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Conserved domains on  [gi|1720390105|ref|XP_030105650|]
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ras/Rap GTPase-activating protein SynGAP isoform X20 [Mus musculus]

Protein Classification

RasGAP domain-containing protein( domain architecture ID 11639727)

RasGAP (Ras GTPase-activating protein) domain-containing protein may function as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF3498 super family cl26404
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
 116-695 0e+00

Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 433 to 538 amino acids in length. This domain is found associated with pfam00616, pfam00168. This domain has two conserved sequence motifs: DLQ and PLSFQNP.


The actual alignment was detected with superfamily member pfam12004:

Pssm-ID: 463427 [Multi-domain]  Cd Length: 511  Bit Score: 550.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 116 LNDISTALRNPN-IQRQPSRQSERTRSQPMVLRGPSAEMQgYMMRDLNSS-MDMARLPSPTKEKPpppppgggkDLFYVS 193
Cdd:pfam12004   1 LRDITTALTNPTpIQQQLRRFSEHSSSPPVPGRSISSGLQ-KMFEDPDDGlSDFTRLPSPTPENK---------DLFFVT 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 194 RPPLARSSPAYCTSSSDITEPEQKMLSVNKSVSMLDLQGdgpgGRLNSSSVSNlAAVGDLLHSSQASLTAALGLRPAPAG 273
Cdd:pfam12004  71 RPPLLQPSPARSSSYSDANEPDQQLPNGNKSLSMVDLQD----SRSLQGSPSP-PLHDAPLNLSQAGSQASVGLRPAWAA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 274 RLSQGSGSSItAAGMRLSQMGVTTdGVPAQQLRIPLSFQNPLFHMAADGPGPPAGHGGSsghgppsshhhhhhhhhhrgg 353
Cdd:pfam12004 146 RTSQGNPQSA-PQVRRPLQTPVTQ-GTRPQQLLAPLSFQNPVYHMAAGLPVSPRGLGSP--------------------- 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 354 EPPGDTFAPFHGYSKSEDLSSGVPkpPAASILHSHSYSDEFGPSGTDFTRRQLSLQDSLQHMLSPPQITIGPQRPAPSGP 433
Cdd:pfam12004 203 DSSSETHSSFSSHSNSEDLSSAAA--NKKSGPSNSSYSEDFARRSTEFTRRQLSLTELQHQPAVPRQNSAGPQRRIDQQG 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 434 GGGSGggsgggqpppLQRGKSQQLTVSAAQKPRPSSGNLlQSPEPSYGPARPRQQSLSKEGsiggsggsgggggggLKPS 513
Cdd:pfam12004 281 LGGPP----------LTRGRTPPSLLNSASYPRPSSGSL-MSSSPDWPPARLRQQSSSSKG---------------DSPE 334

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 514 ITK--QHSQTPSTLNP-TMPASERTVAWVSNMPHLSADIESAHIE-REEYKLKEysksmdesrldrEYEEEIHSLKERLH 589
Cdd:pfam12004 335 TKQrtQHQQVPSPVNPsTLSPVERTAAWVLNMNGQYEEEESSGPEsREELKQAE------------KYEQEISKLKERLR 402

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 590 MSNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRRDHPAMAEPLpEPKKR 669
Cdd:pfam12004 403 VSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMAVEEELKKDHAEMQAVI-DSKQK 481

                         570       580
                  ....*....|....*....|....*.
gi 1720390105 670 LLDAQERQLPPLGPTNPRVTLAPPWN 695
Cdd:pfam12004 482 IIDAQEKRIASLDAANARLMSALTQL 507
RasGAP super family cl02569
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...
 1-126 9.18e-71

Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Proteins having a RasGAP domain include p120GAP, IQGAP, Rab5-activating protein 6, and Neurofibromin, among others. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP exhibit no similarity at their amino acid sequence level. RasGTPases function as molecular switches in a large number of signaling pathways. They are in the on state when bound to GTP, and in the off state when bound to GDP. The RasGAP domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator.


The actual alignment was detected with superfamily member cd05136:

Pssm-ID: 470620  Cd Length: 324  Bit Score: 233.63  E-value: 9.18e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105   1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGY 80
Cdd:cd05136   199 LSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKEEYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGY 278

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720390105  81 IDLGRELSTLHALLWEVLPQLSKEALLKLGPLPRLLNDISTALRNP 126
Cdd:cd05136   279 IDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITEALRNP 324
 
Name Accession Description Interval E-value
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
 116-695 0e+00

Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 433 to 538 amino acids in length. This domain is found associated with pfam00616, pfam00168. This domain has two conserved sequence motifs: DLQ and PLSFQNP.


