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Conserved domains on  [gi|1046900658|ref|XP_017451222|]
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dixin isoform X5 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DIX pfam00778
DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in ...
 523-598 1.45e-36

DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in homo- and hetero-oligomerization. It is involved in the homo- oligomerization of mouse axin. The axin DIX domain also interacts with the dishevelled DIX domain. The DIX domain has also been called the DAX domain.


:

Pssm-ID: 459936  Cd Length: 77  Bit Score: 130.72  E-value: 1.45e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046900658 523 TKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDREGSHRYHFKALDPEFGTVKEEVFHDDDAIPGWEGKIVAWV 598
Cdd:pfam00778   2 TKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 77
CH_SF super family cl00030
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 1-48 1.06e-26

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


The actual alignment was detected with superfamily member cd21213:

Pssm-ID: 469584  Cd Length: 107  Bit Score: 104.30  E-value: 1.06e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1046900658   1 MKSNVERVLQFVASKNIRMHQTSAKDIVEGNLKSIMRLVLALAAHFKP 48
Cdd:cd21213    60 RKENVEKVLQFMASKRIRMHQTSAKDIVDGNLKAIMRLILALAAHFKP 107
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 201-395 8.63e-08

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 8.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 201 EEQLLEQQEHLEKEMEEAKKMISGLQALLLngslpEDEQERpvalcepgvnpeeqlIIIRSRLDQSMEENQDLKKELLKC 280
Cdd:COG1196   339 LEELEEELEEAEEELEEAEAELAEAEEALL-----EAEAEL---------------AEAEEELEELAEELLEALRAAAEL 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 281 KQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKDLGQKDRLLQQQQAK 360
Cdd:COG1196   399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1046900658 361 LEDALRKLSDASYQ-----QVDLERELEQKDVLLAHRVKG 395
Cdd:COG1196   479 LAELLEELAEAAARlllllEAEADYEGFLEGVKAALLLAG 518
 
Name Accession Description Interval E-value
DIX pfam00778
DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in ...
 523-598 1.45e-36

DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in homo- and hetero-oligomerization. It is involved in the homo- oligomerization of mouse axin. The axin DIX domain also interacts with the dishevelled DIX domain. The DIX domain has also been called the DAX domain.


Pssm-ID: 459936  Cd Length: 77  Bit Score: 130.72  E-value: 1.45e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046900658 523 TKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDREGSHRYHFKALDPEFGTVKEEVFHDDDAIPGWEGKIVAWV 598
Cdd:pfam00778   2 TKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 77
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
 1-48 1.06e-26

calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409062  Cd Length: 107  Bit Score: 104.30  E-value: 1.06e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1046900658   1 MKSNVERVLQFVASKNIRMHQTSAKDIVEGNLKSIMRLVLALAAHFKP 48
Cdd:cd21213    60 RKENVEKVLQFMASKRIRMHQTSAKDIVDGNLKAIMRLILALAAHFKP 107
DAX smart00021
Domain present in Dishevelled and axin; Domain of unknown function.
 523-599 2.79e-19

Domain present in Dishevelled and axin; Domain of unknown function.


Pssm-ID: 197474  Cd Length: 83  Bit Score: 82.46  E-value: 2.79e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046900658  523 TKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDREGsHRYHFKALDPEF-GTVKEEVFHDDDAIPGWEGKIVAWVE 599
Cdd:smart00021   4 TKVIYHLDDEETPYLVKVPVPAERVTLGDFKEVLTKKN-YKYYFKSMDDDFgGVVKEEIRDDSARLPCFNGRVVSWLV 80
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 201-395 8.63e-08

