NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|49903314|gb|AAH76636|]
View 

Ralbp1 protein [Mus musculus]

Protein Classification

Rho GTPase-activating protein( domain architecture ID 10138155)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
190-371 8.43e-118

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: 348.66  E-value: 8.43e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 190 FGVPLVDAVERTMMYDGVRLPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDREESPNLEEYEPNTVASLLKQ 269
Cdd:cd04381   1 FGASLSLAVERSRCHDGIDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRRESPNLEEYEPPTVASLLKQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 270 YLRDLPENLLTKELMPRFEEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISIVLSPT 349
Cdd:cd04381  81 YLRELPEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNISIVLSPT 160
                       170       180
                ....*....|....*....|..
gi 49903314 350 VQISNRVLYVLFTHVQELFGTV 371
Cdd:cd04381 161 VQISNRLLYALLTHCQELFGNV 182
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
421-599 2.80e-09

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: 60.34  E-value: 2.80e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 421 KDLSKEERLWEVQRILTALK-----RKLREAKRQECETKIAQEIASLSKEDVSKEEM----NENEEVINILLAQENEILT 491
Cdd:COG1196 216 RELKEELKELEAELLLLKLReleaeLEELEAELEELEAELEELEAELAELEAELEELrlelEELELELEEAQAEEYELLA 295
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 492 EQEELLAMEQFLRRQIASEKEEIDRLRAEIAEIQSRQQHGRSETEEYSSDSESESEDEEELQLILEDLQRQNEELEIKNN 571
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
                       170       180
                ....*....|....*....|....*...
gi 49903314 572 HLNQAVHEEREAIIELRVQLRLLQMQRA 599
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLE 403
 
Name Accession Description Interval E-value
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
190-371 8.43e-118

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: 348.66  E-value: 8.43e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 190 FGVPLVDAVERTMMYDGVRLPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDREESPNLEEYEPNTVASLLKQ 269
Cdd:cd04381   1 FGASLSLAVERSRCHDGIDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRRESPNLEEYEPPTVASLLKQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 270 YLRDLPENLLTKELMPRFEEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISIVLSPT 349
Cdd:cd04381  81 YLRELPEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNISIVLSPT 160
                       170       180
                ....*....|....*....|..
gi 49903314 350 VQISNRVLYVLFTHVQELFGTV 371
Cdd:cd04381 161 VQISNRLLYALLTHCQELFGNV 182
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
208-350 3.53e-51

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: 174.76  E-value: 3.53e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314    208 RLPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDREESPN--LEEYEPNTVASLLKQYLRDLPENLLTKELMP 285
Cdd:smart00324   2 PIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDldLSEYDVHDVAGLLKLFLRELPEPLITYELYE 81
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 49903314    286 RFEEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISIVLSPTV 350
Cdd:smart00324  82 EFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTL 146
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
210-349 1.05e-49

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 169.65  E-value: 1.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314   210 PAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDREESP--NLEEYEPNTVASLLKQYLRDLPENLLTKELMPRF 287
Cdd:pfam00620   1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVdlDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49903314   288 EEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISIVLSPT 349
Cdd:pfam00620  81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPT 142
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
421-599 2.80e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 2.80e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 421 KDLSKEERLWEVQRILTALK-----RKLREAKRQECETKIAQEIASLSKEDVSKEEM----NENEEVINILLAQENEILT 491
Cdd:COG1196 216 RELKEELKELEAELLLLKLReleaeLEELEAELEELEAELEELEAELAELEAELEELrlelEELELELEEAQAEEYELLA 295
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 492 EQEELLAMEQFLRRQIASEKEEIDRLRAEIAEIQSRQQHGRSETEEYSSDSESESEDEEELQLILEDLQRQNEELEIKNN 571
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
                       170       180
                ....*....|....*....|....*...
gi 49903314 572 HLNQAVHEEREAIIELRVQLRLLQMQRA 599
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLE 403
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
398-598 4.13e-07

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: 53.52  E-value: 4.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314    398 IKEEIRRQeflLNCLHRDLQGGIKDLSKEERLWEVQRIL-----TALKRKLREAKRQ------ECETKIAQEIASLSKED 466
Cdd:TIGR02168  194 ILNELERQ---LKSLERQAEKAERYKELKAELRELELALlvlrlEELREELEELQEElkeaeeELEELTAELQELEEKLE 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314    467 VSKEEMNENEEVINILLAQENEILTEQEELLAMEQFLRRQIASEKEEIDRLRAEIAEIQSRQQHGRSETEEYSSDSESES 546
Cdd:TIGR02168  271 ELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 49903314    547 EDEEELQLILEDLQRQNEELEIKNNHLNQAVHEEREAIIELRVQLRLLQMQR 598
Cdd:TIGR02168  351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
422-530 1.57e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 41.20  E-value: 1.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 422 DLSKEERLWE-VQRILTALKRKLREAKrQECEtKIAQEIASLSKE-DVSKEEMNENEEVINILLAQENEILTEQE--ELL 497
Cdd:cd22656 108 DDEELEEAKKtIKALLDDLLKEAKKYQ-DKAA-KVVDKLTDFENQtEKDQTALETLEKALKDLLTDEGGAIARKEikDLQ 185
                        90       100       110
                ....*....|....*....|....*....|....
gi 49903314 498 AMEQFLRRQIASE-KEEIDRLRAEIAEIQSRQQH 530
Cdd:cd22656 186 KELEKLNEEYAAKlKAKIDELKALIADDEAKLAA 219
 
Name Accession Description Interval E-value
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
190-371 8.43e-118

