd:cd10206   411 LLAWKGGAVLACLDSAQELWITRKEWQRLGVRA 443
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
162-330 1.14e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.64  E-value: 1.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  162 LNVLDNKKRTALTKVCSSQLYQHEAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESK 241
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  242 NKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSS 321
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                  ....*....
gi 767919377  322 HHHVICQLL 330
Cdd:COG0666   164 GNLEIVKLL 172
ASKHA_NBD_ScArp7-like cd10212
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein7 (Arp7) and ...
681-1036 2.53e-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: 95.17  E-value: 2.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  681 LVIDNGSGMCKAGFAGDDAPRAVFPS-IVGCPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEKIW 759
Cdd:cd10212     6 VVIHNGSHRTVAGFSNVELPQCIIPSsYIKRTDEGGEAEFIFGTYNMIDAAAEKRNGDEVYTLVDSQGLPYNWDALEMQW 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  760 HHTFYNELRVAPEEHPILLTEAPLNPKANR---EKMTQIMFETFNTPAMYVAIQAMLSLYTSGRTTGIVMDSGDGVTHTV 836
Cdd:cd10212    86 RYLYDTQLKVSPEELPLVITMPATNGKPDMailERYYELAFDKLNVPVFQIVIEPLAIALSMGKSSAFVIDIGASGCNVT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  837 PIYDGNALPHATLRLDLAG----------------------------RELTDYLMKILT--------------------E 868
Cdd:cd10212   166 PIIDGIVVKNAVVRSKFGGdfldfqvherlaplikeendmenmadeqKRSTDVWYEASTwiqqfkstmlqvsekdlfelE 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  869 RGYRFTT---MAEREIVRDIKEKLCYVALDFEQEMAMVASSSSLEKsyelPDGQVITIS-NEWFRCPEALFQPCFLGMES 944
Cdd:cd10212   246 RYYKEQAdiyAKQQEQLKQMDQQLQYTALTGSPNNPLVQKKNFLFK----PLNKTLTLDlKECYQFAEYLFKPQLISDKF 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  945 C---GIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSmMKIRIIAPP---KRKYSVWVGGSI 1018
Cdd:cd10212   322 SpedGLGPLMAKSVKKAPEQVYSLLLTNVIITGSTSLIEGMEQRIIKELSIRFPQ-YKLTTFANQvmmDRKIQGWLGALT 400
                         410
                  ....*....|....*....
gi 767919377 1019 LASLSTFQ-QMWISKQEYD 1036
Cdd:cd10212   401 MANLPSWSlGKWYSKEDYE 419
Ank_2 pfam12796
Ankyrin repeats (3 copies);
216-308 3.21e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 3.21e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   216 LHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIkKKANLNALDrYGRTALILAVCCGSASIVS 295
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 767919377   296 LLLEQNIDVSSQD 308
Cdd:pfam12796   79 LLLEKGADINVKD 91
CCDC144C pfam14915
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ...
621-674 2.31e-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: 83.88  E-value: 2.31e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767919377   621 NSMLREEIAMLRLELDTMKHQSQLRKKKYLEDIESVKKKNDNLLKALQLNELTM 674
Cdd:pfam14915    1 NCMLQDEIAMLRLEIDTIKNQNQEKEKKYLEDIEILKEKNDDLQKTLKLNEETL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
140-242 8.44e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 8.44e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   140 LHLASANGNSGVVKLLLDRRCQLNVLDNKKRTALtkvcssqlyqHEAVQCQEDECALMLLEHGtDPNIPDeYGNTTLHYA 219
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTAL----------HLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYA 68
                           90       100
                   ....*....|....*....|...
gi 767919377   220 IYNEDKLMAKALLLYGADIESKN 242
Cdd:pfam12796   69 ARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
121-277 2.07e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 82.79  E-value: 2.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  121 IVMLRDTDVNKQDKQKRTALHLASAN--GNSGVVKLLLDRRCQLNVLDNKKRTALtkvcssqlyqHEAVQCQEDECAL-- 196
Cdd:PHA03100   91 LLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLL----------HLYLESNKIDLKIlk 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  197 ----------------MLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQV 260
Cdd:PHA03100  161 llidkgvdinaknrvnYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI 240
                         170
                  ....*....|....*..