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 8.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 201 EEQLLEQQEHLEKEMEEAKKMISGLQALLLngslpEDEQERpvalcepgvnpeeqlIIIRSRLDQSMEENQDLKKELLKC 280
Cdd:COG1196   339 LEELEEELEEAEEELEEAEAELAEAEEALL-----EAEAEL---------------AEAEEELEELAEELLEALRAAAEL 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 281 KQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKDLGQKDRLLQQQQAK 360
Cdd:COG1196   399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1046900658 361 LEDALRKLSDASYQ-----QVDLERELEQKDVLLAHRVKG 395
Cdd:COG1196   479 LAELLEELAEAAARlllllEAEADYEGFLEGVKAALLLAG 518
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 201-391 2.65e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 2.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658  201 EEQLLEQQEHLEKEMEEAKKMISGLQALL--LNGSLPEDEQERpVALCEPGVNPEEQLIIIRSRLDQSMEENQDLKKELL 278
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELEERLeeAEEELAEAEAEI-EELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658  279 KCKQEARNLQGIKDALQQRLT--QQDTSVLQLKQELLRANMDkdelhnqnvDLQRKLDERNRLLGEYKKDLGQKDRLLQQ 356
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEdlEEQIEELSEDIESLAAEIE---------ELEELIEELESELEALLNERASLEEALAL 891

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1046900658  357 QQAKLEDALRKLSDASYQQVDLERELEQKDVLLAH 391
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQ 926
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 205-402 2.80e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 50.50  E-value: 2.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658  205 LEQQEHLEKEMEEAKKMISGLQALLLNGSLPEDEQERPVALCEPGVNPEEQLI--------IIRSRLDQSMEENQDLKKE 276
Cdd:pfam15921  460 LEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIeatnaeitKLRSRVDLKLQELQHLKNE 539

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658  277 llkcKQEARNLQGIKDALQQRLTQQDTSVLQLKQELlrANMDK---------DELHNQNVDLQRKLDERNRLLGEYKKDL 347
Cdd:pfam15921  540 ----GDHLRNVQTECEALKLQMAEKDKVIEILRQQI--ENMTQlvgqhgrtaGAMQVEKAQLEKEINDRRLELQEFKILK 613

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046900658  348 GQKDRLLQQQQAKLED---ALRKLSDASYQQVDLERELEQKDVLLAHRVKGDTDEVTN 402
Cdd:pfam15921  614 DKKDAKIRELEARVSDlelEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNS 671
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 4-47 9.88e-04

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 39.19  E-value: 9.88e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1046900658   4 NVERVLQFVASK-NIRMHQTSAKDIVEGNLKSIMRLVLALAAHFK 47
Cdd:pfam00307  64 NINLALDVAEKKlGVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQ 108
 
Name Accession Description Interval E-value
DIX pfam00778
DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in ...
 523-598 1.45e-36

DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in homo- and hetero-oligomerization. It is involved in the homo- oligomerization of mouse axin. The axin DIX domain also interacts with the dishevelled DIX domain. The DIX domain has also been called the DAX domain.


Pssm-ID: 459936  Cd Length: 77  Bit Score: 130.72  E-value: 1.45e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046900658 523 TKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDREGSHRYHFKALDPEFGTVKEEVFHDDDAIPGWEGKIVAWV 598
Cdd:pfam00778   2 TKVIYYLCDEPVPYRIKIHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGTVKEEITDDDDILPLWEGKIVAKV 77
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
 1-48 1.06e-26

calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409062  Cd Length: 107  Bit Score: 104.30  E-value: 1.06e-26
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1046900658   1 MKSNVERVLQFVASKNIRMHQTSAKDIVEGNLKSIMRLVLALAAHFKP 48
Cdd:cd21213    60 RKENVEKVLQFMASKRIRMHQTSAKDIVDGNLKAIMRLILALAAHFKP 107
DAX smart00021
Domain present in Dishevelled and axin; Domain of unknown function.
 523-599 2.79e-19

Domain present in Dishevelled and axin; Domain of unknown function.


Pssm-ID: 197474  Cd Length: 83  Bit Score: 82.46  E-value: 2.79e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046900658  523 TKVLYFTDRSLTPFMVNIPKRLGEVTLKDFKAAIDREGsHRYHFKALDPEF-GTVKEEVFHDDDAIPGWEGKIVAWVE 599
Cdd:smart00021   4 TKVIYHLDDEETPYLVKVPVPAERVTLGDFKEVLTKKN-YKYYFKSMDDDFgGVVKEEIRDDSARLPCFNGRVVSWLV 80
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 201-395 8.63e-08