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: 348.66  E-value: 8.43e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 190 FGVPLVDAVERTMMYDGVRLPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDREESPNLEEYEPNTVASLLKQ 269
Cdd:cd04381   1 FGASLSLAVERSRCHDGIDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRRESPNLEEYEPPTVASLLKQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 270 YLRDLPENLLTKELMPRFEEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISIVLSPT 349
Cdd:cd04381  81 YLRELPEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNISIVLSPT 160
                       170       180
                ....*....|....*....|..
gi 49903314 350 VQISNRVLYVLFTHVQELFGTV 371
Cdd:cd04381 161 VQISNRLLYALLTHCQELFGNV 182
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
208-350 3.53e-51

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: 174.76  E-value: 3.53e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314    208 RLPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDREESPN--LEEYEPNTVASLLKQYLRDLPENLLTKELMP 285
Cdd:smart00324   2 PIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDldLSEYDVHDVAGLLKLFLRELPEPLITYELYE 81
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 49903314    286 RFEEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISIVLSPTV 350
Cdd:smart00324  82 EFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTL 146
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
210-349 1.05e-49

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 169.65  E-value: 1.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314   210 PAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDREESP--NLEEYEPNTVASLLKQYLRDLPENLLTKELMPRF 287
Cdd:pfam00620   1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVdlDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49903314   288 EEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISIVLSPT 349
Cdd:pfam00620  81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPT 142
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
210-350 1.95e-45

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: 159.00  E-value: 1.95e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 210 PAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDREESP-NLEEYEPNTVASLLKQYLRDLPENLLTKELMPRFE 288
Cdd:cd00159   1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIdDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEFI 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49903314 289 EACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISIVLSPTV 350
Cdd:cd00159  81 ELAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTL 142
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
190-350 2.22e-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: 2.22e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 190 FGVPLVDAVERtmmyDGVRLPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDRE------ESPNLEEYEPNTV 263
Cdd:cd04398   1 FGVPLEDLILR----EGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDplnvllISPEDYESDIHSV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 264 ASLLKQYLRDLPENLLTKELMPRFEEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNIS 343
Cdd:cd04398  77 ASLLKLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLA 156

                ....*..
gi 49903314 344 IVLSPTV 350
Cdd:cd04398 157 IIWGPTL 163
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
189-370 3.57e-33

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: 125.93  E-value: 3.57e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 189 IFGVPLVDAVE-RTMMYDGVRLPAVFRECVDYMEKHG-MKCEGVYRVSGIKSKVDELKAAYDREESPNL----EEYEPNT 262
Cdd:cd04400   1 IFGSPLEEAVElSSHKYNGRDLPSVVYRCIEYLDKNRaIYEEGIFRLSGSASVIKQLKERFNTEYDVDLfsssLYPDVHT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 263 VASLLKQYLRDLPENLLTKELMPRFEEACGK-TTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQN 341
Cdd:cd04400  81 VAGLLKLYLRELPTLILGGELHNDFKRLVEEnHDRSQRALELKDLVSQLPQANYDLLYVLFSFLRKIIEHSDVNKMNLRN 160
                       170       180
                ....*....|....*....|....*....
gi 49903314 342 ISIVLSPTVQISNRVLYVLFTHVQELFGT 370
Cdd:cd04400 161 VCIVFSPTLNIPAGIFVLFLTDFDCIFGG 189
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
186-349 1.73e-32

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: 124.49  E-value: 1.73e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 186 VKPIFGVPLVDAVERTmmydGVRLPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDREE-SPNLEEY--EPNT 262
Cdd:cd04386   1 EKPVFGTPLEEHLKRT----GREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTfSLPLDEFysDPHA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 263 VASLLKQYLRDLPENLLTKELMPRFEEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNI 342
Cdd:cd04386  77 VASALKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNI 156

                ....*..
gi 49903314 343 SIVLSPT 349
Cdd:cd04386 157 AIVLAPN 163
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
210-350 7.51e-28

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: 110.48  E-value: 7.51e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 210 PAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDREE---SPNLEEYEPNTVASLLKQYLRDLPENLLTKELMPR 286
Cdd:cd04385  16 PVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKDArsvQLREGEYTVHDVADVLKRFLRDLPDPLLTSELHAE 95
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49903314 287 FEEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISIVLSPTV 350
Cdd:cd04385  96 WIEAAELENKDERIARYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTL 159
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
188-348 1.57e-27

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: 109.90  E-value: 1.57e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 188 PIFGVPLVDAVERTmmydGVRLPAVFRECVDYMEKHGMkCEGVYRVSGIKSKVDELKAAYDREESPNLEEYEP----NTV 263
Cdd:cd04384   1 RVFGCDLTEHLLNS----GQDVPQVLKSCTEFIEKHGI-VDGIYRLSGIASNIQRLRHEFDSEQIPDLTKDVYiqdiHSV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 264 ASLLKQYLRDLPENLLTKELMPRFEEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNIS 343
Cdd:cd04384  76 SSLCKLYFRELPNPLLTYQLYEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLA 155

                ....*
gi 49903314 344 IVLSP 348
Cdd:cd04384 156 IVWAP 160
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
190-349 1.34e-26

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: 107.16  E-value: 1.34e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 190 FGVPLVDAV--ERtmmydgvRLPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDREESPNLEEYE--PNTVAS 265
Cdd:cd04373   1 FGVPLANVVtsEK-------PIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQDHNLDLVSKDftVNAVAG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 266 LLKQYLRDLPENLLTKELMPRFEEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISIV 345
Cdd:cd04373  74 ALKSFFSELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSIC 153

