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Conserved domains on  [gi|755548253|ref|XP_011243356|]
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rho GTPase-activating protein 22 isoform X14 [Mus musculus]

Protein Classification

Rho GTPase-activating protein( domain architecture ID 1569)

Rho GTPase-activating protein for Rho/Rac/Cdc42-like small GTPases that act as molecular switches, active in their GTP-bound form but inactive when bound to GDP

CATH:  1.10.555.10
Gene Ontology:  GO:0007165|GO:0005096
PubMed:  17222083|12480336
SCOP:  4001255

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RhoGAP super family cl02570
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 1-47 3.08e-23

RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like small GTPases. Small GTPases (G proteins) cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when bound to GDP. The Rho family of small G proteins, which includes Cdc42Hs, activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. G proteins generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude. The RhoGAPs are one of the major classes of regulators of Rho G proteins.


The actual alignment was detected with superfamily member cd04390:

Pssm-ID: 470621 [Multi-domain]  Cd Length: 199  Bit Score: 95.97  E-value: 3.08e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 755548253   1 MSVQNLATVFGPNILRPQIEDPVTIMEGTSLVQHLMTVLIRKHGQLF 47
Cdd:cd04390  153 MSVQNLATVFGPNILRPKVEDPATIMEGTPQIQQLMTVMISKHEPLF 199
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 286-374 8.93e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.13  E-value: 8.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253   286 QAHVRRCRALQGQVAEL---RAELCQQRTEYKRSLKSIEEGSADLRKQMSRLEEELDQERKKYAMLEIKLRNSERAREDA 362
Cdd:TIGR02168  305 QILRERLANLERQLEELeaqLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384

                           90
                   ....*....|..
gi 755548253   363 ERRNQLLQREME 374
Cdd:TIGR02168  385 RSKVAQLELQIA 396
 
Name Accession Description Interval E-value
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 1-47 3.08e-23

RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP22, 24 and 25-like proteins; longer isoforms of these proteins contain an additional N-terminal pleckstrin homology (PH) domain. ARHGAP25 (KIA0053) has been identified as a GAP for Rac1 and Cdc42. Short isoforms (without the PH domain) of ARHGAP24, called RC-GAP72 and p73RhoGAP, and of ARHGAP22, called p68RacGAP, has been shown to be involved in angiogenesis and endothelial cell capillary formation. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239855 [Multi-domain]  Cd Length: 199  Bit Score: 95.97  E-value: 3.08e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 755548253   1 MSVQNLATVFGPNILRPQIEDPVTIMEGTSLVQHLMTVLIRKHGQLF 47
Cdd:cd04390  153 MSVQNLATVFGPNILRPKVEDPATIMEGTPQIQQLMTVMISKHEPLF 199
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 286-374 8.93e-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: 48.13  E-value: 8.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253   286 QAHVRRCRALQGQVAEL---RAELCQQRTEYKRSLKSIEEGSADLRKQMSRLEEELDQERKKYAMLEIKLRNSERAREDA 362
Cdd:TIGR02168  305 QILRERLANLERQLEELeaqLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384

                           90
                   ....*....|..
gi 755548253   363 ERRNQLLQREME 374
Cdd:TIGR02168  385 RSKVAQLELQIA 396
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 300-376 2.42e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 2.42e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755548253 300 AELRAELCQQRTEYKRSLKSIEEGSADLRKQMSRLEEELDQERKKYAMLEIKLRNSERAREDAERRNQLLQREMEEF 376
Cdd:COG1196  308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 1-43 5.39e-05

GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases. etter domain limits and outliers.


Pssm-ID: 214618  Cd Length: 174  Bit Score: 43.41  E-value: 5.39e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 755548253     1 MSVQNLATVFGPNILRPQIEDPVTIMEgTSLVQHLMTVLIRKH 43
Cdd:smart00324 133 MTARNLAIVFGPTLLRPPDGEVASLKD-IRHQNTVIEFLIENA 174
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
 293-375 2.42e-04

Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.


Pssm-ID: 463600 [Multi-domain]  Cd Length: 139  Bit Score: 41.01  E-value: 2.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253  293 RALQGQVAELRAELCQQRTEYKRSLKSIEEGsadLRKQMSRLEEELD-------QERKKYAMLEIKLRNSERAREDAERR 365
Cdd:pfam12474  40 KLEQRQTQELRRLPKRIRAEQKKRLKMFRES---LKQEKKELKQEVEklpkfqrKEAKRQRKEELELEQKHEELEFLQAQ 116

                          90
                  ....*....|
gi 755548253  366 NQLLQREMEE 375
Cdd:pfam12474 117 SEALERELQQ 126
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 1-18 9.27e-04

RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.


