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Conserved domains on  [gi|767963398|ref|XP_011538307|]
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rho GTPase-activating protein 22 isoform X4 [Homo sapiens]

Protein Classification

PH domain-containing protein; PH domain-containing RhoGEF family protein( domain architecture ID 10351259)

Pleckstrin homology (PH) domain-containing protein may be involved in targeting a protein to the appropriate cellular location or interacting with a binding partner; similar to the PH region of pleckstrin homology domain-containing family A member 2 (PLEKHA2/TAAP2) that binds specifically to phosphatidylinositol 3,4-diphosphate (PtdIns3,4P2)| PH domain-containing RhoGEF family protein may function as a guanine nucleotide exchange factor; similar to Homo sapiens pleckstrin homology domain-containing family G member 4B and Danio rerio quattro

Graphical summary

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List of domain hits

 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 ...
 77-275 9.98e-138

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: 399.51  E-value: 9.98e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  77 GIFGQRLEETVHHERKYGPRLAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGEKPLFDSTTDVHTVASL 156
Cdd:cd04390    1 GVFGQRLEDTVAYERKFGPRLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 157 LKLYLRELPEPVVPFARYEDFLSCAQLLTKDEGEGTLELAKQVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLAT 236
Cdd:cd04390   81 LKLYLRELPEPVIPWAQYEDFLSCAQLLSKDEEKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLAT 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767963398 237 VFGPNILRPQVEDPVTIMEGTSLVQHLMTVLIRKHSQLF 275
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 1.05e-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: 96.17  E-value: 1.05e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 767963398  18 GGAGEREKVPANPEALLLMASSQRDMEDWVQAIRRVIWAPLGGG 61
Cdd:cd13378   73 GGAGDREKVPMNHEAFLLMANSQSDMEDWVKAIRRVIWAPFGGG 116
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 516-606 4.60e-05

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 4.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 516 REHARRSEALQG---LVTELRAELCRQRTEYERSVKRIEEGSADLRKRMSRLEEELDQEKKKYIMLEIKLRNSERAREDA 592
Cdd:COG1196  291 YELLAELARLEQdiaRLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370

                         90
                 ....*....|....
gi 767963398 593 ERRNQLLQREMEEF 606
Cdd:COG1196  371 EAELAEAEEELEEL 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 ...
 77-275 9.98e-138

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: 399.51  E-value: 9.98e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  77 GIFGQRLEETVHHERKYGPRLAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGEKPLFDSTTDVHTVASL 156
Cdd:cd04390    1 GVFGQRLEDTVAYERKFGPRLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 157 LKLYLRELPEPVVPFARYEDFLSCAQLLTKDEGEGTLELAKQVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLAT 236
Cdd:cd04390   81 LKLYLRELPEPVIPWAQYEDFLSCAQLLSKDEEKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLAT 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767963398 237 VFGPNILRPQVEDPVTIMEGTSLVQHLMTVLIRKHSQLF 275
Cdd:cd04390  161 VFGPNILRPKVEDPATIMEGTPQIQQLMTVMISKHEPLF 199
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 99-271 3.95e-58

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: 192.87  E-value: 3.95e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398    99 PLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGEKP-LFDSTTDVHTVASLLKLYLRELPEPVVPFARYEDF 177
Cdd:smart00324   4 PIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPdLDLSEYDVHDVAGLLKLFLRELPEPLITYELYEEF 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398   178 LSCAQLLTKDEGEGTLELAkqVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLATVFGPNILRPQVEDPVTIMEgT 257
Cdd:smart00324  84 IEAAKLEDETERLRALREL--LSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKD-I 160

                          170
                   ....*....|....
gi 767963398   258 SLVQHLMTVLIRKH 271
Cdd:smart00324 161 RHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 99-247 3.69e-56

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 186.60  E-value: 3.69e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398   99 PLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGEKP-LFDSTTDVHTVASLLKLYLRELPEPVVPFARYEDF 177
Cdd:pfam00620   1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVdLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  178 LSCAQLLTKDEGEGTLELAkqVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLATVFGPNILRPQV 247
Cdd:pfam00620  81 IEAAKLPDEEERLEALREL--LRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
PH_RhoGAP2 cd13378
Rho GTPase activating protein 2 Pleckstrin homology (PH) domain; RhoGAP2 (also called RhoGap22 ...
 18-61 1.05e-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: 96.17  E-value: 1.05e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 767963398  18 GGAGEREKVPANPEALLLMASSQRDMEDWVQAIRRVIWAPLGGG 61
Cdd:cd13378   73 GGAGDREKVPMNHEAFLLMANSQSDMEDWVKAIRRVIWAPFGGG 116
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 516-606 4.60e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 4.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 516 REHARRSEALQG---LVTELRAELCRQRTEYERSVKRIEEGSADLRKRMSRLEEELDQEKKKYIMLEIKLRNSERAREDA 592
Cdd:COG1196  291 YELLAELARLEQdiaRLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370

                         90
                 ....*....|....
gi 767963398 593 ERRNQLLQREMEEF 606
Cdd:COG1196  371 EAELAEAEEELEEL 384
THOC7 pfam05615
Tho complex subunit 7; The Tho complex is involved in transcription elongation and mRNA export ...
 538-595 9.89e-05

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


Pssm-ID: 461692 [Multi-domain]  Cd Length: 135  Bit Score: 42.64  E-value: 9.89e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767963398  538 RQRTEYERSVKRIEEGSADLRKRMSRLEEELDQEK--KKYIM---LEIKLRNSERAREDAERR 595
Cdd:pfam05615  72 RERENYEAEKEEIEEEIEAVREEIEELKERLEEAKrtRKNREeydALAEKINENPSREETEKQ 134
PRK14143 PRK14143
heat shock protein GrpE; Provisional
 477-589 3.08e-04

heat shock protein GrpE; Provisional


Pssm-ID: 237624 [Multi-domain]  Cd Length: 238  Bit Score: 42.79  E-value: 3.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 477 PSPLPSSSEDPKSLDLDHSMDEAGAGASNSEPSEPDSPTREHARRSEALQGLVTELRAELCRQRTEYersvKRIeegSAD 556
Cdd:PRK14143  24 SPESSEEVTEQEAELTNPEGDAAEAESSPDSGSAASETAADNAARLAQLEQELESLKQELEELNSQY----MRI---AAD 96

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767963398 557 L---RKRMSRLEEELDQEKKKYIMLEI--KLRNSERAR 589
Cdd:PRK14143  97 FdnfRKRTSREQEDLRLQLKCNTLSEIlpVVDNFERAR 134
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 524-606 1.30e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398   524 ALQGLVTELRAELCRQRTEYERSVKRIEEGSA----------DLRKRMSRLEEELDQEKKKYIMLEIKLRNSERAREDAE 593
Cdd:TIGR02168  292 ALANEISRLEQQKQILRERLANLERQLEELEAqleeleskldELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371

                           90
                   ....*....|...
gi 767963398   594 RRNQLLQREMEEF 606
Cdd:TIGR02168  372 SRLEELEEQLETL 384
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 29-54 3.18e-03

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 37.54  E-value: 3.18e-03
                          10        20
                  ....*....|....*....|....*.
gi 767963398   29 NPEALLLMASSQRDMEDWVQAIRRVI 54
Cdd:pfam00169  79 GKRTYLLQAESEEERKDWIKAIQSAI 104
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 516-606 6.39e-03

