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Conserved domains on  [gi|569000235|ref|XP_006524311|]
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ras/Rap GTPase-activating protein SynGAP isoform X17 [Mus musculus]

Protein Classification

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. ...
116-690 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: 531.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  116 LNDISTALRNPN-IQRQPSRQSERTRSQPMVLRGPSAEMQgYMMRDLNSSIdlqsfmarglnssMDMARLPSPTKEKPpp 194
Cdd:pfam12004   1 LRDITTALTNPTpIQQQLRRFSEHSSSPPVPGRSISSGLQ-KMFEDPDDGL-------------SDFTRLPSPTPENK-- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  195 pppgggkDLFYVSRPPLARSSPAYCTSSSDITEPEQKMLSVNKSVSMLDLQGdgpgGRLNSSSVSNlAAVGDLLHSSQAS 274
Cdd:pfam12004  65 -------DLFFVTRPPLLQPSPARSSSYSDANEPDQQLPNGNKSLSMVDLQD----SRSLQGSPSP-PLHDAPLNLSQAG 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  275 LTAALGLRPAPAGRLSQGSGSSItAAGMRLSQMGVTTdGVPAQQLRIPLSFQNPLFHMAADGPGPPAGHGGSsghgppss 354
Cdd:pfam12004 133 SQASVGLRPAWAARTSQGNPQSA-PQVRRPLQTPVTQ-GTRPQQLLAPLSFQNPVYHMAAGLPVSPRGLGSP-------- 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  355 hhhhhhhhhhrggEPPGDTFAPFHGYSKSEDLSSGVPkpPAASILHSHSYSDEFGPSGTDFTRRQLSLQDSLQHMLSPPQ 434
Cdd:pfam12004 203 -------------DSSSETHSSFSSHSNSEDLSSAAA--NKKSGPSNSSYSEDFARRSTEFTRRQLSLTELQHQPAVPRQ 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  435 ITIGPQRPAPSGPGGGSGggsgggqpppLQRGKSQQLTVSAAQKPRPSSGNLlQSPEPSYGPARPRQQSLSKEGsiggsg 514
Cdd:pfam12004 268 NSAGPQRRIDQQGLGGPP----------LTRGRTPPSLLNSASYPRPSSGSL-MSSSPDWPPARLRQQSSSSKG------ 330
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  515 gsgggggggLKPSITK--QHSQTPSTLNP-TMPASERTVAWVSNMPHLSADIESAHIE-REEYKLKEysksmdesrldrv 590
Cdd:pfam12004 331 ---------DSPETKQrtQHQQVPSPVNPsTLSPVERTAAWVLNMNGQYEEEESSGPEsREELKQAE------------- 388
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  591 kEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRR 670
Cdd:pfam12004 389 -KYEQEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMAVEEELKK 467
                         570       580
                  ....*....|....*....|
gi 569000235  671 DHPAMAEPLpEPKKRLLDAQ 690
Cdd:pfam12004 468 DHAEMQAVI-DSKQKIIDAQ 486
RasGAP super family cl02569
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...
1-126 5.94e-70