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 8.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 201 EEQLLEQQEHLEKEMEEAKKMISGLQALLLngslpEDEQERpvalcepgvnpeeqlIIIRSRLDQSMEENQDLKKELLKC 280
Cdd:COG1196   339 LEELEEELEEAEEELEEAEAELAEAEEALL-----EAEAEL---------------AEAEEELEELAEELLEALRAAAEL 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 281 KQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKDLGQKDRLLQQQQAK 360
Cdd:COG1196   399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1046900658 361 LEDALRKLSDASYQ-----QVDLERELEQKDVLLAHRVKG 395
Cdd:COG1196   479 LAELLEELAEAAARlllllEAEADYEGFLEGVKAALLLAG 518
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 201-384 1.61e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 201 EEQLLEQQEHLEKEMEEAKKMISGLQALLLNGSLPEDEQERPVALCEPGVNPEEQLII-IRSRLDQSMEENQDLKKELLK 279
Cdd:COG1196   255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReLEERLEELEEELAELEEELEE 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 280 CKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKDLGQKDRLLQQQQA 359
Cdd:COG1196   335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414

                         170       180
                  ....*....|....*....|....*
gi 1046900658 360 KLEDALRKLSDASYQQVDLERELEQ 384
Cdd:COG1196   415 RLERLEEELEELEEALAELEEEEEE 439
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
 1-46 2.23e-07

calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.


Pssm-ID: 409061  Cd Length: 105  Bit Score: 49.50  E-value: 2.23e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1046900658   1 MKSNVERVLQFVASKNIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 46
Cdd:cd21212    60 KLENIQACLQFLAALGVDVQGITAEDIVDGNLKAILGLFFSLSRYK 105
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 202-391 8.95e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 8.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 202 EQLLEQQEHLEKEMEEAKKMISGLQALLlngslpedeQERpvalcepgvnpEEQLIIIRSRLDQSMEENQDLKKELLKCK 281
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAEL---------AEL-----------EAELEELRLELEELELELEEAQAEEYELL 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 282 QEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKDLGQKDRLLQQQQAKL 361
Cdd:COG1196   295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                         170       180       190
                  ....*....|....*....|....*....|
gi 1046900658 362 EDALRKLSDASYQQVDLERELEQKDVLLAH 391
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELAAQLEE 404
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 201-391 2.65e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 2.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658  201 EEQLLEQQEHLEKEMEEAKKMISGLQALL--LNGSLPEDEQERpVALCEPGVNPEEQLIIIRSRLDQSMEENQDLKKELL 278
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELEERLeeAEEELAEAEAEI-EELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658  279 KCKQEARNLQGIKDALQQRLT--QQDTSVLQLKQELLRANMDkdelhnqnvDLQRKLDERNRLLGEYKKDLGQKDRLLQQ 356
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEdlEEQIEELSEDIESLAAEIE---------ELEELIEELESELEALLNERASLEEALAL 891

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1046900658  357 QQAKLEDALRKLSDASYQQVDLERELEQKDVLLAH 391
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQ 926
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 205-402 2.80e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 50.50  E-value: 2.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658  205 LEQQEHLEKEMEEAKKMISGLQALLLNGSLPEDEQERPVALCEPGVNPEEQLI--------IIRSRLDQSMEENQDLKKE 276
Cdd:pfam15921  460 LEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIeatnaeitKLRSRVDLKLQELQHLKNE 539

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658  277 llkcKQEARNLQGIKDALQQRLTQQDTSVLQLKQELlrANMDK---------DELHNQNVDLQRKLDERNRLLGEYKKDL 347
Cdd:pfam15921  540 ----GDHLRNVQTECEALKLQMAEKDKVIEILRQQI--ENMTQlvgqhgrtaGAMQVEKAQLEKEINDRRLELQEFKILK 613

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046900658  348 GQKDRLLQQQQAKLED---ALRKLSDASYQQVDLERELEQKDVLLAHRVKGDTDEVTN 402
Cdd:pfam15921  614 DKKDAKIRELEARVSDlelEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNS 671
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
253-383 4.70e-06

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 49.63  E-value: 4.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 253 EEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRL---------TQQDTSVLQLKQELLRANMDKDEL- 322
Cdd:COG3206   204 KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLgsgpdalpeLLQSPVIQQLRAQLAELEAELAELs 283