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.10  E-value: 6.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 516 REHARRSEALQGLVTELRAELCRQRTEYERSvkrIEEGSADLRKRMSRLEEELDQEKKKyiMLEIKLRNSERA-REDAER 594
Cdd:cd16269  204 RAKAEAAEQERKLLEEQQRELEQKLEDQERS---YEEHLRQLKEKMEEERENLLKEQER--ALESKLKEQEALlEEGFKE 278

                         90
                 ....*....|..
gi 767963398 595 RNQLLQREMEEF 606
Cdd:cd16269  279 QAELLQEEIRSL 290
 
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 ...
 77-275 9.98e-138

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: 399.51  E-value: 9.98e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  77 GIFGQRLEETVHHERKYGPRLAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGEKPLFDSTTDVHTVASL 156
Cdd:cd04390    1 GVFGQRLEDTVAYERKFGPRLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 157 LKLYLRELPEPVVPFARYEDFLSCAQLLTKDEGEGTLELAKQVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLAT 236
Cdd:cd04390   81 LKLYLRELPEPVIPWAQYEDFLSCAQLLSKDEEKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLAT 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767963398 237 VFGPNILRPQVEDPVTIMEGTSLVQHLMTVLIRKHSQLF 275
Cdd:cd04390  161 VFGPNILRPKVEDPATIMEGTPQIQQLMTVMISKHEPLF 199
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 99-267 3.68e-60

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: 197.91  E-value: 3.68e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  99 PLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGEKPLFDSTTDVHTVASLLKLYLRELPEPVVPFARYEDFL 178
Cdd:cd00159    1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 179 SCAQLLTKDEGEgtLELAKQVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLATVFGPNILRPQVEDPVTIMEGTS 258
Cdd:cd00159   81 ELAKIEDEEERI--EALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSDDELLEDIKK 158


                 ....*....
gi 767963398 259 LVQHLMTVL 267
Cdd:cd00159  159 LNEIVEFLI 167
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 99-271 3.95e-58

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: 192.87  E-value: 3.95e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398    99 PLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGEKP-LFDSTTDVHTVASLLKLYLRELPEPVVPFARYEDF 177
Cdd:smart00324   4 PIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPdLDLSEYDVHDVAGLLKLFLRELPEPLITYELYEEF 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398   178 LSCAQLLTKDEGEGTLELAkqVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLATVFGPNILRPQVEDPVTIMEgT 257
Cdd:smart00324  84 IEAAKLEDETERLRALREL--LSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKD-I 160

                          170
                   ....*....|....
gi 767963398   258 SLVQHLMTVLIRKH 271
Cdd:smart00324 161 RHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 99-247 3.69e-56

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 186.60  E-value: 3.69e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398   99 PLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGEKP-LFDSTTDVHTVASLLKLYLRELPEPVVPFARYEDF 177
Cdd:pfam00620   1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVdLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  178 LSCAQLLTKDEGEGTLELAkqVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLATVFGPNILRPQV 247
Cdd:pfam00620  81 IEAAKLPDEEERLEALREL--LRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 78-275 6.42e-42

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: 150.30  E-value: 6.42e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  78 IFGQRLEEtvhHERKYGPRLApLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCG--EKPLFDSTTDVHTVAS 155
Cdd:cd04386    4 VFGTPLEE---HLKRTGREIA-LPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGtfSLPLDEFYSDPHAVAS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 156 LLKLYLRELPEPVVPFARYEDFLSCAQLltKDEGEGTLELAKQVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLA 235
Cdd:cd04386   80 ALKSYLRELPDPLLTYNLYEDWVQAANK--PDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIA 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767963398 236 TVFGPNILRPQVEDPVTIMEGTSLVQHLMTV-LIRKHSQLF 275
Cdd:cd04386  158 IVLAPNLLWAKNEGSLAEMAAGTSVHVVAIVeLIISHADWF 198
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 78-268 2.44e-40

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: 145.68  E-value: 2.44e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  78 IFGQRLEEtVHHERKYGPRLaPLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGEKPLFDSTTDVHTVASLL 157
Cdd:cd04393    2 VFGVPLQE-LQQAGQPENGV-PAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEEVDLSKEADVCSAASLL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 158 KLYLRELPEPVVPFARYEDFLSCAQlLTKDEGEGTLELAKQVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLATV 237
Cdd:cd04393   80 RLFLQELPEGLIPASLQIRLMQLYQ-DYNGEDEFGRKLRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTAENLAAV 158

                        170       180       190
                 ....*....|....*....|....*....|...
gi 767963398 238 FGPNI--LRPQVEDpvtiMEGTSLVQHLMTVLI 268
Cdd:cd04393  159 FGPDVfhVYTDVED----MKEQEICSRIMAKLL 187
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 74-246 1.05e-39

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: 144.02  E-value: 1.05e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  74 LPPGIFGQRLEETVHHERKYGPrlAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGEKPLFDSTTDVHTV 153
Cdd:cd04404    1 LPTQQFGVSLQFLKEKNPEQEP--IPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYNMGEPVDFDQYEDVHLP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 154 ASLLKLYLRELPEPVVPFARYEDFLSCAQLLTKDEGEGTLELakqVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQN 233
Cdd:cd04404   79 AVILKTFLRELPEPLLTFDLYDDIVGFLNVDKEERVERVKQL---LQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSN 155

                        170
                 ....*....|...
gi 767963398 234 LATVFGPNILRPQ 246
Cdd:cd04404  156 LAVVFGPNLLWAK 168
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 77-251 1.23e-34

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: 129.85  E-value: 1.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  77 GIFGQRLEETVhherKYGPRLAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGEKPLFDSTT--DVHTVA 154
Cdd:cd04383    1 KLFNGSLEEYI----QDSGQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGEDPLADDQNdhDINSVA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 155 SLLKLYLRELPEPVVPFARYEDFLSCAQLltKDEGEGTLELAKQVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNL 234
Cdd:cd04383   77 GVLKLYFRGLENPLFPKERFEDLMSCVKL--ENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNL 154

                        170
                 ....*....|....*...
gi 767963398 235 ATVFGPNILR-PQVEDPV 251
Cdd:cd04383  155 AICFGPTLMPvPEGQDQV 172
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
 78-242 1.48e-34

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: 129.40  E-value: 1.48e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  78 IFGQRLEETV----HHERKYGprlAPLLVEQCVDFI-RERGLTEEGLFRMPGQANLVRDLQDSFDC-GEKPLFDSTT--D 149
Cdd:cd04400    1 IFGSPLEEAVelssHKYNGRD---LPSVVYRCIEYLdKNRAIYEEGIFRLSGSASVIKQLKERFNTeYDVDLFSSSLypD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 150 VHTVASLLKLYLRELPEPVVPFARYEDFLSCAQLLTkDEGEGTLELAKQVSNLPQANYNLLRYICKFLDEVQAYSNVNKM 229
Cdd:cd04400   78 VHTVAGLLKLYLRELPTLILGGELHNDFKRLVEENH-DRSQRALELKDLVSQLPQANYDLLYVLFSFLRKIIEHSDVNKM 156