Pssm-ID: 459875  Cd Length: 148  Bit Score: 39.45  E-value: 9.27e-04
                          10
                  ....*....|....*...
gi 755548253    1 MSVQNLATVFGPNILRPQ 18
Cdd:pfam00620 130 MNAHNLAIVFGPTLLRPP 147
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
294-375 1.21e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253 294 ALQGQVAELRAELCQQRTEYKRSLKSIEEgsadLRKQMSRLEEELDQERKKYAMLEIKLRNSERAREDAERRNQLLQREM 373
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAHNEEAES----LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393


                 ..
gi 755548253 374 EE 375
Cdd:PRK02224 394 EE 395
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 293-367 2.09e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 37.16  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253 293 RALQGQVAELRAELcqqrTEYKRSLKSIEEGSADLRKQMSRLEEELDQERKKYAMLEIKLR-----NSE-------RARE 360
Cdd:cd22887    7 QELEKRLAELEAEL----ASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRklqeeNDElverwmaKKQQ 82


                 ....*..
gi 755548253 361 DAERRNQ 367
Cdd:cd22887   83 EADKMNE 89
 
Name Accession Description Interval E-value
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 1-47 3.08e-23

RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP22, 24 and 25-like proteins; longer isoforms of these proteins contain an additional N-terminal pleckstrin homology (PH) domain. ARHGAP25 (KIA0053) has been identified as a GAP for Rac1 and Cdc42. Short isoforms (without the PH domain) of ARHGAP24, called RC-GAP72 and p73RhoGAP, and of ARHGAP22, called p68RacGAP, has been shown to be involved in angiogenesis and endothelial cell capillary formation. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239855 [Multi-domain]  Cd Length: 199  Bit Score: 95.97  E-value: 3.08e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 755548253   1 MSVQNLATVFGPNILRPQIEDPVTIMEGTSLVQHLMTVLIRKHGQLF 47
Cdd:cd04390  153 MSVQNLATVFGPNILRPKVEDPATIMEGTPQIQQLMTVMISKHEPLF 199
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 286-374 8.93e-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: 48.13  E-value: 8.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253   286 QAHVRRCRALQGQVAEL---RAELCQQRTEYKRSLKSIEEGSADLRKQMSRLEEELDQERKKYAMLEIKLRNSERAREDA 362
Cdd:TIGR02168  305 QILRERLANLERQLEELeaqLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384

                           90
                   ....*....|..
gi 755548253   363 ERRNQLLQREME 374
Cdd:TIGR02168  385 RSKVAQLELQIA 396
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 1-40 1.21e-05

RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in KIAA1688-like proteins; KIAA1688 is a protein of unknown function that contains a RhoGAP domain and a myosin tail homology 4 (MyTH4) domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239854  Cd Length: 187  Bit Score: 45.46  E-value: 1.21e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 755548253   1 MSVQNLATVFGPNILRPQIEDPVTIMEGTSLVQHLMTVLI 40
Cdd:cd04389  146 MDVSNLAMVFAPNILRCTSDDPRVIFENTRKEMSFLRTLI 185
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 300-376 2.42e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 2.42e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755548253 300 AELRAELCQQRTEYKRSLKSIEEGSADLRKQMSRLEEELDQERKKYAMLEIKLRNSERAREDAERRNQLLQREMEEF 376
Cdd:COG1196  308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 286-376 3.49e-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: 46.20  E-value: 3.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253   286 QAHVRRCRALQGQVAELRAELCQQRTEYKRSLKSIEEGSA---DLRKQMSRLEEELDQERKKYAMLEIKLRNSERAREDA 362
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESkldELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370

                           90
                   ....*....|....
gi 755548253   363 ERRNQLLQREMEEF 376
Cdd:TIGR02168  371 ESRLEELEEQLETL 384
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 1-43 5.39e-05

GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases. etter domain limits and outliers.