                ....
gi 49903314 346 LSPT 349
Cdd:cd04373 154 FWPT 157
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
207-350 3.31e-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: 106.17  E-value: 3.31e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 207 VRLPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYD---REESPNLEEYEPNTVASLLKQYLRDLPENLLTKEL 283
Cdd:cd04387  14 SKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDtnnKDVSVMLSEMDVNAIAGTLKLYFRELPEPLFTDEL 93
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 49903314 284 MPRFEEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISIVLSPTV 350
Cdd:cd04387  94 YPNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTL 160
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
190-349 8.07e-25

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: 102.08  E-value: 8.07e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 190 FGVPLVDAVERtmmyDGVRLPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDREESPNL---EEYEPNTVASL 266
Cdd:cd04403   1 FGCHLEALCQR----ENSTVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDHDEKLDLddsKWEDIHVITGA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 267 LKQYLRDLPENLLTKELMPRFEEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISIVL 346
Cdd:cd04403  77 LKLFFRELPEPLFPYSLFNDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVF 156

                ...
gi 49903314 347 SPT 349
Cdd:cd04403 157 GPT 159
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
190-350 2.72e-24

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: 100.59  E-value: 2.72e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 190 FGVPLVDAVErtmmyDGVRLPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDRE-ESPNLEEYEPNTVASLLK 268
Cdd:cd04377   1 FGVSLSSLTS-----EDRSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDpDSVNLEDYPIHVITSVLK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 269 QYLRDLPENLLTKELMPRFEEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISIVLSP 348
Cdd:cd04377  76 QWLRELPEPLMTFELYENFLRAMELEEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAP 155

                ..
gi 49903314 349 TV 350
Cdd:cd04377 156 CI 157
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
208-350 4.43e-24

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: 99.90  E-value: 4.43e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 208 RLPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDRE-ESPNLEE--YEP-NTVASLLKQYLRDLPENLLTKEL 283
Cdd:cd04372  15 QRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDgEKADISAtvYPDiNVITGALKLYFRDLPIPVITYDT 94
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 49903314 284 MPRFEEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISIVLSPTV 350
Cdd:cd04372  95 YPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGPTL 161
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
190-368 5.00e-24

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: 100.10  E-value: 5.00e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 190 FGVPLVDAVERTMMYDGVrlPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDREESPNLEEYE-PNTVASLLK 268
Cdd:cd04404   6 FGVSLQFLKEKNPEQEPI--PPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYNMGEPVDFDQYEdVHLPAVILK 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 269 QYLRDLPENLLTKELMPrFEEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISIVLSP 348
Cdd:cd04404  84 TFLRELPEPLLTFDLYD-DIVGFLNVDKEERVERVKQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAVVFGP 162
                       170       180       190
                ....*....|....*....|....*....|...
gi 49903314 349 --------TVQIS-----NRVLYVLFTHVQELF 368
Cdd:cd04404 163 nllwakdaSMSLSainpiNTFTKFLLDHQDEIF 195
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
188-350 1.28e-23

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: 98.69  E-value: 1.28e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 188 PIFGVPLVDAVERTMMYDGVrlPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDREESPNL-EEYEPNTVASL 266
Cdd:cd04393   1 KVFGVPLQELQQAGQPENGV--PAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEEVDLsKEADVCSAASL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 267 LKQYLRDLPENLLTKELMPRFEEACGKTT-EMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISIV 345
Cdd:cd04393  79 LRLFLQELPEGLIPASLQIRLMQLYQDYNgEDEFGRKLRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTAENLAAV 158

                ....*
gi 49903314 346 LSPTV 350
Cdd:cd04393 159 FGPDV 163
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
189-348 7.42e-23

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: 97.03  E-value: 7.42e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 189 IFGVPLVDAVERTM-MYDGVRLPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDR---EESPNLEEYEPNTVA 264
Cdd:cd04391   1 LFGVPLSTLLERDQkKVPGSKVPLIFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEAkfyEGTFLWDQVKQHDAA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 265 SLLKQYLRDLPENLLTKELMPRFEEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISI 344
Cdd:cd04391  81 SLLKLFIRELPQPLLTVEYLPAFYSVQGLPSKKDQLQALNLLVLLLPEANRDTLKALLEFLQKVVDHEEKNKMNLWNVAM 160

                ....
gi 49903314 345 VLSP 348
Cdd:cd04391 161 IMAP 164
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
190-363 3.50e-22

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: 94.77  E-value: 3.50e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 190 FGVPLVDAverTMMYDGVRLPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDR--EESPNLEEY--EPNTVAS 265
Cdd:cd04395   2 FGVPLDDC---PPSSENPYVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRggFDIDLQDPRwrDVNVVSS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 266 LLKQYLRDLPENLLTKELMPRFEEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISIV 345
Cdd:cd04395  79 LLKSFFRKLPEPLFTNELYPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIV 158
                       170
                ....*....|....*....
gi 49903314 346 LSPT-VQISNRVLYVLFTH 363
Cdd:cd04395 159 FGPTlVRTSDDNMETMVTH 177
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
208-350 1.14e-21

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: 93.13  E-value: 1.14e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 208 RLPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDREES-PNLEEYEPNTVASLLKQYLRDLPENLLTKELMPR 286
Cdd:cd04382  16 MIPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTvPNLSKVDIHVICGCLKDFLRSLKEPLITFALWKE 95
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49903314 287 FEEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKElETKMNIQNISIVLSPTV 350
Cdd:cd04382  96 FMEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQSP-ECKMDINNLARVFGPTI 158
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
189-350 2.47e-21