gi 767919377  261 VKFLIKKKANLNALDRY 277
Cdd:PHA03100  241 FKLLLNNGPSIKTIIET 257
PHA03100 PHA03100
ankyrin repeat protein; Provisional
121-333 3.01e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 82.41  E-value: 3.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  121 IVMLrDTDVNKQDKQKRTALHLASANGNSGVVKLLLDRRCQLNVLDNKKRTALTKvcssqLYQHEAVQCQEDECALMLLE 200
Cdd:PHA03100   21 IIME-DDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHY-----LSNIKYNLTDVKEIVKLLLE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  201 HGTDPNIPDEYGNTTLHYAIYN--EDKLMAKALLLYGADIESKNKHGLTPL--LLGVHEQKQQVVKFLIKKKANLNALDR 276
Cdd:PHA03100   95 YGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLhlYLESNKIDLKILKLLIDKGVDINAKNR 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767919377  277 ygrtalilavccgsasiVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDY 333
Cdd:PHA03100  175 -----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDL 214
PHA03095 PHA03095
ankyrin-like protein; Provisional
197-322 3.67e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 82.38  E-value: 3.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  197 MLLEHGTDPNIPDEYGNTTLHYAIYN---EDKLMAKALLLYGADIESKNKHGLTPL-LLGVHEQKQQVVKFLIKKKANLN 272
Cdd:PHA03095   32 RLLAAGADVNFRGEYGKTPLHLYLHYsseKVKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGADVN 111
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767919377  273 ALDRYGRTalILAVCCGSASI----VSLLLEQNIDVSSQDLSGQTAREYAVSSH 322
Cdd:PHA03095  112 AKDKVGRT--PLHVYLSGFNInpkvIRLLLRKGADVNALDLYGMTPLAVLLKSR 163
PHA02878 PHA02878
ankyrin repeat protein; Provisional
114-334 3.89e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 82.62  E-value: 3.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  114 KVARKDLIVMLRDTDVNKQDKQKRTALHlasaNGNSGVVKLLLdrrcqLNVLDNKKRTALTKVCssqlyQHEAVQCQEDE 193
Cdd:PHA02878   83 KLGMKEMIRSINKCSVFYTLVAIKDAFN----NRNVEIFKIIL-----TNRYKNIQTIDLVYID-----KKSKDDIIEAE 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  194 CALMLLEHGTDPNIPDEY-GNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLN 272
Cdd:PHA02878  149 ITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767919377  273 ALDRYGRTALILAVC-CGSASIVSLLLEQNIDVSSQD-LSGQTAREYAVSSHHhvICQLLSDYK 334
Cdd:PHA02878  229 ARDKCGNTPLHISVGyCKDYDILKLLLEHGVDVNAKSyILGLTALHSSIKSER--KLKLLLEYG 290
PHA03100 PHA03100
ankyrin repeat protein; Provisional
117-305 6.74e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.25  E-value: 6.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  117 RKDLIVMLRDT--DVNKQDKQKRTALHLAS-----ANGNSGVVKLLLDRRCQLNVLDNKKRTAL-----TKVCSSQLYQh 184
Cdd:PHA03100   47 NIDVVKILLDNgaDINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLlyaisKKSNSYSIVE- 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  185 eavqcqedecalMLLEHGTDPNIPDEYGNTTLH-YAIYNEDKL-MAKALLL----------------YGADIESKNKHGL 246
Cdd:PHA03100  126 ------------YLLDNGANVNIKNSDGENLLHlYLESNKIDLkILKLLIDkgvdinaknrvnyllsYGVPINIKDVYGF 193
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767919377  247 TPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVS 305
Cdd:PHA03100  194 TPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
Ank_2 pfam12796
Ankyrin repeats (3 copies);
106-209 2.37e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.37  E-value: 2.37e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   106 LHRAAWWGKVarkDLIVML--RDTDVNKQDKQKRTALHLASANGNSGVVKLLLDrRCQLNVlDNKKRTALtkvcssqlyq 183
Cdd:pfam12796    1 LHLAAKNGNL---ELVKLLleNGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNL-KDNGRTAL---------- 65
                           90       100
                   ....*....|....*....|....*.
