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Conserved domains on  [gi|157822153|ref|NP_001100767|]
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rho GTPase-activating protein 22 [Rattus norvegicus]

Protein Classification

Rho GTPase-activating protein( domain architecture ID 107455)

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; contains a Pleckstrin homology (PH) domain

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 ...
61-190 2.99e-77

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: 241.96  E-value: 2.99e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153  61 GIFGQRLEDTVHHERKFGPRLAPLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGEKPLFD----------- 129
Cdd:cd04390    1 GVFGQRLEDTVAYERKFGPRLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDsdtdvhtvasl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153 130 ----------------------------------------------------------RFLDEVQAHSDVNKMSVQNLAT 151
Cdd:cd04390   81 lklylrelpepvipwaqyedflscaqllskdeekglgelmkqvsilpkvnynllsyicRFLDEVQSNSSVNKMSVQNLAT 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 157822153 152 VFGPNILRPQVEDPVTIMEGTSLVQHLMTVLIRKHGQLF 190
Cdd:cd04390  161 VFGPNILRPKVEDPATIMEGTPQIQQLMTVMISKHEPLF 199
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
18-61 2.40e-23

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13378:

Pssm-ID: 473070  Cd Length: 116  Bit Score: 95.01  E-value: 2.40e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 157822153  18 GGAAEREKVPANPEALLLMASSQRDMEDWVQAIRRVIWAPLGGG 61
Cdd:cd13378   73 GGAGDREKVPMNHEAFLLMANSQSDMEDWVKAIRRVIWAPFGGG 116
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
433-523 9.88e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 9.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153   433 QAHVRRCRALQGQVAELRAELCHQRIEYQRSLKSIEEGNS---DLRKQMCRLEEELDQEKKKYAMLEIKLRNSERAREDA 509
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESkldELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
                           90
                   ....*....|....
gi 157822153   510 ERRNQLLQREMEEF 523
Cdd:TIGR02168  371 ESRLEELEEQLETL 384
 
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 ...
61-190 2.99e-77

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: 241.96  E-value: 2.99e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153  61 GIFGQRLEDTVHHERKFGPRLAPLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGEKPLFD----------- 129
Cdd:cd04390    1 GVFGQRLEDTVAYERKFGPRLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDsdtdvhtvasl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153 130 ----------------------------------------------------------RFLDEVQAHSDVNKMSVQNLAT 151
Cdd:cd04390   81 lklylrelpepvipwaqyedflscaqllskdeekglgelmkqvsilpkvnynllsyicRFLDEVQSNSSVNKMSVQNLAT 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 157822153 152 VFGPNILRPQVEDPVTIMEGTSLVQHLMTVLIRKHGQLF 190
Cdd:cd04390  161 VFGPNILRPKVEDPATIMEGTPQIQQLMTVMISKHEPLF 199
PH_RhoGAP2 cd13378
Rho GTPase activating protein 2 Pleckstrin homology (PH) domain; RhoGAP2 (also called RhoGap22 ...
18-61 2.40e-23

Rho GTPase activating protein 2 Pleckstrin homology (PH) domain; RhoGAP2 (also called RhoGap22 or ArhGap22) are involved in cell polarity, cell morphology and cytoskeletal organization. They activate a GTPase belonging to the RAS superfamily of small GTP-binding proteins. The encoded protein is insulin-responsive, is dependent on the kinase Akt, and requires the Akt-dependent 14-3-3 binding protein which binds sequentially to two serine residues resulting in regulation of cell motility. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 241529  Cd Length: 116  Bit Score: 95.01  E-value: 2.40e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 157822153  18 GGAAEREKVPANPEALLLMASSQRDMEDWVQAIRRVIWAPLGGG 61
Cdd:cd13378   73 GGAGDREKVPMNHEAFLLMANSQSDMEDWVKAIRRVIWAPFGGG 116
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
83-186 2.27e-20

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: 88.48  E-value: 2.27e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153    83 PLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGEK--------------------------PLFD------- 129
Cdd:smart00324   4 PIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDpdldlseydvhdvagllklflrelpePLITyelyeef 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153   130 -----------------------------------RFLDEVQAHSDVNKMSVQNLATVFGPNILRPQVEDPVTIMEgTSL 174
Cdd:smart00324  84 ieaakledeterlralrellsllppanratlryllAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKD-IRH 162
                          170
                   ....*....|..
gi 157822153   175 VQHLMTVLIRKH 186
Cdd:smart00324 163 QNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
83-162 3.66e-20

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 86.83  E-value: 3.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153   83 PLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGEKPLFD--------------------------------- 129
Cdd:pfam00620   1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDLDleeedvhvvasllklflrelpeplltfelyeef 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157822153  130 -----------------------------------RFLDEVQAHSDVNKMSVQNLATVFGPNILRPQV 162
Cdd:pfam00620  81 ieaaklpdeeerlealrellrklppanrdtlryllAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
433-523 9.88e-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: 45.43  E-value: 9.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153   433 QAHVRRCRALQGQVAELRAELCHQRIEYQRSLKSIEEGNS---DLRKQMCRLEEELDQEKKKYAMLEIKLRNSERAREDA 509
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESkldELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
                           90
                   ....*....|....
gi 157822153   510 ERRNQLLQREMEEF 523
Cdd:TIGR02168  371 ESRLEELEEQLETL 384
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
433-537 1.60e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153 433 QAHVRRCRALQGQVAELRAELCHQR-----IEYQRSLKSIEEGNSDLRKQMCRLEEELDQEKKKYAMLEIKLRNSERARE 507
Cdd:COG4717   84 EEKEEEYAELQEELEELEEELEELEaeleeLREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEE 163
                         90       100       110
                 ....*....|....*....|....*....|
gi 157822153 508 DAERRNQLLQREMEEFFATLGSLTAGTKGA 537
Cdd:COG4717  164 ELEELEAELAELQEELEELLEQLSLATEEE 193
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
394-522 8.78e-04