Pssm-ID: 214618  Cd Length: 174  Bit Score: 43.41  E-value: 5.39e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 755548253     1 MSVQNLATVFGPNILRPQIEDPVTIMEgTSLVQHLMTVLIRKH 43
Cdd:smart00324 133 MTARNLAIVFGPTLLRPPDGEVASLKD-IRHQNTVIEFLIENA 174
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
293-375 1.48e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 1.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253 293 RALQGQVAELRAELCQQRTEykrsLKSIEEGSADLRKQMSRLEEELDQERKKYAMLEIKLRNSERAREDAERRNQLLQRE 372
Cdd:COG4372   41 DKLQEELEQLREELEQAREE----LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEE 116


                 ...
gi 755548253 373 MEE 375
Cdd:COG4372  117 LEE 119
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 1-39 1.54e-04

RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like small GTPases. Small GTPases (G proteins) cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when bound to GDP. The Rho family of small G proteins, which includes Cdc42Hs, activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. G proteins generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude. The RhoGAPs are one of the major classes of regulators of Rho G proteins.


Pssm-ID: 238090 [Multi-domain]  Cd Length: 169  Bit Score: 41.90  E-value: 1.54e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 755548253   1 MSVQNLATVFGPNILRPQIEDPVTIMEGTSLVQHLMTVL 39
Cdd:cd00159  129 MTASNLAIVFAPTLLRPPDSDDELLEDIKKLNEIVEFLI 167
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
286-388 1.56e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253 286 QAHVRRCRALQGQVAELRAELCQQRTEYK-----RSLKSIEEGSADLRKQMSRLEEELDQERKKYAMLEIKLRNSERARE 360
Cdd:COG4717   84 EEKEEEYAELQEELEELEEELEELEAELEelreeLEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEE 163

                         90       100
                 ....*....|....*....|....*...
gi 755548253 361 DAERRNQLLQREMEEFFSTLGSLTTGTK 388
Cdd:COG4717  164 ELEELEAELAELQEELEELLEQLSLATE 191
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
 293-375 2.42e-04

Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.


Pssm-ID: 463600 [Multi-domain]  Cd Length: 139  Bit Score: 41.01  E-value: 2.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253  293 RALQGQVAELRAELCQQRTEYKRSLKSIEEGsadLRKQMSRLEEELD-------QERKKYAMLEIKLRNSERAREDAERR 365
Cdd:pfam12474  40 KLEQRQTQELRRLPKRIRAEQKKRLKMFRES---LKQEKKELKQEVEklpkfqrKEAKRQRKEELELEQKHEELEFLQAQ 116

                          90
                  ....*....|
gi 755548253  366 NQLLQREMEE 375
Cdd:pfam12474 117 SEALERELQQ 126
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
293-374 2.50e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.08  E-value: 2.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253 293 RALQGQVAELRAELcqqRTEYKRSLKSIEEGSADLRKQMSRLEEELDQERKKYAML---EIKLRNSERAREDAERR-NQL 368
Cdd:COG3206  294 IALRAQIAALRAQL---QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELyESL 370


                 ....*.
gi 755548253 369 LQREME 374
Cdd:COG3206  371 LQRLEE 376
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 290-376 2.74e-04

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: 42.22  E-value: 2.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253 290 RRCRALQGQVAELRAELcqqrTEYKRSLKSIEEGSADLRKQMSRLEEELDQERKKYAMLEIKLRNSERARE--------- 360
Cdd:COG1579   24 HRLKELPAELAELEDEL----AALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyealqkeie 99

                         90
                 ....*....|....*.
gi 755548253 361 DAERRNQLLQREMEEF 376
Cdd:COG1579  100 SLKRRISDLEDEILEL 115
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
293-375 3.19e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 3.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253 293 RALQGQVAELRAELCQQRTEYKRSLKSIEEgsadLRKQMSRLEEELDQERKKYAMLEIKLRNSERAREDAERRNQLLQRE 372
Cdd:COG4372   90 QAAQAELAQAQEELESLQEEAEELQEELEE----LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165


                 ...
gi 755548253 373 MEE 375
Cdd:COG4372  166 LAA 168
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 300-385 3.64e-04

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 40.37  E-value: 3.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253  300 AELRAELCQQRT-EYKRSLKSIEEGSADLRKQMSRLEEELDQERKKYAMLEIKLRNSERAREDAE---RRNQLLQREMEE 375
Cdd:pfam12718  12 AQERAEELEEKVkELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNEnltRKIQLLEEELEE 91

                          90
                  ....*....|
gi 755548253  376 FFSTLGSLTT 385
Cdd:pfam12718  92 SDKRLKETTE 101
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
295-380 5.22e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 5.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253 295 LQGQVAELRAELCQQRTEYKR---SLKSIEEGS--ADLRKQMSRLEEELDQERKKYAMLEIKLRNSERAREDAERRNQ-- 367
Cdd:COG4717  437 LEEELEELEEELEELREELAEleaELEQLEEDGelAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLpp 516

                         90
                 ....*....|...
gi 755548253 368 LLQReMEEFFSTL 380
Cdd:COG4717  517 VLER-ASEYFSRL 528
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
293-375 7.65e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 7.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253 293 RALQGQVAELRAELCQQRTEYKRSLKSIEEgsadLRKQMSRLEEELDQERKKYAMLEIKLRNSERAREDAERRNQLLQRE 372
Cdd:COG4372   48 EQLREELEQAREELEQLEEELEQARSELEQ----LEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123


                 ...
gi 755548253 373 MEE 375
Cdd:COG4372  124 RQD 126
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 303-376 8.66e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 38.75  E-value: 8.66e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755548253  303 RAElcQQRTEYKRSLKSIEEgsadlrkQMSRLEEELDQERKKYAMLEIKLRNSERAREDAERRNQLLQREMEEF 376
Cdd:pfam20492   3 EAE--REKQELEERLKQYEE-------ETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERL 67
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 1-18 9.27e-04

RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.


Pssm-ID: 459875  Cd Length: 148  Bit Score: 39.45  E-value: 9.27e-04
                          10
                  ....*....|....*...
gi 755548253    1 MSVQNLATVFGPNILRPQ 18
Cdd:pfam00620 130 MNAHNLAIVFGPTLLRPP 147
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
287-375 9.44e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 9.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253 287 AHVRRCRALQGQVAELRAELCQQRTEYKRSLK-----SIEEGSADLRKQMSRLEEELDQERKKYAMLEIKLrnsERARED 361
Cdd:COG4717  392 EQAEEYQELKEELEELEEQLEELLGELEELLEaldeeELEEELEELEEELEELEEELEELREELAELEAEL---EQLEED 468

                         90
                 ....*....|....
gi 755548253 362 AERRNQLLQREMEE 375
Cdd:COG4717  469 GELAELLQELEELK 482
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 295-375 1.04e-03

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: 41.20  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253   295 LQGQVAELRAELCQQRTEYKRSLKSIEEGSAD----------LRKQMSRLEEELDQERKKYAMLEIKLRNSERAREDAER 364
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQieqlkeelkaLREALDELRAELTLLNEEAANLRERLESLERRIAATER 838

                           90
                   ....*....|.
gi 755548253   365 RNQLLQREMEE 375
Cdd:TIGR02168  839 RLEDLEEQIEE 849
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
294-375 1.21e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253 294 ALQGQVAELRAELCQQRTEYKRSLKSIEEgsadLRKQMSRLEEELDQERKKYAMLEIKLRNSERAREDAERRNQLLQREM 373
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAHNEEAES----LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393


                 ..
gi 755548253 374 EE 375
Cdd:PRK02224 394 EE 395
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 298-385 1.22e-03

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 38.32  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253  298 QVAELRAELCQQRTEYKRSLKSIEEGSADLRKQMSRLEEEL---DQERKKYamlEIKLRNSERAREDAERRNQLLQREME 374
Cdd:pfam13863   7 EMFLVQLALDAKREEIERLEELLKQREEELEKKEQELKEDLikfDKFLKEN---DAKRRRALKKAEEETKLKKEKEKEIK 83

                          90
                  ....*....|.
gi 755548253  375 EFFSTLGSLTT 385
Cdd:pfam13863  84 KLTAQIEELKS 94
THOC7 pfam05615
Tho complex subunit 7; The Tho complex is involved in transcription elongation and mRNA export ...
 308-365 1.59e-03

Tho complex subunit 7; The Tho complex is involved in transcription elongation and mRNA export from the nucleus.