gi 767919377   184 HEAVQCQEDECALMLLEHGTDPNIPD 209
Cdd:pfam12796   66 HYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
128-301 3.65e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.22  E-value: 3.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  128 DVNKQDKQKRTALH--LASANGNSGVVKLLLDRRCQLNVLDNKKRTAL--------------------------TKVCSS 179
Cdd:PHA03095  109 DVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLavllksrnanvellrllidagadvyaVDDRFR 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  180 QLYQHEAVQCQEDECAL-MLLEHGTDPNIPDEYGNTTLHY-AIYNEDK--LMAKaLLLYGADIESKNKHGLTPLLLGVHE 255
Cdd:PHA03095  189 SLLHHHLQSFKPRARIVrELIRAGCDPAATDMLGNTPLHSmATGSSCKrsLVLP-LLIAGISINARNRYGQTPLHYAAVF 267
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 767919377  256 QKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQN 301
Cdd:PHA03095  268 NNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKN 313
PHA03095 PHA03095
ankyrin-like protein; Provisional
128-327 3.71e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.22  E-value: 3.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  128 DVNKQDKQKRTALHLASANGNS-GVVKLLLDRRCQLNVLDNKKRTALtKVCSSQLYQHEAVqcqedecALMLLEHGTDPN 206
Cdd:PHA03095   75 DVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPL-HVYLSGFNINPKV-------IRLLLRKGADVN 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  207 IPDEYGNTTLHYAIYNEDKLMA--KALLLYGADIESKNKHGLTplLLGVHEQ----KQQVVKFLIKKKANLNALDRYGRT 280
Cdd:PHA03095  147 ALDLYGMTPLAVLLKSRNANVEllRLLIDAGADVYAVDDRFRS--LLHHHLQsfkpRARIVRELIRAGCDPAATDMLGNT 224
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 767919377  281 ALILAVCCGS--ASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVIC 327
Cdd:PHA03095  225 PLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRAC 273
PHA02876 PHA02876
ankyrin repeat protein; Provisional
128-333 4.04e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 76.64  E-value: 4.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  128 DVNKQDKQKRTALHLASANGNSGVVKLLLDRRCQLNVLDNKKRTAL-------------------TKVCSSQLYQHEAVQ 188
Cdd:PHA02876  170 DVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLecavdsknidtikaiidnrSNINKNDLSLLKAIR 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  189 CQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNE--DKLMAKaLLLYGADIESKNKHGLTPL-LLGVHEQKQQVVKFLI 265
Cdd:PHA02876  250 NEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPslSRLVPK-LLERGADVNAKNIKGETPLyLMAKNGYDTENIRTLI 328
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767919377  266 KKKANLNALDRYGRTALILAVCCG-SASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDY 333
Cdd:PHA02876  329 MLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDY 397
PHA02874 PHA02874
ankyrin repeat protein; Provisional
121-332 7.73e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.84  E-value: 7.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  121 IVMLRDTDVNKQDKQKRTALHLASANGNSGVVKLLLDRRCQLNVLDNKKRTAL---TKVCSSQLYQHE----------AV 187
Cdd:PHA02874   20 IIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLltaIKIGAHDIIKLLidngvdtsilPI 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  188 QCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKK 267
Cdd:PHA02874  100 PCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK 179
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767919377  268 KANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSD 332
Cdd:PHA02874  180 GAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINN 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
260-340 1.38e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.67  E-value: 1.38e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   260 VVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEqNIDVSSQDlSGQTAREYAVSSHHHVICQLLSDYKEKQML 339
Cdd:pfam12796   12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINV 89

                   .
gi 767919377   340 K 340
Cdd:pfam12796   90 K 90
PHA02876 PHA02876
ankyrin repeat protein; Provisional
106-333 2.30e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 64.70  E-value: 2.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  106 LHRAAWWGKVARKDLIVMLRDTDVNKQDKQKRTALHLASANG-NSGVVKLLLDRRCQLNVLDNKKRTALTKVCSSQLYQh 184
Cdd:PHA02876  277 LHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNK- 355
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  185 eavqcqedECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQV-VKF 263
Cdd:PHA02876  356 --------DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKT 427
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767919377  264 LIKKKANLNALDRYGRTALILAvCCGSA--SIVSLLLEQNIDVSSQDLSGQTAREYAVSshHHVICQLLSDY 333
Cdd:PHA02876  428 LIDRGANVNSKNKDLSTPLHYA-CKKNCklDVIEMLLDNGADVNAINIQNQYPLLIALE--YHGIVNILLHY 496
PHA02875 PHA02875
ankyrin repeat protein; Provisional
137-303 5.98e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.70  E-value: 5.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  137 RTALHLASANGNSGVVKLLLDRRCQLN-VLDNKKRTALtkvcssqlyqHEAVQCQEDECALMLLEHGTDPNIPDEYGNTT 215
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPL----------HLATILKKLDIMKLLIARGADPDIPNTDKFSP 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  216 LHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGR-TALILAVCCGSASIV 294
Cdd:PHA02875  139 LHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIV 218

                  ....*....