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 41.86  E-value: 8.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153  394 PSPLPSSSEGHPSPDLGHSLDEACVGSGSSEPNDPGS---PSQAHVRRCRALQGQVAELRAELCHQR-IEYQRSLKSIEE 469
Cdd:pfam15709 280 LSSKYDAEESQVSIDGRSSPTQTFVVTGNMESEEERSeedPSKALLEKREQEKASRDRLRAERAEMRrLEVERKRREQEE 359
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153  470 GNSDLRKQMCR---LEEELDQEKKKYAMlEIKLRNS----ERAREDAERRNQLLQREMEE 522
Cdd:pfam15709 360 QRRLQQEQLERaekMREELELEQQRRFE-EIRLRKQrleeERQRQEEEERKQRLQLQAAQ 418
PRK09039 PRK09039
peptidoglycan -binding protein;
441-538 1.65e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 40.72  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153 441 ALQGQVAELRAELCHQRIEYQRSLKSIEEGNSD---LRKQMCRLEEELDQEKKKYAMLEIKLRNSERAREDA-ERRNQLL 516
Cdd:PRK09039 113 AAEGRAGELAQELDSEKQVSARALAQVELLNQQiaaLRRQLAALEAALDASEKRDRESQAKIADLGRRLNVAlAQRVQEL 192
                         90       100
                 ....*....|....*....|..
gi 157822153 517 QREMEEFFATLGSLTAGTKGAR 538
Cdd:PRK09039 193 NRYRSEFFGRLREILGDREGIR 214
PH pfam00169
PH domain; PH stands for pleckstrin homology.
29-54 2.72e-03

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 37.54  E-value: 2.72e-03
                          10        20
                  ....*....|....*....|....*.
gi 157822153   29 NPEALLLMASSQRDMEDWVQAIRRVI 54
Cdd:pfam00169  79 GKRTYLLQAESEEERKDWIKAIQSAI 104
 
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 ...
61-190 2.99e-77

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: 241.96  E-value: 2.99e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153  61 GIFGQRLEDTVHHERKFGPRLAPLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGEKPLFD----------- 129
Cdd:cd04390    1 GVFGQRLEDTVAYERKFGPRLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDsdtdvhtvasl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153 130 ----------------------------------------------------------RFLDEVQAHSDVNKMSVQNLAT 151
Cdd:cd04390   81 lklylrelpepvipwaqyedflscaqllskdeekglgelmkqvsilpkvnynllsyicRFLDEVQSNSSVNKMSVQNLAT 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 157822153 152 VFGPNILRPQVEDPVTIMEGTSLVQHLMTVLIRKHGQLF 190
Cdd:cd04390  161 VFGPNILRPKVEDPATIMEGTPQIQQLMTVMISKHEPLF 199
PH_RhoGAP2 cd13378
Rho GTPase activating protein 2 Pleckstrin homology (PH) domain; RhoGAP2 (also called RhoGap22 ...
18-61 2.40e-23

Rho GTPase activating protein 2 Pleckstrin homology (PH) domain; RhoGAP2 (also called RhoGap22 or ArhGap22) are involved in cell polarity, cell morphology and cytoskeletal organization. They activate a GTPase belonging to the RAS superfamily of small GTP-binding proteins. The encoded protein is insulin-responsive, is dependent on the kinase Akt, and requires the Akt-dependent 14-3-3 binding protein which binds sequentially to two serine residues resulting in regulation of cell motility. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 241529  Cd Length: 116  Bit Score: 95.01  E-value: 2.40e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 157822153  18 GGAAEREKVPANPEALLLMASSQRDMEDWVQAIRRVIWAPLGGG 61
Cdd:cd13378   73 GGAGDREKVPMNHEAFLLMANSQSDMEDWVKAIRRVIWAPFGGG 116
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
83-182 2.65e-21

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: 90.82  E-value: 2.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153  83 PLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGEK-------------------------PLFD-------- 129
Cdd:cd00159    1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDiddledydvhdvasllklylrelpePLIPfelydefi 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153 130 ----------------------------------RFLDEVQAHSDVNKMSVQNLATVFGPNILRPQVEDPVTIMEGTSLV 175
Cdd:cd00159   81 elakiedeeeriealkellkslppenrdllkyllKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSDDELLEDIKKLN 160

                 ....*..
gi 157822153 176 QHLMTVL 182
Cdd:cd00159  161 EIVEFLI 167
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
83-186 2.27e-20

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: 88.48  E-value: 2.27e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153    83 PLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGEK--------------------------PLFD------- 129
Cdd:smart00324   4 PIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDpdldlseydvhdvagllklflrelpePLITyelyeef 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153   130 -----------------------------------RFLDEVQAHSDVNKMSVQNLATVFGPNILRPQVEDPVTIMEgTSL 174
Cdd:smart00324  84 ieaakledeterlralrellsllppanratlryllAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKD-IRH 162
                          170
                   ....*....|..
gi 157822153   175 VQHLMTVLIRKH 186
Cdd:smart00324 163 QNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
83-162 3.66e-20