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: 233.24  E-value: 5.94e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235   1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGY 80
Cdd:cd05136  199 LSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKEEYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGY 278
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 569000235  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. ...
116-690 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: 531.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  116 LNDISTALRNPN-IQRQPSRQSERTRSQPMVLRGPSAEMQgYMMRDLNSSIdlqsfmarglnssMDMARLPSPTKEKPpp 194
Cdd:pfam12004   1 LRDITTALTNPTpIQQQLRRFSEHSSSPPVPGRSISSGLQ-KMFEDPDDGL-------------SDFTRLPSPTPENK-- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  195 pppgggkDLFYVSRPPLARSSPAYCTSSSDITEPEQKMLSVNKSVSMLDLQGdgpgGRLNSSSVSNlAAVGDLLHSSQAS 274
Cdd:pfam12004  65 -------DLFFVTRPPLLQPSPARSSSYSDANEPDQQLPNGNKSLSMVDLQD----SRSLQGSPSP-PLHDAPLNLSQAG 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  275 LTAALGLRPAPAGRLSQGSGSSItAAGMRLSQMGVTTdGVPAQQLRIPLSFQNPLFHMAADGPGPPAGHGGSsghgppss 354
Cdd:pfam12004 133 SQASVGLRPAWAARTSQGNPQSA-PQVRRPLQTPVTQ-GTRPQQLLAPLSFQNPVYHMAAGLPVSPRGLGSP-------- 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  355 hhhhhhhhhhrggEPPGDTFAPFHGYSKSEDLSSGVPkpPAASILHSHSYSDEFGPSGTDFTRRQLSLQDSLQHMLSPPQ 434
Cdd:pfam12004 203 -------------DSSSETHSSFSSHSNSEDLSSAAA--NKKSGPSNSSYSEDFARRSTEFTRRQLSLTELQHQPAVPRQ 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  435 ITIGPQRPAPSGPGGGSGggsgggqpppLQRGKSQQLTVSAAQKPRPSSGNLlQSPEPSYGPARPRQQSLSKEGsiggsg 514
Cdd:pfam12004 268 NSAGPQRRIDQQGLGGPP----------LTRGRTPPSLLNSASYPRPSSGSL-MSSSPDWPPARLRQQSSSSKG------ 330
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  515 gsgggggggLKPSITK--QHSQTPSTLNP-TMPASERTVAWVSNMPHLSADIESAHIE-REEYKLKEysksmdesrldrv 590
Cdd:pfam12004 331 ---------DSPETKQrtQHQQVPSPVNPsTLSPVERTAAWVLNMNGQYEEEESSGPEsREELKQAE------------- 388
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  591 kEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRR 670
Cdd:pfam12004 389 -KYEQEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMAVEEELKK 467
                         570       580
                  ....*....|....*....|
gi 569000235  671 DHPAMAEPLpEPKKRLLDAQ 690
Cdd:pfam12004 468 DHAEMQAVI-DSKQKIIDAQ 486
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
1-126 5.94e-70

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: 233.24  E-value: 5.94e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235   1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGY 80
Cdd:cd05136  199 LSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKEEYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGY 278
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 569000235  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 3.41e-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: 3.41e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235     1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGY 80
Cdd:smart00323 213 VSPKLFNLVDEHPDPTTRRTLTLIAKVLQNLANLSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEILVDKVSDST 292
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 569000235    81 IDLGRELSTLHALLWEVLPQLSKEaLLKLGPLPRLLND 118
Cdd:smart00323 293 TISGRELSLLHSLLLENGDALKRE-LNNEDPLGKLLFK 329
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
568-695 2.99e-07

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: 54.30  E-value: 2.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235   568 IEREEYKLKEYSKSMDESRLDRVKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQ---YQARLEQSEKRLR 644
Cdd:TIGR02169  267 LEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEidkLLAEIEELEREIE 346
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 569000235   645 QQQVEKDsQIKSIIGRLMLVEEELRRDHPAMAEPLPEPKKRLLDAQVEITM 695
Cdd:TIGR02169  347 EERKRRD-KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK 396
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
561-689 9.46e-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: 47.61  E-value: 9.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235 561 ADIEsAHIEREEYKLKEYSKSM--DESRLDRV---KEYE---EEIHSLKERLhmsnRKLEEYERRLLSQEEQTSKILMQY 632
Cdd:COG1579   55 EDLE-KEIKRLELEIEEVEARIkkYEEQLGNVrnnKEYEalqKEIESLKRRI----SDLEDEILELMERIEELEEELAEL 129
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 569000235 633 QARLEQSEKRLRQQQVEKDSQIKSIIGRLmlveEELRRDHPAMAEPLPEpkkRLLDA 689
Cdd:COG1579  130 EAELAELEAELEEKKAELDEELAELEAEL----EELEAEREELAAKIPP---ELLAL 179
PRK12704 PRK12704
phosphodiesterase; Provisional
560-670 3.20e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.47  E-value: 3.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235 560 SADIESAHIEREEyKLKEYSKSMDESRLDRVKEYEEEIHSLKERLHMS----NRKLEEYERRLLSQEEQTSK---ILMQY 632
Cdd:PRK12704  30 EAKIKEAEEEAKR-ILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKElrerRNELQKLEKRLLQKEENLDRkleLLEKR 108
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 569000235 633 QARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRR 670
Cdd:PRK12704 109 EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
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 569000235    1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLAN 33
Cdd:pfam00616 175 VNPDLFGLVDHQISPKQRRNLTLIAKVLQNLAN 207
UDM1_RNF168 cd22265
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; ...
591-642 1.60e-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: 37.92  E-value: 1.60e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 569000235 591 KEYEEEIHSLKERLHM----SNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKR 642
Cdd:cd22265    9 QEYEEEISKLEAERRAleeeENRASEEYIQKLLAEEEEEEKLAEERRRAEEEQLKE 64
 