Pssm-ID: 461692 [Multi-domain]  Cd Length: 135  Bit Score: 38.40  E-value: 1.59e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755548253  308 QQRTEYKRSLKSIEEGSADLRKQMSRLEEELDQERKKYAM-----LEIKLRNSERAREDAERR 365
Cdd:pfam05615  72 RERENYEAEKEEIEEEIEAVREEIEELKERLEEAKRTRKNreeydALAEKINENPSREETEKQ 134
PRK09039 PRK09039
peptidoglycan -binding protein;
294-391 1.63e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 40.33  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253 294 ALQGQVAELRAELCQQRTEYKRSLKSIE---EGSADLRKQMSRLEEELDQERKKYAMLEIKLRNSERAREDA-ERRNQLL 369
Cdd:PRK09039 113 AAEGRAGELAQELDSEKQVSARALAQVEllnQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVAlAQRVQEL 192

                         90       100
                 ....*....|....*....|..
gi 755548253 370 QREMEEFFSTLGSLTTGTKGSR 391
Cdd:PRK09039 193 NRYRSEFFGRLREILGDREGIR 214
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 286-375 1.75e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 1.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253 286 QAHVRRCRALQGQVAELRAELCQQRTEYKRSLKSIEEGSADLR---KQMSRLEEELDQERKKYAMLEIKLRNSERAREDA 362
Cdd:COG1196  249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellAELARLEQDIARLEERRRELEERLEELEEELAEL 328

                         90
                 ....*....|...
gi 755548253 363 ERRNQLLQREMEE 375
Cdd:COG1196  329 EEELEELEEELEE 341
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 290-383 1.97e-03

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: 40.43  E-value: 1.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253   290 RRCRALQGQVAELRAELCQQRTEY----------KRSLKSIEEGSADLRKQMSRLEEELDQERKKYAMLEIKLRNSERAR 359
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLeslerriaatERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER 882

                           90       100
                   ....*....|....*....|....
gi 755548253   360 EDAERRNQLLQREMEEFFSTLGSL 383
Cdd:TIGR02168  883 ASLEEALALLRSELEELSEELREL 906
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 301-375 2.09e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.90  E-value: 2.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755548253  301 ELRAELCQQRTEYKRSLKSIEEgsadLRKQMsRLEEELDQERKKYAMLEIKLRNSERAREDAERRNQL-LQREMEE 375
Cdd:pfam13868 205 ELRAKLYQEEQERKERQKEREE----AEKKA-RQRQELQQAREEQIELKERRLAEEAEREEEEFERMLrKQAEDEE 275
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 293-367 2.09e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 37.16  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253 293 RALQGQVAELRAELcqqrTEYKRSLKSIEEGSADLRKQMSRLEEELDQERKKYAMLEIKLR-----NSE-------RARE 360
Cdd:cd22887    7 QELEKRLAELEAEL----ASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLRklqeeNDElverwmaKKQQ 82


                 ....*..
gi 755548253 361 DAERRNQ 367
Cdd:cd22887   83 EADKMNE 89
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 293-383 2.98e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.77  E-value: 2.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253   293 RALQGQVAELRA-------ELCQQRTEYKRSLKSIEEGSADLRKQMSRLEEEL--------DQERKKYAM------LEIK 351
Cdd:pfam01576  341 RSHEAQLQEMRQkhtqaleELTEQLEQAKRNKANLEKAKQALESENAELQAELrtlqqakqDSEHKRKKLegqlqeLQAR 420

                           90       100       110
                   ....*....|....*....|....*....|..
gi 755548253   352 LRNSERAREDAERRNQLLQREMEEFFSTLGSL 383
Cdd:pfam01576  421 LSESERQRAELAEKLSKLQSELESVSSLLNEA 452
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 295-382 3.34e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.77  E-value: 3.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253   295 LQGQVAELRAELCQQRTEYKRSLKSIEEGSAD----------LRKQMSRLEEELDQERKkyamleiklrnserAREDAER 364
Cdd:pfam01576  227 LQAQIAELRAQLAKKEEELQAALARLEEETAQknnalkkireLEAQISELQEDLESERA--------------ARNKAEK 292

                           90       100
                   ....*....|....*....|..
gi 755548253   365 RNQLLQREME----EFFSTLGS 382
Cdd:pfam01576  293 QRRDLGEELEalktELEDTLDT 314
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 300-376 3.77e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.39  E-value: 3.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253   300 AELRAELCQQ--RTEYKRSLKSIEEGSADLRKQMSR----LEEELDQERKKYAM-------LEIKLRNSE-------RAR 359
Cdd:pfam01576  714 AKLRLEVNMQalKAQFERDLQARDEQGEEKRRQLVKqvreLEAELEDERKQRAQavaakkkLELDLKELEaqidaanKGR 793

                           90
                   ....*....|....*..
gi 755548253   360 EDAERRNQLLQREMEEF 376
Cdd:pfam01576  794 EEAVKQLKKLQAQMKDL 810
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 312-376 4.24e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 37.17  E-value: 4.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755548253  312 EYKRSLKSIEEGSADLRKQMSRLEEELDQERKKYamlEIKLRNSERAREDAERRNQLLQREMEEF 376
Cdd:pfam03938  16 EGKAAQAQLEKKFKKRQAELEAKQKELQKLYEEL---QKDGALLEEEREEKEQELQKKEQELQQL 77
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
285-372 4.51e-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: 4.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253  285 TQAHVRRCRALQGQVAELRA------ELCQQRTEYKRSLKSIEEGSADLRKQMSRLEEELDQerkkyamLEIKLRNSERA 358
Cdd:COG4913   663 VASAEREIAELEAELERLDAssddlaALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ-------AEEELDELQDR 735

                          90
                  ....*....|....
gi 755548253  359 REDAERRNQLLQRE 372
Cdd:COG4913   736 LEAAEDLARLELRA 749
Filament pfam00038
Intermediate filament protein;
304-375 4.81e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 38.75  E-value: 4.81e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755548253  304 AELCQQRTEYKRSLKSIEEGSADLRKQMSRLEEELDQERKKYAMLEIKLRNSE----RAREDAERRNQLLQREMEE 375
Cdd:pfam00038 199 EELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEeryeLQLADYQELISELEAELQE 274
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
304-380 4.97e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 4.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253 304 AELCQQRTEYKRSLKSIEEGSADLRKQMSRL----EEELD---QERKKYAMLEIKLRNSERAREDAERRNQLLQREMEEF 376
Cdd:PRK03918 552 EELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEerlKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKA 631


                 ....
gi 755548253 377 FSTL 380
Cdd:PRK03918 632 FEEL 635
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 293-375 5.01e-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: 38.59  E-value: 5.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253 293 RALQGQVAELRA---ELCQQRTEYKRSLKSIEEGSADLRKQMSRLEEELDQERKKYAMLEIKLRNSERAREDAERRNQLL 369
Cdd:COG4942  146 PARREQAEELRAdlaELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225


                 ....*.
gi 755548253 370 QREMEE 375
Cdd:COG4942  226 EALIAR 231
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 286-383 5.88e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 39.05  E-value: 5.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253   286 QAHVRRCRALQGQVAELRAELCQQRTEYKRSLKSIEEGSADLRKQMSRLEEEL---DQERKKYAMLEIKLRNSERAREDA 362
Cdd:pfam12128  810 PRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLrglRCEMSKLATLKEDANSEQAQGSIG 889

                           90       100
                   ....*....|....*....|.
gi 755548253   363 ERRNQLlqremEEFFSTLGSL 383
Cdd:pfam12128  890 ERLAQL-----EDLKLKRDYL 905
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
293-376 6.11e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 6.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253  293 RALQGQVAELRAELcqqrteykrslKSIEEGSADLR---KQMSRLEEELDQERKKYAMLEIKLRNSERAREDAERRNQLL 369
Cdd:COG4913   664 ASAEREIAELEAEL-----------ERLDASSDDLAaleEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL 732


                  ....*..
gi 755548253  370 QREMEEF 376
Cdd:COG4913   733 QDRLEAA 739
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 286-394 6.44e-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: 38.78  E-value: 6.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253  286 QAHVRRCRALQGQVAELRAELCQQR------TEYKRSLKSIEEGSADLRKQMSRLEEELDqerkkyamleiklRNSERAR 359
Cdd:COG3096   508 QALAQRLQQLRAQLAELEQRLRQQQnaerllEEFCQRIGQQLDAAEELEELLAELEAQLE-------------ELEEQAA 574

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 755548253  360 EDAERRNQlLQREMEEFFSTLGSLTtgtkgSRAPE 394
Cdd:COG3096   575 EAVEQRSE-LRQQLEQLRARIKELA-----ARAPA 603
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 298-376 6.46e-03