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: 92.51  E-value: 2.47e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 189 IFGVPLVDaverTMMYD---GVRL-PAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDREESPNLE-EYEPNTV 263
Cdd:cd04390   2 VFGQRLED----TVAYErkfGPRLvPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDsDTDVHTV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 264 ASLLKQYLRDLPENLLTkelMPRFEE--ACGKTTEMEK---VQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMN 338
Cdd:cd04390  78 ASLLKLYLRELPEPVIP---WAQYEDflSCAQLLSKDEekgLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMS 154
                       170
                ....*....|..
gi 49903314 339 IQNISIVLSPTV 350
Cdd:cd04390 155 VQNLATVFGPNI 166
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
214-349 4.02e-21

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: 91.69  E-value: 4.02e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 214 RECVDYMEKHGMKCEGVYRVSGIKSKVDELKAA-YDREESPNLE------EYEPNTVASLLKQYLRDLPENLLTKELMPR 286
Cdd:cd04374  33 RKCIEAVETRGINEQGLYRVVGVNSKVQKLLSLgLDPKTSTPGDvdldnsEWEIKTITSALKTYLRNLPEPLMTYELHND 112
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49903314 287 FEEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISIVLSPT 349
Cdd:cd04374 113 FINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPT 175
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
189-350 5.76e-21

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: 91.21  E-value: 5.76e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 189 IFGVPLVDAVERTMmydgvrLPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDREESPNLEEYEPNTVASLLK 268
Cdd:cd04402   1 LFGQPLSNICEDDN------LPKPILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNSGVEVDLKAEPVLLLASVLK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 269 QYLRDLPENLLTKELMPRFEEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISIVLSP 348
Cdd:cd04402  75 DFLRNIPGSLLSSDLYEEWMSALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIAP 154

                ..
gi 49903314 349 TV 350
Cdd:cd04402 155 SL 156
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
190-349 1.83e-20

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: 89.79  E-value: 1.83e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 190 FGVPLVDAVERTMmyDGVrlPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDR-EESPNLEEYEPNTVASLLK 268
Cdd:cd04378   1 FGVDFSQVPRDFP--DEV--PFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENgKDLVELSELSPHDISSVLK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 269 QYLRDLPENLLT-----------KEL--MPRFEEACGKTTEMEK-VQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELE 334
Cdd:cd04378  77 LFLRQLPEPLILfrlyndfialaKEIqrDTEEDKAPNTPIEVNRiIRKLKDLLRQLPASNYNTLQHLIAHLYRVAEQFEE 156
                       170
                ....*....|....*
gi 49903314 335 TKMNIQNISIVLSPT 349
Cdd:cd04378 157 NKMSPNNLGIVFGPT 171
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
187-350 1.73e-19

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: 87.47  E-value: 1.73e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 187 KPIFGVPLVDAVERTmmydGVRLPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDRE-ESPNLEEYEPNTVAS 265
Cdd:cd04375   2 KNVFGVPLLVNLQRT----GQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESStDNVNYDGQQAYDVAD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 266 LLKQYLRDLPENLLTKELMPRFEEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISIV 345
Cdd:cd04375  78 MLKQYFRDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAVC 157

                ....*
gi 49903314 346 LSPTV 350
Cdd:cd04375 158 LAPSL 162
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
209-350 1.82e-19

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: 86.58  E-value: 1.82e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 209 LPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDRE-ESPNLEEYEPNTVASLLKQYLRDLPENLLTKELMPRF 287
Cdd:cd04407  15 VPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADpENVKLENYPIHAITGLLKQWLRELPEPLMTFAQYNDF 94
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49903314 288 EEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISIVLSPTV 350
Cdd:cd04407  95 LRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCL 157
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
209-350 5.01e-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: 85.44  E-value: 5.01e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 209 LPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDRE-ESPNLEEYEPNTVASLLKQYLRDLPENLLTKELMPRF 287
Cdd:cd04406  15 VPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDaNSVNLDDYNIHVIASVFKQWLRDLPNPLMTFELYEEF 94
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49903314 288 EEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISIVLSPTV 350
Cdd:cd04406  95 LRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCI 157
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
209-350 5.32e-17

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: 79.86  E-value: 5.32e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 209 LPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDREESP-NLEEYEPNTVASLLKQYLRDLPENLLT------- 280
Cdd:cd04408  16 VPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLvDLSGHSPHDITSVLKHFLKELPEPVLPfqlyddf 95
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 49903314 281 ----KELMPRFEEACGKT-TEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISIVLSPTV 350
Cdd:cd04408  96 ialaKELQRDSEKAAESPsIVENIIRSLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDNKMSPNNLGIVFGPTL 170
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
190-350 1.84e-16

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: 78.70  E-value: 1.84e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 190 FGVPLVDAVERTMmyDGVrlPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDR-EESPNLEEYEPNTVASLLK 268
Cdd:cd04409   1 FGADFAQVAKKSP--DGI--PFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENgKDLVELSELSPHDISNVLK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 269 QYLRDLPENL-----------LTKELMPRFEEACGKTTEMEK-----------VQEFQRLLRELPECNHLLLSWLIVHLD 326
Cdd:cd04409  77 LYLRQLPEPLilfrlynefigLAKESQHVNETQEAKKNSDKKwpnmctelnriLLKSKDLLRQLPAPNYNTLQFLIVHLH 156
                       170       180
                ....*....|....*....|....
gi 49903314 327 HVIAKELETKMNIQNISIVLSPTV 350
Cdd:cd04409 157 RVSEQAEENKMSASNLGIIFGPTL 180
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
206-373 3.79e-16

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: 77.08  E-value: 3.79e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 206 GVRLPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDREESP---NLEEYEPNTVASLLKQYLRDLPENLLTKE 282
Cdd:cd04383  15 GQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGEDPladDQNDHDINSVAGVLKLYFRGLENPLFPKE 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 283 lmpRFEE--ACGKT-TEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISIVLSPTV----QISNR 355
Cdd:cd04383  95 ---RFEDlmSCVKLeNPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICFGPTLmpvpEGQDQ 171
                       170
                ....*....|....*...
gi 49903314 356 VLYVlfTHVQELFGTVVL 373
Cdd:cd04383 172 VSCQ--AHVNELIKTIII 187
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
190-367 1.12e-15