gi 767919377  295 SLLLEQNID 303
Cdd:PHA02875  219 RLFIKRGAD 227
PHA02874 PHA02874
ankyrin repeat protein; Provisional
148-319 1.16e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.90  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  148 NSGVVKLLLDRRCQLNVLDNKKRTALtkvcssqlyqHEAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLM 227
Cdd:PHA02874  103 EKDMIKTILDCGIDVNIKDAELKTFL----------HYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDI 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  228 AKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVcCGSASIVSLLLeQNIDVSSQ 307
Cdd:PHA02874  173 IKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLI-NNASINDQ 250
                         170
                  ....*....|..
gi 767919377  308 DLSGQTAREYAV 319
Cdd:PHA02874  251 DIDGSTPLHHAI 262
PHA02878 PHA02878
ankyrin repeat protein; Provisional
128-253 1.17e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.82  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  128 DVNKQDKQK-RTALHLASANGNSGVVKLLLDRRCQLNVLDNKKRTALTKVCSSQ-------LYQHEAVQCQEDECA---- 195
Cdd:PHA02878  159 DINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYnkpivhiLLENGASTDARDKCGntpl 238
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767919377  196 -------------LMLLEHGTDPNIPDE-YGNTTLHYAIYNEDKLmaKALLLYGADIESKNKHGLTPLLLGV 253
Cdd:PHA02878  239 hisvgyckdydilKLLLEHGVDVNAKSYiLGLTALHSSIKSERKL--KLLLEYGADINSLNSYKLTPLSSAV 308
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
119-277 1.93e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.81  E-value: 1.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  119 DLIVMLRDTDVNkqDKQKRTALHLASANGNSGVVKLLLDRRCQLNVLDNKKRTALTKVCSSQLYQHEAVqcqedecaLML 198
Cdd:PLN03192  543 ELLKAKLDPDIG--DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRI--------LYH 612
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767919377  199 LEHGTDPNIpdeyGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRY 277
Cdd:PLN03192  613 FASISDPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
PHA02875 PHA02875
ankyrin repeat protein; Provisional
184-307 2.09e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.78  E-value: 2.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  184 HEAVQCQEDECALMLLEHGTDPN-IPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVK 262
Cdd:PHA02875   73 HDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIE 152
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 767919377  263 FLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQ--NIDVSSQ 307
Cdd:PHA02875  153 LLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSgaNIDYFGK 199
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
143-316 3.95e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 60.65  E-value: 3.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  143 ASANGNSGVVKLLLDRRCQLNVLDNKKRTALtkvcssqlyqHEAVQCQEDECALMLLEHGTDPNIPDEYGNTTL------ 216
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPL----------HIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisa 601
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  217 -HYAIYNedklmakalLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVS 295
Cdd:PLN03192  602 kHHKIFR---------ILYHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVR 672
                         170       180
                  ....*....|....*....|....*
gi 767919377  296 LLLEQNIDVSS----QDLSGQTARE 316
Cdd:PLN03192  673 LLIMNGADVDKantdDDFSPTELRE 697
PHA02875 PHA02875
ankyrin repeat protein; Provisional
106-272 5.48e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.62  E-value: 5.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  106 LHRAAWWGKVARKDLIVMLRDTDVNKQDKQKRTALHLASANGNSGVVKLLLDRRCQLNVLDNKKRTALtkvcssqlyqHE 185
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL----------HL 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  186 AVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHG-LTPLLLGVHEQKQQVVKFL 264
Cdd:PHA02875  142 AVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLF 221

                  ....*...