                        170
                 ....*....|....*
gi 767963398 230 SVQNLATVFGP--NI 242
Cdd:cd04400  157 NLRNVCIVFSPtlNI 171
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 79-275 1.01e-33

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: 127.52  E-value: 1.01e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  79 FGQRLEET-VHHERKYgprlAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCG--EKPLFDST-TDVHTVA 154
Cdd:cd04395    2 FGVPLDDCpPSSENPY----VPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRGgfDIDLQDPRwRDVNVVS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 155 SLLKLYLRELPEPVVPFARYEDFLSCAQLltKDEGEGTLELAKQVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNL 234
Cdd:cd04395   78 SLLKSFFRKLPEPLFTNELYPDFIEANRI--EDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNL 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767963398 235 ATVFGPNILRPQvEDPVTIMegtslVQHL------MTVLIRKHSQLF 275
Cdd:cd04395  156 AIVFGPTLVRTS-DDNMETM-----VTHMpdqckiVETLIQHYDWFF 196
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 93-267 1.36e-33

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: 127.02  E-value: 1.36e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  93 YGPRLAPL---LVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGEKPLFDSTTDVHTVASLLKLYLRELPEPVV 169
Cdd:cd04382    9 FDPSTSPMipaLIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLSKVDIHVICGCLKDFLRSLKEPLI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 170 PFARYEDFLSCAQLLTKDEGEgtLELAKQVSNLPQANYNLLRYICKFLDEVqAYSNVNKMSVQNLATVFGPNI---LRPQ 246
Cdd:cd04382   89 TFALWKEFMEAAEILDEDNSR--AALYQAISELPQPNRDTLAFLILHLQRV-AQSPECKMDINNLARVFGPTIvgySVPN 165

                        170       180
                 ....*....|....*....|.
gi 767963398 247 VeDPVTIMEGTSLVQHLMTVL 267
Cdd:cd04382  166 P-DPMTILQDTVRQPRVVERL 185
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 79-243 2.18e-33

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: 126.36  E-value: 2.18e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  79 FGQRLEETVHHERKygprLAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCG-------EKPLFDSttDVH 151
Cdd:cd04398    1 FGVPLEDLILREGD----NVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDplnvlliSPEDYES--DIH 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 152 TVASLLKLYLRELPEPVVPFARYEDFLSCAQLltKDEGEGTLELAKQVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSV 231
Cdd:cd04398   75 SVASLLKLFFRELPEPLLTKALSREFIEAAKI--EDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSV 152

                        170
                 ....*....|..
gi 767963398 232 QNLATVFGPNIL 243
Cdd:cd04398  153 NNLAIIWGPTLM 164
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 99-275 4.10e-31

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: 119.93  E-value: 4.10e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  99 PLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDC-GEKPLFDSTT--DVHTVASLLKLYLRELPEPVVPFARYE 175
Cdd:cd04372   17 PMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRdGEKADISATVypDINVITGALKLYFRDLPIPVITYDTYP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 176 DFLSCAQLLTKDEgegTLELAKQ-VSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLATVFGPNILRPQVEDPVTIM 254
Cdd:cd04372   97 KFIDAAKISNPDE---RLEAVHEaLMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGPTLMRPPEDSALTTL 173

                        170       180
                 ....*....|....*....|.
gi 767963398 255 EGTSLVQHLMTVLIRKHSQLF 275
Cdd:cd04372  174 NDMRYQILIVQLLITNEDVLF 194
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 79-248 7.28e-31

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: 119.03  E-value: 7.28e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  79 FGQRLEETVHHERKYGPRLapllVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGEKPLFDSTT--DVHTVASL 156
Cdd:cd04403    1 FGCHLEALCQRENSTVPKF----VRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDHDEKLDLDDSKweDIHVITGA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 157 LKLYLRELPEPVVPFARYEDFLSCAQLltKDEGEGTLELAKQVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLAT 236
Cdd:cd04403   77 LKLFFRELPEPLFPYSLFNDFVAAIKL--SDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAI 154

                        170
                 ....*....|..
gi 767963398 237 VFGPNILRPQVE 248
Cdd:cd04403  155 VFGPTLLRPEQE 166
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 99-278 2.36e-30

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: 118.31  E-value: 2.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  99 PLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGEKPLFDSTTDVHTVASLLKLYLRELPEPVVPFARYEDFL 178
Cdd:cd04376   10 PRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVLDENHSVHDVAALLKEFFRDMPDPLLPRELYTAFI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 179 ScAQLLTKDEGEGTLELAKQVsnLPQANYNLLRYICKFLDEVQAYSNV-----------NKMSVQNLATVFGPNILRPQ- 246
Cdd:cd04376   90 G-TALLEPDEQLEALQLLIYL--LPPCNCDTLHRLLKFLHTVAEHAADsidedgqevsgNKMTSLNLATIFGPNLLHKQk 166

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 767963398 247 ------VEDPVTIMEGTSLVQHLMTvLIRKHSQLFTAP 278
Cdd:cd04376  167 sgerefVQASLRIEESTAIINVVQT-MIDNYEELFMVS 203
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 79-268 7.59e-30

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: 116.34  E-value: 7.59e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  79 FGQRLEETVHHERKYGPRLA-PLLVEQCVDFIRERGLTE-EGLFRMPGQANLVRDLQDSFDCGEKPLfDSTTDVHTVASL 156
Cdd:cd04389    1 FGSSLEEIMDRQKEKYPELKlPWILTFLSEKVLALGGFQtEGIFRVPGDIDEVNELKLRVDQWDYPL-SGLEDPHVPASL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 157 LKLYLRELPEPVVPFARYEDFLScaqllTKDEGEGTLELakqVSNLPQANYNLLRYICKFLDEVQAYSNV--NKMSVQNL 234
Cdd:cd04389   80 LKLWLRELEEPLIPDALYQQCIS-----ASEDPDKAVEI---VQKLPIINRLVLCYLINFLQVFAQPENVahTKMDVSNL 151

                        170       180       190
                 ....*....|....*....|....*....|....
gi 767963398 235 ATVFGPNILRPQVEDPVTIMEGTSLVQHLMTVLI 268
Cdd:cd04389  152 AMVFAPNILRCTSDDPRVIFENTRKEMSFLRTLI 185
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 79-258 1.19e-28

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: 112.92  E-value: 1.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  79 FGQRLEETVHHERKygprlAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGEKPLFDSTTDVHTVASLLK 158
Cdd:cd04377    1 FGVSLSSLTSEDRS-----VPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPDSVNLEDYPIHVITSVLK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 159 LYLRELPEPVVPFARYEDFLSCAQLltKDEGEGTLELAKQVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLATVF 238
Cdd:cd04377   76 QWLRELPEPLMTFELYENFLRAMEL--EEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVF 153

                        170       180
                 ....*....|....*....|.
gi 767963398 239 GPNILR-PQVEDPVTIMEGTS 258
Cdd:cd04377  154 APCILRcPDTADPLQSLQDVS 174
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 92-260 3.57e-28

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: 112.13  E-value: 3.57e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  92 KYGPRLAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGeKPLFD-STTDVHTVASLLKLYLRELPEPVVP 170
Cdd:cd04378   10 RDFPDEVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENG-KDLVElSELSPHDISSVLKLFLRQLPEPLIL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 171 FARYEDFLSCAQLLTKDEGEGT------------LELAKQVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLATVF 238
Cdd:cd04378   89 FRLYNDFIALAKEIQRDTEEDKapntpievnriiRKLKDLLRQLPASNYNTLQHLIAHLYRVAEQFEENKMSPNNLGIVF 168

                        170       180
                 ....*....|....*....|...
gi 767963398 239 GPNILRPQVED-PVTImegTSLV 260
Cdd:cd04378  169 GPTLIRPRPGDaDVSL---SSLV 188
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
 102-255 1.58e-27

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: 110.18  E-value: 1.58e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 102 VEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSF------DCGEKPLFDSTTDVHTVASLLKLYLRELPEPVVPFARYE 175
Cdd:cd04374   32 VRKCIEAVETRGINEQGLYRVVGVNSKVQKLLSLGldpktsTPGDVDLDNSEWEIKTITSALKTYLRNLPEPLMTYELHN 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 176 DFLSCAQLLTKDEGEGtlELAKQVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLATVFGPNILRPQVEDPVTIME 255
Cdd:cd04374  112 DFINAAKSENLESRVN--AIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLLRPQEETVAAIMD 189
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 99-270 3.43e-27

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: 108.54  E-value: 3.43e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  99 PLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGEKPLFDSTTDVHTVASLLKLYLRELPEPVVPFARYEDFL 178
Cdd:cd04407   16 PIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLRELPEPLMTFAQYNDFL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 179 SCAQLLTKDEgegtlELA---KQVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLATVFGPNILR-PQVEDPVTIM 254
Cdd:cd04407   96 RAVELPEKQE-----QLQaiyRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLRcPDSSDPLTSM 170

                        170
                 ....*....|....*.
gi 767963398 255 EGTSLVQHLMTVLIRK 270
Cdd:cd04407  171 KDVAKTTTCVEMLIKE 186
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
 97-249 5.02e-26

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: 105.78  E-value: 5.02e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  97 LAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGEKPLFD--STTDVHTVASLLKLYLRELPEPVVPFARY 174
Cdd:cd04387   15 KVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVmlSEMDVNAIAGTLKLYFRELPEPLFTDELY 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767963398 175 EDFLSCAQLltKDEGEGTLELAKQVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLATVFGPNILRPQVED 249
Cdd:cd04387   95 PNFAEGIAL--SDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTLLRPSEKE 167
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 99-243 5.31e-25

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: 103.64  E-value: 5.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  99 PLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGE---KPLFDSTTDVHTVASLLKLYLRELPEPVVPFARYE 175
Cdd:cd04396   33 PVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPPdygKSFDWDGYTVHDAASVLRRYLNNLPEPLVPLDLYE 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 176 DF---------------LSCAQLLTKDEGEGTLELAKQVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLATVFGP 240
Cdd:cd04396  113 EFrnplrkrprilqymkGRINEPLNTDIDQAIKEYRDLITRLPNLNRQLLLYLLDLLAVFARNSDKNLMTASNLAAIFQP 192


                 ...
gi 767963398 241 NIL 243
Cdd:cd04396  193 GIL 195
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 99-275 9.77e-25

RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP20-like proteins. ArhGAP20, also known as KIAA1391 and RA-RhoGAP, contains a RhoGAP, a RA, and a PH domain, and ANXL repeats. ArhGAP20 is activated by Rap1 and induces inactivation of Rho, which in turn leads to neurite outgrowth. 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: 239867  Cd Length: 192  Bit Score: 101.99  E-value: 9.77e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  99 PLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGEKPLFDSTTdVHTVASLLKLYLRELPEPVVPFARYEDFL 178
Cdd:cd04402   16 PKPILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNSGVEVDLKAEP-VLLLASVLKDFLRNIPGSLLSSDLYEEWM 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 179 SCAQllTKDEGEGTLELAKQVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLATVFGPNILRPQVEDPVTiMEGTS 258
Cdd:cd04402   95 SALD--QENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIAPSLLWPPASSELQ-NEDLK 171

                        170
                 ....*....|....*..
gi 767963398 259 LVQHLMTVLIRKHSQLF 275
Cdd:cd04402  172 KVTSLVQFLIENCQEIF 188
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 95-268 1.04e-24

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: 101.38  E-value: 1.04e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  95 PRLAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDC-GEKPLFDSTTDVHTVASLLKLYLRELPEPVVPFAR 173
Cdd:cd04373   12 EKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQdHNLDLVSKDFTVNAVAGALKSFFSELPDPLIPYSM 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 174 YEDFLSCAQLLtkDEGEGTLELAKQVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLATVFGPNILRPQVEDpVTI 253
Cdd:cd04373   92 HLELVEAAKIN--DREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWPTLMRPDFTS-MEA 168

                        170
                 ....*....|....*
gi 767963398 254 MEGTSLVQHLMTVLI 268
Cdd:cd04373  169 LSATRIYQTIIETFI 183
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 99-265 1.82e-24

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: 100.85  E-value: 1.82e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  99 PLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSF--DCGEKPLFDSTTDVHTVASLLKLYLRELPEPVVPFARYED 176
Cdd:cd04385   16 PVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFrkDARSVQLREGEYTVHDVADVLKRFLRDLPDPLLTSELHAE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 177 FLSCAQLLTKDEGegtLELAKQV-SNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLATVFGPNILRPQVEDPVTIME 255
Cdd:cd04385   96 WIEAAELENKDER---IARYKELiRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTLFQTDEHSVGQTSH 172

                        170
                 ....*....|
gi 767963398 256 GTSLVQHLMT 265
Cdd:cd04385  173 EVKVIEDLID 182
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 79-242 2.59e-24

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: 100.20  E-value: 2.59e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  79 FGQRLEETVHHERKY-GPRLaPLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGEKPLFDSTtDVHTVASLL 157
Cdd:cd04381    1 FGASLSLAVERSRCHdGIDL-PLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRRESPNLEEY-EPPTVASLL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 158 KLYLRELPEPVVP---FARYEDflSCAqllTKDEGEGTLELAKQVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNL 234
Cdd:cd04381   79 KQYLRELPEPLLTkelMPRFEE--ACG---RPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNI 153


                 ....*...
gi 767963398 235 ATVFGPNI 242
Cdd:cd04381  154 SIVLSPTV 161
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 78-279 3.05e-24

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: 101.27  E-value: 3.05e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  78 IFGQRLEETVHHERKYGPRL-APLLVEQCVDFIRERGLTEEGLFRMPGQA----NLVRDLQDSFDCGEKpLFDSTTdVHT 152
Cdd:cd04391    1 LFGVPLSTLLERDQKKVPGSkVPLIFQKLINKLEERGLETEGILRIPGSAqrvkFLCQELEAKFYEGTF-LWDQVK-QHD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 153 VASLLKLYLRELPEPVVPFARYEDFLSCAQLLTKDEGEGTLELAkqVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQ 232
Cdd:cd04391   79 AASLLKLFIRELPQPLLTVEYLPAFYSVQGLPSKKDQLQALNLL--VLLLPEANRDTLKALLEFLQKVVDHEEKNKMNLW 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767963398 233 NLATVFGPNILRPQVEDPVTI------MEGTSLVQHLMTVLIRKHSQLFTAPV 279
Cdd:cd04391  157 NVAMIMAPNLFPPRGKHSKDNeslqeeVNMAAGCANIMRLLIRYQDLLWTVPS 209
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 79-262 4.68e-24

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: 100.65  E-value: 4.68e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  79 FGQRLEETVhherKYGPRLAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGEKPLFDSTTDVHTVASLLK 158
Cdd:cd04409    1 FGADFAQVA----KKSPDGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSPHDISNVLK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 159 LYLRELPEPVVPFARYEDFLSCAQ------------LLTKDEGEGT--------LELAKQVSNLPQANYNLLRYICKFLD 218
Cdd:cd04409   77 LYLRQLPEPLILFRLYNEFIGLAKesqhvnetqeakKNSDKKWPNMctelnrilLKSKDLLRQLPAPNYNTLQFLIVHLH 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767963398 219 EVQAYSNVNKMSVQNLATVFGPNILRP-QVEDPVTImegTSLVQH 262
Cdd:cd04409  157 RVSEQAEENKMSASNLGIIFGPTLIRPrPTDATVSL---SSLVDY 198
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
 92-253 5.44e-24

RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP (Gem interacting protein). 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. 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: 239873  Cd Length: 200  Bit Score: 99.89  E-value: 5.44e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  92 KYGPRLAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGEKPLFDSTTDVHTVASLLKLYLRELPEPVVPF 171
Cdd:cd04408   10 RDFPEEVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVDLSGHSPHDITSVLKHFLKELPEPVLPF 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 172 ARYEDFLSCAQLLTKDEGEGTLE----------LAKQVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLATVFGPN 241
Cdd:cd04408   90 QLYDDFIALAKELQRDSEKAAESpsiveniirsLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDNKMSPNNLGIVFGPT 169

                        170
                 ....*....|..
gi 767963398 242 ILRPQVEDPVTI 253
Cdd:cd04408  170 LLRPLVGGDVSM 181
PH_RhoGAP2 cd13378
Rho GTPase activating protein 2 Pleckstrin homology (PH) domain; RhoGAP2 (also called RhoGap22 ...
 18-61 1.05e-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: 96.17  E-value: 1.05e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 767963398  18 GGAGEREKVPANPEALLLMASSQRDMEDWVQAIRRVIWAPLGGG 61
Cdd:cd13378   73 GGAGDREKVPMNHEAFLLMANSQSDMEDWVKAIRRVIWAPFGGG 116
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 104-250 1.68e-23

RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in OCRL1-like proteins. OCRL1 (oculocerebrorenal syndrome of Lowe 1)-like proteins contain two conserved domains: a central inositol polyphosphate 5-phosphatase domain and a C-terminal Rho GAP domain, this GAP domain lacks the catalytic residue and therefore maybe inactive. OCRL-like proteins are type II inositol polyphosphate 5-phosphatases that can hydrolyze lipid PI(4,5)P2 and PI(3,4,5)P3 and soluble Ins(1,4,5)P3 and Ins(1,3,4,5)P4, but their individual specificities vary. The functionality of the RhoGAP domain is still unclear. 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: 239845  Cd Length: 220  Bit Score: 98.95  E-value: 1.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 104 QCVDFIRERGLTEEGLFRMPGQ----ANLVRDLQDSFDCGeKPlFDSTTDVHTVASLLKLYLRELPEPVVPFARYEDFLS 179
Cdd:cd04380   56 RLVDYLYTRGLAQEGLFEEPGLpsepGELLAEIRDALDTG-SP-FNSPGSAESVAEALLLFLESLPDPIIPYSLYERLLE 133

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767963398 180 CAQLLTKDegegtlelAKQV--SNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLATVFGPNILRPQVEDP 250
Cdd:cd04380  134 AVANNEED--------KRQVirISLPPVHRNVFVYLCSFLRELLSESADRGLDENTLATIFGRVLLRDPPRAG 198
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 99-248 5.38e-23

RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of CdGAP-like proteins; CdGAP contains an N-terminal RhoGAP domain and a C-terminal proline-rich region, and it is active on both Cdc42 and Rac1 but not RhoA. CdGAP is recruited to focal adhesions via the interaction with the scaffold protein actopaxin (alpha-parvin). 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: 239849 [Multi-domain]  Cd Length: 195  Bit Score: 96.80  E-value: 5.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  99 PLLVEQCVDFIRERGLTEeGLFRMPGQANLVRDLQDSFDCGEKP---LFDSTTDVHTVASLLKLYLRELPEPVVPFARYE 175
Cdd:cd04384   19 PQVLKSCTEFIEKHGIVD-GIYRLSGIASNIQRLRHEFDSEQIPdltKDVYIQDIHSVSSLCKLYFRELPNPLLTYQLYE 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767963398 176 DFLSCAQlltKDEGEGTLELAKQV-SNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLATVFGPNILR-PQVE 248
Cdd:cd04384   98 KFSEAVS---AASDEERLEKIHDViQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVWAPNLLRsKQIE 169
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 79-274 8.53e-23

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: 96.77  E-value: 8.53e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  79 FGQRLEETVhhERKYGPRLAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGEKPL---FDSTTDVHTVAS 155
Cdd:cd04379    1 FGVPLSRLV--EREGESRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAVelsEELYPDINVITG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 156 LLKLYLRELPEPVVPFARYEDFLSCAQLLTKDEGEGTLELA-KQVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNL 234
Cdd:cd04379   79 VLKDYLRELPEPLITPQLYEMVLEALAVALPNDVQTNTHLTlSIIDCLPLSAKATLLLLLDHLSLVLSNSERNKMTPQNL 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 767963398 235 ATVFGPNILRPQVEDPVTIMEGTSLVQHLMTVLIRKHSQL 274
Cdd:cd04379  159 AVCFGPVLMFCSQEFSRYGISPTSKMAAVSTVDFKQHIEV 198
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 78-243 1.48e-22

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: 96.00  E-value: 1.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  78 IFGQRLEETVH-HERKYGpRLAPLLVEQCvDFIrERGLTEEGLFRMPGQANLVRDLQDSFDCGEKPLfdSTTDVHTVASL 156
Cdd:cd04394    1 VFGVPLHSLPHsTVPEYG-NVPKFLVDAC-TFL-LDHLSTEGLFRKSGSVVRQKELKAKLEGGEACL--SSALPCDVAGL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 157 LKLYLRELPEPVVPFARYEDFLSCAQLLTKDEGEGTLELAKQVsnLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLAT 236
Cdd:cd04394   76 LKQFFRELPEPLLPYDLHEALLKAQELPTDEERKSATLLLTCL--LPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAV 153


                 ....*..
gi 767963398 237 VFGPNIL 243
Cdd:cd04394  154 IFAPNLF 160
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 102-278 1.13e-21

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: 93.68  E-value: 1.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 102 VEQCVDFIrERGLTEEGLFRMPGqaNLVR--DLQDSFDCGEKPLFDSTT-DVHTVASLLKLYLRELPEPVVPFARYEDFL 178
Cdd:cd04392   13 IYQLIEYL-EKNLRVEGLFRKPG--NSARqqELRDLLNSGTDLDLESGGfHAHDCATVLKGFLGELPEPLLTHAHYPAHL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 179 SCAQLLTKDEGE---GTLELAKQVSN-------LPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLATVFGPNILRPQVE 248
Cdd:cd04392   90 QIADLCQFDEKGnktSAPDKERLLEAlqlllllLPEENRNLLKLILDLLYQTAKHEDKNKMSADNLALLFTPHLICPRNL 169

                        170       180       190
                 ....*....|....*....|....*....|
gi 767963398 249 DPVTIMEGTSLVQHLMTVLIRKHSQLFTAP 278
Cdd:cd04392  170 TPEDLHENAQKLNSIVTFMIKHSQKLFKAP 199
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 99-252 9.31e-21

RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal LRG1-like proteins. Yeast Lrg1p is required for efficient cell fusion, and mother-daughter cell separation, possibly through acting as a RhoGAP specifically regulating 1,3-beta-glucan synthesis. 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: 239862  Cd Length: 213  Bit Score: 90.89  E-value: 9.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  99 PLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCG--EKPLFDSTTDVHtVASLLKLYLRELPEPVVPFARYED 176
Cdd:cd04397   28 PALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNptEVPDLSKENPVQ-LAALLKKFLRELPDPLLTFKLYRL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 177 FLSCAQLLTKDEGEGTLELAkqVSNLPQANYNLLRYICKFLDEVQAYSNV-----NKMSVQNLATVFGPNILRPQVEDPV 251
Cdd:cd04397  107 WISSQKIEDEEERKRVLHLV--YCLLPKYHRDTMEVLFSFLKWVSSFSHIdeetgSKMDIHNLATVITPNILYSKTDNPN 184


                 .
gi 767963398 252 T 252
Cdd:cd04397  185 T 185
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 96-258 2.54e-19

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: 86.21  E-value: 2.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  96 RLAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDCGEKPLFDSTTDVHTVASLLKLYLRELPEPVVPFARYE 175
Cdd:cd04406   13 RSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVNLDDYNIHVIASVFKQWLRDLPNPLMTFELYE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 176 DFLSCAQLLTKDEG-EGTLELAKQVSnlpQANYNLLRYICKFLDEVQAYSNVNKMSVQNLATVFGPNILR-PQVEDPVTI 253
Cdd:cd04406   93 EFLRAMGLQERRETvRGVYSVIDQLS---RTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCILRcPDTTDPLQS 169


                 ....*
gi 767963398 254 MEGTS 258
Cdd:cd04406  170 VQDIS 174
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 95-255 1.55e-16

RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in the p85 isoforms of the regulatory subunit of the class IA PI3K (phosphatidylinositol 3'-kinase). This domain is also called Bcr (breakpoint cluster region protein) homology (BH) domain. Class IA PI3Ks are heterodimers, containing a regulatory subunit (p85) and a catalytic subunit (p110) and are activated by growth factor receptor tyrosine kinases (RTKs); this activation is mediated by the p85 subunit. p85 isoforms, alpha and beta, contain a C-terminal p110-binding domain flanked by two SH2 domains, an N-terminal SH3 domain, and a RhoGAP domain flanked by two proline-rich regions. 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: 239853  Cd Length: 200  Bit Score: 78.38  E-value: 1.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  95 PRLAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVrDLQDSFDCGEKPLFDSTTDVHTVASLLKLYLRELPEPVVPFARY 174
Cdd:cd04388   12 PDVAPPLLIKLVEAIEKKGLESSTLYRTQSSSSLT-ELRQILDCDAASVDLEQFDVAALADALKRYLLDLPNPVIPAPVY 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 175 EDFLSCAQ-LLTKDEGEGTLELAKQVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLATVFGPNILRPQV------ 247
Cdd:cd04388   91 SEMISRAQeVQSSDEYAQLLRKLIRSPNLPHQYWLTLQYLLKHFFRLCQSSSKNLLSARALAEIFSPLLFRFQPassdsp 170


                 ....*...
gi 767963398 248 EDPVTIME 255
Cdd:cd04388  171 EFHIRIIE 178
PH_RhoGap24 cd13379
Rho GTPase activating protein 24 Pleckstrin homology (PH) domain; RhoGap24 (also called ...
 20-61 4.32e-16

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: 74.62  E-value: 4.32e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 767963398  20 AGEREKVPANPEALLLMASSQRDMEDWVQAIRRVIWAPLGGG 61
Cdd:cd13379   73 GGDRERMTANHETYLLMASTQNDMEDWVKSIRRVIWAPFGGG 114
PH_RhoGap25-like cd13263
Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; ...
 20-61 1.02e-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: 70.49  E-value: 1.02e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 767963398  20 AGEREKVPANPEALLLMASSQRDMEDWVQAIRRVIWAPLGGG 61
Cdd:cd13263   73 GGGGDRMTSNHDSYLLMANSQAEMEEWVKVIRRVIGSPFGGG 114
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 78-242 1.11e-13

RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of DLC1-like proteins. DLC1 shows in vitro GAP activity towards RhoA and CDC42. Beside its C-terminal GAP domain, DLC1 also contains a SAM (sterile alpha motif) and a START (StAR-related lipid transfer action) domain. DLC1 has tumor suppressor activity in cell culture. 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: 239840  Cd Length: 220  Bit Score: 70.52  E-value: 1.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  78 IFGQRLeeTVHHERkYGPRLaPLLVEQCVDFIRERGLTEEGLFRMPGQANLVRDLQDSFDC-GEKPLFDSTTdVHTVASL 156
Cdd:cd04375    4 VFGVPL--LVNLQR-TGQPL-PRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESsTDNVNYDGQQ-AYDVADM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 157 LKLYLRELPEPVVPFARYEDFLSCAQLLTKDEGEGTLELAkqVSNLPQANYNLLRYICKFLDEVQAYSNVNKMSVQNLAT 236
Cdd:cd04375   79 LKQYFRDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCA--ILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAV 156


                 ....*.
gi 767963398 237 VFGPNI 242
Cdd:cd04375  157 CLAPSL 162
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 146-275 1.01e-06

RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal RGD2-like proteins. Yeast Rgd2 is a GAP protein for Cdc42 and Rho5. 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: 239864  Cd Length: 212  Bit Score: 50.02  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 146 STTDVHTVASLLKLYLRELPEPVVPFARYEDfLSCAQLLTKDEGEGTLE-----LAKQVSNLPQANYNLLRYICKFLD-- 218
Cdd:cd04399   74 KKFEPSTVASVLKLYLLELPDSLIPHDIYDL-IRSLYSAYPPSQEDSDTariqgLQSTLSQLPKSHIATLDAIITHFYrl 152

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767963398 219 -EVQAYSNVNKMSVQNLATVFGPNILRPQVEDPVTImeGTSLVQHLMTVLIRKHSQLF 275
Cdd:cd04399  153 iEITKMGESEEEYADKLATSLSREILRPIIESLLTI--GDKHGYKFFRDLLTHKDQIF 208
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 516-606 4.60e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 4.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 516 REHARRSEALQG---LVTELRAELCRQRTEYERSVKRIEEGSADLRKRMSRLEEELDQEKKKYIMLEIKLRNSERAREDA 592
Cdd:COG1196  291 YELLAELARLEQdiaRLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370

                         90
                 ....*....|....
gi 767963398 593 ERRNQLLQREMEEF 606
Cdd:COG1196  371 EAELAEAEEELEEL 384
THOC7 pfam05615
Tho complex subunit 7; The Tho complex is involved in transcription elongation and mRNA export ...
 538-595 9.89e-05

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


Pssm-ID: 461692 [Multi-domain]  Cd Length: 135  Bit Score: 42.64  E-value: 9.89e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767963398  538 RQRTEYERSVKRIEEGSADLRKRMSRLEEELDQEK--KKYIM---LEIKLRNSERAREDAERR 595
Cdd:pfam05615  72 RERENYEAEKEEIEEEIEAVREEIEELKERLEEAKrtRKNREeydALAEKINENPSREETEKQ 134
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 533-614 1.88e-04

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


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 41.91  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  533 RAELCRQRT-EYERSVKRIEEGSADLRKRMSRLEEELDQEKKKYIMLEIKLRNSERAREDAE---RRNQLLQREMEEFFS 608
Cdd:pfam12718  15 RAEELEEKVkELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNEnltRKIQLLEEELEESDK 94


                  ....*.
gi 767963398  609 TLGSLT 614
Cdd:pfam12718  95 RLKETT 100
PRK14143 PRK14143
heat shock protein GrpE; Provisional
 477-589 3.08e-04

heat shock protein GrpE; Provisional


Pssm-ID: 237624 [Multi-domain]  Cd Length: 238  Bit Score: 42.79  E-value: 3.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 477 PSPLPSSSEDPKSLDLDHSMDEAGAGASNSEPSEPDSPTREHARRSEALQGLVTELRAELCRQRTEYersvKRIeegSAD 556
Cdd:PRK14143  24 SPESSEEVTEQEAELTNPEGDAAEAESSPDSGSAASETAADNAARLAQLEQELESLKQELEELNSQY----MRI---AAD 96

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767963398 557 L---RKRMSRLEEELDQEKKKYIMLEI--KLRNSERAR 589
Cdd:PRK14143  97 FdnfRKRTSREQEDLRLQLKCNTLSEIlpVVDNFERAR 134
PRK09039 PRK09039
peptidoglycan -binding protein;
483-621 7.47e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 42.26  E-value: 7.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 483 SSEDPKSLDLDHSMDEAGAGASNSEpSEPD---SPTREHARRSEALQGLVTELRAELCRQRTEYERSVKRIE---EGSAD 556
Cdd:PRK09039  70 SLERQGNQDLQDSVANLRASLSAAE-AERSrlqALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVEllnQQIAA 148

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767963398 557 LRKRMSRLEEELDQEKKkyimleiklRNSERAREDAE----------RRNQLLQREMEEFFSTLGSLTVGAKGAR 621
Cdd:PRK09039 149 LRRQLAALEAALDASEK---------RDRESQAKIADlgrrlnvalaQRVQELNRYRSEFFGRLREILGDREGIR 214
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
491-605 7.92e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.54  E-value: 7.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 491 DLDHSMDEAGAGASNSEPSEPDSPTREHARRSEALQGLVTELRAELCRQRTEYERSVKRIEEGSADLRKRMSRLEEELdQ 570
Cdd:COG2433  384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREI-R 462

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767963398 571 EKKKYIMLEIKLRNSERAREDAERRNQLLQREMEE 605
Cdd:COG2433  463 KDREISRLDREIERLERELEEERERIEELKRKLER 497
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 516-605 1.09e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 516 REHARRSEALQGLVTELRAELCRQRTEYERSVKRIEEGSADLR---KRMSRLEEELDQEKKKYIMLEIKLRNSERAREDA 592
Cdd:COG1196  249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellAELARLEQDIARLEERRRELEERLEELEEELAEL 328

                         90
                 ....*....|...
gi 767963398 593 ERRNQLLQREMEE 605
Cdd:COG1196  329 EEELEELEEELEE 341
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 531-613 1.14e-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: 39.09  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  531 ELRAELCRQRTEYERSVKRIEEGSADLRKRMSRLEEELdQEKKKYIM-LEIKLRNSERAREDAERRNQLLQREMEEFFST 609
Cdd:pfam13863  10 LVQLALDAKREEIERLEELLKQREEELEKKEQELKEDL-IKFDKFLKeNDAKRRRALKKAEEETKLKKEKEKEIKKLTAQ 88


                  ....
gi 767963398  610 LGSL 613
Cdd:pfam13863  89 IEEL 92
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 477-605 1.15e-03

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: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  477 PSPLPSSSEDPKSLDLDHSMDEAGAGASNSEPSEPDS---PTREHARRSEALQGLVTELRAELCRQR-TEYERSVKRIEE 552
Cdd:pfam15709 280 LSSKYDAEESQVSIDGRSSPTQTFVVTGNMESEEERSeedPSKALLEKREQEKASRDRLRAERAEMRrLEVERKRREQEE 359

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  553 G---SADLRKRMSRLEEELDQEKKKyIMLEIKLRNS----ERAREDAERRNQLLQREMEE 605
Cdd:pfam15709 360 QrrlQQEQLERAEKMREELELEQQR-RFEEIRLRKQrleeERQRQEEEERKQRLQLQAAQ 418
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 524-606 1.30e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398   524 ALQGLVTELRAELCRQRTEYERSVKRIEEGSA----------DLRKRMSRLEEELDQEKKKYIMLEIKLRNSERAREDAE 593
Cdd:TIGR02168  292 ALANEISRLEQQKQILRERLANLERQLEELEAqleeleskldELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371

                           90
                   ....*....|...
gi 767963398   594 RRNQLLQREMEEF 606
Cdd:TIGR02168  372 SRLEELEEQLETL 384
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 516-606 1.35e-03

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


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 39.16  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  516 REHARRSEALQGLvTELRAELcrqrTEYERSVKRIEEGSADLRKRMSRLEEELDQEKKkyiMLEIKLRNSERAREDAERR 595
Cdd:pfam07926  47 RELVLHAEDIKAL-QALREEL----NELKAEIAELKAEAESAKAELEESEESWEEQKK---ELEKELSELEKRIEDLNEQ 118

                          90
                  ....*....|.
gi 767963398  596 NQLLQREMEEF 606
Cdd:pfam07926 119 NKLLHDQLESL 129
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 517-605 1.93e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 1.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 517 EHARRS-----EALQGLVTELRAELCRQRTEY---ERSVKRIEEGSADLRKRMSRLEE----------------ELDQEK 572
Cdd:COG1579   23 EHRLKElpaelAELEDELAALEARLEAAKTELedlEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkeyealqkEIESLK 102

                         90       100       110
                 ....*....|....*....|....*....|...
gi 767963398 573 KKYIMLEIKLRNSERAREDAERRNQLLQREMEE 605
Cdd:COG1579  103 RRISDLEDEILELMERIEELEEELAELEAELAE 135
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 516-605 2.85e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 2.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 516 REHARRSEALQGLVTELRAELCRQRTEYERSVKRIEEgsadLRKRMSRLEEELDQEKKKYIMLEIKLRNSERAREDAERR 595
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELEE----LRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310

                         90
                 ....*....|
gi 767963398 596 NQLLQREMEE 605
Cdd:COG1196  311 RRELEERLEE 320
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 517-605 3.07e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 3.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398   517 EHARRSEAlqglvTELRAELCRQRTEYERSVKRIEEGSADLRKRMSRLEEELDQEKKKYIMLEIKLRNSERAREDAERRN 596
Cdd:TIGR02168  766 LEERLEEA-----EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840


                   ....*....
gi 767963398   597 QLLQREMEE 605
Cdd:TIGR02168  841 EDLEEQIEE 849
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 29-54 3.18e-03

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 37.54  E-value: 3.18e-03
                          10        20
                  ....*....|....*....|....*.
gi 767963398   29 NPEALLLMASSQRDMEDWVQAIRRVI 54
Cdd:pfam00169  79 GKRTYLLQAESEEERKDWIKAIQSAI 104
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
516-605 3.37e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 3.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 516 REHARRSEALQGLVTELRAELCRQRTEYERSVKRIEEgsadLRKRMSRLEEELDQEKKKYIMLEIKLRNSERAREDAERR 595
Cdd:COG4372   34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQ----ARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109

                         90
                 ....*....|
gi 767963398 596 NQLLQREMEE 605
Cdd:COG4372  110 AEELQEELEE 119
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 517-613 3.76e-03

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: 40.44  E-value: 3.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398   517 EHARRSEALQGLVTELRAELCRQRTEYERSVKRIEEgsadLRKRMSRLEEELDQE---------------KKKYIMLEIK 581
Cdd:TIGR02169  227 ELLKEKEALERQKEAIERQLASLEEELEKLTEEISE----LEKRLEEIEQLLEELnkkikdlgeeeqlrvKEKIGELEAE 302

                           90       100       110
                   ....*....|....*....|....*....|..
gi 767963398   582 LRNSERAREDAERRNQLLQREMEEFFSTLGSL 613
Cdd:TIGR02169  303 IASLERSIAEKERELEDAEERLAKLEAEIDKL 334
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 533-606 4.52e-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: 37.59  E-value: 4.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767963398  533 RAElcRQRTEYERSVKRIEEgsaDLRKRMSRLEEEldQEKKKyiMLEIKLRNSERAREDAERRNQLLQREMEEF 606
Cdd:pfam20492   3 EAE--REKQELEERLKQYEE---ETKKAQEELEES--EETAE--ELEEERRQAEEEAERLEQKRQEAEEEKERL 67
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 520-615 5.09e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 39.88  E-value: 5.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  520 RRSEALQGLVTELRAELCRQRTEYERSVKrieegsaDLRKRMSRLEEELDQEKKKYIMLEIKLRNSERARED-AERRNQL 598
Cdd:pfam07888  48 QAQEAANRQREKEKERYKRDREQWERQRR-------ELESRVAELKEELRQSREKHEELEEKYKELSASSEElSEEKDAL 120

                          90       100
                  ....*....|....*....|....*.
gi 767963398  599 LQ---------REMEEFFSTLGSLTV 615
Cdd:pfam07888 121 LAqraaheariRELEEDIKTLTQRVL 146
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 516-606 6.39e-03

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.10  E-value: 6.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 516 REHARRSEALQGLVTELRAELCRQRTEYERSvkrIEEGSADLRKRMSRLEEELDQEKKKyiMLEIKLRNSERA-REDAER 594
Cdd:cd16269  204 RAKAEAAEQERKLLEEQQRELEQKLEDQERS---YEEHLRQLKEKMEEERENLLKEQER--ALESKLKEQEALlEEGFKE 278

                         90
                 ....*....|..
gi 767963398 595 RNQLLQREMEEF 606
Cdd:cd16269  279 QAELLQEEIRSL 290
RhoGAP_fMSB1 cd04401
RhoGAP_fMSB1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 101-269 6.53e-03

RhoGAP_fMSB1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal MSB1-like proteins. Msb1 was originally identified as a multicopy suppressor of temperature sensitive cdc42 mutation. Msb1 is a positive regulator of the Pkc1p-MAPK pathway and 1,3-beta-glucan synthesis, both pathways involve Rho1 regulation. 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: 239866  Cd Length: 198  Bit Score: 38.48  E-value: 6.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 101 LVEQCVDFIRERGLTEEGLFR--MPGQAN-----LVRDLQDSFDC---GEKPLFD--STTDVHTVASLLKLYLRELPEPV 168
Cdd:cd04401    9 LIHNITEELKSRGLDTPLLFLpfRPELSPdkvrsLINSFFPSQNGqlqGTAELLDelRYADPHTLILVLKWIWSRLPGSK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 169 VPFAR-YEDFlscaQLLTKDEGEGT---LELAKQVsnLPQANYNLLRYicKFLD---EVQAYSNVNKMSVQNLATVFGPN 241
Cdd:cd04401   89 VIWWEvYEEF----KARERRSNYPAdafLDLLPQC--LSSPAHASILY--DFFDllsSIAAHSSVNGMSGRKLSKMAGPW 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767963398 242 I--LRPQVEDPVTIMEG-------TSLVQHLMTVLIR 269
Cdd:cd04401  161 AfgKPTGATGPPSFQEGldawvraANATEHLFLAYLR 197
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 517-605 7.77e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 7.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398   517 EHARRSEALQGLVTELRAELCRQRTEYERSVKRIEEGSA---DLRKRMSRLEEELDQEKKKYIMLE--IKLRNSERAR-- 589
Cdd:TIGR02168  327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAeleELESRLEELEEQLETLRSKVAQLElqIASLNNEIERle 406

                           90
                   ....*....|....*....
gi 767963398   590 ---EDAERRNQLLQREMEE 605
Cdd:TIGR02168  407 arlERLEDRRERLQQEIEE 425
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
517-594 7.83e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 7.83e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767963398 517 EHARRSEALqglvTELRAELCRQRTEYERSVKRIEEGSADLRKrmsrLEEELDqEKKKYIMleiKLRNSERAREDAER 594
Cdd:PRK03918 660 EYEELREEY----LELSRELAGLRAELEELEKRREEIKKTLEK----LKEELE-EREKAKK---ELEKLEKALERVEE 725
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
523-605 8.04e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 8.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398 523 EALQGLVTELRAELCRQRTEYERSVKRIEEgsadLRKRMSRLEEELDQEKKKYIMLEIKLRNSERAREDAERRNQLLQRE 602
Cdd:COG4372   90 QAAQAELAQAQEELESLQEEAEELQEELEE----LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165


                 ...
gi 767963398 603 MEE 605
Cdd:COG4372  166 LAA 168
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
 523-605 9.34e-03

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


Pssm-ID: 463600 [Multi-domain]  Cd Length: 139  Bit Score: 36.77  E-value: 9.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767963398  523 EALQGLVTELRAELCRQRTEYERSVKRIEEGsadLRKRMSRLEEELD-------QEKKKYIMLEIKLRNSERAREDAERR 595
Cdd:pfam12474  40 KLEQRQTQELRRLPKRIRAEQKKRLKMFRES---LKQEKKELKQEVEklpkfqrKEAKRQRKEELELEQKHEELEFLQAQ 116

                          90
                  ....*....|
gi 767963398  596 NQLLQREMEE 605
Cdd:pfam12474 117 SEALERELQQ 126
 
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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