Name Accession Description Interval E-value
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
116-690 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: 531.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  116 LNDISTALRNPN-IQRQPSRQSERTRSQPMVLRGPSAEMQgYMMRDLNSSIdlqsfmarglnssMDMARLPSPTKEKPpp 194
Cdd:pfam12004   1 LRDITTALTNPTpIQQQLRRFSEHSSSPPVPGRSISSGLQ-KMFEDPDDGL-------------SDFTRLPSPTPENK-- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  195 pppgggkDLFYVSRPPLARSSPAYCTSSSDITEPEQKMLSVNKSVSMLDLQGdgpgGRLNSSSVSNlAAVGDLLHSSQAS 274
Cdd:pfam12004  65 -------DLFFVTRPPLLQPSPARSSSYSDANEPDQQLPNGNKSLSMVDLQD----SRSLQGSPSP-PLHDAPLNLSQAG 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  275 LTAALGLRPAPAGRLSQGSGSSItAAGMRLSQMGVTTdGVPAQQLRIPLSFQNPLFHMAADGPGPPAGHGGSsghgppss 354
Cdd:pfam12004 133 SQASVGLRPAWAARTSQGNPQSA-PQVRRPLQTPVTQ-GTRPQQLLAPLSFQNPVYHMAAGLPVSPRGLGSP-------- 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  355 hhhhhhhhhhrggEPPGDTFAPFHGYSKSEDLSSGVPkpPAASILHSHSYSDEFGPSGTDFTRRQLSLQDSLQHMLSPPQ 434
Cdd:pfam12004 203 -------------DSSSETHSSFSSHSNSEDLSSAAA--NKKSGPSNSSYSEDFARRSTEFTRRQLSLTELQHQPAVPRQ 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  435 ITIGPQRPAPSGPGGGSGggsgggqpppLQRGKSQQLTVSAAQKPRPSSGNLlQSPEPSYGPARPRQQSLSKEGsiggsg 514
Cdd:pfam12004 268 NSAGPQRRIDQQGLGGPP----------LTRGRTPPSLLNSASYPRPSSGSL-MSSSPDWPPARLRQQSSSSKG------ 330
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  515 gsgggggggLKPSITK--QHSQTPSTLNP-TMPASERTVAWVSNMPHLSADIESAHIE-REEYKLKEysksmdesrldrv 590
Cdd:pfam12004 331 ---------DSPETKQrtQHQQVPSPVNPsTLSPVERTAAWVLNMNGQYEEEESSGPEsREELKQAE------------- 388
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  591 kEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRR 670
Cdd:pfam12004 389 -KYEQEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMAVEEELKK 467
                         570       580
                  ....*....|....*....|
gi 569000235  671 DHPAMAEPLpEPKKRLLDAQ 690
Cdd:pfam12004 468 DHAEMQAVI-DSKQKIIDAQ 486
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
1-126 5.94e-70

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: 233.24  E-value: 5.94e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235   1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGY 80
Cdd:cd05136  199 LSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKEEYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGY 278
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 569000235  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 3.41e-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: 3.41e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235     1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGY 80
Cdd:smart00323 213 VSPKLFNLVDEHPDPTTRRTLTLIAKVLQNLANLSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEILVDKVSDST 292
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 569000235    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 7.22e-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: 7.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235   1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLElewgsmqqflyeisnldtlTNSSSFEGY 80
Cdd:cd05137  225 LNPKLFGLLKDHPRPRAQRTLTLIAKVLQNLANLTTFGQKEPWMEPMNEFLT-------------------THREELKDY 285