gi 767919377  265 IKKKANLN 272
Cdd:PHA02875  222 IKRGADCN 229
PHA02876 PHA02876
ankyrin repeat protein; Provisional
185-313 6.85e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.08  E-value: 6.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  185 EAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFL 264
Cdd:PHA02876  151 ERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAI 230
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767919377  265 IKKKANL-----------------------------NALDRYGRTALILAVCCGSAS-IVSLLLEQNIDVSSQDLSGQT 313
Cdd:PHA02876  231 IDNRSNInkndlsllkairnedletslllydagfsvNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGET 309
PHA02875 PHA02875
ankyrin repeat protein; Provisional
186-332 1.15e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.46  E-value: 1.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  186 AVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESK-NKHGLTPLLLGVHEQKQQVVKFL 264
Cdd:PHA02875   42 AMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLL 121
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  265 IKKKA--NLNALDRYgrTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSD 332
Cdd:PHA02875  122 IARGAdpDIPNTDKF--SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLD 189
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
134-313 3.50e-08

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: 57.33  E-value: 3.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  134 KQKRTA---LHLASANGNSGVVK-LLLDRRCqlnvlDNKKR-----TALtkvcssqlyqHEAVQCQEDECALMLLEhgTD 204
Cdd:cd22192    12 QQKRISespLLLAAKENDVQAIKkLLKCPSC-----DLFQRgalgeTAL----------HVAALYDNLEAAVVLME--AA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  205 P---NIP---DEY-GNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLtplllgvheqkqqvvkFLIKKKANLNaldRY 277
Cdd:cd22192    75 PelvNEPmtsDLYqGETALHIAVVNQNLNLVRELIARGADVVSPRATGT----------------FFRPGPKNLI---YY 135
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 767919377  278 GRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQT 313
Cdd:cd22192   136 GEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171
ASKHA_NBD_MamK cd24009
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ...
688-892 7.94e-08

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: 55.29  E-value: 7.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  688 GMCKAGFAGDDAPRAVFPSIVGCPRqqGMMGGMHQKESYV-GKEAQSKRGILTLKYPMEHGIITNWDDmekiwhhtfyNE 766
Cdd:cd24009     9 GTSRSAVVTSRGKRFSFRSVVGYPK--DIIARKLLGKEVLfGDEALENRLALDLRRPLEDGVIKEGDD----------RD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  767 LRVAPE--EHPILLTEAPLNPK-------------ANREKMTQIMFETFNTpAMYVAiQAMLSLYTSGRTTG-IVMDSGD 830
Cdd:cd24009    77 LEAAREllQHLIELALPGPDDEiyavigvparasaENKQALLEIARELVDG-VMVVS-EPFAVAYGLDRLDNsLIVDIGA 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767919377  831 GVTHTVPIYdgNALPHAT--LRLDLAGRELTDYLMKILTER--GYRFTtmaeREIVRDIKEKLCYV 892
Cdd:cd24009   155 GTTDLCRMK--GTIPTEEdqITLPKAGDYIDEELVDLIKERypEVQLT----LNMARRWKEKYGFV 214
Ank_5 pfam13857
Ankyrin repeats (many copies);
198-249 8.22e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.65  E-value: 8.22e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767919377   198 LLEHGT-DPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPL 249
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
186-335 2.48e-07

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: 54.70  E-value: 2.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   186 AVQCQEDECALMLLEHGTDPNIpdeyGNTTLHyAIYNEDKLMAKALLLYGADIESKNK--------------HGLTPLLL 251
Cdd:TIGR00870   60 AIENENLELTELLLNLSCRGAV----GDTLLH-AISLEYVDAVEAILLHLLAAFRKSGplelandqytseftPGITALHL 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   252 GVHEQKQQVVKFLIKKKANLNA--------------LDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREY 317
Cdd:TIGR00870  135 AAHRQNYEIVKLLLERGASVPAracgdffvksqgvdSFYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHL 214
                          170
                   ....*....|....*...