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046900658 323 ------HNQNVDLQRKLD--------ERNRLLGEYKKD---LGQKDRLLQQQQAKLEDALRKLSDASYQQVDLERELE 383
Cdd:COG3206   284 arytpnHPDVIALRAQIAalraqlqqEAQRILASLEAEleaLQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
202-385 5.47e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.53  E-value: 5.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658  202 EQLLEQQEHL---EKEMEEAKKMISGLQALLLNGSLPEDEQERpvalcepgvnpEEQLIIIRSRLD--QSMEENQDLKKE 276
Cdd:COG4913    228 DALVEHFDDLeraHEALEDAREQIELLEPIRELAERYAAARER-----------LAELEYLRAALRlwFAQRRLELLEAE 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658  277 LLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMD-KDELHNQNVDLQRKLDERNRLLGEYKKDLGQKD---- 351
Cdd:COG4913    297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGlplp 376

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1046900658  352 ----------RLLQQQQAKLEDALRKLSDASYQQVDLERELEQK 385
Cdd:COG4913    377 asaeefaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 201-385 3.56e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 3.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658  201 EEQLLEQQEHLEKEMEEAKKMISGLQALL--LNGSLpEDEQERPVALCEPGVNPEEQLIIIRSRLDQ-------SMEENQ 271
Cdd:TIGR02169  310 IAEKERELEDAEERLAKLEAEIDKLLAEIeeLEREI-EEERKRRDKLTEEYAELKEELEDLRAELEEvdkefaeTRDELK 388

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658  272 DLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDErnrllgeykkdlgqKD 351
Cdd:TIGR02169  389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK--------------QE 454

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1046900658  352 RLLQQQQAKLEDALRKLSDASYQQVDLERELEQK 385
Cdd:TIGR02169  455 WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 211-384 3.82e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 3.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658  211 LEKEMEEAKKMISGLQALLLNGSLPEDEQERPVAlcepgvnpEEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGI 290
Cdd:TIGR02168  218 LKAELRELELALLVLRLEELREELEELQEELKEA--------EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658  291 KDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKDLGQKDRLLQQQQAKLEDALRKLSD 370
Cdd:TIGR02168  290 LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369

                          170
                   ....*....|....
gi 1046900658  371 ASYQQVDLERELEQ 384
Cdd:TIGR02168  370 LESRLEELEEQLET 383
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 202-420 6.93e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.53  E-value: 6.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 202 EQLLEQQEHLEKEMEEAKKMISGLQALL--LNGSLPEDEQERPVAlcepgvnpEEQLIIIRSRLDQSMEENQDLKKELLK 279
Cdd:COG4942    30 EQLQQEIAELEKELAALKKEEKALLKQLaaLERRIAALARRIRAL--------EQELAALEAELAELEKEIAELRAELEA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 280 CKQEARNL------QGIKDALQQRLTQQDTS------------VLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLG 341
Cdd:COG4942   102 QKEELAELlralyrLGRQPPLALLLSPEDFLdavrrlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 342 EYKKDLGQKDRLLQQQQAKLEDALRKLSDASYQQVDLERELEQKDVLLAH--RVKGDTDEVTNYNSHSSQRNGFVLPVAG 419
Cdd:COG4942   182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARleAEAAAAAERTPAAGFAALKGKLPWPVSG 261


                  .
gi 1046900658 420 R 420
Cdd:COG4942   262 R 262
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 3-39 1.81e-04

first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409063  Cd Length: 105  Bit Score: 41.22  E-value: 1.81e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1046900658   3 SNVERVLQFVASKNIRMHQTSAKDIVEGNLKSIMRLV 39
Cdd:cd21214    64 ANVNKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMI 100
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
 4-47 1.88e-04

first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409035  Cd Length: 107  Bit Score: 41.21  E-value: 1.88e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1046900658   4 NVERVLQFVASKNIRMHQTSAKDIVEGNLKSIMRLVLALAAHFK 47
Cdd:cd21186    62 NVNRALQVLEQNNVKLVNISSNDIVDGNPKLTLGLVWSIILHWQ 105
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 243-390 3.83e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.28  E-value: 3.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 243 VALCEPGVNPEEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMD---- 318
Cdd:COG3883     5 ALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEieer 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 319 KDELHNQNVDLQRK-----------------------------LDERNRLLGEYKKDLGQKDRLLQQQQAKLEDALRKLS 369
Cdd:COG3883    85 REELGERARALYRSggsvsyldvllgsesfsdfldrlsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164