Pssm-ID: 463427 [Multi-domain]  Cd Length: 511  Bit Score: 550.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 116 LNDISTALRNPN-IQRQPSRQSERTRSQPMVLRGPSAEMQgYMMRDLNSS-MDMARLPSPTKEKPpppppgggkDLFYVS 193
Cdd:pfam12004   1 LRDITTALTNPTpIQQQLRRFSEHSSSPPVPGRSISSGLQ-KMFEDPDDGlSDFTRLPSPTPENK---------DLFFVT 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 194 RPPLARSSPAYCTSSSDITEPEQKMLSVNKSVSMLDLQGdgpgGRLNSSSVSNlAAVGDLLHSSQASLTAALGLRPAPAG 273
Cdd:pfam12004  71 RPPLLQPSPARSSSYSDANEPDQQLPNGNKSLSMVDLQD----SRSLQGSPSP-PLHDAPLNLSQAGSQASVGLRPAWAA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 274 RLSQGSGSSItAAGMRLSQMGVTTdGVPAQQLRIPLSFQNPLFHMAADGPGPPAGHGGSsghgppsshhhhhhhhhhrgg 353
Cdd:pfam12004 146 RTSQGNPQSA-PQVRRPLQTPVTQ-GTRPQQLLAPLSFQNPVYHMAAGLPVSPRGLGSP--------------------- 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 354 EPPGDTFAPFHGYSKSEDLSSGVPkpPAASILHSHSYSDEFGPSGTDFTRRQLSLQDSLQHMLSPPQITIGPQRPAPSGP 433
Cdd:pfam12004 203 DSSSETHSSFSSHSNSEDLSSAAA--NKKSGPSNSSYSEDFARRSTEFTRRQLSLTELQHQPAVPRQNSAGPQRRIDQQG 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 434 GGGSGggsgggqpppLQRGKSQQLTVSAAQKPRPSSGNLlQSPEPSYGPARPRQQSLSKEGsiggsggsgggggggLKPS 513
Cdd:pfam12004 281 LGGPP----------LTRGRTPPSLLNSASYPRPSSGSL-MSSSPDWPPARLRQQSSSSKG---------------DSPE 334

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 514 ITK--QHSQTPSTLNP-TMPASERTVAWVSNMPHLSADIESAHIE-REEYKLKEysksmdesrldrEYEEEIHSLKERLH 589
Cdd:pfam12004 335 TKQrtQHQQVPSPVNPsTLSPVERTAAWVLNMNGQYEEEESSGPEsREELKQAE------------KYEQEISKLKERLR 402

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 590 MSNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRRDHPAMAEPLpEPKKR 669
Cdd:pfam12004 403 VSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMAVEEELKKDHAEMQAVI-DSKQK 481

                         570       580
                  ....*....|....*....|....*.
gi 1720390105 670 LLDAQERQLPPLGPTNPRVTLAPPWN 695
Cdd:pfam12004 482 IIDAQEKRIASLDAANARLMSALTQL 507
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
 1-126 9.18e-71

Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras GTPase-activating proteins includes DAB2IP, nGAP, and Syn GAP. Disabled 2 interactive protein, (DAB2IP; also known as ASK-interacting protein 1 (AIP1)), is a member of the GTPase-activating proteins, down-regulates Ras-mediated signal pathways, and mediates TNF-induced activation of ASK1-JNK signaling pathways. The mechanism by which TNF signaling is coupled to DAB2IP is not known.


Pssm-ID: 213338  Cd Length: 324  Bit Score: 233.63  E-value: 9.18e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105   1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGY 80
Cdd:cd05136   199 LSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKEEYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGY 278

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720390105  81 IDLGRELSTLHALLWEVLPQLSKEALLKLGPLPRLLNDISTALRNP 126
Cdd:cd05136   279 IDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITEALRNP 324
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
 1-118 2.72e-31

GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the GTPase activity of Ras, thereby "switching" it into an "off" position. Improved domain limits from structure.


Pssm-ID: 214617  Cd Length: 344  Bit Score: 125.50  E-value: 2.72e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105    1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGY 80
Cdd:smart00323 213 VSPKLFNLVDEHPDPTTRRTLTLIAKVLQNLANLSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEILVDKVSDST 292

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1720390105   81 IDLGRELSTLHALLWEVLPQLSKEaLLKLGPLPRLLND 118
Cdd:smart00323 293 TISGRELSLLHSLLLENGDALKRE-LNNEDPLGKLLFK 329
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 552-677 1.63e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 49.92  E-value: 1.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 552 AHIEREEYKLKEYSKSMDESRLDREYE---EEIHSLKERLhmsnRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKRLR 628
Cdd:COG1579    66 LEIEEVEARIKKYEEQLGNVRNNKEYEalqKEIESLKRRI----SDLEDEILELMERIEELEEELAELEAELAELEAELE 141

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1720390105 629 QQQVEKDSQIKSIIGRLmlveEELRRDHPAMAEPLPEpkkRLLDAQERQ 677
Cdd:COG1579   142 EKKAELDEELAELEAEL----EELEAEREELAAKIPP---ELLALYERI 183
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 543-676 8.09e-06

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: 49.30  E-value: 8.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105  543 PHLSADIESAHIEREEYKLKEYSKSMDESRldrEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQ---YQAR 619
Cdd:TIGR02169  261 SELEKRLEEIEQLLEELNKKIKDLGEEEQL---RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEidkLLAE 337

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720390105  620 LEQSEKRLRQQQVEKDsQIKSIIGRLMLVEEELRRDHPAMAEPLPEPKKRLLDAQER 676
Cdd:TIGR02169  338 IEELEREIEEERKRRD-KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
 1-33 5.66e-05

GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the GTPase activity of Ras, thereby "switching" it into an "off" position.


Pssm-ID: 459871  Cd Length: 207  Bit Score: 44.97  E-value: 5.66e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1720390105   1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLAN 33
Cdd:pfam00616 175 VNPDLFGLVDHQISPKQRRNLTLIAKVLQNLAN 207
PRK12704 PRK12704
phosphodiesterase; Provisional
 546-678 1.93e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.77  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 546 SADIESAHIEREEyKLKEYSKSMDESRLDREYE--EEIHSLKERLHMS----NRKLEEYERRLLSQEEQTSK---ILMQY 616
Cdd:PRK12704   30 EAKIKEAEEEAKR-ILEEAKKEAEAIKKEALLEakEEIHKLRNEFEKElrerRNELQKLEKRLLQKEENLDRkleLLEKR 108

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720390105 617 QARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRRdhpAMAEPLPEPKKRLLDAQERQL 678
Cdd:PRK12704  109 EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER---ISGLTAEEAKEILLEKVEEEA 167
UDM1_RNF168 cd22265
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; ...
 573-626 5.49e-03

UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; RING finger protein 168 (RNF168) is an E3 ubiquitin-protein ligase that promotes noncanonical K27 ubiquitination to signal DNA damage. Together with RNF8, RNF168 functions as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. This model corresponds to the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) domain of RNF168, which comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409018 [Multi-domain]  Cd Length: 73  Bit Score: 36.38  E-value: 5.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720390105 573 LDREYEEEIHSLKERLHM----SNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKR 626
Cdd:cd22265     7 LRQEYEEEISKLEAERRAleeeENRASEEYIQKLLAEEEEEEKLAEERRRAEEEQLKE 64
 
Name Accession Description Interval E-value
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
 116-695 0e+00

Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 433 to 538 amino acids in length. This domain is found associated with pfam00616, pfam00168. This domain has two conserved sequence motifs: DLQ and PLSFQNP.


Pssm-ID: 463427 [Multi-domain]  Cd Length: 511  Bit Score: 550.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 116 LNDISTALRNPN-IQRQPSRQSERTRSQPMVLRGPSAEMQgYMMRDLNSS-MDMARLPSPTKEKPpppppgggkDLFYVS 193
Cdd:pfam12004   1 LRDITTALTNPTpIQQQLRRFSEHSSSPPVPGRSISSGLQ-KMFEDPDDGlSDFTRLPSPTPENK---------DLFFVT 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 194 RPPLARSSPAYCTSSSDITEPEQKMLSVNKSVSMLDLQGdgpgGRLNSSSVSNlAAVGDLLHSSQASLTAALGLRPAPAG 273
Cdd:pfam12004  71 RPPLLQPSPARSSSYSDANEPDQQLPNGNKSLSMVDLQD----SRSLQGSPSP-PLHDAPLNLSQAGSQASVGLRPAWAA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 274 RLSQGSGSSItAAGMRLSQMGVTTdGVPAQQLRIPLSFQNPLFHMAADGPGPPAGHGGSsghgppsshhhhhhhhhhrgg 353
Cdd:pfam12004 146 RTSQGNPQSA-PQVRRPLQTPVTQ-GTRPQQLLAPLSFQNPVYHMAAGLPVSPRGLGSP--------------------- 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 354 EPPGDTFAPFHGYSKSEDLSSGVPkpPAASILHSHSYSDEFGPSGTDFTRRQLSLQDSLQHMLSPPQITIGPQRPAPSGP 433
Cdd:pfam12004 203 DSSSETHSSFSSHSNSEDLSSAAA--NKKSGPSNSSYSEDFARRSTEFTRRQLSLTELQHQPAVPRQNSAGPQRRIDQQG 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 434 GGGSGggsgggqpppLQRGKSQQLTVSAAQKPRPSSGNLlQSPEPSYGPARPRQQSLSKEGsiggsggsgggggggLKPS 513
Cdd:pfam12004 281 LGGPP----------LTRGRTPPSLLNSASYPRPSSGSL-MSSSPDWPPARLRQQSSSSKG---------------DSPE 334

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 514 ITK--QHSQTPSTLNP-TMPASERTVAWVSNMPHLSADIESAHIE-REEYKLKEysksmdesrldrEYEEEIHSLKERLH 589
Cdd:pfam12004 335 TKQrtQHQQVPSPVNPsTLSPVERTAAWVLNMNGQYEEEESSGPEsREELKQAE------------KYEQEISKLKERLR 402

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 590 MSNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRRDHPAMAEPLpEPKKR 669
Cdd:pfam12004 403 VSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMAVEEELKKDHAEMQAVI-DSKQK 481

                         570       580
                  ....*....|....*....|....*.
gi 1720390105 670 LLDAQERQLPPLGPTNPRVTLAPPWN 695
Cdd:pfam12004 482 IIDAQEKRIASLDAANARLMSALTQL 507
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
 1-126 9.18e-71

Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras GTPase-activating proteins includes DAB2IP, nGAP, and Syn GAP. Disabled 2 interactive protein, (DAB2IP; also known as ASK-interacting protein 1 (AIP1)), is a member of the GTPase-activating proteins, down-regulates Ras-mediated signal pathways, and mediates TNF-induced activation of ASK1-JNK signaling pathways. The mechanism by which TNF signaling is coupled to DAB2IP is not known.


Pssm-ID: 213338  Cd Length: 324  Bit Score: 233.63  E-value: 9.18e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105   1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGY 80
Cdd:cd05136   199 LSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKEEYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGY 278

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720390105  81 IDLGRELSTLHALLWEVLPQLSKEALLKLGPLPRLLNDISTALRNP 126
Cdd:cd05136   279 IDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITEALRNP 324
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
 1-118 2.72e-31

GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the GTPase activity of Ras, thereby "switching" it into an "off" position. Improved domain limits from structure.


Pssm-ID: 214617  Cd Length: 344  Bit Score: 125.50  E-value: 2.72e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105    1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGY 80
Cdd:smart00323 213 VSPKLFNLVDEHPDPTTRRTLTLIAKVLQNLANLSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEILVDKVSDST 292

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1720390105   81 IDLGRELSTLHALLWEVLPQLSKEaLLKLGPLPRLLND 118
Cdd:smart00323 293 TISGRELSLLHSLLLENGDALKRE-LNNEDPLGKLLFK 329
RasGAP_CLA2_BUD2 cd05137
Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein ...
 1-82 7.32e-16

Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein (GAP) for BUD1/RSR1 and is necessary for proper bud-site selection in yeast. BUD2 has sequence similarity to the catalytic domain of RasGAPs, and stimulates the hydrolysis of BUD1-GTP to BUD1-GDP. Elimination of Bud2p activity by mutation causes a random budding pattern with no growth defect. Overproduction of Bud2p also alters the budding pattern.


Pssm-ID: 213339 [Multi-domain]  Cd Length: 356  Bit Score: 79.92  E-value: 7.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105   1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLElewgsmqqflyeisnldtlTNSSSFEGY 80
Cdd:cd05137   225 LNPKLFGLLKDHPRPRAQRTLTLIAKVLQNLANLTTFGQKEPWMEPMNEFLT-------------------THREELKDY 285


                  ..
gi 1720390105  81 ID 82
Cdd:cd05137   286 ID 287
RasGAP cd04519
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...
 1-67 1.22e-15

Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Proteins having a RasGAP domain include p120GAP, IQGAP, Rab5-activating protein 6, and Neurofibromin, among others. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP exhibit no similarity at their amino acid sequence level. RasGTPases function as molecular switches in a large number of signaling pathways. They are in the on state when bound to GTP, and in the off state when bound to GDP. The RasGAP domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator.


Pssm-ID: 213328  Cd Length: 256  Bit Score: 77.53  E-value: 1.22e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720390105   1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLELEWGSMQQFLYEISN 67
Cdd:cd04519   190 VSPELFGLVPDEPSEQARRNLTLISKVLQSLANGVEFGDKEPFMKPLNDFIKSNKPKLKQFLDELSS 256
RasGAP_GAPA cd05132
Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to ...
 2-116 2.96e-14

Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to bind to small GTPases, which are yet to be identified. IQGAP proteins are integral components of cytoskeletal regulation. Results from truncated GAPAs indicated that almost the entire region of GAPA homologous to IQGAP is required for cytokinesis in Dictyostelium. More members of the IQGAP family are emerging, and evidence suggests that there are both similarities and differences in their function.


Pssm-ID: 213334  Cd Length: 352  Bit Score: 74.70  E-value: 2.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105   2 SPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFtSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGYI 81
Cdd:cd05132   205 SPQAYMLVDGKPSDNTRRTLTLIAKLLQNLANKPSY-SKEPYMAPLQPFVEENKERLNKFLNDLCEVDDFYESLELDQYI 283

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1720390105  82 DLGR----------ELSTLHALLWEVLPQLSKEALLKLGPLPRLL 116
Cdd:cd05132   284 ALSKkdlsinitlnEIYNTHSLLVKHLAELAPDHNDHLRLILQEL 328
RasGAP_GAP1_like cd05128
Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras ...
 1-66 1.35e-13

Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras GTPase-activating proteins includes GAP1(m) (or RASA2), GAP1_IP4BP (or RASA3), Ca2+ -promoted Ras inactivator (CAPRI, or RASAL4), and Ras GTPase activating-like proteins (RASAL) or RASAL1. The members are characterized by a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin homology domain that is associated with a Bruton's tyrosine kinase motif. While this domain structure is conserved, a small change in the function of each individual domain and the interaction between domains has a marked effect on the regulation of each protein.


Pssm-ID: 213330  Cd Length: 269  Bit Score: 71.51  E-value: 1.35e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720390105   1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTS----KEDFL-GFMNEFLELEW-GSMQQFLYEIS 66
Cdd:cd05128   196 LNPKLFGLREEHPDPQTARTLTLISKTIQTLGNLGSSSSglgvKEAYMsPLYERFTDEQHvDAVKKFLDRIS 267
RasGAP_p120GAP cd05391
Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates ...
 1-116 3.26e-12

Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates hydrolysis of bound GTP to GDP. Once the Ras regulator p120GAP, a member of the GAP protein family, is recruited to the membrane, it is transiently immobilized to interact with Ras-GTP. The down-regulation of Ras by p120GAP is a critical step in the regulation of many cellular processes, which is disrupted in approximately 30% of human cancers. p120GAP contains SH2, SH3, PH, calcium- and lipid-binding domains, suggesting its involvement in a complex network of cellular interactions in vivo.


Pssm-ID: 213340  Cd Length: 328  Bit Score: 68.28  E-value: 3.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105   1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLtNSSSFEGY 80
Cdd:cd05391   197 LNPRMFNIISETPSPTAARTLTLVAKSLQNLANLVEFGAKEPYMEGVNPFIKKNKERMIMFLDELGNVPEL-PDTTEHSR 275

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1720390105  81 IDLGRELSTLHALLWEVLPQLsKEALLKLGPLPRLL 116
Cdd:cd05391   276 TDLSRDLAALHEICVAHSDEL-RTLSNERGALKKLL 310
RasGAP_Neurofibromin_like cd05392
Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins ...
 1-104 5.11e-12

Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins include the Saccharomyces cerevisiae RasGAP proteins Ira1 and Ira2, the closest homolog of neurofibromin, which is responsible for the human autosomal dominant disease neurofibromatosis type I (NF1). The RasGAP Ira1/2 proteins are negative regulators of the Ras-cAMP signaling pathway and conserved from yeast to human. In yeast Ras proteins are activated by GEFs, and inhibited by two GAPs, Ira1 and Ira2. Ras proteins activate the cAMP/protein kinase A (PKA) pathway, which controls metabolism, stress resistance, growth, and meiosis. Recent studies showed that the kelch proteins Gpb1 and Gpb2 inhibit Ras activity via association with Ira1 and Ira2. Gpb1/2 bind to a conserved C-terminal domain of Ira1/2, and loss of Gpb1/2 results in a destabilization of Ira1 and Ira2, leading to elevated levels of Ras2-GTP and uninhibited cAMP-PKA signaling. Since the Gpb1/2 binding domain on Ira1/2 is conserved in the human neurofibromin protein, the studies suggest that an analogous signaling mechanism may contribute to the neoplastic development of NF1.


Pssm-ID: 213341  Cd Length: 317  Bit Score: 67.69  E-value: 5.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105   1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGY 80
Cdd:cd05392   189 VSPESENLLDPPPTPEARRSLILIAKVLQNIANGVLFSLKEPYLESLNEFLKKNSDRIQQFLSEVSTIPPTDPIFDESDE 268

                          90       100
                  ....*....|....*....|....
gi 1720390105  81 IDLGRELSTLHALLWEVLPQLSKE 104
Cdd:cd05392   269 EPITADLRYLHKFLYLHFLEIRKE 292
RasGAP_RASA3 cd05134
Ras-GTPase Activating Domain of RASA3; RASA3 (or GAP1_IP4BP) is a member of the GAP1 family ...
 1-67 1.70e-08

Ras-GTPase Activating Domain of RASA3; RASA3 (or GAP1_IP4BP) is a member of the GAP1 family and has been shown to specifically bind 1,3,4,5-tetrakisphosphate (IP4). Thus, RASA3 may function as an IP4 receptor. The members of GAP1 family are characterized by a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin-homology domain that is associated with a Bruton's tyrosine kinase motif. Purified RASA3 stimulates GAP activity on Ras with about a five-fold lower potency than p120RasGAP, but shows no GAP-stimulating activity at all against Rac or Rab3A.


Pssm-ID: 213336  Cd Length: 269  Bit Score: 56.19  E-value: 1.70e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720390105   1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTS---KEDFLG-FMNEFLELEWG-SMQQFLYEISN 67
Cdd:cd05134   196 LSPNLFQLTPHHPDPQTSRTLTLISKTIQTLGSLSKSKSanfKESYMAaFYDYFNEQKYAdAVKNFLDLISS 267
RasGAP_Neurofibromin cd05130
Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the ...
 2-96 2.75e-07

Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the neurofibromatosis type 1 gene (NF1) and shares a region of similarity with catalytic domain of the mammalian p120RasGAP protein and an extended similarity with the Saccharomyces cerevisiae RasGAP proteins Ira1 and Ira2. Neurofibromin has been shown to function as a GAP (GTPase-activating protein) which inhibits low molecular weight G proteins such as Ras by stimulating their intrinsic GTPase activity. NF1 is a common genetic disorder characterized by various symptoms ranging from predisposition for the development of tumors to learning disability or mental retardation. Loss of neurofibromin activity can be correlated to the increase in Ras-GTP concentration in neurofibromas of NF1 of patients, supporting the notion that unregulated Ras signaling may contribute to their development.


Pssm-ID: 213332 [Multi-domain]  Cd Length: 332  Bit Score: 53.09  E-value: 2.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105   2 SPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTsKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLT--NSSSFEG 79
Cdd:cd05130   200 SPYEYGILDREPPPRVKRGLKLMSKILQNIANHVLFT-KEAHMLPFNDFLRNHFEAGRRFFSSIASDCGAVdgPSSKYLS 278

                          90
                  ....*....|....*..
gi 1720390105  80 YIDLGRELStLHALLWE 96
Cdd:cd05130   279 FINDANVLA-LHRLLWN 294
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 552-677 1.63e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 49.92  E-value: 1.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 552 AHIEREEYKLKEYSKSMDESRLDREYE---EEIHSLKERLhmsnRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKRLR 628
Cdd:COG1579    66 LEIEEVEARIKKYEEQLGNVRNNKEYEalqKEIESLKRRI----SDLEDEILELMERIEELEEELAELEAELAELEAELE 141

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1720390105 629 QQQVEKDSQIKSIIGRLmlveEELRRDHPAMAEPLPEpkkRLLDAQERQ 677
Cdd:COG1579   142 EKKAELDEELAELEAEL----EELEAEREELAAKIPP---ELLALYERI 183
RasGAP_RASA2 cd05394
Ras-GTPase Activating Domain of RASA2; RASA2 (or GAP1(m)) is a member of the GAP1 family of ...
 1-67 3.54e-06

Ras-GTPase Activating Domain of RASA2; RASA2 (or GAP1(m)) is a member of the GAP1 family of Ras GTPase-activating proteins that includes GAP1_IP4BP (or RASA3), CAPRI, and RASAL. In vitro, RASA2 has been shown to bind inositol 1,3,4,5-tetrakisphosphate (IP4), the water soluble inositol head group of the lipid second messenger phosphatidylinositol 3,4,5-trisphosphate (PIP3). In vivo studies also demonstrated that RASA2 binds PIP3, and it is recruited to the plasma membrane following agonist stimulation of PI 3-kinase. Furthermore, the membrane translocation is a consequence of the ability of its pleckstrin homology (PH) domain to bind PIP3.


Pssm-ID: 213342  Cd Length: 272  Bit Score: 49.12  E-value: 3.54e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720390105   1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTS------KEDFL-GFMNEFLELEW-GSMQQFLYEISN 67
Cdd:cd05394   196 VSPHTFQLRPHHPDAQTSRTLTLISKTIQTLGSWGSLSKsklssfKETFMcDFFKMFQEEKYiEKVKKFLDEISS 270
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 543-676 8.09e-06

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: 49.30  E-value: 8.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105  543 PHLSADIESAHIEREEYKLKEYSKSMDESRldrEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQ---YQAR 619
Cdd:TIGR02169  261 SELEKRLEEIEQLLEELNKKIKDLGEEEQL---RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEidkLLAE 337

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720390105  620 LEQSEKRLRQQQVEKDsQIKSIIGRLMLVEEELRRDHPAMAEPLPEPKKRLLDAQER 676
Cdd:TIGR02169  338 IEELEREIEEERKRRD-KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 554-656 2.05e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 48.04  E-value: 2.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105  554 IEREEYKLKEYSKSMDESRLDREYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKRLRQQQVE 633
Cdd:pfam02463  169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248

                           90       100
                   ....*....|....*....|...
gi 1720390105  634 KDSQIKSIIGRLMLVEEELRRDH 656
Cdd:pfam02463  249 EQEEIESSKQEIEKEEEKLAQVL 271
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 545-675 2.33e-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: 48.13  E-value: 2.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105  545 LSADIESAHIEREEY--KLKEYSKSMDESRL-DREYEEEIHSLKERLHMSNRKLEEYERRLLSQEE---QTSKILMQYQA 618
Cdd:TIGR02168  244 LQEELKEAEEELEELtaELQELEEKLEELRLeVSELEEEIEELQKELYALANEISRLEQQKQILRErlaNLERQLEELEA 323

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720390105  619 RLEQSEKRLRQQQVEKDsQIKSIIGRLMLVEEELRRDHPAMAEPLPEPKKRLLDAQE 675
Cdd:TIGR02168  324 QLEELESKLDELAEELA-ELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
RNase_Y_N pfam12072
RNase Y N-terminal region;
549-678 2.45e-05

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 45.65  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 549 IESAHIEREEYKLKEYSKSMDES-RLDREYEEEIhslKERlhmsNRKLEEYERRLLSQEEQTSK---ILMQYQARLEQSE 624
Cdd:pfam12072  40 IEEAKKEAETKKKEALLEAKEEIhKLRAEAEREL---KER----RNELQRQERRLLQKEETLDRkdeSLEKKEESLEKKE 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720390105 625 KRL--RQQQVE-KDSQIKSIIGRLMlveEELRRDHPAMAEplpEPKKRLLDAQERQL 678
Cdd:pfam12072 113 KELeaQQQQLEeKEEELEELIEEQR---QELERISGLTSE---EAKEILLDEVEEEL 163
RasGAP_RASAL cd05135
Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like ...
 1-69 4.61e-05

Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like protein (RASAL) or RASAL1 is a member of the GAP1 family, and a Ca2+ sensor responding in-phase to repetitive Ca2+ signals by associating with the plasma membrane and deactivating Ras. It contains a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin-homology domain that is associated with a Bruton's tyrosine kinase motif. RASAL, like Ca2+ -promoted Ras inactivator (CAPRI, or RASAL4), is a cytosolic protein that undergoes a rapid translocation to the plasma membrane in response to receptor-mediated elevation in the concentration of intracellular free Ca2+, a translocation that activates its ability to function as a RasGAP. However, unlike RASAL4, RASAL undergoes an oscillatory translocation to the plasma membrane that occurs in synchrony with repetitive Ca2+ spikes.


Pssm-ID: 213337  Cd Length: 287  Bit Score: 45.96  E-value: 4.61e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720390105   1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSK--FTSKEDFLGFMNEFLELEWGSMQQFLYEISNLD 69
Cdd:cd05135   217 LTPKLFQLREQHADPRTSRTLLLLAKAVQSIGNLGLqlGQGKEQWMAPLHPFILQSVARVKDFLDRLIDID 287
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
 1-33 5.66e-05

GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the GTPase activity of Ras, thereby "switching" it into an "off" position.


Pssm-ID: 459871  Cd Length: 207  Bit Score: 44.97  E-value: 5.66e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1720390105   1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLAN 33
Cdd:pfam00616 175 VNPDLFGLVDHQISPKQRRNLTLIAKVLQNLAN 207
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 538-685 1.08e-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: 45.83  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105  538 WVSNMPHLSADIESAHIERE--EYKLKEYSKSMDESRLDR-EYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILM 614
Cdd:TIGR02169  810 IEARLREIEQKLNRLTLEKEylEKEIQELQEQRIDLKEQIkSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKK 889

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105  615 Q---YQARLEQSEKRLRQQQVE---KDSQIKSIIGRLMLVEEELRRDHPAMAEPLPEPKKRL--------LDAQERQLPP 680
Cdd:TIGR02169  890 ErdeLEAQLRELERKIEELEAQiekKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELsledvqaeLQRVEEEIRA 969


                   ....*
gi 1720390105  681 LGPTN 685
Cdd:TIGR02169  970 LEPVN 974
PRK12704 PRK12704
phosphodiesterase; Provisional
 546-678 1.93e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.77  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 546 SADIESAHIEREEyKLKEYSKSMDESRLDREYE--EEIHSLKERLHMS----NRKLEEYERRLLSQEEQTSK---ILMQY 616
Cdd:PRK12704   30 EAKIKEAEEEAKR-ILEEAKKEAEAIKKEALLEakEEIHKLRNEFEKElrerRNELQKLEKRLLQKEENLDRkleLLEKR 108

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720390105 617 QARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRRdhpAMAEPLPEPKKRLLDAQERQL 678
Cdd:PRK12704  109 EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER---ISGLTAEEAKEILLEKVEEEA 167
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 558-677 5.18e-04

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 43.40  E-value: 5.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105  558 EYKLKEYSKSMDESRLDREYEEEIHSLKERLHMSNRKLEEYERRLLSQE------EQTSKILMQYQARLEQSEKRLRQQQ 631
Cdd:PRK11448   128 DFKPGPFVPPEDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQqelvalEGLAAELEEKQQELEAQLEQLQEKA 207

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720390105  632 VEKDSQIK--------SIIGRLMLVEEELRrdhpamaeplpepkkRLLDAQERQ 677
Cdd:PRK11448   208 AETSQERKqkrkeitdQAAKRLELSEEETR---------------ILIDQQLRK 246
MutS2 COG1193
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
549-668 8.21e-04

dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];


Pssm-ID: 440806 [Multi-domain]  Cd Length: 784  Bit Score: 42.82  E-value: 8.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 549 IESA--HIEREEYKLKEYSKSMDESRldREYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQY---------- 616
Cdd:COG1193   502 IERAreLLGEESIDVEKLIEELERER--RELEEEREEAERLREELEKLREELEEKLEELEEEKEEILEKAreeaeeilre 579

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720390105 617 -QARLEQSEKRLRQQQVEKDsQIKSIIGRLMLVEEELRRDHPAMAEPLPEPKK 668
Cdd:COG1193   580 aRKEAEELIRELREAQAEEE-ELKEARKKLEELKQELEEKLEKPKKKAKPAKP 631
RasGAP_RASA4 cd05395
Ras-GTPase Activating Domain of RASA4; Ras GTPase activating-like 4 protein (RASAL4), also ...
 1-40 1.40e-03

Ras-GTPase Activating Domain of RASA4; Ras GTPase activating-like 4 protein (RASAL4), also known as Ca2+ -promoted Ras inactivator (CAPRI), is a member of the GAP1 family. Members of the GAP1 family are characterized by a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin-homology domain that is associated with a Bruton's tyrosine kinase motif. RASAL4, like RASAL, is a cytosolic protein that undergoes a rapid translocation to the plasma membrane in response to a receptor-mediated elevation in the concentration of intracellular free Ca2+ ([Ca2+]i). However, unlike RASAL, RASAL4 does not sense oscillations in [Ca2+]i.


Pssm-ID: 213343 [Multi-domain]  Cd Length: 287  Bit Score: 41.40  E-value: 1.40e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1720390105   1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSK 40
Cdd:cd05395   217 MSPKLFHLREKHADARTSRTLLLLAKAVQNVGNMDTLASR 256
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 549-680 1.61e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.74  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 549 IESA--HIEREEYKLKEYSKSMDESRldREYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQ----YQARLEQ 622
Cdd:PRK00409  504 IEEAkkLIGEDKEKLNELIASLEELE--RELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEaekeAQQAIKE 581

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720390105 623 SE-------KRLRQQQVEKDSQIKsiigrlmlvEEELRRDHPAMAEPLPEPKKRLLDAQERQLPP 680
Cdd:PRK00409  582 AKkeadeiiKELRQLQKGGYASVK---------AHELIEARKRLNKANEKKEKKKKKQKEKQEEL 637
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 545-678 3.22e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 3.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105 545 LSADIESAHIEREEY--KLKEYSKSMDESRLDR-EYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQtskilmqyQARLE 621
Cdd:COG1196   244 LEAELEELEAELEELeaELAELEAELEELRLELeELELELEEAQAEEYELLAELARLEQDIARLEER--------RRELE 315

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720390105 622 QSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRRDHPAMAeplpEPKKRLLDAQERQL 678
Cdd:COG1196   316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELE----EAEAELAEAEEALL 368
RasGAP_IQGAP_like cd05127
Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family ...
 2-119 3.73e-03

Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family represents IQ motif containing GTPase activating protein (IQGAP) which associated with the Ras GTP-binding protein. A primary function of IQGAP proteins is to modulate cytoskeletal architecture. There are three known IQGAP family members: IQGAP1, IQGAP2 and IQGAP3. Human IQGAP1 and IQGAP2 share 62% identity. IQGAPs are multi-domain molecules having a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeats, a single WW domain, four IQ motifs that mediate interactions with calmodulin, and a RasGAP related domain that binds active Rho family GTPases. IQGAP is an essential regulator of cytoskeletal function. IQGAP1 negatively regulates Ras family GTPases by stimulating their intrinsic GTPase activity, the protein actually lacks GAP activity. Both IQGAP1 and IQGAP2 specifically bind to Cdc42 and Rac1, but not to RhoA. Despite of their similarities to part of the sequence of RasGAP, neither IQGAP1 nor IQGAP2 interacts with Ras. IQGAP3, only present in mammals, regulates the organization of the cytoskeleton under the regulation of Rac1 and Cdc42 in neuronal cells. The depletion of IQGAP3 is shown to impair neurite or axon outgrowth in neuronal cells with disorganized cytoskeleton.


Pssm-ID: 213329 [Multi-domain]  Cd Length: 331  Bit Score: 40.26  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390105   2 SPSLFGLMQEYPDEQTS----RTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLELEWGSMQQFLYEIS---------NL 68
Cdd:cd05127   190 APEAFDIIDLSVGGQLSplqrRNLGSIAKVLQQAASGKLFGGENPYLSPLNPYISESHEKFKKFFLEACtvpeaeehfNI 269

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720390105  69 DTLTNSSSFEG---YIDLgRELSTLHALLWEVLPQLS-------KEALLKLGPLPRLLNDI 119
Cdd:cd05127   270 DEYSDLTMLTKptiYISL-QEIFATHKLLLEHQDEIApdpddplRELLDDLGPAPTIESLL 329
UDM1_RNF168 cd22265
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; ...
 573-626 5.49e-03

UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; RING finger protein 168 (RNF168) is an E3 ubiquitin-protein ligase that promotes noncanonical K27 ubiquitination to signal DNA damage. Together with RNF8, RNF168 functions as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. This model corresponds to the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) domain of RNF168, which comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409018 [Multi-domain]  Cd Length: 73  Bit Score: 36.38  E-value: 5.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720390105 573 LDREYEEEIHSLKERLHM----SNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKR 626
Cdd:cd22265     7 LRQEYEEEISKLEAERRAleeeENRASEEYIQKLLAEEEEEEKLAEERRRAEEEQLKE 64
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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