gi 767919377   318 AVsshhhVICQLLSDYKE 335
Cdd:TIGR00870  215 LV-----MENEFKAEYEE 227
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
135-268 3.01e-07

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: 54.63  E-value: 3.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  135 QKRTALHLASANGNSGVVKLLLDRRCQLNvldnKKR---TALTKVCSSQLYQHEAV----QCQEDECAL-MLLEHGTDPN 206
Cdd:cd22192    88 QGETALHIAVVNQNLNLVRELIARGADVV----SPRatgTFFRPGPKNLIYYGEHPlsfaACVGNEEIVrLLIEHGADIR 163
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767919377  207 IPDEYGNTTLHYAIYNEDKLMAKAL--LLYGADIES--------KNKHGLTPLLLGVHEQKQQVVKFLIKKK 268
Cdd:cd22192   164 AQDSLGNTVLHILVLQPNKTFACQMydLILSYDKEDdlqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
Ank_4 pfam13637
Ankyrin repeats (many copies);
245-298 4.10e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 4.10e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767919377   245 GLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLL 298
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
128-173 7.54e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 7.54e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 767919377   128 DVNKQDKQKRTALHLASANGNSGVVKLLLDRRCQLNVLDNKKRTAL 173
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA03100 PHA03100
ankyrin repeat protein; Provisional
199-334 8.94e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.75  E-value: 8.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  199 LEHGTDPNIPDEYgnTTLHYAI--YNEDKLmaKALLLYGADIESKNKHGLTPLLLGVHEQKQQ-----VVKFLIKKKANL 271
Cdd:PHA03100   24 EDDLNDYSYKKPV--LPLYLAKeaRNIDVV--KILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANV 99
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767919377  272 NALDRYGRTALILAVCC--GSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHV--ICQLLSDYK 334
Cdd:PHA03100  100 NAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKG 166
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
106-268 1.23e-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: 52.57  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  106 LHRAAWWGKVARKDLIVML----RDTDVNKQ-------DK--QKRTALHLASANGNSGVVKLLLDRRCQLNVLDNK---K 169
Cdd:cd21882    30 LHKAALNLNDGVNEAIMLLleaaPDSGNPKElvnapctDEfyQGQTALHIAIENRNLNLVRLLVENGADVSARATGrffR 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  170 RTALTKVCSSQLYQHEAVQCQEDECALMLLEHGTDP---NIPDEYGNTTLHYAIYNEDKL---------MAKALLLYGAD 237
Cdd:cd21882   110 KSPGNLFYFGELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNTVLHALVLQADNTpensafvcqMYNLLLSYGAH 189
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767919377  238 I-------ESKNKHGLTPLLLGVHEQKQQVVKFLIKKK 268
Cdd:cd21882   190 LdptqqleEIPNHQGLTPLKLAAVEGKIVMFQHILQRE 227
Ank_4 pfam13637
Ankyrin repeats (many copies);
106-156 1.32e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 1.32e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767919377   106 LHRAAWWGKVarkDLIVMLRDT--DVNKQDKQKRTALHLASANGNSGVVKLLL 156
Cdd:pfam13637    5 LHAAAASGHL---ELLRLLLEKgaDINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
229-314 1.48e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.95  E-value: 1.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  229 KALLLYGADIESKNKHGLTPLLLGVH---EQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGS-ASIVSLLLEQNIDV 304
Cdd:PHA03095   31 RRLLAAGADVNFRGEYGKTPLHLYLHyssEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADV 110
                          90
                  ....*....|
gi 767919377  305 SSQDLSGQTA 314
Cdd:PHA03095  111 NAKDKVGRTP 120
Ank_4 pfam13637
Ankyrin repeats (many copies);
193-232 5.36e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 5.36e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 767919377   193 ECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALL 232
Cdd:pfam13637   15 ELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
282-349 7.67e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.11  E-value: 7.67e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767919377   282 LILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYKEKQM-------LKISSENSNPE 349
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLkdngrtaLHYAARSGHLE 75
Ank_5 pfam13857
Ankyrin repeats (many copies);
269-318 9.57e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 9.57e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 767919377   269 ANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYA 318
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
212-265 2.12e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 2.12e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767919377   212 GNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLI 265
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
184-327 3.31e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 47.74  E-value: 3.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  184 HEAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLL--YGADI-ESKNKHGLTPlLLGVHEQKQQV 260
Cdd:PHA02946   77 HIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERINLLvqYGAKInNSVDEEGCGP-LLACTDPSERV 155
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767919377  261 VKFLIKKKANLNALDRYGRTALILAVCCGS--ASIVSLLLEQNIDVSSQDLSGQTAReyavsshhHVIC 327
Cdd:PHA02946  156 FKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPDHDGNTPL--------HIVC 216
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
224-311 3.66e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 3.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  224 DKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNID 303
Cdd:PTZ00322   94 DAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173

                  ....*...