                         170       180
                  ....*....|....*....|.
gi 1046900658 370 DASYQQVDLERELEQKDVLLA 390
Cdd:COG3883   165 ELEAAKAELEAQQAEQEALLA 185
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 202-383 4.80e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 43.27  E-value: 4.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 202 EQLLEQQEHLEKEMEEAKKMISGLQALLLN-----GSLPE--DEQERPValcepgvnpeEQLIIIRSRLDQS-MEENQDL 273
Cdd:pfam10174 404 ENLQEQLRDKDKQLAGLKERVKSLQTDSSNtdtalTTLEEalSEKERII----------ERLKEQREREDRErLEELESL 473

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 274 KKELLKCKQEArnlqgikDALQQRLTQQDTSVLQLKQEL--LRANMDKDELHNQNVD--LQRKLDERNRLLGEYKK---- 345
Cdd:pfam10174 474 KKENKDLKEKV-------SALQPELTEKESSLIDLKEHAssLASSGLKKDSKLKSLEiaVEQKKEECSKLENQLKKahna 546

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1046900658 346 --------DLGQKDRLLQQQQAkledalRKLSDASYQQVDLERELE 383
Cdd:pfam10174 547 eeavrtnpEINDRIRLLEQEVA------RYKEESGKAQAEVERLLG 586
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
249-402 5.81e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 5.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658  249 GVNPEEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSV---------LQLKQEL--LRANM 317
Cdd:COG4913    605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvasaereiAELEAELerLDASS 684

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658  318 DK--------DELHNQNVDLQRKLDERNRLLGEYKKDLGQKDRLLQQQQAKLEDA-------LRKLSDASYQQVDLEREL 382
Cdd:COG4913    685 DDlaaleeqlEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAedlarleLRALLEERFAAALGDAVE 764

                          170       180
                   ....*....|....*....|
gi 1046900658  383 EQKDVLLAHRVKGDTDEVTN 402
Cdd:COG4913    765 RELRENLEERIDALRARLNR 784
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 202-376 5.96e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 5.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658  202 EQLLEQQEHLEKEMEEAKKMISGLQAlllngSLPEDEQERPVALCEPGVNpEEQLIIIRSRLDQSMEENQDLKKELLKCK 281
Cdd:TIGR02168  841 EDLEEQIEELSEDIESLAAEIEELEE-----LIEELESELEALLNERASL-EEALALLRSELEELSEELRELESKRSELR 914

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658  282 QEARNLQGIKDALQQRLTQQDTSVLQLKQELL-RANMDKD---ELHNQNVDLQRKLDERNRLLGEYKKDLG--------- 348
Cdd:TIGR02168  915 RELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEeaeALENKIEDDEEEARRRLKRLENKIKELGpvnlaaiee 994

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1046900658  349 ---QKDRL--LQQQQAKLEDALRKLSDA--------------SYQQV 376
Cdd:TIGR02168  995 yeeLKERYdfLTAQKEDLTEAKETLEEAieeidrearerfkdTFDQV 1041
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 4-46 8.25e-04

first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409077  Cd Length: 108  Bit Score: 39.39  E-value: 8.25e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1046900658   4 NVERVLQFVASKNIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 46
Cdd:cd21228    66 NVSVALEFLERESIKLVSIDSSAIVDGNLKLILGLIWTLILHY 108
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
192-372 8.26e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 8.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 192 PGTYLEATWE-EQLLEQQEHLEKEMEEAKKMISGLQALLLNGSLPEDEQERpvalcepgvnpEEQLIIIRSRLD---QSM 267
Cdd:COG4717    87 EEEYAELQEElEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL-----------EAELAELPERLEeleERL 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 268 EENQDLKKELLKCKQEARNLQGIKDALQQRLTqqdtsvLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKDL 347
Cdd:COG4717   156 EELRELEEELEELEAELAELQEELEELLEQLS------LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229