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: 76.25  E-value: 1.12e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 190 FGVPLVDAVER--TMMYDGV-----RLPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDRE--ESPNLEEYEP 260
Cdd:cd04397   1 FGVPLEILVEKfgADSTLGVgpgklRIPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNptEVPDLSKENP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 261 NTVASLLKQYLRDLPENLLTKELMPRFEEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLD-----HVIAKELET 335
Cdd:cd04397  81 VQLAALLKKFLRELPDPLLTFKLYRLWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKwvssfSHIDEETGS 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 49903314 336 KMNIQNISIVLSPTV--------------QISNRVLYVLFTHVQEL 367
Cdd:cd04397 161 KMDIHNLATVITPNIlysktdnpntgdeyFLAIEAVNYLIENNEEF 206
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
189-348 3.53e-15

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: 74.43  E-value: 3.53e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 189 IFGVPLvDAVERTMMYDGVRLPAVFRECVDYMEKHgMKCEGVYRVSGIKSKVDELKAAYDREESpNLEEYEPNTVASLLK 268
Cdd:cd04394   1 VFGVPL-HSLPHSTVPEYGNVPKFLVDACTFLLDH-LSTEGLFRKSGSVVRQKELKAKLEGGEA-CLSSALPCDVAGLLK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 269 QYLRDLPENLLTKELMPRFEEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISIVLSP 348
Cdd:cd04394  78 QFFRELPEPLLPYDLHEALLKAQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAVIFAP 157
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
190-348 5.37e-15

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: 73.58  E-value: 5.37e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 190 FGVPLVDAVER-TMMYDGVRLPAV---FRECVDYMEkhGMKCEGVYRVSGIKSKVDELKAAYDREESPNLEEYEPNTVAS 265
Cdd:cd04389   1 FGSSLEEIMDRqKEKYPELKLPWIltfLSEKVLALG--GFQTEGIFRVPGDIDEVNELKLRVDQWDYPLSGLEDPHVPAS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 266 LLKQYLRDLPENLLTKELmprFEEACGKTTEMEKVQEfqrLLRELPECNHLLLSWLIvHLDHVIAKEL---ETKMNIQNI 342
Cdd:cd04389  79 LLKLWLRELEEPLIPDAL---YQQCISASEDPDKAVE---IVQKLPIINRLVLCYLI-NFLQVFAQPEnvaHTKMDVSNL 151

                ....*.
gi 49903314 343 SIVLSP 348
Cdd:cd04389 152 AMVFAP 157
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
209-350 5.72e-15

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: 74.01  E-value: 5.72e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 209 LPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDREESPNL-EEYEPNTVASLLKQYLRDLPENLLTKELMPRF 287
Cdd:cd04376   9 VPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVLdENHSVHDVAALLKEFFRDMPDPLLPRELYTAF 88
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49903314 288 EEAcGKTTEMEKVQEFQRLLRELPECN----HLLLSWLIV---HLDHVIAKELE----TKMNIQNISIVLSPTV 350
Cdd:cd04376  89 IGT-ALLEPDEQLEALQLLIYLLPPCNcdtlHRLLKFLHTvaeHAADSIDEDGQevsgNKMTSLNLATIFGPNL 161
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
190-366 8.00e-14

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: 70.96  E-value: 8.00e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 190 FGVPLVDAVERTMmyDGVRLPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDREESP---NLEEY-EPNTVAS 265
Cdd:cd04379   1 FGVPLSRLVEREG--ESRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAvelSEELYpDINVITG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 266 LLKQYLRDLPENLLTKELMPRFEEACGKTTEMEKVQEFQRLLRELPECNHLLLSWLIVHLDH---VIAKELETKMNIQNI 342
Cdd:cd04379  79 VLKDYLRELPEPLITPQLYEMVLEALAVALPNDVQTNTHLTLSIIDCLPLSAKATLLLLLDHlslVLSNSERNKMTPQNL 158
                       170       180
                ....*....|....*....|....
gi 49903314 343 SIVLSPtvqisnrvlyVLFTHVQE 366
Cdd:cd04379 159 AVCFGP----------VLMFCSQE 172
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
217-350 9.66e-13

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: 67.49  E-value: 9.66e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 217 VDYMEKHgMKCEGVYRVSGIKSKVDELKAAYDREESPNLE--EYEPNTVASLLKQYLRDLPENLLTKELMP--------- 285
Cdd:cd04392  17 IEYLEKN-LRVEGLFRKPGNSARQQELRDLLNSGTDLDLEsgGFHAHDCATVLKGFLGELPEPLLTHAHYPahlqiadlc 95
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 49903314 286 RFEEACGKTTEMEK---VQEFQRLLRELPECNHLLLSWLIVHLDHVIAKELETKMNIQNISIVLSPTV 350
Cdd:cd04392  96 QFDEKGNKTSAPDKerlLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKNKMSADNLALLFTPHL 163
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
189-350 2.10e-12