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 86.83  E-value: 3.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153   83 PLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGEKPLFD--------------------------------- 129
Cdd:pfam00620   1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDLDleeedvhvvasllklflrelpeplltfelyeef 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157822153  130 -----------------------------------RFLDEVQAHSDVNKMSVQNLATVFGPNILRPQV 162
Cdd:pfam00620  81 ieaaklpdeeerlealrellrklppanrdtlryllAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
PH_RhoGap24 cd13379
Rho GTPase activating protein 24 Pleckstrin homology (PH) domain; RhoGap24 (also called ...
20-61 2.67e-15

Rho GTPase activating protein 24 Pleckstrin homology (PH) domain; RhoGap24 (also called ARHGAP24, p73RhoGAp, and Filamin-A-associated RhoGAP) like other RhoGAPs are involved in cell polarity, cell morphology and cytoskeletal organization. They act as GTPase activators for the Rac-type GTPases by converting them to an inactive GDP-bound state and control actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity and are able to suppress RAC1 and CDC42 activity in vitro. Overexpression of these proteins induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 241530  Cd Length: 114  Bit Score: 71.93  E-value: 2.67e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 157822153  20 AAEREKVPANPEALLLMASSQRDMEDWVQAIRRVIWAPLGGG 61
Cdd:cd13379   73 GGDRERMTANHETYLLMASTQNDMEDWVKSIRRVIWAPFGGG 114
PH_RhoGap25-like cd13263
Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; ...
20-61 1.79e-14

Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; RhoGAP25 (also called ArhGap25) like other RhoGaps are involved in cell polarity, cell morphology and cytoskeletal organization. They act as GTPase activators for the Rac-type GTPases by converting them to an inactive GDP-bound state and control actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity and are able to suppress RAC1 and CDC42 activity in vitro. Overexpression of these proteins induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. This hierarchy contains RhoGAP22, RhoGAP24, and RhoGAP25. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270083  Cd Length: 114  Bit Score: 69.72  E-value: 1.79e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 157822153  20 AAEREKVPANPEALLLMASSQRDMEDWVQAIRRVIWAPLGGG 61
Cdd:cd13263   73 GGGGDRMTSNHDSYLLMANSQAEMEEWVKVIRRVIGSPFGGG 114
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
62-190 4.61e-13

RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Nadrin-like proteins. Nadrin, also named Rich-1, has been shown to be involved in the regulation of Ca2+-dependent exocytosis in neurons and recently has been implicated in tight junction maintenance in mammalian epithelium. 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: 239851  Cd Length: 203  Bit Score: 68.25  E-value: 4.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153  62 IFGQRLEDtvhHERKFGPRLApLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGE----------------- 124
Cdd:cd04386    4 VFGTPLEE---HLKRTGREIA-LPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTfslpldefysdphavas 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153 125 ----------KPLFD------------------------------------------RFLDEVQAHSDVNKMSVQNLATV 152
Cdd:cd04386   80 alksylrelpDPLLTynlyedwvqaankpdederlqaiwrilnklprenrdnlryliKFLSKLAQKSDENKMSPSNIAIV 159
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 157822153 153 FGPNILRPQVEDPVTIMEGTSLVQHLMTV-LIRKHGQLF 190
Cdd:cd04386  160 LAPNLLWAKNEGSLAEMAAGTSVHVVAIVeLIISHADWF 198
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
63-161 6.62e-13

RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of p50RhoGAP-like proteins; p50RhoGAP, also known as RhoGAP-1, contains a C-terminal RhoGAP domain and an N-terminal Sec14 domain which binds phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). It is ubiquitously expressed and preferentially active on Cdc42. This subgroup also contains closely related ARHGAP8. 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: 239869 [Multi-domain]  Cd Length: 195  Bit Score: 67.36  E-value: 6.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153  63 FGQRLEDTVHHERKFGPrlAPLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGE------------------ 124
Cdd:cd04404    6 FGVSLQFLKEKNPEQEP--IPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYNMGEpvdfdqyedvhlpavilk 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153 125 -------KPL--FD---------------------------------------RFLDEVQAHSDVNKMSVQNLATVFGPN 156
Cdd:cd04404   84 tflrelpEPLltFDlyddivgflnvdkeervervkqllqtlpeenyqvlkyliKFLVQVSAHSDQNKMTNSNLAVVFGPN 163

                 ....*
gi 157822153 157 ILRPQ 161
Cdd:cd04404  164 LLWAK 168
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
83-183 8.99e-10

RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of FAM13A1, isoform a-like proteins. The function of FAM13A1a is unknown. 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 up several orders of magnitude.


Pssm-ID: 239858 [Multi-domain]  Cd Length: 189  Bit Score: 58.24  E-value: 8.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153  83 PLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGE-------------------------------------- 124
Cdd:cd04393   21 PAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEevdlskeadvcsaasllrlflqelpeglipaslqirlm 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153 125 -------------------------------KPLFdRFLDEVQAHSDVNKMSVQNLATVFGPNI--LRPQVEDpvtiMEG 171
Cdd:cd04393  101 qlyqdyngedefgrklrdllqqlppvnysllKFLC-HFLSNVASQHHENRMTAENLAAVFGPDVfhVYTDVED----MKE 175
                        170
                 ....*....|..
gi 157822153 172 TSLVQHLMTVLI 183
Cdd:cd04393  176 QEICSRIMAKLL 187
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
77-182 3.21e-09

RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in MgcRacGAP proteins. MgcRacGAP plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling. ii) after phosphorylation by aurora B MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain a N-terminal C1-like domain, and a C-terminal RhoGAP 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: 239847  Cd Length: 193  Bit Score: 56.53  E-value: 3.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153  77 FGPRLAPL---LVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGEK-------------------------PLF 128
Cdd:cd04382    9 FDPSTSPMipaLIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTvpnlskvdihvicgclkdflrslkePLI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153 129 DR-----FLDEV--------------------QAHSD----------------VNKMSVQNLATVFGPNI---LRPQVeD 164
Cdd:cd04382   89 TFalwkeFMEAAeildednsraalyqaiselpQPNRDtlaflilhlqrvaqspECKMDINNLARVFGPTIvgySVPNP-D 167
                        170
                 ....*....|....*...
gi 157822153 165 PVTIMEGTSLVQHLMTVL 182
Cdd:cd04382  168 PMTILQDTVRQPRVVERL 185
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
63-169 3.75e-09

RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP21-like proteins. ArhGAP21 is a multi-domain protein, containing RhoGAP, PH and PDZ domains, and is believed to play a role in the organization of the cell-cell junction complex. It has been shown to function as a GAP of Cdc42 and RhoA, and to interact with alpha-catenin and Arf6. 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: 239860  Cd Length: 196  Bit Score: 56.64  E-value: 3.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153  63 FGQRLED--TVHHERkfgprLAPLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGE---------------- 124
Cdd:cd04395    2 FGVPLDDcpPSSENP-----YVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRGGfdidlqdprwrdvnvv 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153 125 ------------KPLFD------------------------------------------RFLDEVQAHSDVNKMSVQNLA 150
Cdd:cd04395   77 ssllksffrklpEPLFTnelypdfieanriedpverlkelrrlihslpdhhyetlkhliRHLKTVADNSEVNKMEPRNLA 156
                        170
                 ....*....|....*....
gi 157822153 151 TVFGPNILRPQvEDPVTIM 169
Cdd:cd04395  157 IVFGPTLVRTS-DDNMETM 174
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
81-164 9.80e-09

RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr (breakpoint cluster region protein)-like proteins. Bcr is a multidomain protein with a variety of enzymatic functions. It contains a RhoGAP and a Rho GEF domain, a Ser/Thr kinase domain, an N-terminal oligomerization domain, and a C-terminal PDZ binding domain, in addition to PH and C2 domains. Bcr is a negative regulator of: i) RacGTPase, via the Rho GAP domain, ii) the Ras-Raf-MEK-ERK pathway, via phosphorylation of the Ras binding protein AF-6, and iii) the Wnt signaling pathway through binding beta-catenin. Bcr can form a complex with beta-catenin and Tcf1. The Wnt signaling pathway is involved in cell proliferation, differentiation, and cell renewal. Bcr was discovered as a fusion partner of Abl. The Bcr-Abl fusion is characteristic for a large majority of chronic myelogenous leukemias (CML). 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: 239852 [Multi-domain]  Cd Length: 196  Bit Score: 55.32  E-value: 9.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153  81 LAPLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGEK---------------------------PLF-DRF- 131
Cdd:cd04387   15 KVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKdvsvmlsemdvnaiagtlklyfrelpePLFtDELy 94
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157822153 132 ----------------------------------------LDEVQAHSDVNKMSVQNLATVFGPNILRPQVED 164
Cdd:cd04387   95 pnfaegialsdpvakescmlnlllslpdpnlvtflfllhhLKRVAEREEVNKMSLHNLATVFGPTLLRPSEKE 167
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
83-142 1.21e-08

RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in srGAPs. srGAPs are components of the intracellular part of Slit-Robo signalling pathway that is important for axon guidance and cell migration. srGAPs contain an N-terminal FCH domain, a central RhoGAP domain and a C-terminal SH3 domain; this SH3 domain interacts with the intracellular proline-rich-tail of the Roundabout receptor (Robo). This interaction with Robo then activates the rhoGAP domain which in turn inhibits Cdc42 activity. 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: 239848  Cd Length: 188  Bit Score: 54.73  E-value: 1.21e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153  83 PLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGEKPLFDrfldeVQAHSDVN 142
Cdd:cd04383   19 PLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGEDPLAD-----DQNDHDIN 73
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
83-190 3.97e-08

RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of chimaerins. Chimaerins are a family of phorbolester- and diacylglycerol-responsive GAPs specific for the Rho-like GTPase Rac. Chimaerins exist in two alternative splice forms that each contain a C-terminal GAP domain, and a central C1 domain which binds phorbol esters, inducing a conformational change that activates the protein; one splice form is lacking the N-terminal Src homology-2 (SH2) 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: 239837 [Multi-domain]  Cd Length: 194  Bit Score: 53.67  E-value: 3.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153  83 PLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDC-GEK---------------------------PL-----FD 129
Cdd:cd04372   17 PMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRdGEKadisatvypdinvitgalklyfrdlpiPVitydtYP 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153 130 RFLD-------------------------------------EVQAHSDVNKMSVQNLATVFGPNILRPQVEDPVTIMEGT 172
Cdd:cd04372   97 KFIDaakisnpderleavhealmllppahyetlrylmehlkRVTLHEKDNKMNAENLGIVFGPTLMRPPEDSALTTLNDM 176
                        170
                 ....*....|....*...
gi 157822153 173 SLVQHLMTVLIRKHGQLF 190
Cdd:cd04372  177 RYQILIVQLLITNEDVLF 194
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
63-163 4.40e-08

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: 53.16  E-value: 4.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153  63 FGQRLEDTVHHERKfgprLAPLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGEK----------------- 125
Cdd:cd04403    1 FGCHLEALCQRENS----TVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDHDEKldlddskwedihvitga 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153 126 ----------PLFD------------------------------------------RFLDEVQAHSDVNKMSVQNLATVF 153
Cdd:cd04403   77 lklffrelpePLFPyslfndfvaaiklsdyeqrvsavkdlikslpkpnhdtlkmlfRHLCRVIEHGEKNRMTTQNLAIVF 156
                        170
                 ....*....|
gi 157822153 154 GPNILRPQVE 163
Cdd:cd04403  157 GPTLLRPEQE 166
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
83-193 1.32e-07

RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP6-like proteins. ArhGAP6 shows GAP activity towards RhoA, but not towards Cdc42 and Rac1. ArhGAP6 is often deleted in microphthalmia with linear skin defects syndrome (MLS); MLS is a severe X-linked developmental disorder. 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: 239841  Cd Length: 206  Bit Score: 52.06  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153  83 PLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCG-------------------------EKPLFDR------- 130
Cdd:cd04376   10 PRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGidvvldenhsvhdvaallkeffrdmPDPLLPRelytafi 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153 131 ----------------------------------FLDEVQAHSDV-----------NKMSVQNLATVFGPNILRPQ---- 161
Cdd:cd04376   90 gtallepdeqlealqlliyllppcncdtlhrllkFLHTVAEHAADsidedgqevsgNKMTSLNLATIFGPNLLHKQksge 169
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 157822153 162 ---VEDPVTIMEGTSLVQHLMTvLIRKHGQLFATP 193
Cdd:cd04376  170 refVQASLRIEESTAIINVVQT-MIDNYEELFMVS 203
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
142-183 7.54e-07

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: 49.70  E-value: 7.54e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 157822153 142 NKMSVQNLATVFGPNILRPQVEDPVTIMEGTSLVQHLMTVLI 183
Cdd:cd04389  144 TKMDVSNLAMVFAPNILRCTSDDPRVIFENTRKEMSFLRTLI 185
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
83-180 8.98e-07

RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in ARAPs. ARAPs (also known as centaurin deltas) contain, besides the RhoGAP domain, an Arf GAP, ankyrin repeat ras-associating, and PH domains. Since their ArfGAP activity is PIP3-dependent, ARAPs are considered integration points for phosphoinositide, Arf and Rho signaling. 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: 239850  Cd Length: 184  Bit Score: 49.23  E-value: 8.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153  83 PLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSF---------DCGEKPLFD------RFLDE------------- 134
Cdd:cd04385   16 PVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFrkdarsvqlREGEYTVHDvadvlkRFLRDlpdplltselhae 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153 135 -----------------------------------------VQAHSDVNKMSVQNLATVFGPNILRPQVEDPVTIMEGTS 173
Cdd:cd04385   96 wieaaelenkderiarykelirrlppinratlkvlighlyrVQKHSDENQMSVHNLALVFGPTLFQTDEHSVGQTSHEVK 175

                 ....*..
gi 157822153 174 LVQHLMT 180
Cdd:cd04385  176 VIEDLID 182
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
62-195 9.82e-07

RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP18-like proteins. The function of ArhGAP18 is unknown. 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: 239856  Cd Length: 216  Bit Score: 49.65  E-value: 9.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153  62 IFGQRLEDTVHHERKFGPRL-APLLVEQCVDFIRERGLSEEGLFRMPGQA----NLVRDLQDSFDCGEK----------- 125
Cdd:cd04391    1 LFGVPLSTLLERDQKKVPGSkVPLIFQKLINKLEERGLETEGILRIPGSAqrvkFLCQELEAKFYEGTFlwdqvkqhdaa 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153 126 ------------PLFD------------------------------------------RFLDEVQAHSDVNKMSVQNLAT 151
Cdd:cd04391   81 sllklfirelpqPLLTveylpafysvqglpskkdqlqalnllvlllpeanrdtlkallEFLQKVVDHEEKNKMNLWNVAM 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 157822153 152 VFGPNILRPQVEDPVTI------MEGTSLVQHLMTVLIRKHGQLFATPSF 195
Cdd:cd04391  161 IMAPNLFPPRGKHSKDNeslqeeVNMAAGCANIMRLLIRYQDLLWTVPSF 210
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
63-158 1.82e-06

RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal RGD1-like proteins. Yeast Rgd1 is a GAP protein for Rho3 and Rho4 and plays a role in low-pH response. 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: 239863  Cd Length: 192  Bit Score: 48.55  E-value: 1.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153  63 FGQRLEDTVHHERKfgprLAPLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFD--------------------- 121
Cdd:cd04398    1 FGVPLEDLILREGD----NVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDkdplnvllispedyesdihsv 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153 122 CGEKPLFDR---------------------------------------------------FLDEVQAHSDVNKMSVQNLA 150
Cdd:cd04398   77 ASLLKLFFRelpeplltkalsrefieaakiedesrrrdalhglindlpdanyatlralmfHLARIKEHESVNRMSVNNLA 156

                 ....*...
gi 157822153 151 TVFGPNIL 158
Cdd:cd04398  157 IIWGPTLM 164
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
130-170 2.45e-06

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: 48.54  E-value: 2.45e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 157822153 130 RFLDEVQAHSDVNKMSVQNLATVFGPNILRPQVEDPVTIME 170
Cdd:cd04374  149 KHLTNVSDHSKKNLMTVSNLGVVFGPTLLRPQEETVAAIMD 189
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
63-121 4.23e-06

RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of p190-like proteins. p190, also named RhoGAP5, plays a role in neuritogenesis and axon branch stability. p190 shows a preference for Rho, over Rac and Cdc42, and consists of an N-terminal GTPase domain and a C-terminal GAP domain. The central portion of p190 contains important regulatory phosphorylation sites. 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: 239838  Cd Length: 185  Bit Score: 47.45  E-value: 4.23e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157822153  63 FGQRLEDTVHHERKFgprlaPLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFD 121
Cdd:cd04373    1 FGVPLANVVTSEKPI-----PIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFD 54
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
63-173 2.25e-05

RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in class IX myosins. Class IX myosins contain a characteristic head domain, a neck domain, a tail domain which contains a C6H2-zinc binding motif and a RhoGAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons. 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: 239842  Cd Length: 186  Bit Score: 45.12  E-value: 2.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153  63 FGQRLEDTVHHERKfgprlAPLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCG------------------- 123
Cdd:cd04377    1 FGVSLSSLTSEDRS-----VPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDpdsvnledypihvitsvlk 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153 124 ----EKP-------LFDRFL---------DEVQA----------------------------HSDVNKMSVQNLATVFGP 155
Cdd:cd04377   76 qwlrELPeplmtfeLYENFLrameleekqERVRAlysvleqlpranlntlerlifhlvrvalQEEVNRMSANALAIVFAP 155
                        170
                 ....*....|....*....
gi 157822153 156 NILR-PQVEDPVTIMEGTS 173
Cdd:cd04377  156 CILRcPDTADPLQSLQDVS 174
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
132-193 7.59e-05

RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP19-like proteins. The function of ArhGAP19 is unknown. 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: 239857  Cd Length: 208  Bit Score: 43.99  E-value: 7.59e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157822153 132 LDEVQAHSDVNKMSVQNLATVFGPNILRPQVEDPVTIMEGTSLVQHLMTVLIRKHGQLFATP 193
Cdd:cd04392  138 LYQTAKHEDKNKMSADNLALLFTPHLICPRNLTPEDLHENAQKLNSIVTFMIKHSQKLFKAP 199
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
63-121 7.99e-05

RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in SYD-1_like proteins. Syd-1, first identified and best studied in C.elegans, has been shown to play an important role in neuronal development by specifying axonal properties. 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: 239844  Cd Length: 207  Bit Score: 43.99  E-value: 7.99e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157822153  63 FGQRLEDTVhhERKFGPRLAPLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFD 121
Cdd:cd04379    1 FGVPLSRLV--EREGESRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFE 57
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
433-523 9.88e-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: 45.43  E-value: 9.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153   433 QAHVRRCRALQGQVAELRAELCHQRIEYQRSLKSIEEGNS---DLRKQMCRLEEELDQEKKKYAMLEIKLRNSERAREDA 509
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESkldELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
                           90
                   ....*....|....
gi 157822153   510 ERRNQLLQREMEEF 523
Cdd:TIGR02168  371 ESRLEELEEQLETL 384
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
433-537 1.60e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153 433 QAHVRRCRALQGQVAELRAELCHQR-----IEYQRSLKSIEEGNSDLRKQMCRLEEELDQEKKKYAMLEIKLRNSERARE 507
Cdd:COG4717   84 EEKEEEYAELQEELEELEEELEELEaeleeLREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEE 163
                         90       100       110
                 ....*....|....*....|....*....|
gi 157822153 508 DAERRNQLLQREMEEFFATLGSLTAGTKGA 537
Cdd:COG4717  164 ELEELEAELAELQEELEELLEQLSLATEEE 193
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
62-157 2.43e-04

RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of fungal BEM3-like proteins. Bem3 is a GAP protein of Cdc42, and is specifically involved in the control of the initial assembly of the septin ring in yeast bud 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: 239865 [Multi-domain]  Cd Length: 190  Bit Score: 42.35  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153  62 IFGQRLEDTVHHERKFGPRLA-PLLVEQCVDFI-RERGLSEEGLFRMPGQANLVRDLQDSFDCG---------------- 123
Cdd:cd04400    1 IFGSPLEEAVELSSHKYNGRDlPSVVYRCIEYLdKNRAIYEEGIFRLSGSASVIKQLKERFNTEydvdlfssslypdvht 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153 124 ------------EKPLFDR-------------------------------------------FLDEVQAHSDVNKMSVQN 148
Cdd:cd04400   81 vagllklylrelPTLILGGelhndfkrlveenhdrsqralelkdlvsqlpqanydllyvlfsFLRKIIEHSDVNKMNLRN 160
                        170
                 ....*....|.
gi 157822153 149 LATVFGP--NI 157
Cdd:cd04400  161 VCIVFSPtlNI 171
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
63-131 4.28e-04

RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in RalBP1 proteins, also known as RLIP, RLIP76 or cytocentrin. RalBP1 plays an important role in endocytosis during interphase. During mitosis, RalBP1 transiently associates with the centromere and has been shown to play an essential role in the proper assembly of the mitotic apparatus. RalBP1 is an effector of the Ral GTPase which itself is an effector of Ras. RalBP1 contains a RhoGAP domain, which shows weak activity towards Rac1 and Cdc42, but not towards Ral, and a Ral effector domain binding motif. 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: 239846 [Multi-domain]  Cd Length: 182  Bit Score: 41.27  E-value: 4.28e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153  63 FGQRLEDTVHHERKF-GPRLaPLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGEKPLFDRF 131
Cdd:cd04381    1 FGASLSLAVERSRCHdGIDL-PLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRRESPNLEEY 69
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
132-175 4.67e-04

RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP (Gem interacting protein) and PARG1 (PTPL1-associated RhoGAP1). GMIP plays important roles in neurite growth and axonal guidance, and interacts with Gem, a member of the RGK subfamily of the Ras small GTPase superfamily, through the N-terminal half of the protein. GMIP contains a C-terminal RhoGAP domain. GMIP inhibits RhoA function, but is inactive towards Rac1 and Cdc41. PARG1 interacts with Rap2, also a member of the Ras small GTPase superfamily whose exact function is unknown, and shows strong preference for Rho. 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: 239843  Cd Length: 203  Bit Score: 41.64  E-value: 4.67e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 157822153 132 LDEVQAHSDVNKMSVQNLATVFGPNILRPQVED-PVTImegTSLV 175
Cdd:cd04378  147 LYRVAEQFEENKMSPNNLGIVFGPTLIRPRPGDaDVSL---SSLV 188
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
433-530 5.56e-04

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: 42.75  E-value: 5.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153   433 QAHVRRCRALQGQVAELRAELchQRIEYQRS-----LKSIEEGNSDLRKQMCRL-EEELDQEKKKYAMLEIKLRNSERAR 506
Cdd:TIGR02169  233 EALERQKEAIERQLASLEEEL--EKLTEEISelekrLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSI 310
                           90       100
                   ....*....|....*....|....
gi 157822153   507 EDAERRNQLLQREMEEFFATLGSL 530
Cdd:TIGR02169  311 AEKERELEDAEERLAKLEAEIDKL 334
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
132-177 5.65e-04

RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of PARG1 (PTPL1-associated RhoGAP1). PARG1 was originally cloned as an interaction partner of PTPL1, an intracellular protein-tyrosine phosphatase. PARG1 interacts with Rap2, also a member of the Ras small GTPase superfamily whose exact function is unknown, and shows strong preference for Rho. 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: 239874  Cd Length: 211  Bit Score: 41.33  E-value: 5.65e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 157822153 132 LDEVQAHSDVNKMSVQNLATVFGPNILRP-QVEDPVTImegTSLVQH 177
Cdd:cd04409  155 LHRVSEQAEENKMSASNLGIIFGPTLIRPrPTDATVSL---SSLVDY 198
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
394-522 8.78e-04

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 41.86  E-value: 8.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153  394 PSPLPSSSEGHPSPDLGHSLDEACVGSGSSEPNDPGS---PSQAHVRRCRALQGQVAELRAELCHQR-IEYQRSLKSIEE 469
Cdd:pfam15709 280 LSSKYDAEESQVSIDGRSSPTQTFVVTGNMESEEERSeedPSKALLEKREQEKASRDRLRAERAEMRrLEVERKRREQEE 359
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153  470 GNSDLRKQMCR---LEEELDQEKKKYAMlEIKLRNS----ERAREDAERRNQLLQREMEE 522
Cdd:pfam15709 360 QRRLQQEQLERaekMREELELEQQRRFE-EIRLRKQrleeERQRQEEEERKQRLQLQAAQ 418
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
83-153 8.91e-04

RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal SAC7 and BAG7-like proteins. Both proteins are GTPase activating proteins of Rho1, but differ functionally in vivo: SAC7, but not BAG7, is involved in the control of Rho1-mediated activation of the PKC-MPK1 pathway. 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: 239861  Cd Length: 225  Bit Score: 40.86  E-value: 8.91e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157822153  83 PLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFDCGekPLFDRFLDEvqahsdvNKMSVQNLATVF 153
Cdd:cd04396   33 PVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTP--PDYGKSFDW-------DGYTVHDAASVL 94
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
117-185 1.07e-03

RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXB. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons 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: 239872 [Multi-domain]  Cd Length: 186  Bit Score: 40.36  E-value: 1.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153 117 QDSFDCGEKPLFDrfLDEVQAHSDVNKMSVQNLATVFGPNILR-PQVEDPVTIMEGTSLVQHLMTVLIRK 185
Cdd:cd04407  119 TANHNTLERLIFH--LVKVALEEDVNRMSPNALAIVFAPCLLRcPDSSDPLTSMKDVAKTTTCVEMLIKE 186
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
447-523 1.37e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 1.37e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157822153 447 AELRAELCHQRIEYQRSLKSIEEGNSDLRKQMCRLEEELDQEKKKYAMLEIKLRNSERAREDAERRNQLLQREMEEF 523
Cdd:COG1196  308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
PRK09039 PRK09039
peptidoglycan -binding protein;
441-538 1.65e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 40.72  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153 441 ALQGQVAELRAELCHQRIEYQRSLKSIEEGNSD---LRKQMCRLEEELDQEKKKYAMLEIKLRNSERAREDA-ERRNQLL 516
Cdd:PRK09039 113 AAEGRAGELAQELDSEKQVSARALAQVELLNQQiaaLRRQLAALEAALDASEKRDRESQAKIADLGRRLNVAlAQRVQEL 192
                         90       100
                 ....*....|....*....|..
gi 157822153 517 QREMEEFFATLGSLTAGTKGAR 538
Cdd:PRK09039 193 NRYRSEFFGRLREILGDREGIR 214
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
447-522 1.74e-03

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: 38.82  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153  447 AELRAELCHQRI-EYQRSLKSIEEGNSDLRKQMCRLEEELDQEKKKYAMLEIKLRNSERAREDAE---RRNQLLQREMEE 522
Cdd:pfam12718  12 AQERAEELEEKVkELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNEnltRKIQLLEEELEE 91
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
440-533 1.75e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 1.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153 440 RALQGQVAELRAELchQRIEYQrsLKSIEEGN--SDLRKQMCRLEEELDQEKKKYAMLEIKLRNSERAREDAERRNQ--L 515
Cdd:COG4717  442 EELEEELEELREEL--AELEAE--LEQLEEDGelAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLppV 517
                         90
                 ....*....|....*...
gi 157822153 516 LQReMEEFFAtlgSLTAG 533
Cdd:COG4717  518 LER-ASEYFS---RLTDG 531
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
440-521 2.18e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.77  E-value: 2.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153 440 RALQGQVAELRAELchqRIEYQRSLKSIEEGNSDLRKQMCRLEEELDQEKKKYAML---EIKLRNSERAREDAERR-NQL 515
Cdd:COG3206  294 IALRAQIAALRAQL---QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELyESL 370

                 ....*.
gi 157822153 516 LQREME 521
Cdd:COG3206  371 LQRLEE 376
PH pfam00169
PH domain; PH stands for pleckstrin homology.
29-54 2.72e-03

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 37.54  E-value: 2.72e-03
                          10        20
                  ....*....|....*....|....*.
gi 157822153   29 NPEALLLMASSQRDMEDWVQAIRRVI 54
Cdd:pfam00169  79 GKRTYLLQAESEEERKDWIKAIQSAI 104
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
440-522 4.21e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 4.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153 440 RALQGQVAELRAELCHQRIEYQRSLKSIEEGNSDLRkqmcRLEEELDQEKKKYAMLEIKLRNSERAREDAERRNQLLQRE 519
Cdd:COG4372   41 DKLQEELEQLREELEQAREELEQLEEELEQARSELE----QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEE 116

                 ...
gi 157822153 520 MEE 522
Cdd:COG4372  117 LEE 119
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
440-531 6.13e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 6.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153 440 RALQGQVAELRAELchqrIEYQRSLKSIEEGNSDLRKQMCRLEEELDQEKKKYAMLEIKLRNSERAREDAERRNQLLQRE 519
Cdd:COG4372   90 QAAQAELAQAQEEL----ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
                         90
                 ....*....|..
gi 157822153 520 MEEFFATLGSLT 531
Cdd:COG4372  166 LAALEQELQALS 177
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
80-121 6.23e-03

RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXA. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons. 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: 239871  Cd Length: 186  Bit Score: 38.06  E-value: 6.23e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 157822153  80 RLAPLLVEQCVDFIRERGLSEEGLFRMPGQANLVRDLQDSFD 121
Cdd:cd04406   13 RSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLD 54
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
450-523 7.07e-03

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: 36.82  E-value: 7.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157822153  450 RAElcHQRIEYQRSLKSIEEgnsdlrkQMCRLEEELDQEKKKYAMLEIKLRNSERAREDAERRNQLLQREMEEF 523
Cdd:pfam20492   3 EAE--REKQELEERLKQYEE-------ETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERL 67
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
445-532 7.44e-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: 36.78  E-value: 7.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153  445 QVAELRAELCHQRIEYQRslksIEEGNSDLRKQMCRLEEELDQEKKKYAM----LEIKLRNSERAREDAERRNQLLQREM 520
Cdd:pfam13863   7 EMFLVQLALDAKREEIER----LEELLKQREEELEKKEQELKEDLIKFDKflkeNDAKRRRALKKAEEETKLKKEKEKEI 82
                          90
                  ....*....|..
gi 157822153  521 EEFFATLGSLTA 532
Cdd:pfam13863  83 KKLTAQIEELKS 94
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
128-158 7.80e-03

RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP11A-like proteins. The mouse homolog of human ArhGAP11A has been detected as a gene exclusively expressed in immature ganglion cells, potentially playing a role in retinal development. The exact function of ArhGAP11A is unknown. 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: 239859 [Multi-domain]  Cd Length: 202  Bit Score: 37.84  E-value: 7.80e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 157822153 128 FDRFLDEVQAHSDVNKMSVQNLATVFGPNIL 158
Cdd:cd04394  130 FFSFLYDVAQRCSENKMDSSNLAVIFAPNLF 160
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
433-541 8.27e-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: 39.17  E-value: 8.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153  433 QAHVRRCRALQGQVAELRaelchQRIEYQRSLKSIEEGNSDLRKQMCRLEEELDQEkkkYAMLEIKL-RNSERAREDAER 511
Cdd:COG3096   508 QALAQRLQQLRAQLAELE-----QRLRQQQNAERLLEEFCQRIGQQLDAAEELEEL---LAELEAQLeELEEQAAEAVEQ 579
                          90       100       110
                  ....*....|....*....|....*....|
gi 157822153  512 RNQlLQREMEEFFATLGSLTagtkgARAPE 541
Cdd:COG3096   580 RSE-LRQQLEQLRARIKELA-----ARAPA 603
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
447-523 8.59e-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: 39.00  E-value: 8.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822153   447 AELRAELCHQ--RIEYQRSLKSIEEGNSDLRKQMCR----LEEELDQEKKKYAM-------LEIKLRNSE-------RAR 506
Cdd:pfam01576  714 AKLRLEVNMQalKAQFERDLQARDEQGEEKRRQLVKqvreLEAELEDERKQRAQavaakkkLELDLKELEaqidaanKGR 793
                           90
                   ....*....|....*..
gi 157822153   507 EDAERRNQLLQREMEEF 523
Cdd:pfam01576  794 EEAVKQLKKLQAQMKDL 810
 
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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