                         170       180
                  ....*....|....*....|....*..
gi 1046900658 348 GQ--KDRLLQQQQAKLEDALRKLSDAS 372
Cdd:COG4717   230 EQleNELEAAALEERLKEARLLLLIAA 256
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 4-47 9.88e-04

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 39.19  E-value: 9.88e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1046900658   4 NVERVLQFVASK-NIRMHQTSAKDIVEGNLKSIMRLVLALAAHFK 47
Cdd:pfam00307  64 NINLALDVAEKKlGVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQ 108
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 4-46 1.01e-03

first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409064  Cd Length: 107  Bit Score: 38.92  E-value: 1.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1046900658   4 NVERVLQFVASKNIRMHQTSAKDIVEGNLKSIMRLVLALAAHF 46
Cdd:cd21215    65 NVNKALEFIKSRGVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
253-384 1.16e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 253 EEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRK 332
Cdd:COG4372    44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1046900658 333 LDERNRLLGEYKKDLGQKDRLLQQQQAKLEDALRKLSDASYQQVDLERELEQ 384
Cdd:COG4372   124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA 175
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 260-390 1.83e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 260 RSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRL 339
Cdd:COG4942    26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046900658 340 LGE-----YK-------------KDLGQKDR-------LLQQQQAKLEDALRKLSDASYQQVDLERELEQKDVLLA 390
Cdd:COG4942   106 LAEllralYRlgrqpplalllspEDFLDAVRrlqylkyLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 197-394 2.43e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.11  E-value: 2.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658  197 EATWEEQLLEQQEHLEKEMEEAKKMISGLQAL---------LLNGSLPEDEQERPvaLCEPGVNPEEQLIIIRSRLDQSM 267
Cdd:TIGR00618  544 EEDVYHQLTSERKQRASLKEQMQEIQQSFSILtqcdnrskeDIPNLQNITVRLQD--LTEKLSEAEDMLACEQHALLRKL 621

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658  268 EE---NQDLKKELLKCKQEARNLQGIKDALQQRLTQQDtsvlqLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYK 344
Cdd:TIGR00618  622 QPeqdLQDVRLHLQQCSQELALKLTALHALQLTLTQER-----VREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWK 696

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1046900658  345 KDLGQKDRLLQQQQAKLEDALRKLSDASYQQVDLERELEQKDVLLAHRVK 394
Cdd:TIGR00618  697 EMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLK 746
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
202-371 3.02e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 3.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658  202 EQLLEQQEHLEKEMEEAKKMISGLQALLlngslpeDEQERPVALCEPGVNPEEQLIIIRS-------------RLDQSME 268
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAEL-------DALQERREALQRLAEYSWDEIDVASaereiaeleaeleRLDASSD 685

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658  269 ENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDEL-HNQNVDLQRKLDERNRLLGEYKKdL 347
Cdd:COG4913    686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAeDLARLELRALLEERFAAALGDAV-E 764

                          170       180
                   ....*....|....*....|....
gi 1046900658  348 GQKDRLLQQQQAKLEDALRKLSDA 371
Cdd:COG4913    765 RELRENLEERIDALRARLNRAEEE 788
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
200-375 4.06e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.51  E-value: 4.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 200 WEEQLLEQQEHLEKEMEEAKKMISGlqalllngslpedeqerpvalcepgvnpEEQLIIIRSRLDQSMEENQDLKKELLK 279
Cdd:COG1340   134 EEKELVEKIKELEKELEKAKKALEK----------------------------NEKLKELRAELKELRKEAEEIHKKIKE 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 280 CKQEArnlQGIKDALQQRLTQQDtsvlQLKQELlranmdkDELHNQNVDLQRKLDERNRLLGEYKKDLGQKDRLLQQQQA 359
Cdd:COG1340   186 LAEEA---QELHEEMIELYKEAD----ELRKEA-------DELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRK 251