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: 67.05  E-value: 2.10e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 189 IFGVPLVDAV-----------ERTMMYDGVRLPAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDRE----ESP 253
Cdd:cd04396   1 VFGVSLEESLkyasvaisivdEDGEQYVYGYIPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPpdygKSF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 254 NLEEYEPNTVASLLKQYLRDLPENLLTKELMPRFEEACGKTTEM-----------------EKVQEFQRLLRELPECNHL 316
Cdd:cd04396  81 DWDGYTVHDAASVLRRYLNNLPEPLVPLDLYEEFRNPLRKRPRIlqymkgrineplntdidQAIKEYRDLITRLPNLNRQ 160
                       170       180       190
                ....*....|....*....|....*....|....
gi 49903314 317 LLSWLIVHLDHVIAKELETKMNIQNISIVLSPTV 350
Cdd:cd04396 161 LLLYLLDLLAVFARNSDKNLMTASNLAAIFQPGI 194
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
421-599 2.80e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 2.80e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 421 KDLSKEERLWEVQRILTALK-----RKLREAKRQECETKIAQEIASLSKEDVSKEEM----NENEEVINILLAQENEILT 491
Cdd:COG1196 216 RELKEELKELEAELLLLKLReleaeLEELEAELEELEAELEELEAELAELEAELEELrlelEELELELEEAQAEEYELLA 295
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 492 EQEELLAMEQFLRRQIASEKEEIDRLRAEIAEIQSRQQHGRSETEEYSSDSESESEDEEELQLILEDLQRQNEELEIKNN 571
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
                       170       180
                ....*....|....*....|....*...
gi 49903314 572 HLNQAVHEEREAIIELRVQLRLLQMQRA 599
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLE 403
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
398-600 1.74e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 1.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 398 IKEEIRRQEFLLNCLH-RDLQGGIKDLSKEERLWEVQRILTALKRKLREAKRQECETKIAQEIASLS----KEDVSKEEM 472
Cdd:COG1196 218 LKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEeaqaEEYELLAEL 297
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 473 NENEEVINILLAQENEILTEQEELLAMEQFLRRQIASEKEEIDRLRAEIAEIQSRQQHgrSETEEYSSDSESESEDEEEL 552
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE--AEAELAEAEEALLEAEAELA 375
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 49903314 553 QLILEDLQRQNEELEIKNNHLNQAVHEEREAIIELRVQLRLLQMQRAK 600
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
398-598 4.13e-07

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: 53.52  E-value: 4.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314    398 IKEEIRRQeflLNCLHRDLQGGIKDLSKEERLWEVQRIL-----TALKRKLREAKRQ------ECETKIAQEIASLSKED 466
Cdd:TIGR02168  194 ILNELERQ---LKSLERQAEKAERYKELKAELRELELALlvlrlEELREELEELQEElkeaeeELEELTAELQELEEKLE 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314    467 VSKEEMNENEEVINILLAQENEILTEQEELLAMEQFLRRQIASEKEEIDRLRAEIAEIQSRQQHGRSETEEYSSDSESES 546
Cdd:TIGR02168  271 ELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 49903314    547 EDEEELQLILEDLQRQNEELEIKNNHLNQAVHEEREAIIELRVQLRLLQMQR 598
Cdd:TIGR02168  351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
398-600 5.32e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 5.32e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 398 IKEEIRRQEFLLNCLHRDLQGGIKDLSKEERlwevQRILTALKRKLREAKRQECETKIAQEIASLSKEDVSKEEMNENEE 477
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQ----DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 478 VINILLAQENEILTEQEELLAMEQflrRQIASEKEEIDRLRAEIAEIQSRQQHGRSETEEYSSDSESESEDEEELQLILE 557
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAE---AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 49903314 558 DLQRQNEELEIKNNHLNQAVHEEREAIIELRVQLRLLQMQRAK 600
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
391-595 2.16e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 2.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314    391 LPETQAGIKEEIRRQEFLLNCLHRDLQGGIKDLSKEERLWEVQRILTALKRKLREAKRQECEtKIAQEIASLSKEDVS-K 469
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQLSKELTElE 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314    470 EEMNENEEVINILLAQENEILTEQEELLA-MEQF------LRRQIASEKEEIDRLRAEIAEIQSRQQHGRSETEEYSSDS 542
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAqIEQLkeelkaLREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314    543 ESESEDEEELQLI-------LEDLQRQNEELEIKNNHLNQAVHEEREAIIELRVQLRLLQ 595
Cdd:TIGR02168  841 EDLEEQIEELSEDieslaaeIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
400-599 7.92e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 7.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314    400 EEIRRQEFLLNCLHRDLQGGIKDLSKEERLWEVQRILTALKRKLREAKRQECETKIAQ----------EIASLSKE-DVS 468
Cdd:TIGR02168  715 EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeelaeaeaEIEELEAQiEQL 794
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314    469 KEEMNENEEVINIL---LAQENEILTEQEELLAMEQF-----------LRRQIASEKEEIDRLRAEIAEIQSRQQHGRSE 534
Cdd:TIGR02168  795 KEELKALREALDELraeLTLLNEEAANLRERLESLERriaaterrledLEEQIEELSEDIESLAAEIEELEELIEELESE 874
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 49903314    535 TEEYSSDSESESEDEEELQLILEDLQRQNEELEIKNNHLNQAVHEEREAIIELRVQLRLLQMQRA 599
Cdd:TIGR02168  875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
431-601 9.65e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 9.65e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 431 EVQRILTALKR---KLREAKRQECETKIAQEIASLSKEDVSKEEMNENEEVINILLAQENEILTEQEELLAMEQFLRRQI 507
Cdd:COG1196 197 ELERQLEPLERqaeKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEL 276
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 508 ASEKEEIDRLRAEIAEIQSRQQHgrseteeYSSDSESESEDEEELQLILEDLQRQNEELEIKNNHLNQAVHEEREAIIEL 587
Cdd:COG1196 277 EELELELEEAQAEEYELLAELAR-------LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
                       170
                ....*....|....
gi 49903314 588 RVQLRLLQMQRAKS 601
Cdd:COG1196 350 EEELEEAEAELAEA 363
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
400-601 1.13e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.90  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314    400 EEIRRQEFLLNCLHRDLQGGIKDLSKE------------ERLWEVQRILTALKRKLREAKRQECE-----TKIAQEIASL 462
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQKELYALANEisrleqqkqilrERLANLERQLEELEAQLEELESKLDElaeelAELEEKLEEL 349
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314    463 SKEDVSKEEMNENEEVINILLAQENEILTEQEELLAMEQF-LRRQIASEKEEIDRLRAEIAEIQSRQQhgRSETEEYSSD 541
Cdd:TIGR02168  350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAqLELQIASLNNEIERLEARLERLEDRRE--RLQQEIEELL 427
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49903314    542 SESESEDEEELQLILEDLQRQNEELEIKNNHLNQAVHEEREAIIELRVQLRLL--QMQRAKS 601
Cdd:TIGR02168  428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAerELAQLQA 489
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
398-629 3.18e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 46.68  E-value: 3.18e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 398 IKEEIRRQEFLLNCLHRDLQGGIKDLSK-EERLWEVQRILTALKRKLREAKRQEceTKIAQEIASLSKEDVSKEE----- 471
Cdd:COG4942  32 LQQEIAELEKELAALKKEEKALLKQLAAlERRIAALARRIRALEQELAALEAEL--AELEKEIAELRAELEAQKEelael 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 472 -----MNENEEVINILLAQENeilteQEELLAMEQFLRRQIASEKEEIDRLRAEIAEIQSRQQHGRSETEEYSSDSESES 546
Cdd:COG4942 110 lralyRLGRQPPLALLLSPED-----FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 547 EDEEELQLILEDLQRQNEELEIKNNHLNQAVHEEREAIIELRVQLRLLQMQRAKSEQQPQEEEEPERRGGIgPPPCDGVL 626
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL-PWPVSGRV 263