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 36.46  E-value: 6.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755548253  298 QVAELRAELcqqrTEYKRSLKSIEEGSADLRKQMSRLEEELDQERKkyaMLEIKLRNSERAREDAERRNQLLQREMEEF 376
Cdd:pfam07926  58 ALQALREEL----NELKAEIAELKAEAESAKAELEESEESWEEQKK---ELEKELSELEKRIEDLNEQNKLLHDQLESL 129
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 296-376 6.47e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 37.94  E-value: 6.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253 296 QGQVAELRAELC-QQRTEYKRSLKSIEEGsadLRKQMSRLEEELDQERKKYA-----MLEIKLRNSERA-REDAERRNQL 368
Cdd:cd16269  206 KAEAAEQERKLLeEQQRELEQKLEDQERS---YEEHLRQLKEKMEEERENLLkeqerALESKLKEQEALlEEGFKEQAEL 282


                 ....*...
gi 755548253 369 LQREMEEF 376
Cdd:cd16269  283 LQEEIRSL 290
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 1-20 6.98e-03

RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP27 (also called CAMGAP1), ARHGAP15, 12 and 9-like proteins; This subgroup of ARHGAPs are multidomain proteins that contain RhoGAP, PH, SH3 and WW domains. Most members that are studied show GAP activity towards Rac1, some additionally show activity towards Cdc42. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239868 [Multi-domain]  Cd Length: 187  Bit Score: 37.37  E-value: 6.98e-03
                         10        20
                 ....*....|....*....|
gi 755548253   1 MSVQNLATVFGPNILRPQIE 20
Cdd:cd04403  147 MTTQNLAIVFGPTLLRPEQE 166
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 293-376 8.02e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 8.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253 293 RALQGQVAEL---RAELCQQRTEYKRSLKSIEEGSADLRKQMSRLEEELDQERKKYAMLEIKLRNSERAREDAERRNQLL 369
Cdd:COG1196  312 RELEERLEELeeeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391


                 ....*..
gi 755548253 370 QREMEEF 376
Cdd:COG1196  392 LRAAAEL 398
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
293-370 8.52e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 37.96  E-value: 8.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253 293 RALQGQVAELRAE---LCQQRTEYKRSLKSIEEGSADLRKQMSRLEEELDQERKKYAMLEIKLRNSERAREDAERRNQLL 369
Cdd:COG4372  111 EELQEELEELQKErqdLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190


                 .
gi 755548253 370 Q 370
Cdd:COG4372  191 E 191
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 300-375 8.78e-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: 37.82  E-value: 8.78e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755548253 300 AELRAELCQQRTEYKRSLKSIEEGSADLRKQMSRLEEELDQERKKYAMLEIKLRNSERAREDAERRNQLLQREMEE 375
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
 1-27 8.90e-03

RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase regulator associated with focal adhesion kinase); Graf is a multi-domain protein, containing SH3 and PH domains, that binds focal adhesion kinase and influences cytoskeletal changes mediated by Rho proteins. Graf exhibits GAP activity toward RhoA and Cdc42, but only weakly activates Rac1. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239839  Cd Length: 203  Bit Score: 37.37  E-value: 8.90e-03
                         10        20
                 ....*....|....*....|....*..
gi 755548253   1 MSVQNLATVFGPNILRPQIEDPVTIME 27
Cdd:cd04374  163 MTVSNLGVVFGPTLLRPQEETVAAIMD 189
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 291-376 9.23e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 37.98  E-value: 9.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253  291 RCRALQGQVAELRAELcQQRTEYKRSLKS-IEEgsadLRKQMSRLEEELDQERKK-YAMLEIKLRNSERAREDAERRNQL 368
Cdd:pfam13868  53 RERALEEEEEKEEERK-EERKRYRQELEEqIEE----REQKRQEEYEEKLQEREQmDEIVERIQEEDQAEAEEKLEKQRQ 127


                  ....*...
gi 755548253  369 LQREMEEF 376
Cdd:pfam13868 128 LREEIDEF 135
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 282-376 9.48e-03

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: 38.11  E-value: 9.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755548253   282 GSPTQAHVRRCRALQGQVAELrAELCQQRTEYKRSLKSIEEGSADLRKQMSRLEEELDQERK-------KYAMLEIKLRN 354
Cdd:TIGR02168  659 GVITGGSAKTNSSILERRREI-EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKeleelsrQISALRKDLAR 737

                           90       100
                   ....*....|....*....|..
gi 755548253   355 SERAREDAERRNQLLQREMEEF 376
Cdd:TIGR02168  738 LEAEVEQLEERIAQLSKELTEL 759
 
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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