                         170
                  ....*....|....*.
gi 1046900658 360 KLEDALRKLSDASYQQ 375
Cdd:COG1340   252 KQRALKREKEKEELEE 267
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 266-390 4.15e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 4.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 266 SMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKK 345
Cdd:COG1579     1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1046900658 346 DLGQ--KDRLLQQQQAKLEDALRKLSDASYQQVDLERELEQKDVLLA 390
Cdd:COG1579    81 QLGNvrNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELA 127
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
 1-43 4.60e-03

calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409135  Cd Length: 105  Bit Score: 36.93  E-value: 4.60e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1046900658   1 MKSNVERVLQFVASKNIRMHQTSAKDIVEGNLKSIMRLVLALA 43
Cdd:cd21286    60 MIENVDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSLS 102
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
209-384 5.33e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 5.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 209 EHLEKEMEEAKKmISGLQALLLNGSLPEDEQERPVALCEpgvnpEEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQ 288
Cdd:COG4717    49 ERLEKEADELFK-PQGRKPELNLKELKELEEELKEAEEK-----EEEYAELQEELEELEEELEELEAELEELREELEKLE 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 289 GIKDALQQRLTQQdtsvlQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKDLGQKDRLLQQ----QQAKLEDA 364
Cdd:COG4717   123 KLLQLLPLYQELE-----ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQlslaTEEELQDL 197

                         170       180
                  ....*....|....*....|
gi 1046900658 365 LRKLSDASYQQVDLERELEQ 384
Cdd:COG4717   198 AEELEELQQRLAELEEELEE 217
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 201-384 6.00e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.94  E-value: 6.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658  201 EEQLLEQQEHLEKEMEEAKKMISGL----QALllngslpeDEQ--------------ERPVALCE-PGVNPE---EQLII 258
Cdd:COG3096    374 AEQLAEAEARLEAAEEEVDSLKSQLadyqQAL--------DVQqtraiqyqqavqalEKARALCGlPDLTPEnaeDYLAA 445

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658  259 IRSRLDQSMEENQDLKKEL---------------LKCK-----------QEARNLqgIKDALQQRLTQQDTSvlQLKQEL 312
Cdd:COG3096    446 FRAKEQQATEEVLELEQKLsvadaarrqfekayeLVCKiageversqawQTAREL--LRRYRSQQALAQRLQ--QLRAQL 521

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046900658  313 LRAnmdKDELHNQNvDLQRKLDERNRLLGEYKKDLGQKDRLLQQQQAKLEDALRKLSDASYQQVDLERELEQ 384
Cdd:COG3096    522 AEL---EQRLRQQQ-NAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQ 589
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
253-390 7.45e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 7.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 253 EEQLIIIRSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRK 332
Cdd:COG4372    51 REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658 333 LDERNRLLGEYKKDLGQKDRLLQQQQAKLEDALRKLS--DASYQQVDLERELEQKDVLLA 390
Cdd:COG4372   131 RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAalEQELQALSEAEAEQALDELLK 190
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 4-47 7.84e-03

first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409037  Cd Length: 105  Bit Score: 36.23  E-value: 7.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1046900658   4 NVERVLQFVASKNIRMHQTSAKDIVEGNLKSIMRLVLALAAHFK 47
Cdd:cd21188    62 NVQTALDFLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
196-400 8.55e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 8.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658  196 LEATWEE--QLLEQQEHLEKEMEEAKKMISGLQALLLNGSLPEDEQERPVAlcepgvnpEEQLIIIRSRLDQSMEENQDL 273
Cdd:COG4913    257 IRELAERyaAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARL--------EAELERLEARLDALREELDEL 328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046900658  274 KKELLK--------CKQEARNLQGIKDALQQRLTQQDTSVLQLKqelLRANMDKDELHNQNVDLQRKLDERNRLLGEYKK 345
Cdd:COG4913    329 EAQIRGnggdrleqLEREIERLERELEERERRRARLEALLAALG---LPLPASAEEFAALRAEAAALLEALEEELEALEE 405

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1046900658  346 DLGQKDRLLQQQQAKLEDALRKLSDASYQQVDLERELEQKDVLLAHRVKGDTDEV 400
Cdd:COG4913    406 ALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAEL 460
 
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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