                ...
gi 49903314 627 EVR 629
Cdd:COG4942 264 VRR 266
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
424-600 3.68e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 46.30  E-value: 3.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 424 SKEERLWEVQRILTALKRKLREAKRQEceTKIAQEIASLSKEdvskeeMNENEEVINILLAQENEILTEQEELlameqfl 503
Cdd:COG4942  24 EAEAELEQLQQEIAELEKELAALKKEE--KALLKQLAALERR------IAALARRIRALEQELAALEAELAEL------- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 504 RRQIASEKEEIDRLRAEIAE-IQSRQQHGRSETEEYSSDSESESEDEEELQLI----------LEDLQRQNEELEIKNNH 572
Cdd:COG4942  89 EKEIAELRAELEAQKEELAElLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLkylaparreqAEELRADLAELAALRAE 168
                       170       180
                ....*....|....*....|....*...
gi 49903314 573 LNQAVHEEREAIIELRVQLRLLQMQRAK 600
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAE 196
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
399-600 4.69e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 4.69e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 399 KEEIRRQEFLLNCLHRDLQGGIKDLSKEERLWEVQRILTALKRKLREAKRQECETKIAQEIASLS----KEDVSKEEMNE 474
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAeaeeALLEAEAELAE 376
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 475 NEEVINILLAQENEILTEQEELLAMEQFLRRQIASEKEEIDRLRAEIAEIQSRQQHgrseteeyssdsesesedeEELQL 554
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE-------------------LEEEE 437
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 49903314 555 I-----LEDLQRQNEELEIKNNHLNQAVHEEREAIIELRVQLRLLQMQRAK 600
Cdd:COG1196 438 EeeeeaLEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
457-595 5.44e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 5.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314    457 QEIASLSKE-DVSKEEMNENEEVINILLAQENEILTEQEELLAMEQFLRRQIASEKEEIDRLRAEIAEIQSRQQHGRSET 535
Cdd:TIGR02168  677 REIEELEEKiEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314    536 EEYSSDSESESEDEEELQLILEDLQRQNEELEIKNNHLNQAVHEEREAIIELRVQLRLLQ 595
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
400-636 1.13e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.44  E-value: 1.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314    400 EEIRRQEFLLNCLHRDLQGGIKDLskEERLWEVQRILTALKRKLR--EAKRQECETKIAQ---EIASL------SKEDVS 468
Cdd:TIGR02169  719 GEIEKEIEQLEQEEEKLKERLEEL--EEDLSSLEQEIENVKSELKelEARIEELEEDLHKleeALNDLearlshSRIPEI 796
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314    469 KEEMNENEEVINILLAQENEILTEQEELLAMEQFLRRQIASEKEEIDRLRAEIAEIQSRQQHGRSETEEYSSDSESesed 548
Cdd:TIGR02169  797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE---- 872
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314    549 eeeLQLI-------LEDLQRQNEELEIKNNHLNQAVHEEREAIIELRVQLRLLQMQRAKSEQQPQEEEEPERRgGIGPPP 621
Cdd:TIGR02169  873 ---LEAAlrdlesrLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE-DEEIPE 948
                          250
                   ....*....|....*
gi 49903314    622 CDGVLEVRVAKEQAK 636
Cdd:TIGR02169  949 EELSLEDVQAELQRV 963
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
210-348 8.90e-04