gi 767919377  304 VSSQDLSG 311
Cdd:PTZ00322  174 HFELGANA 181
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
195-266 4.41e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 4.41e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767919377  195 ALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIK 266
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PHA02798 PHA02798
ankyrin-like protein; Provisional
120-336 1.07e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.98  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  120 LIVMLRDTDVNKQDKQKRTALHLASANG---NSGVVKLLLDRRCQLNVLDNKKRTALtkvcssQLYQHEAVQCQEDECAL 196
Cdd:PHA02798   93 KILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFMIENGADTTLLDKDGFTML------QVYLQSNHHIDIEIIKL 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  197 mLLEHGTDPN-IPDEYGNTTLH-YAIYN---------------------EDKLMAKALLLY------------------- 234
Cdd:PHA02798  167 -LLEKGVDINtHNNKEKYDTLHcYFKYNidridadilklfvdngfiinkENKSHKKKFMEYlnsllydnkrfkknildfi 245
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  235 --GADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQ 312
Cdd:PHA02798  246 fsYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNKNTISYTYY 325
                         250       260
                  ....*....|....*....|....
gi 767919377  313 TAREYAVSSHHHVICQLLSDYKEK 336
Cdd:PHA02798  326 KLRKHILNVEGDFINQLEFDIIKK 349
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
153-313 2.76e-04

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: 44.87  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  153 KLLLDRRCQLNVLDNK--KRTALTKVC--SSQLYQHEAVqcqeDECALMLLEHGTDPNIP---------DEY--GNTTLH 217
Cdd:cd21882     3 ELLGLLECLRWYLTDSayQRGATGKTClhKAALNLNDGV----NEAIMLLLEAAPDSGNPkelvnapctDEFyqGQTALH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  218 YAIYNEDKLMAKALLLYGADIESKNKhgltplllGVHEQKQQVVKFLikkkanlnaldrYGRTALILAVCCGSASIVSLL 297
Cdd:cd21882    79 IAIENRNLNLVRLLVENGADVSARAT--------GRFFRKSPGNLFY------------FGELPLSLAACTNQEEIVRLL 138
                         170
                  ....*....|....*....
gi 767919377  298 LE---QNIDVSSQDLSGQT 313
Cdd:cd21882   139 LEngaQPAALEAQDSLGNT 157
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
261-333 3.51e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.50  E-value: 3.51e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767919377  261 VKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDY 333
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
138-268 4.44e-04

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: 44.30  E-value: 4.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   138 TALHLASANGNSGVVKLLLDR------RCQLNVLDNKKRTALTKVCSSQLYQHEAVQcQEDECALmLLEHGTDPNIPDEY 211
Cdd:TIGR00870  130 TALHLAAHRQNYEIVKLLLERgasvpaRACGDFFVKSQGVDSFYHGESPLNAAACLG-SPSIVAL-LSEDPADILTADSL 207
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767919377   212 GNTTLHYAIYNED------KL---MAKALLLYGADIESK-------NKHGLTPLLLGVHEQKQQVVKFLIKKK 268
Cdd:TIGR00870  208 GNTLLHLLVMENEfkaeyeELscqMYNFALSLLDKLRDSkelevilNHQGLTPLKLAAKEGRIVLFRLKLAIK 280
Ank_5 pfam13857
Ankyrin repeats (many copies);
155-219 5.44e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 5.44e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767919377   155 LLDRR-CQLNVLDNKKRTALtkvcssqlyqHEAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYA 219
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPL----------HVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
137-167 6.85e-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: 6.85e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 767919377   137 RTALHLASA-NGNSGVVKLLLDRRCQLNVLDN 167
Cdd:pfam00023    3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
211-243 6.85e-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: 6.85e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 767919377   211 YGNTTLHYAIYNEDKL-MAKALLLYGADIESKNK 243
Cdd:pfam00023    1 DGNTPLHLAAGRRGNLeIVKLLLSKGADVNARDK 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
253-323 1.14e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.74  E-value: 1.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767919377  253 VHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHH 323
Cdd:PHA02876  153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN 223
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
343-580 1.43e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 42.68  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   343 SENSNPEQdlkltSEEESQRFKGSENSQPEKMSQEPEINKDGDREVEEEMKKHESNNVGLLENLSNGVTAGNGDDGLIPQ 422
Cdd:TIGR00927  655 AEGENGEE-----SGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEGTEDE 729
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   423 RKSRTPENQQFPDNESE---EYHRICELVSDYKEKQMPKYSSENSNPEQDLKLTSEEESQRLKGSEnGQPEKRSQEPEIN 499
Cdd:TIGR00927  730 GEIETGEEGEEVEDEGEgeaEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEMKGDE-GAEGKVEHEGETE 808
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377   500 KDGDRELENFMAIEEMKKHGSTHVGFPE-NLTNGATAGNGDDGLIPPRKSRTPESQQFPDTENEEYHSDEQNDTQKQFCE 578
Cdd:TIGR00927  809 AGEKDEHEGQSETQADDTEVKDETGEQElNAENQGEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEE 888

                   ..
gi 767919377   579 EQ 580
Cdd:TIGR00927  889 EN 890
PHA02946 PHA02946
ankyin-like protein; Provisional
198-351 1.55e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 42.35  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  198 LLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPL--LLGVHEQKQQVVKFLIKKKANL-NAL 274
Cdd:PHA02946   58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINLLVQYGAKInNSV 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  275 DRYGRTALiLAVCCGSASIVSLLLEQNIDVSSQDLSGQtareyavsshHHVICQLLSDYKEKQ----MLKISSENSNPEQ 350
Cdd:PHA02946  138 DEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGK----------NHIHRHLMSDNPKAStiswMMKLGISPSKPDH 206

                  .
gi 767919377  351 D 351
Cdd:PHA02946  207 D 207
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
233-313 1.98e-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: 42.05  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  233 LYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDR--------------YGRTALILAVCCGSASIVSLLL 298
Cdd:cd22194   129 FINAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLALAACTNQPEIVQLLM 208
                          90
                  ....*....|....*.
gi 767919377  299 EQ-NIDVSSQDLSGQT 313
Cdd:cd22194   209 EKeSTDITSQDSRGNT 224
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
277-308 2.16e-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: 2.16e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 767919377   277 YGRTALILAVC-CGSASIVSLLLEQNIDVSSQD 308
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02798 PHA02798
ankyrin-like protein; Provisional
197-305 2.66e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.74  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  197 MLLEHGTDPNIPDEYGNTTL-----HYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHE---QKQQVVKFLIKKK 268
Cdd:PHA02798   56 LFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENG 135
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 767919377  269 ANLNALDRYGRTALILAV---CCGSASIVSLLLEQNIDVS 305
Cdd:PHA02798  136 ADTTLLDKDGFTMLQVYLqsnHHIDIEIIKLLLEKGVDIN 175
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
135-164 4.77e-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: 35.64  E-value: 4.77e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 767919377    135 QKRTALHLASANGNSGVVKLLLDRRCQLNV 164
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
211-239 6.22e-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: 6.22e-03
                            10        20
                    ....*....|....*....|....*....
gi 767919377    211 YGNTTLHYAIYNEDKLMAKALLLYGADIE 239
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
264-494 7.16e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 40.24  E-value: 7.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  264 LIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYkekqmlkisS 343
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF---------A 614
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919377  344 ENSNPEQ--DLKLTSEEesqrfKGSENSQPEKMSQEPEI---NKDGDREVEEEMKKHESNNVGLLenLSNG--VTAGNGD 416
Cdd:PLN03192  615 SISDPHAagDLLCTAAK-----RNDLTAMKELLKQGLNVdseDHQGATALQVAMAEDHVDMVRLL--IMNGadVDKANTD 687
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767919377  417 DGLIPQRKSRTPEnqqfpdnESEEYHRIceLVSDYKEKQMPKYSSENSNPEQDLKLTSEEESQRLKGS-ENGQPEKRSQ 494
Cdd:PLN03192  688 DDFSPTELRELLQ-------KRELGHSI--TIVDSVPADEPDLGRDGGSRPGRLQGTSSDNQCRPRVSiYKGHPLLRNE 757
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
137-164 7.67e-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: 34.93  E-value: 7.67e-03
                           10        20
                   ....*....|....*....|....*...
gi 767919377   137 RTALHLASANGNSGVVKLLLDRRCQLNV 164
Cdd:pfam13606    3 NTPLHLAARNGRLEIVKLLLENGADINA 30
 
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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