                 ..
gi 569000235  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 1.77e-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: 77.15  E-value: 1.77e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569000235   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 1.82e-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: 75.47  E-value: 1.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235   2 SPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFtSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGYI 81
Cdd:cd05132  205 SPQAYMLVDGKPSDNTRRTLTLIAKLLQNLANKPSY-SKEPYMAPLQPFVEENKERLNKFLNDLCEVDDFYESLELDQYI 283
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 569000235  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 3.05e-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: 70.74  E-value: 3.05e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000235   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 3.85e-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: 3.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235   1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLtNSSSFEGY 80
Cdd:cd05391  197 LNPRMFNIISETPSPTAARTLTLVAKSLQNLANLVEFGAKEPYMEGVNPFIKKNKERMIMFLDELGNVPEL-PDTTEHSR 275
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 569000235  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 7.51e-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: 67.31  E-value: 7.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235   1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGY 80
Cdd:cd05392  189 VSPESENLLDPPPTPEARRSLILIAKVLQNIANGVLFSLKEPYLESLNEFLKKNSDRIQQFLSEVSTIPPTDPIFDESDE 268
                         90       100
                 ....*....|....*....|....
gi 569000235  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 2.31e-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: 2.31e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000235   1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTS---KEDFLG-FMNEFLELEWG-SMQQFLYEISN 67
Cdd:cd05134  196 LSPNLFQLTPHHPDPQTSRTLTLISKTIQTLGSLSKSKSanfKESYMAaFYDYFNEQKYAdAVKNFLDLISS 267
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
568-695 2.99e-07

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: 54.30  E-value: 2.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235   568 IEREEYKLKEYSKSMDESRLDRVKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQ---YQARLEQSEKRLR 644
Cdd:TIGR02169  267 LEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEidkLLAEIEELEREIE 346
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 569000235   645 QQQVEKDsQIKSIIGRLMLVEEELRRDHPAMAEPLPEPKKRLLDAQVEITM 695
Cdd:TIGR02169  347 EERKRRD-KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK 396
RasGAP_Neurofibromin cd05130
Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the ...
2-96 4.17e-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: 52.71  E-value: 4.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235   2 SPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTsKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLT--NSSSFEG 79
Cdd:cd05130  200 SPYEYGILDREPPPRVKRGLKLMSKILQNIANHVLFT-KEAHMLPFNDFLRNHFEAGRRFFSSIASDCGAVdgPSSKYLS 278
                         90
                 ....*....|....*..
gi 569000235  80 YIDLGRELStLHALLWE 96
Cdd:cd05130  279 FINDANVLA-LHRLLWN 294
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
559-694 5.26e-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: 50.44  E-value: 5.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235   559 LSADIESAHIEREEY--KLKEYSKSMDESRLdRVKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEE---QTSKILMQYQ 633
Cdd:TIGR02168  244 LQEELKEAEEELEELtaELQELEEKLEELRL-EVSELEEEIEELQKELYALANEISRLEQQKQILRErlaNLERQLEELE 322
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569000235   634 ARLEQSEKRLRQQQVEKDsQIKSIIGRLMLVEEELRRDHPAMAEPLPEPKKRLLDAQVEIT 694
Cdd:TIGR02168  323 AQLEELESKLDELAEELA-ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
RasGAP_RASA2 cd05394
Ras-GTPase Activating Domain of RASA2; RASA2 (or GAP1(m)) is a member of the GAP1 family of ...
1-67 7.08e-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: 48.35  E-value: 7.08e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569000235   1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTS------KEDFL-GFMNEFLELEW-GSMQQFLYEISN 67
Cdd:cd05394  196 VSPHTFQLRPHHPDAQTSRTLTLISKTIQTLGSWGSLSKsklssfKETFMcDFFKMFQEEKYiEKVKKFLDEISS 270
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
561-689 9.46e-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: 47.61  E-value: 9.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235 561 ADIEsAHIEREEYKLKEYSKSM--DESRLDRV---KEYE---EEIHSLKERLhmsnRKLEEYERRLLSQEEQTSKILMQY 632
Cdd:COG1579   55 EDLE-KEIKRLELEIEEVEARIkkYEEQLGNVrnnKEYEalqKEIESLKRRI----SDLEDEILELMERIEELEEELAEL 129
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 569000235 633 QARLEQSEKRLRQQQVEKDSQIKSIIGRLmlveEELRRDHPAMAEPLPEpkkRLLDA 689
Cdd:COG1579  130 EAELAELEAELEEKKAELDEELAELEAEL----EELEAEREELAAKIPP---ELLAL 179
PRK12704 PRK12704
phosphodiesterase; Provisional
560-670 3.20e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.47  E-value: 3.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235 560 SADIESAHIEREEyKLKEYSKSMDESRLDRVKEYEEEIHSLKERLHMS----NRKLEEYERRLLSQEEQTSK---ILMQY 632
Cdd:PRK12704  30 EAKIKEAEEEAKR-ILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKElrerRNELQKLEKRLLQKEENLDRkleLLEKR 108
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 569000235 633 QARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRR 670
Cdd:PRK12704 109 EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
RasGAP_RASAL cd05135
Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like ...
1-69 5.04e-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: 5.04e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569000235   1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSK--FTSKEDFLGFMNEFLELEWGSMQQFLYEISNLD 69
Cdd:cd05135  217 LTPKLFQLREQHADPRTSRTLLLLAKAVQSIGNLGLqlGQGKEQWMAPLHPFILQSVARVKDFLDRLIDID 287
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
552-682 5.34e-05

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: 46.98  E-value: 5.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235   552 WVSNMPHLSADIESAHIERE--EYKLKEYSKSMDESRlDRVKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKIL 629
Cdd:TIGR02169  810 IEARLREIEQKLNRLTLEKEylEKEIQELQEQRIDLK-EQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLK 888
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 569000235   630 MQ---YQARLEQSEKRLRQQQVE---KDSQIKSIIGRLMLVEEELRRDHPAMAEPLPEP 682
Cdd:TIGR02169  889 KErdeLEAQLRELERKIEELEAQiekKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP 947
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 569000235    1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLAN 33
Cdd:pfam00616 175 VNPDLFGLVDHQISPKQRRNLTLIAKVLQNLAN 207
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
576-670 1.85e-04

Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442818 [Multi-domain]  Cd Length: 125  Bit Score: 41.76  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235 576 KEYSKSM-----DESR--LDRV-KEYE---EEIHSLKERLHMSNRKLEEYERR-------LLSQEEQTSKILMQYQARLE 637
Cdd:COG3599   11 KEFKKGFrgydeDEVDefLDEVaEDYErliRENKELKEKLEELEEELEEYRELeetlqktLVVAQETAEEVKENAEKEAE 90
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 569000235 638 Q--SEKRLRQQQVEKDSQIKSIigRLMLVEEELRR 670
Cdd:COG3599   91 LiiKEAELEAEKIIEEAQEKAR--KIVREIEELKR 123
RNase_Y_N pfam12072
RNase Y N-terminal region;
563-671 4.49e-04

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 42.18  E-value: 4.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  563 IESAHIEREEYKLKEYSKSMDESRLDRVkEYEEEIhslKERlhmsNRKLEEYERRLLSQEEQTSK---ILMQYQARLEQS 639
Cdd:pfam12072  40 IEEAKKEAETKKKEALLEAKEEIHKLRA-EAEREL---KER----RNELQRQERRLLQKEETLDRkdeSLEKKEESLEKK 111
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 569000235  640 EKRL--RQQQVE-KDSQIKSIIG-----------------RLML---VEEELRRD 671
Cdd:pfam12072 112 EKELeaQQQQLEeKEEELEELIEeqrqelerisgltseeaKEILldeVEEELRHE 166
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
559-669 5.25e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 5.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235 559 LSADIESAHIEREEY--KLKEYSKSMDESRLdRVKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQyQARL 636
Cdd:COG1196  244 LEAELEELEAELEELeaELAELEAELEELRL-ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER-LEEL 321
                         90       100       110
                 ....*....|....*....|....*....|...
gi 569000235 637 EQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELR 669
Cdd:COG1196  322 EEELAELEEELEELEEELEELEEELEEAEEELE 354
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
558-693 6.73e-04

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: 43.51  E-value: 6.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235   558 HLSADIE--SAHIEREEYKLKEYSKSMDESRlDRVKEYEEEIHSLKERLHMSNRKLEEYERR-----------------L 618
Cdd:TIGR02168  313 NLERQLEelEAQLEELESKLDELAEELAELE-EKLEELKEELESLEAELEELEAELEELESRleeleeqletlrskvaqL 391
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235   619 LSQEEQTSKILMQYQARLEQSEKRLRQQQVEK--------DSQIKSIIGRLMLVE---EELRRDHPAMAEPLPEPKKRLL 687
Cdd:TIGR02168  392 ELQIASLNNEIERLEARLERLEDRRERLQQEIeellkkleEAELKELQAELEELEeelEELQEELERLEEALEELREELE 471

                   ....*.
gi 569000235   688 DAQVEI 693
Cdd:TIGR02168  472 EAEQAL 477
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
545-670 1.07e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235 545 ASERTVAWVSNMPHLSADIESAhieREEYKLKEYSKSMDESRLDRVK----EYEEEIHSLKERLHMSNRKLEEYERRLLS 620
Cdd:COG4372   29 LSEQLRKALFELDKLQEELEQL---REELEQAREELEQLEEELEQARseleQLEEELEELNEQLQAAQAELAQAQEELES 105
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 569000235 621 QEEQTSKI---LMQYQA---RLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRR 670
Cdd:COG4372  106 LQEEAEELqeeLEELQKerqDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
569-669 1.12e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235 569 EREEYKLKEYSKSMDESRLDR----VKEYEEEIHSLKERLHMSNRKLEEYERRL--LSQEEQTSKILMQYQARLEQSEKR 642
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEeingIEERIKELEEKEERLEELKKKLKELEKRLeeLEERHELYEEAKAKKEELERLKKR 380
                         90       100
                 ....*....|....*....|....*...
gi 569000235 643 LRQQQVEK-DSQIKSIIGRLMLVEEELR 669
Cdd:PRK03918 381 LTGLTPEKlEKELEELEKAKEEIEEEIS 408
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
563-647 1.29e-03

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 40.03  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  563 IESAHIEREEYKLKEYSKSMdESRLDRVKEYEEEIHSLKERL----HMSNRKLEEYERRL----LSQEEQTSKILMQYQA 634
Cdd:pfam15346  43 VEEARKIMEKQVLEELERER-EAELEEERRKEEEERKKREELerilEENNRKIEEAQRKEaeerLAMLEEQRRMKEERQR 121
                          90
                  ....*....|...
gi 569000235  635 RLEQSEKRLRQQQ 647
Cdd:pfam15346 122 REKEEEEREKREQ 134
MutS2 COG1193
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
563-684 1.48e-03

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


Pssm-ID: 440806 [Multi-domain]  Cd Length: 784  Bit Score: 42.05  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235 563 IESA--HIEREEYKLKEYSKSMDESRldrvKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQY-------- 632
Cdd:COG1193  502 IERAreLLGEESIDVEKLIEELERER----RELEEEREEAERLREELEKLREELEEKLEELEEEKEEILEKAreeaeeil 577
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 569000235 633 ---QARLEQSEKRLRQQQVEKDsQIKSIIGRLMLVEEELRRDHPAMAEPLPEPKK 684
Cdd:COG1193  578 reaRKEAEELIRELREAQAEEE-ELKEARKKLEELKQELEEKLEKPKKKAKPAKP 631
UDM1_RNF168 cd22265
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; ...
591-642 1.60e-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: 37.92  E-value: 1.60e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 569000235 591 KEYEEEIHSLKERLHM----SNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKR 642
Cdd:cd22265    9 QEYEEEISKLEAERRAleeeENRASEEYIQKLLAEEEEEEKLAEERRRAEEEQLKE 64
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
563-684 1.70e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.12  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235 563 IESA--HIEREEYKLKEYSKSMDESRLdRVKEYEEEIHSLK---ERLHMS----NRKLEEYERRLLS-QEEQTSKILMQY 632
Cdd:PRK00409 504 IEEAkkLIGEDKEKLNELIASLEELER-ELEQKAEEAEALLkeaEKLKEEleekKEKLQEEEDKLLEeAEKEAQQAIKEA 582
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 569000235 633 QARLEQSEKRLRQQQVEKDSQIKSiigrlMLVEEELRRDHPAmAEPLPEPKK 684
Cdd:PRK00409 583 KKEADEIIKELRQLQKGGYASVKA-----HELIEARKRLNKA-NEKKEKKKK 628
RasGAP_RASA4 cd05395
Ras-GTPase Activating Domain of RASA4; Ras GTPase activating-like 4 protein (RASAL4), also ...
1-40 1.81e-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: 41.01  E-value: 1.81e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 569000235   1 MSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSK 40
Cdd:cd05395  217 MSPKLFHLREKHADARTSRTLLLLAKAVQNVGNMDTLASR 256
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
559-676 2.11e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.68  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235 559 LSADIES--AHIEREEYKL------KEY---SKSMDESRLdRVKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSK 627
Cdd:COG1579   64 LELEIEEveARIKKYEEQLgnvrnnKEYealQKEIESLKR-RISDLEDEILELMERIEELEEELAELEAELAELEAELEE 142
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 569000235 628 ILMQYQARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRRDHPAMA 676
Cdd:COG1579  143 KKAELDEELAELEAELEELEAEREELAAKIPPELLALYERIRKRKNGLA 191
MAT1 pfam06391
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ...
568-656 2.69e-03

CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.


Pssm-ID: 461894 [Multi-domain]  Cd Length: 202  Bit Score: 39.92  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  568 IEREEYKLKEY---SKSMDESRLDRVKEYEEEIHSLKERLHmsnrklEEYERRLLSQEEQTSKILMQYQARLEQSEKRLR 644
Cdd:pfam06391  88 LSQEEEELEELlelEKREKEERRKEEKQEEEEEKEKKEKAK------QELIDELMTSNKDAEEIIAQHKKTAKKRKSERR 161
                          90
                  ....*....|..
gi 569000235  645 QQQVEKDSQIKS 656
Cdd:pfam06391 162 RKLEELNRVLEQ 173
RasGAP_IQGAP_like cd05127
Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family ...
2-119 2.92e-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: 40.65  E-value: 2.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235   2 SPSLFGLMQEYPDEQTS----RTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLELEWGSMQQFLYEIS---------NL 68
Cdd:cd05127  190 APEAFDIIDLSVGGQLSplqrRNLGSIAKVLQQAASGKLFGGENPYLSPLNPYISESHEKFKKFFLEACtvpeaeehfNI 269
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569000235  69 DTLTNSSSFEG---YIDLgRELSTLHALLWEVLPQLS-------KEALLKLGPLPRLLNDI 119
Cdd:cd05127  270 DEYSDLTMLTKptiYISL-QEIFATHKLLLEHQDEIApdpddplRELLDDLGPAPTIESLL 329
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
569-692 3.02e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.26  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  569 EREEYKLKEYSKSMDESRLDRVKEYEEEIHSLKERL--HMSNRKLEEYER-----RLLSQEEQtskilmQYQARLEQSEK 641
Cdd:pfam17380 409 EERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERarEMERVRLEEQERqqqveRLRQQEEE------RKRKKLELEKE 482
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 569000235  642 RLRQQQVEKDsqiksiigRLMLVEEELRRDHPAMAEplPEPKKRLLDAQVE 692
Cdd:pfam17380 483 KRDRKRAEEQ--------RRKILEKELEERKQAMIE--EERKRKLLEKEME 523
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
558-670 3.27e-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: 3.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235 558 HLSADIESAHIEREEYKLKEysksmdESRLDRVKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQyQARLE 637
Cdd:COG1196  313 ELEERLEELEEELAELEEEL------EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE-LEELA 385
                         90       100       110
                 ....*....|....*....|....*....|...
gi 569000235 638 QSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRR 670
Cdd:COG1196  386 EELLEALRAAAELAAQLEELEEAEEALLERLER 418
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
562-671 4.84e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.90  E-value: 4.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  562 DIESAHIEREEYKLKEYSKSMDESRLDRVKEYEEEIHSLKER------------LHMSNRKLEEYERRLLS----QEEQT 625
Cdd:pfam13868 183 EREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEReeaekkarqrqeLQQAREEQIELKERRLAeeaeREEEE 262
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 569000235  626 SKILMQYQARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRRD 671
Cdd:pfam13868 263 FERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAA 308
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
583-687 5.14e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 5.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235 583 DESRLDRVKE------YEEEIHSLKERLHMSNRKLEEYErRLLSQEEQTSKILMQYQARLEQSEKRLRqqqvEKDSQIKS 656
Cdd:PRK03918 144 DESREKVVRQilglddYENAYKNLGEVIKEIKRRIERLE-KFIKRTENIEELIKEKEKELEEVLREIN----EISSELPE 218
                         90       100       110
                 ....*....|....*....|....*....|.
gi 569000235 657 IIGRLMLVEEELRRdHPAMAEPLPEPKKRLL 687
Cdd:PRK03918 219 LREELEKLEKEVKE-LEELKEEIEELEKELE 248
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
584-670 5.21e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 5.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235 584 ESRLDRVKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKRLRQQQVEKDSQIKSIIGRLML 663
Cdd:COG4717  145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224

                 ....*..
gi 569000235 664 VEEELRR 670
Cdd:COG4717  225 LEEELEQ 231
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
554-671 5.27e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 5.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235 554 SNMPHLSADIESAHIEREEY-KLKEY---SKSMDESRLDRVKEYEEEIHSLKERLHMSN---RKLEEYERRLLSQEEQT- 625
Cdd:PRK03918 214 SELPELREELEKLEKEVKELeELKEEieeLEKELESLEGSKRKLEEKIRELEERIEELKkeiEELEEKVKELKELKEKAe 293
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235 626 -----SKILMQYQARLEQSEKRLR---------QQQVEKDSQIKSIIGRLMLVEEELRRD 671
Cdd:PRK03918 294 eyiklSEFYEEYLDELREIEKRLSrleeeingiEERIKELEEKEERLEELKKKLKELEKR 353
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
559-680 5.49e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 5.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  559 LSADIESAHIEREEYKlkeysKSMDESRLDRVKEYEEEIHSLKERLHMSNRKLEEYERRL-------------------- 618
Cdd:COG4913   314 LEARLDALREELDELE-----AQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLaalglplpasaeefaalrae 388
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569000235  619 ----LSQEEQTSKILMQYQARLEQSEKRLRQQQVEKDSQIKS-------IIGRLMLVEEELRRDHPAMAEPLP 680
Cdd:COG4913   389 aaalLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASlerrksnIPARLLALRDALAEALGLDEAELP 461
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
569-692 5.68e-03

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 37.59  E-value: 5.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  569 EREEYKLKEYsksmdesrLDRVKEYEEEI----------HSLKERLHMSNRKLEEyERRLLSQEEQTSKILMQ---YQAR 635
Cdd:pfam20492   2 EEAEREKQEL--------EERLKQYEEETkkaqeeleesEETAEELEEERRQAEE-EAERLEQKRQEAEEEKErleESAE 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 569000235  636 LEQSEK-RLRQQQVEKDSQIKsiigrlMLVEEELRRDhpAMAEPLpepKKRLLDAQVE 692
Cdd:pfam20492  73 MEAEEKeQLEAELAEAQEEIA------RLEEEVERKE--EEARRL---QEELEEAREE 119
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
591-670 5.95e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 40.32  E-value: 5.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235  591 KEYEEEIHSLKERLHMSNRKLEEYERRLLSQE------EQTSKILMQYQARLEQSEKRLRQQQVEKDSQIK--------S 656
Cdd:PRK11448  145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQqelvalEGLAAELEEKQQELEAQLEQLQEKAAETSQERKqkrkeitdQ 224
                          90
                  ....*....|....
gi 569000235  657 IIGRLMLVEEELRR 670
Cdd:PRK11448  225 AAKRLELSEEETRI 238
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
568-661 7.51e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 7.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235 568 IEREEYKLKEYSKSMDESRlDRVKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKIlmqyQARLEQSEKRLRQQQ 647
Cdd:COG4942   22 AAEAEAELEQLQQEIAELE-KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL----EAELAELEKEIAELR 96
                         90
                 ....*....|....
gi 569000235 648 VEKDSQIKSIIGRL 661
Cdd:COG4942   97 AELEAQKEELAELL 110
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
549-704 9.16e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.61  E-value: 9.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235 549 TVAWVSNMPHLSADIESAHIEreeyklkEYSKSMDESRLDRVKE----YEEEIHSLKERLHMSNRKLEEYERR--LLSQE 622
Cdd:COG3206  139 EISYTSPDPELAAAVANALAE-------AYLEQNLELRREEARKalefLEEQLPELRKELEEAEAALEEFRQKngLVDLS 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000235 623 EQTSkilmQYQARLEQsekrLRQQQVEKDSQIKSIIGRLMLVEEELRRDHPAMAEPLPEP-----KKRLLDAQVEIT-MS 696
Cdd:COG3206  212 EEAK----LLLQQLSE----LESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPviqqlRAQLAELEAELAeLS 283

                 ....*...
gi 569000235 697 FIFSVSHP 704
Cdd:COG3206  284 ARYTPNHP 291
 
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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