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: 41.01  E-value: 8.90e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 210 PAVFRECVDYMEKHGMKCEGVYRVSGIKSKVDELKAAYDREESPNLEEYEPNTVASLLKQYLRDLPENLLTKelmPRFEE 289
Cdd:cd04388  16 PPLLIKLVEAIEKKGLESSTLYRTQSSSSLTELRQILDCDAASVDLEQFDVAALADALKRYLLDLPNPVIPA---PVYSE 92
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 49903314 290 ACGKTTEMEKVQEFQRLLRELPECNH------LLLSWLIVHLDHVIAKELETKMNIQNISIVLSP 348
Cdd:cd04388  93 MISRAQEVQSSDEYAQLLRKLIRSPNlphqywLTLQYLLKHFFRLCQSSSKNLLSARALAEIFSP 157
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
427-586 1.16e-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: 42.36  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314    427 ERLWEVQRILTALKRKLREAKRQECETKIAQEIASLSKEDVSKEemneneevINILLAQENEILTEQEELLAMEQFLRRQ 506
Cdd:TIGR02169  681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKE--------IEQLEQEEEKLKERLEELEEDLSSLEQE 752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314    507 IASEKEEIDRLRAEIAEIQsrqqhgrseteeyssdsesesEDEEELQLILEDLQRQ--NEELEIKNNHLN--QAVHEERE 582
Cdd:TIGR02169  753 IENVKSELKELEARIEELE---------------------EDLHKLEEALNDLEARlsHSRIPEIQAELSklEEEVSRIE 811

                   ....
gi 49903314    583 AIIE 586
Cdd:TIGR02169  812 ARLR 815
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
405-599 1.16e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 1.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 405 QEFLLNCLHRDLQGGIKDLSKE--ERLWEVQRILTALKRKLREAKRQEceTKIAQEIASLSKedvSKEEMNENEEVINIL 482
Cdd:COG4717  40 LAFIRAMLLERLEKEADELFKPqgRKPELNLKELKELEEELKEAEEKE--EEYAELQEELEE---LEEELEELEAELEEL 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 483 LAQEN--EILTEQEELLAMEQFLRRQIASEKEEIDRLRAEIAEIQSRQQHGRSETEEYSSDSESESEDEEELQLI----L 556
Cdd:COG4717 115 REELEklEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAteeeL 194
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 49903314 557 EDLQRQNEELEIKNNHLNQAVHEEREAIIELRVQLRLLQMQRA 599
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
422-530 1.57e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 41.20  E-value: 1.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 422 DLSKEERLWE-VQRILTALKRKLREAKrQECEtKIAQEIASLSKE-DVSKEEMNENEEVINILLAQENEILTEQE--ELL 497
Cdd:cd22656 108 DDEELEEAKKtIKALLDDLLKEAKKYQ-DKAA-KVVDKLTDFENQtEKDQTALETLEKALKDLLTDEGGAIARKEikDLQ 185
                        90       100       110
                ....*....|....*....|....*....|....
gi 49903314 498 AMEQFLRRQIASE-KEEIDRLRAEIAEIQSRQQH 530
Cdd:cd22656 186 KELEKLNEEYAAKlKAKIDELKALIADDEAKLAA 219
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
250-329 3.02e-03

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: 39.62  E-value: 3.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 250 EESPNLEEYEPNTVASLLKQYLRDLPENLLT-------KELMPRFEEACGKTTEmEKVQEFQRLLRELPECNHLLLSWLI 322
Cdd:cd04399  68 KEVIILKKFEPSTVASVLKLYLLELPDSLIPhdiydliRSLYSAYPPSQEDSDT-ARIQGLQSTLSQLPKSHIATLDAII 146

                ....*..
gi 49903314 323 VHLDHVI 329
Cdd:cd04399 147 THFYRLI 153
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
393-524 6.16e-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: 40.04  E-value: 6.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314    393 ETQAGIKEEIRRQEFLLNCLHRDLQGGIKDL-SKEERLWEVQRILTALKRKLREAkrqecETKIAQEIASLSKEDVSKEE 471
Cdd:TIGR02168  852 EDIESLAAEIEELEELIEELESELEALLNERaSLEEALALLRSELEELSEELREL-----ESKRSELRRELEELREKLAQ 926
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 49903314    472 MNENEEVINILLAQENEILTEQ-----EELLAMEQFLRRQIASEKEEIDRLRAEIAEI 524
Cdd:TIGR02168  927 LELRLEGLEVRIDNLQERLSEEysltlEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
424-600 9.07e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 9.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 424 SKEERLWEVQRILTALKRKLREAKRQEceTKIAQEIASLSKE-DVSKEEMNENEEVINIL---LAQENEILTEQ------ 493
Cdd:COG3883  20 AKQKELSELQAELEAAQAELDALQAEL--EELNEEYNELQAElEALQAEIDKLQAEIAEAeaeIEERREELGERaralyr 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314 494 -----------------EELLAMEQFLRRQIASEKEEIDRLRAEIAEIQSRQQhgrseteeyssdsesesedeeELQLIL 556
Cdd:COG3883  98 sggsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKA---------------------ELEAKL 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 49903314 557 EDLQRQNEELEIKNNHLNQAVHEEREAIIELRVQLRLLQMQRAK 600
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAE 200
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
399-587 9.42e-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: 39.28  E-value: 9.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314    399 KEEIRRQeflLNCLHRDLQGGIKDLSK-EERLWEVQRILTALKRKLREAKRQEC---ETKIAQ---EIASL-SKEDVSKE 470
Cdd:TIGR02169  239 KEAIERQ---LASLEEELEKLTEEISElEKRLEEIEQLLEELNKKIKDLGEEEQlrvKEKIGEleaEIASLeRSIAEKER 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49903314    471 EMNENEEVINILLAQENEILTEQEEL---LAMEQFLRRQIASE----KEEIDRLRAEIAEIQSRQQHGRSETEEYSSDSE 543
Cdd:TIGR02169  316 ELEDAEERLAKLEAEIDKLLAEIEELereIEEERKRRDKLTEEyaelKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 49903314    544 SESEDEEELQLILEDLQRQNEELEIKNNHLNQAVHEEREAIIEL 587
Cdd:TIGR02169  396 KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL 439
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH