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Conserved domains on  [gi|1137509602|ref|XP_019905956|]
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ras/Rap GTPase-activating protein SynGAP isoform X3 [Esox lucius]

Protein Classification

ras GTPase-activating protein( domain architecture ID 11686121)

ras GTPase-activating protein containing a DUF3498 domain, similar to Danio rerio synaptic Ras GTPase activating protein 1b

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
 342-665 0e+00

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: 622.30  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  342 RYQTMSILPMELYKEFAEYITNNYRTLCAVLEPLLSVKSKEEVAYALVHILQSTGKAKDFLSDMAMCEVDRFmDREHLIF 421
Cdd:cd05136      1 RYQSVDILPLEVYKEFLEYLTNNYLDLCEVLEPVLSVKAKEELATALVHILQSTGKAKEFLTDLVMAEVDRL-DDEHLIF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  422 RENTLATKAIEEYLKLIGHRYLKDAIGEFIRALYESEENCEVDPMRTPPS-VLADHQANLRMCCELALCKIVNSHCVFPR 500
Cdd:cd05136     80 RGNTLATKAMEAYLKLVGQKYLQETLGEFIRALYESEEDCEVDPSKCPPSaSLSRNQANLRRSVELAWCKILSSHCVFPR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  501 ELKDVFASWRVRCAERGREDIADRLISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLASFSKFSGKE 580
Cdd:cd05136    160 ELREVFSSWRERLEERGREDIADRLISASLFLRFLCPAILSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  581 DHMCFMNEFLEMEWGSMQQFLYEISNMDTGSNVGGFEGYIDLGRELSMLHSLLWEVMAQLSKDAILKLGPLPRLLNDISV 660
Cdd:cd05136    240 EYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITE 319


                   ....*
gi 1137509602  661 ALRNP 665
Cdd:cd05136    320 ALRNP 324
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 72-263 5.38e-126

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


The actual alignment was detected with superfamily member cd13375:

Pssm-ID: 473070  Cd Length: 189  Bit Score: 387.90  E-value: 5.38e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602   72 PIAPPQTfrQQSFLSRRLKGSIKRAKSQPKLDRTSSFrHMILPRFRSADQERTRLMQSFKESHSHESLLSPSSAAEALDL 151
Cdd:cd13375      1 PTAPFRP--SQGFLSRRLKSSIKRTKSQPKLDRTSSF-RQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALDL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  152 TLDEDAVIKPVHSSILGQEYCFEVTTLSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARDLPAKK 231
Cdd:cd13375     78 NLDEDSIIKPVHSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKK 157

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1137509602  232 RYYCELCLDDMLYARTTSKPRTDTVFWGEHFE 263
Cdd:cd13375    158 RYYCELCLDDMLYARTTSKPRTDTVFWGEHFE 189
DUF3498 super family cl26404
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
 655-1308 1.13e-105

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: 345.59  E-value: 1.13e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  655 LNDISVALRNPQLHRQashQPDRQQDRLLTRPAFNRLVSSDFQSlMMRDLNSS-IDISRLPSPTsgvsgggvhsshvnmg 733
Cdd:pfam12004    1 LRDITTALTNPTPIQQ---QLRRFSEHSSSPPVPGRSISSGLQK-MFEDPDDGlSDFTRLPSPT---------------- 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  734 sfpdrdpRGSKDIFYVTRPPLARSSPAYCTSSSDITEPDPKVLSVNKSVSMMDLQDSRVNSIS-NLHSVGDMLNSSQASI 812
Cdd:pfam12004   61 -------PENKDLFFVTRPPLLQPSPARSSSYSDANEPDQQLPNGNKSLSMVDLQDSRSLQGSpSPPLHDAPLNLSQAGS 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  813 -AGLGhsfgnLGGPARVGGHLSAGSSGGSGLRLSQMggPIYHMGGPTDSLSqqqqqvaaamhfPLSFQNPLFHLAADGP- 890
Cdd:pfam12004  134 qASVG-----LRPAWAARTSQGNPQSAPQVRRPLQT--PVTQGTRPQQLLA------------PLSFQNPVYHMAAGLPv 194

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  891 --RGQPHGHSQGQPPPLllapepenahhqqgyarafgHGGFSRSEDLSAlrpqSSLVQPSIVHSHSYSDDYTRQNqnAEY 968
Cdd:pfam12004  195 spRGLGSPDSSSETHSS--------------------FSSHSNSEDLSS----AAANKKSGPSNSSYSEDFARRS--TEF 248

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  969 ARRQLSLQvqeNLQQQILMglTPQTATGTGTPTSVATPPstvhpvrhgsvaPPPPQRLKSQLSISpgatSTPPKARPQSR 1048
Cdd:pfam12004  249 TRRQLSLT---ELQHQPAV--PRQNSAGPQRRIDQQGLG------------GPPLTRGRTPPSLL----NSASYPRPSSG 307

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602 1049 NLllQSPESSFGG---RQNSpqqqqqqqhqlSVKQSDSPApglphqsssardsqgapqggngettdtptkstkqpqqqsq 1125
Cdd:pfam12004  308 SL--MSSSPDWPParlRQQS-----------SSSKGDSPE---------------------------------------- 334

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602 1126 qqpppqqhlLKPTVNKQGSQSP---ATLTPTpnERTVAWVSNMPHLSADIEiLRSSSNLEDLKLKEysksmdesrmdrvk 1202
Cdd:pfam12004  335 ---------TKQRTQHQQVPSPvnpSTLSPV--ERTAAWVLNMNGQYEEEE-SSGPESREELKQAE-------------- 388

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602 1203 EYEEEIHSLKERLIMSHRKLEEYERRMLSQEQQTSKILSQYQSRLDDSERRLRQQQVEKDSQIKGIINRLMAVEDELR-- 1280
Cdd:pfam12004  389 KYEQEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMAVEEELKkd 468

                          650       660       670
                   ....*....|....*....|....*....|.
gi 1137509602 1281 ---VSAIPEIKPRMFREQEEDSSSLGSADPQ 1308
Cdd:pfam12004  469 haeMQAVIDSKQKIIDAQEKRIASLDAANAR 499
C2_SynGAP_like cd04013
C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and ...
 205-351 1.32e-84

C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and neurofibromin are all members of the Ras-specific GAP (GTPase-activating protein) family. SynGAP regulates the MAP kinase signaling pathway and is critical for cognition and synapse function. Mutations in this gene causes mental retardation in humans. SynGAP contains a PH-like domain, a C2 domain, and a Ras-GAP domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


:

Pssm-ID: 175980 [Multi-domain]  Cd Length: 146  Bit Score: 272.26  E-value: 1.32e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  205 PNKDNSRRVDNVLKLWIIEARDLPAKKRYYCELCLDDMLYARTTSKPRTDTVFWGEHFEFNNLPAIRSLRLHLYKETDKK 284
Cdd:cd04013      1 PNRDNSRRTENSLKLWIIEAKGLPPKKRYYCELCLDKTLYARTTSKLKTDTLFWGEHFEFSNLPPVSVITVNLYRESDKK 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1137509602  285 RRKEKSTYLGLVSIPISSITGRQFVEQWYPVIQPSALAKGGSVGsGKVINASIRLKSRYQTMSILPM 351
Cdd:cd04013     81 KKKDKSQLIGTVNIPVTDVSSRQFVEKWYPVSTPKGNGKSGGKE-GKGESPSIRIKARYQSTRVLPL 146
 
Name Accession Description Interval E-value
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
 342-665 0e+00

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: 622.30  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  342 RYQTMSILPMELYKEFAEYITNNYRTLCAVLEPLLSVKSKEEVAYALVHILQSTGKAKDFLSDMAMCEVDRFmDREHLIF 421
Cdd:cd05136      1 RYQSVDILPLEVYKEFLEYLTNNYLDLCEVLEPVLSVKAKEELATALVHILQSTGKAKEFLTDLVMAEVDRL-DDEHLIF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  422 RENTLATKAIEEYLKLIGHRYLKDAIGEFIRALYESEENCEVDPMRTPPS-VLADHQANLRMCCELALCKIVNSHCVFPR 500
Cdd:cd05136     80 RGNTLATKAMEAYLKLVGQKYLQETLGEFIRALYESEEDCEVDPSKCPPSaSLSRNQANLRRSVELAWCKILSSHCVFPR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  501 ELKDVFASWRVRCAERGREDIADRLISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLASFSKFSGKE 580
Cdd:cd05136    160 ELREVFSSWRERLEERGREDIADRLISASLFLRFLCPAILSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  581 DHMCFMNEFLEMEWGSMQQFLYEISNMDTGSNVGGFEGYIDLGRELSMLHSLLWEVMAQLSKDAILKLGPLPRLLNDISV 660
Cdd:cd05136    240 EYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITE 319


                   ....*
gi 1137509602  661 ALRNP 665
Cdd:cd05136    320 ALRNP 324
PH_SynGAP cd13375
Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain; SynGAP is a member of ...
 72-263 5.38e-126

Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain; SynGAP is a member of the RasSynGAP family along with DOC-2/DAB2-interacting protein (DAB2IP) and neuronal growth-associated protein (nGAP/RASAL2). SynGAP, a neuronal Ras-GAP, has been shown display both Ras-GAP activity and Ras-related protein (Rap)-GAP activity. Saccharomyces cerevisiae Bud2 and GAP1 members CAPRI (Ca2+-promoted Ras inactivator) and RASAL (Ras-GTPase-activating-like protein) also possess this dual activity. Human DOC-2/DAB2-interacting protein (DAB2IP) is encoded by a tumor suppressor gene and a newly recognized member of the Ras-GTPase-activating family. Members here include mammals, amphibians, and bony fish. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270178  Cd Length: 189  Bit Score: 387.90  E-value: 5.38e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602   72 PIAPPQTfrQQSFLSRRLKGSIKRAKSQPKLDRTSSFrHMILPRFRSADQERTRLMQSFKESHSHESLLSPSSAAEALDL 151
Cdd:cd13375      1 PTAPFRP--SQGFLSRRLKSSIKRTKSQPKLDRTSSF-RQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALDL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  152 TLDEDAVIKPVHSSILGQEYCFEVTTLSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARDLPAKK 231
Cdd:cd13375     78 NLDEDSIIKPVHSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKK 157

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1137509602  232 RYYCELCLDDMLYARTTSKPRTDTVFWGEHFE 263
Cdd:cd13375    158 RYYCELCLDDMLYARTTSKPRTDTVFWGEHFE 189
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
 655-1308 1.13e-105

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: 345.59  E-value: 1.13e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  655 LNDISVALRNPQLHRQashQPDRQQDRLLTRPAFNRLVSSDFQSlMMRDLNSS-IDISRLPSPTsgvsgggvhsshvnmg 733
Cdd:pfam12004    1 LRDITTALTNPTPIQQ---QLRRFSEHSSSPPVPGRSISSGLQK-MFEDPDDGlSDFTRLPSPT---------------- 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  734 sfpdrdpRGSKDIFYVTRPPLARSSPAYCTSSSDITEPDPKVLSVNKSVSMMDLQDSRVNSIS-NLHSVGDMLNSSQASI 812
Cdd:pfam12004   61 -------PENKDLFFVTRPPLLQPSPARSSSYSDANEPDQQLPNGNKSLSMVDLQDSRSLQGSpSPPLHDAPLNLSQAGS 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  813 -AGLGhsfgnLGGPARVGGHLSAGSSGGSGLRLSQMggPIYHMGGPTDSLSqqqqqvaaamhfPLSFQNPLFHLAADGP- 890
Cdd:pfam12004  134 qASVG-----LRPAWAARTSQGNPQSAPQVRRPLQT--PVTQGTRPQQLLA------------PLSFQNPVYHMAAGLPv 194

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  891 --RGQPHGHSQGQPPPLllapepenahhqqgyarafgHGGFSRSEDLSAlrpqSSLVQPSIVHSHSYSDDYTRQNqnAEY 968
Cdd:pfam12004  195 spRGLGSPDSSSETHSS--------------------FSSHSNSEDLSS----AAANKKSGPSNSSYSEDFARRS--TEF 248

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  969 ARRQLSLQvqeNLQQQILMglTPQTATGTGTPTSVATPPstvhpvrhgsvaPPPPQRLKSQLSISpgatSTPPKARPQSR 1048
Cdd:pfam12004  249 TRRQLSLT---ELQHQPAV--PRQNSAGPQRRIDQQGLG------------GPPLTRGRTPPSLL----NSASYPRPSSG 307

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602 1049 NLllQSPESSFGG---RQNSpqqqqqqqhqlSVKQSDSPApglphqsssardsqgapqggngettdtptkstkqpqqqsq 1125
Cdd:pfam12004  308 SL--MSSSPDWPParlRQQS-----------SSSKGDSPE---------------------------------------- 334

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602 1126 qqpppqqhlLKPTVNKQGSQSP---ATLTPTpnERTVAWVSNMPHLSADIEiLRSSSNLEDLKLKEysksmdesrmdrvk 1202
Cdd:pfam12004  335 ---------TKQRTQHQQVPSPvnpSTLSPV--ERTAAWVLNMNGQYEEEE-SSGPESREELKQAE-------------- 388

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602 1203 EYEEEIHSLKERLIMSHRKLEEYERRMLSQEQQTSKILSQYQSRLDDSERRLRQQQVEKDSQIKGIINRLMAVEDELR-- 1280
Cdd:pfam12004  389 KYEQEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMAVEEELKkd 468

                          650       660       670
                   ....*....|....*....|....*....|.
gi 1137509602 1281 ---VSAIPEIKPRMFREQEEDSSSLGSADPQ 1308
Cdd:pfam12004  469 haeMQAVIDSKQKIIDAQEKRIASLDAANAR 499
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
 333-657 2.73e-105

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: 338.13  E-value: 2.73e-105
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602   333 INASIRLKSRYQTMSILPMELYKEFAEYITNNYRT-LCAVLEPLLSVKSKEEVAYALVHILQSTGKAKDFLSDMAMCEVD 411
Cdd:smart00323    5 DLGSLRLKTVYTTDFILPSEYYEELLELLLFSLDLsLASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRALIDPEVE 84

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602   412 RfMDREHLIFRENTLATKAIEEYLKLIGHRYLKDAIGEFIRALYESEENCEVDPMRTPPSVLADHQANLRMCCELALCKI 491
Cdd:smart00323   85 R-TDDPNTIFRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEGEDLETNLENLLQYVERLFDAI 163

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602   492 VNSHCVFPRELKDVFASWRVRCAERGRE-DIADRLISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNL 570
Cdd:smart00323  164 INSSDRLPYGLRDICKQLRQAAEKRFPDaDVIYKAVSSFVFLRFFCPAIVSPKLFNLVDEHPDPTTRRTLTLIAKVLQNL 243

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602   571 ASFSKFSGKEDHMCFMNEFLEMEWGSMQQFLYEISNMDTGSNVGGFEGYIDLGRELSMLHSLLWEVMAQLsKDAILKLGP 650
Cdd:smart00323  244 ANLSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEILVDKVSDSTTISGRELSLLHSLLLENGDAL-KRELNNEDP 322


                    ....*..
gi 1137509602   651 LPRLLND 657
Cdd:smart00323  323 LGKLLFK 329
C2_SynGAP_like cd04013
C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and ...
 205-351 1.32e-84

C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and neurofibromin are all members of the Ras-specific GAP (GTPase-activating protein) family. SynGAP regulates the MAP kinase signaling pathway and is critical for cognition and synapse function. Mutations in this gene causes mental retardation in humans. SynGAP contains a PH-like domain, a C2 domain, and a Ras-GAP domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175980 [Multi-domain]  Cd Length: 146  Bit Score: 272.26  E-value: 1.32e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  205 PNKDNSRRVDNVLKLWIIEARDLPAKKRYYCELCLDDMLYARTTSKPRTDTVFWGEHFEFNNLPAIRSLRLHLYKETDKK 284
Cdd:cd04013      1 PNRDNSRRTENSLKLWIIEAKGLPPKKRYYCELCLDKTLYARTTSKLKTDTLFWGEHFEFSNLPPVSVITVNLYRESDKK 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1137509602  285 RRKEKSTYLGLVSIPISSITGRQFVEQWYPVIQPSALAKGGSVGsGKVINASIRLKSRYQTMSILPM 351
Cdd:cd04013     81 KKKDKSQLIGTVNIPVTDVSSRQFVEKWYPVSTPKGNGKSGGKE-GKGESPSIRIKARYQSTRVLPL 146
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
 401-572 4.65e-29

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: 115.85  E-value: 4.65e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  401 FLSDMAMCEVDRFMDREHLiFRENTLATKAIEEYLKL-IGHRYLKDAIGEFIRALYESEE-NCEVDPMR----------- 467
Cdd:pfam00616    1 LISELIEEEIESSDNPNDL-LRGNSLVSKLLETYNRRpRGQEYLKKVLGPLVRKIIEDEDlDLESDPRKiyeslinqeel 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  468 --------------------TPPSVLADHQANLRMCCELALCKIVNSHCVFPREL----KDVFASWRVRCAERGREDIAd 523
Cdd:pfam00616   80 ktgrsdlprdvspeeaiedpEVRQIFEDNLQKLRELADEFLDAIYSSLNQLPYGIryicKQLYELLEEKFPDASEEEIL- 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1137509602  524 RLISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLAS 572
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVDHQISPKQRRNLTLIAKVLQNLAN 207
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 216-312 7.95e-11

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 60.19  E-value: 7.95e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602   216 VLKLWIIEARDLPAKKRY-----YCELCLDDMLY--ARTTSKPRTDTVFWGEHFEFN-NLPAIRSLRLHLYketDKKRRK 287
Cdd:smart00239    1 TLTVKIISARNLPPKDKGgksdpYVKVSLDGDPKekKKTKVVKNTLNPVWNETFEFEvPPPELAELEIEVY---DKDRFG 77

                            90       100
                    ....*....|....*....|....*
gi 1137509602   288 eKSTYLGLVSIPISSITGRQFVEQW 312
Cdd:smart00239   78 -RDDFIGQVTIPLSDLLLGGRHEKL 101
C2 pfam00168
C2 domain;
215-315 1.74e-09

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 56.56  E-value: 1.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  215 NVLKLWIIEARDLPAKKRY-----YCELCL-DDMLYARTTSKPRTDTVFWGEHFEFN-NLPAIRSLRLHLYketDKkRRK 287
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGNgtsdpYVKVYLlDGKQKKKTKVVKNTLNPVWNETFTFSvPDPENAVLEIEVY---DY-DRF 76

                           90       100
                   ....*....|....*....|....*...
gi 1137509602  288 EKSTYLGLVSIPISSITGRQFVEQWYPV 315
Cdd:pfam00168   77 GRDDFIGEVRIPLSELDSGEGLDGWYPL 104
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 82-204 5.05e-05

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 43.69  E-value: 5.05e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602    82 QSFLSRRLKGSIKRAKSqpkldrtssfRHMILprfrsadqeRTRLMQSFKESHSHESllspSSAAEALDLtlDEDAVIKP 161
Cdd:smart00233    4 EGWLYKKSGGGKKSWKK----------RYFVL---------FNSTLLYYKSKKDKKS----YKPKGSIDL--SGCTVREA 58

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 1137509602   162 VHSSILGQEYCFEVTTLSG-TKCFACRSAAERDKWIENLQRAVK 204
Cdd:smart00233   59 PDPDSSKKPHCFEIKTSDRkTLLLQAESEEEREKWVEALRKAIA 102
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1185-1283 1.22e-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: 46.60  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602 1185 KLKEYSKSMDESRMDRVKEYEEEIHSLKERLIMSHRKLEEYERRMLSQEQQTSKI---LSQYQSRLDDSERRLRQQQVEK 1261
Cdd:TIGR02169  273 LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLeaeIDKLLAEIEELEREIEEERKRR 352

                           90       100
                   ....*....|....*....|..
gi 1137509602 1262 DsQIKGIINRLMAVEDELRVSA 1283
Cdd:TIGR02169  353 D-KLTEEYAELKEELEDLRAEL 373
PHA03247 PHA03247
large tegument protein UL36; Provisional
 993-1183 1.84e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  993 TATGTGTPTSVATPPSTVHPVRHGSVAPPPPQRLKSQLSISPG----------------ATSTPPKAR-------PQSRN 1049
Cdd:PHA03247  2817 ALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGgdvrrrppsrspaakpAAPARPPVRrlarpavSRSTE 2896

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602 1050 LLLQSPESSFGGRQNSPQQQQQQQHQLSVKQSDSPAPGLPHQSSSARDSQGAPQGGNGETTDTPTKSTKQPQQQSQQQPP 1129
Cdd:PHA03247  2897 SFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPR 2976

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1137509602 1130 PQQHLLKPTVNKQGSqSPATLTPTPNERTVAWVSNMP-HLSAD------IEILRSSSNLED 1183
Cdd:PHA03247  2977 FRVPQPAPSREAPAS-STPPLTGHSLSRVSSWASSLAlHEETDpppvslKQTLWPPDDTED 3036
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1195-1299 7.16e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 7.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602 1195 ESRMDRVKEYEEEIHSLKERLIMSHRKLEEYERRMLSQEQQTSKILSQYQSRLDDSERRLRQQQVEKDSQIKGIINRLMA 1274
Cdd:COG4717    145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224

                           90       100
                   ....*....|....*....|....*
gi 1137509602 1275 VEDELRvsaipEIKPRMFREQEEDS 1299
Cdd:COG4717    225 LEEELE-----QLENELEAAALEER 244
 
Name Accession Description Interval E-value
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
 342-665 0e+00

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: 622.30  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  342 RYQTMSILPMELYKEFAEYITNNYRTLCAVLEPLLSVKSKEEVAYALVHILQSTGKAKDFLSDMAMCEVDRFmDREHLIF 421
Cdd:cd05136      1 RYQSVDILPLEVYKEFLEYLTNNYLDLCEVLEPVLSVKAKEELATALVHILQSTGKAKEFLTDLVMAEVDRL-DDEHLIF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  422 RENTLATKAIEEYLKLIGHRYLKDAIGEFIRALYESEENCEVDPMRTPPS-VLADHQANLRMCCELALCKIVNSHCVFPR 500
Cdd:cd05136     80 RGNTLATKAMEAYLKLVGQKYLQETLGEFIRALYESEEDCEVDPSKCPPSaSLSRNQANLRRSVELAWCKILSSHCVFPR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  501 ELKDVFASWRVRCAERGREDIADRLISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLASFSKFSGKE 580
Cdd:cd05136    160 ELREVFSSWRERLEERGREDIADRLISASLFLRFLCPAILSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  581 DHMCFMNEFLEMEWGSMQQFLYEISNMDTGSNVGGFEGYIDLGRELSMLHSLLWEVMAQLSKDAILKLGPLPRLLNDISV 660
Cdd:cd05136    240 EYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITE 319


                   ....*
gi 1137509602  661 ALRNP 665
Cdd:cd05136    320 ALRNP 324
PH_SynGAP cd13375
Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain; SynGAP is a member of ...
 72-263 5.38e-126

Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain; SynGAP is a member of the RasSynGAP family along with DOC-2/DAB2-interacting protein (DAB2IP) and neuronal growth-associated protein (nGAP/RASAL2). SynGAP, a neuronal Ras-GAP, has been shown display both Ras-GAP activity and Ras-related protein (Rap)-GAP activity. Saccharomyces cerevisiae Bud2 and GAP1 members CAPRI (Ca2+-promoted Ras inactivator) and RASAL (Ras-GTPase-activating-like protein) also possess this dual activity. Human DOC-2/DAB2-interacting protein (DAB2IP) is encoded by a tumor suppressor gene and a newly recognized member of the Ras-GTPase-activating family. Members here include mammals, amphibians, and bony fish. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270178  Cd Length: 189  Bit Score: 387.90  E-value: 5.38e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602   72 PIAPPQTfrQQSFLSRRLKGSIKRAKSQPKLDRTSSFrHMILPRFRSADQERTRLMQSFKESHSHESLLSPSSAAEALDL 151
Cdd:cd13375      1 PTAPFRP--SQGFLSRRLKSSIKRTKSQPKLDRTSSF-RQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALDL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  152 TLDEDAVIKPVHSSILGQEYCFEVTTLSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARDLPAKK 231
Cdd:cd13375     78 NLDEDSIIKPVHSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKK 157

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1137509602  232 RYYCELCLDDMLYARTTSKPRTDTVFWGEHFE 263
Cdd:cd13375    158 RYYCELCLDDMLYARTTSKPRTDTVFWGEHFE 189
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
 655-1308 1.13e-105

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: 345.59  E-value: 1.13e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  655 LNDISVALRNPQLHRQashQPDRQQDRLLTRPAFNRLVSSDFQSlMMRDLNSS-IDISRLPSPTsgvsgggvhsshvnmg 733
Cdd:pfam12004    1 LRDITTALTNPTPIQQ---QLRRFSEHSSSPPVPGRSISSGLQK-MFEDPDDGlSDFTRLPSPT---------------- 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  734 sfpdrdpRGSKDIFYVTRPPLARSSPAYCTSSSDITEPDPKVLSVNKSVSMMDLQDSRVNSIS-NLHSVGDMLNSSQASI 812
Cdd:pfam12004   61 -------PENKDLFFVTRPPLLQPSPARSSSYSDANEPDQQLPNGNKSLSMVDLQDSRSLQGSpSPPLHDAPLNLSQAGS 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  813 -AGLGhsfgnLGGPARVGGHLSAGSSGGSGLRLSQMggPIYHMGGPTDSLSqqqqqvaaamhfPLSFQNPLFHLAADGP- 890
Cdd:pfam12004  134 qASVG-----LRPAWAARTSQGNPQSAPQVRRPLQT--PVTQGTRPQQLLA------------PLSFQNPVYHMAAGLPv 194

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  891 --RGQPHGHSQGQPPPLllapepenahhqqgyarafgHGGFSRSEDLSAlrpqSSLVQPSIVHSHSYSDDYTRQNqnAEY 968
Cdd:pfam12004  195 spRGLGSPDSSSETHSS--------------------FSSHSNSEDLSS----AAANKKSGPSNSSYSEDFARRS--TEF 248

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  969 ARRQLSLQvqeNLQQQILMglTPQTATGTGTPTSVATPPstvhpvrhgsvaPPPPQRLKSQLSISpgatSTPPKARPQSR 1048
Cdd:pfam12004  249 TRRQLSLT---ELQHQPAV--PRQNSAGPQRRIDQQGLG------------GPPLTRGRTPPSLL----NSASYPRPSSG 307

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602 1049 NLllQSPESSFGG---RQNSpqqqqqqqhqlSVKQSDSPApglphqsssardsqgapqggngettdtptkstkqpqqqsq 1125
Cdd:pfam12004  308 SL--MSSSPDWPParlRQQS-----------SSSKGDSPE---------------------------------------- 334

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602 1126 qqpppqqhlLKPTVNKQGSQSP---ATLTPTpnERTVAWVSNMPHLSADIEiLRSSSNLEDLKLKEysksmdesrmdrvk 1202
Cdd:pfam12004  335 ---------TKQRTQHQQVPSPvnpSTLSPV--ERTAAWVLNMNGQYEEEE-SSGPESREELKQAE-------------- 388

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602 1203 EYEEEIHSLKERLIMSHRKLEEYERRMLSQEQQTSKILSQYQSRLDDSERRLRQQQVEKDSQIKGIINRLMAVEDELR-- 1280
Cdd:pfam12004  389 KYEQEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMAVEEELKkd 468

                          650       660       670
                   ....*....|....*....|....*....|.
gi 1137509602 1281 ---VSAIPEIKPRMFREQEEDSSSLGSADPQ 1308
Cdd:pfam12004  469 haeMQAVIDSKQKIIDAQEKRIASLDAANAR 499
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
 333-657 2.73e-105

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: 338.13  E-value: 2.73e-105
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602   333 INASIRLKSRYQTMSILPMELYKEFAEYITNNYRT-LCAVLEPLLSVKSKEEVAYALVHILQSTGKAKDFLSDMAMCEVD 411
Cdd:smart00323    5 DLGSLRLKTVYTTDFILPSEYYEELLELLLFSLDLsLASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRALIDPEVE 84

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602   412 RfMDREHLIFRENTLATKAIEEYLKLIGHRYLKDAIGEFIRALYESEENCEVDPMRTPPSVLADHQANLRMCCELALCKI 491
Cdd:smart00323   85 R-TDDPNTIFRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEGEDLETNLENLLQYVERLFDAI 163

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602   492 VNSHCVFPRELKDVFASWRVRCAERGRE-DIADRLISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNL 570
Cdd:smart00323  164 INSSDRLPYGLRDICKQLRQAAEKRFPDaDVIYKAVSSFVFLRFFCPAIVSPKLFNLVDEHPDPTTRRTLTLIAKVLQNL 243

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602   571 ASFSKFSGKEDHMCFMNEFLEMEWGSMQQFLYEISNMDTGSNVGGFEGYIDLGRELSMLHSLLWEVMAQLsKDAILKLGP 650
Cdd:smart00323  244 ANLSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEILVDKVSDSTTISGRELSLLHSLLLENGDAL-KRELNNEDP 322


                    ....*..
gi 1137509602   651 LPRLLND 657
Cdd:smart00323  323 LGKLLFK 329
PH_DAB2IP cd13376
DOC-2/Disabled homolog 2-interacting protein Pleckstrin homology (PH) domain; DAB2IP (also ...
 84-263 9.60e-91

DOC-2/Disabled homolog 2-interacting protein Pleckstrin homology (PH) domain; DAB2IP (also called AIP1/ASK1-interacting protein-1 and DIP1/2) is a member of the RasSynGAP family along with Synaptic Ras-GTPase activating protein (SynGAP) and neuronal growth-associated protein (nGAP/RASAL2). DAB2IP is a critical component of many signal transduction pathways mediated by Ras and tumor necrosis factors including apoptosis pathways, and it is involved in the formation of many types of tumors. DAB2IP participates in regulation of gene expression and pluripotency of cells. Human DAB2IP is expressed in the adrenal gland, pancreas, endocardium, stomach, kidney, testis, small intestine, liver, trachea, skin, ovary, endometrium, lung, esophagus and bladder. No expression was observed in the cerebrum, parotid gland, thymus, thyroid gland and spleen. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270179  Cd Length: 182  Bit Score: 291.22  E-value: 9.60e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602   84 FLSRRLKGSIKRAKSQPKLDRTSSFRHmILPRFRSADQERTRLMQSFKESHSHESLLSPSSAAEALDLTLDEDAVIKPVH 163
Cdd:cd13376      4 FLSRRLKGSIKRTKSQPKLDRNSSFRH-ILPGFRSVDNERSHLMPRLKESRSHESLLSPSSAVEALDLSMEEEVVIKPVH 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  164 SSILGQEYCFEVTTLSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARDLPAKKRYYCELCLDDML 243
Cdd:cd13376     83 SSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRVENMLKLWIIEAKDLPAKKKYLCELCLDDVL 162

                          170       180
                   ....*....|....*....|
gi 1137509602  244 YARTTSKPRTDTVFWGEHFE 263
Cdd:cd13376    163 YARTTCKLKTDNVFWGEHFE 182
C2_SynGAP_like cd04013
C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and ...
 205-351 1.32e-84

C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and neurofibromin are all members of the Ras-specific GAP (GTPase-activating protein) family. SynGAP regulates the MAP kinase signaling pathway and is critical for cognition and synapse function. Mutations in this gene causes mental retardation in humans. SynGAP contains a PH-like domain, a C2 domain, and a Ras-GAP domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175980 [Multi-domain]  Cd Length: 146  Bit Score: 272.26  E-value: 1.32e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  205 PNKDNSRRVDNVLKLWIIEARDLPAKKRYYCELCLDDMLYARTTSKPRTDTVFWGEHFEFNNLPAIRSLRLHLYKETDKK 284
Cdd:cd04013      1 PNRDNSRRTENSLKLWIIEAKGLPPKKRYYCELCLDKTLYARTTSKLKTDTLFWGEHFEFSNLPPVSVITVNLYRESDKK 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1137509602  285 RRKEKSTYLGLVSIPISSITGRQFVEQWYPVIQPSALAKGGSVGsGKVINASIRLKSRYQTMSILPM 351
Cdd:cd04013     81 KKKDKSQLIGTVNIPVTDVSSRQFVEKWYPVSTPKGNGKSGGKE-GKGESPSIRIKARYQSTRVLPL 146
RasGAP cd04519
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...
 352-606 7.84e-74

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: 246.25  E-value: 7.84e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  352 ELYKEFAEYITNNYRTLCAVLEPLLSVKSKEEVAYALVHILQSTGKAKDFLSDMAMCEVDRFMDrEHLIFRENTLATKAI 431
Cdd:cd04519      1 EEYRLLSLLLTESPLALLRELSQVLPVKDKEEVATALLRIFESRGLALEFLRYLVRSEVKNTKN-PNTLFRGNSLATKLL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  432 EEYLKLIGHRYLKDAIGEFIRALYESEENCEVDPMRTPPSVLADHQANLRMCCELALCKIVNSHCVFPRELKDVFASWRV 511
Cdd:cd04519     80 DQYMKLVGQEYLKETLSPLIREILESKESCEIDTKLPVGEDLEENLENLLELVNKLVDRILSSLDRLPPELRYVFKILRE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  512 RCAERGRED--IADRLISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLASFSKFSGKEDHMCFMNEF 589
Cdd:cd04519    160 FLAERFPEEpdEAYQAVSGFLFLRFICPAIVSPELFGLVPDEPSEQARRNLTLISKVLQSLANGVEFGDKEPFMKPLNDF 239

                          250
                   ....*....|....*..
gi 1137509602  590 LEMEWGSMQQFLYEISN 606
Cdd:cd04519    240 IKSNKPKLKQFLDELSS 256
PH_RasSynGAP-like cd13262
Synaptic Ras-GTPase activating protein family Pleckstrin homology (PH) domain; The RasSynGAP ...
 84-213 5.15e-52

Synaptic Ras-GTPase activating protein family Pleckstrin homology (PH) domain; The RasSynGAP family is composed of members: DAB2IP, nGAP, and SynGAP. Neuronal growth-associated proteins (nGAPs) are growth cone markers found in multiple types of neurons. There are many nGAPs including Cap1 (Adenylate cyclase-associated protein 1), Capzb (Capping protein (actin filament) muscle Z-line, beta), Clptm1 (Cleft lip and palate associated transmembrane protein 1), Cotl1 (Coactosin-like 1), Crmp1 (Collapsin response mediator protein 1), Cyfip1 (Cytoplasmic FMR1 interacting protein 1), Fabp7 (Fatty acid binding protein 7, brain), Farp2 (FERM, RhoGEF and pleckstrin domain protein 2), Gap43 (Growth associated protein 43), Gnao1 (Guanine nucleotide binding protein (G protein), alpha activating activity polypeptide O), Gnai2 (Guanine nucleotide binding protein (G protein), alpha inhibiting 2), Pacs1 (Phosphofurin acidic cluster sorting protein 1), Rtn1 (Reticulon 1), Sept2 (Septin 2), Snap25 (Synaptosomal-associated protein 25), Strap (Serine/threonine kinase receptor associated protein), Stx7 (Syntaxin 7), and Tmod2 (Tropomodulin 2). SynGAP, a neuronal Ras-GAP, has been shown display both Ras-GAP activity and Ras-related protein (Rap)-GAP activity. Saccharomyces cerevisiae Bud2 and GAP1 members CAPRI (Ca2+-promoted Ras inactivator) and RASAL (Ras-GTPase-activating-like protein) also possess this dual activity. Human DOC-2/DAB2-interacting protein (DAB2IP) is encoded by a tumor suppressor gene and a newly recognized member of the Ras-GTPase-activating family. DAB2IP is a critical component of many signal transduction pathways mediated by Ras and tumor necrosis factors including apoptosis pathways, and it is involved in the formation of many types of tumors. DAB2IP participates in regulation of gene expression and pluripotency of cells. It has been reported that DAB2IP was expressed in different tumor tissues. Little information is available concerning the expression levels of DAB2IP in normal tissues and cells, however, and no studies of its expression patterns during the development of human embryos have been reported. DAB2IP was expressed primarily in cell cytoplasm throughout the fetal development. The expression levels varied among tissues and different gestational ages. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270082  Cd Length: 125  Bit Score: 178.78  E-value: 5.15e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602   84 FLSRRLKGSIKRAKSQPKLDRTSSFRhmiLPRFRSADQERtrlMQSFKESHSHESLLSPSSAAEalDLTLDEDAVIKPVH 163
Cdd:cd13262      4 FFSRRLKGPLKRTKSVTKLERKSSKR---LPRTRLARAPA---GPRLRGSRSHESLLSSSSAAL--DLSADEDVVIRPLH 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1137509602  164 SSILGQEYCFEVTTLSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRV 213
Cdd:cd13262     76 SSILGRKHCFQVTTSEGTRCFSCRSAAERDRWIEDLRRAAQPNKDNCRRT 125
PH_nGAP cd13373
Neuronal growth-associated proteins Pleckstrin homology (PH) domain; nGAP (also called RASAL2 ...
 79-219 5.99e-52

Neuronal growth-associated proteins Pleckstrin homology (PH) domain; nGAP (also called RASAL2/RAS protein activator like-3) is a member of the RasSynGAP family along with DOC-2/DAB2-interacting protein (DAB2IP) and synaptic RasGAP (SynGAP). nGAPs are growth cone markers found in multiple types of neurons. There are many nGAPs including Cap1 (Adenylate cyclase-associated protein 1), Capzb (Capping protein (actin filament) muscle Z-line, beta), Clptm1 (Cleft lip and palate associated transmembrane protein 1), Cotl1 (Coactosin-like 1), Crmp1 (Collapsin response mediator protein 1), Cyfip1 (Cytoplasmic FMR1 interacting protein 1), Fabp7 (Fatty acid binding protein 7, brain), Farp2 (FERM, RhoGEF and pleckstrin domain protein 2), Gap43 (Growth associated protein 43), Gnao1 (Guanine nucleotide binding protein (G protein), alpha activating activity polypeptide O), Gnai2 (Guanine nucleotide binding protein (G protein), alpha inhibiting 2), Pacs1 (Phosphofurin acidic cluster sorting protein 1), Rtn1 (Reticulon 1), Sept2 (Septin 2), Snap25 (Synaptosomal-associated protein 25), Strap (Serine/threonine kinase receptor associated protein), Stx7 (Syntaxin 7), and Tmod2 (Tropomodulin 2). PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270176  Cd Length: 138  Bit Score: 179.15  E-value: 5.99e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602   79 FRQQSFLSRRLKGSIKRAKSQPKLDRTSSFRhmiLPRFRSADqERTRLMQSFKESHSHESLLSPSSAAEALDLTLDEDAV 158
Cdd:cd13373      2 FKVSGFFSKRLKGSIKRTKSQSKLDRNTSFR---LPSLRSAD-DRSRGLPKLKESRSHESLLSPGSAVEALDLGREEKVS 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1137509602  159 IKPVHSSILGQEYCFEVTTLSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKL 219
Cdd:cd13373     78 VKPLHSSILGQDFCFEVTYSSGSKCFSCSSAAERDKWMENLRRTVQPNKDNCRRAENVLRL 138
RasGAP_GAP1_like cd05128
Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras ...
 365-605 3.72e-51

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: 181.68  E-value: 3.72e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  365 YRTLCAVLEPLLSVkSKEEVAYALVHILQSTGKAKDFLSDMAMCEVDRFMDrEHLIFRENTLATKAIEEYLKLIGHRYLK 444
Cdd:cd05128     20 TASAVYLLEELVKV-DKDDVARPLVRIFLHHGQIVPLLRALASREISKTQD-PNTLFRGNSLASKCMDEFMKLVGMQYLH 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  445 DAIGEFIRALYESEENCEVDPMRTP-PSVLADHQANLRMCCELALCKIVNS--HCvfPRELKDVFASWRVRCAER--GRE 519
Cdd:cd05128     98 ETLKPVIDEIFSEKKSCEIDPSKLKdGEVLETNLANLRGYVERVFKAITSSarRC--PTLMCEIFSDLRESAAQRfpDNE 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  520 DIADRLISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLASF----SKFSGKEDHMC-FMNEFLEMEW 594
Cdd:cd05128    176 DVPYTAVSGFIFLRFFAPAILNPKLFGLREEHPDPQTARTLTLISKTIQTLGNLgsssSGLGVKEAYMSpLYERFTDEQH 255

                          250
                   ....*....|..
gi 1137509602  595 -GSMQQFLYEIS 605
Cdd:cd05128    256 vDAVKKFLDRIS 267
RasGAP_CLA2_BUD2 cd05137
Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein ...
 348-591 3.48e-50

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: 181.99  E-value: 3.48e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  348 ILPMELYKEFAEYITNNYRTLCAVLEPLLSVKSKEEVAYALVHILQSTGKAKDFLSDMAMCEVD-------------RFM 414
Cdd:cd05137      9 VLPSKNYKPLEELLHNFDLGLTLQIAELVPGDKLERLSEILLDIFQASGREDEWFMALVEDEIDgidkstsknkdmgKSS 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  415 DREH-LIFRENTLATKAIEEYLKLIGHRYLKDAIGEFIRALYESEENCEVDPMRTPPSV-------LADHQANLRMCCEL 486
Cdd:cd05137     89 NNEAnLLFRGNSLLTKSLEKYMRRIGKEYLEKSIGDVIRKICEENKDCEVDPSRVKESDsiekeedLEENWENLISLTEE 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  487 ALCKIVNSHCVFPRELKDVFASWRvRCAERGREDIADRL----ISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTL 562
Cdd:cd05137    169 IWNSIYITSNDCPPELRKILKHIR-AKVEDRYGDFLRTVtlnsVSGFLFLRFFCPAILNPKLFGLLKDHPRPRAQRTLTL 247

                          250       260
                   ....*....|....*....|....*....
gi 1137509602  563 IAKVVQNLASFSKFSGKEDHMCFMNEFLE 591
Cdd:cd05137    248 IAKVLQNLANLTTFGQKEPWMEPMNEFLT 276
RasGAP_Neurofibromin_like cd05392
Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins ...
 350-609 2.01e-42

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: 158.22  E-value: 2.01e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  350 PMELYKEFAEYITNNYRTLCAVLEpLLSVKSKEEVAYALVHILQSTGKAKDFLSDMAMCEVDRfMDREHLIFRENTLATK 429
Cdd:cd05392      2 KSEAYDELLELLIEDPQLLLAIAE-VCPSSEVDLLAQSLLNLFETRNRLLPLISWLIEDEISH-TSRAADLFRRNSVATR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  430 AIEEYLKLIGHRYLKDAIGEFIRALYESEENCEVDPMRTPPSVLADHQANLRMCCELALCKIVNSHCVFPRELKDVFASW 509
Cdd:cd05392     80 LLTLYAKSVGNKYLRKVLRPLLTEIVDNKDYFEVEKIKPDDENLEENADLLMKYAQMLLDSITDSVDQLPPSFRYICNTI 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  510 RvRCAERGREDIADRLISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLASFSKFSGKEDHMCFMNEF 589
Cdd:cd05392    160 Y-ESVSKKFPDAALIAVGGFLFLRFICPAIVSPESENLLDPPPTPEARRSLILIAKVLQNIANGVLFSLKEPYLESLNEF 238

                          250       260
                   ....*....|....*....|
gi 1137509602  590 LEMEWGSMQQFLYEISNMDT 609
Cdd:cd05392    239 LKKNSDRIQQFLSEVSTIPP 258
RasGAP_RASA3 cd05134
Ras-GTPase Activating Domain of RASA3; RASA3 (or GAP1_IP4BP) is a member of the GAP1 family ...
 379-606 3.70e-37

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: 141.31  E-value: 3.70e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  379 KSKEEVAYALVHILQSTGKAKDFLSDMAMCEVDRFMDrEHLIFRENTLATKAIEEYLKLIGHRYLKDAIGEFIRALYESE 458
Cdd:cd05134     33 REKQEAAIPLVRLFLHYGKIVPFISAIASAEVNRTQD-PNTIFRGNSLTSKCIDETMKLAGMHYLQVTLKPIIDEICQEH 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  459 ENCEVDPMRTPPSV-LADHQANLRMCCELALCKIVNSHCVFPRELKDVFASWRVRCAERGREDIADRL--ISSSLFLRFL 535
Cdd:cd05134    112 KPCEIDPVKLKDGEnLENNRENLRQYVDRIFRVITKSGVSCPTVMCDIFFSLRESAAKRFQVDPDVRYtaVSSFIFLRFF 191

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1137509602  536 CPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLASFSK---FSGKEDHMC-FMNEFLEMEWG-SMQQFLYEISN 606
Cdd:cd05134    192 APAILSPNLFQLTPHHPDPQTSRTLTLISKTIQTLGSLSKsksANFKESYMAaFYDYFNEQKYAdAVKNFLDLISS 267
RasGAP_RASAL cd05135
Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like ...
 367-608 1.04e-31

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: 126.08  E-value: 1.04e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  367 TLCAVLEPLLSVKSKEEVAYALVHILQSTGKAKDFLSDMAMCEVDRFMDREHLiFRENTLATKAIEEYLKLIGHRYLKDA 446
Cdd:cd05135     26 TPLAMLEEVTTGESRQDVATKLVKIFLGQGLVVPFLDYLNTREVGRTTDPNTL-FRSNSLASKSMEQFMKVVGMPYLHEV 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  447 IGEFIRALYESEENCEVDPMRTPPS---------VLADHQ------ANLRMCCELALCKIVNSHCVFPRELKDVFASWRV 511
Cdd:cd05135    105 LKPVINRIFEEKKYVELDPCKIDLNrtrrisfkgSLSEAQvresslELLQGYLGSIIDAIVGSVDQCPPVMRVAFKQLHK 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  512 RCAER----GREDIADRLISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLASFSK--FSGKEDHMCF 585
Cdd:cd05135    185 RVEERfpeaEHQDVKYLAISGFLFLRFFAPAILTPKLFQLREQHADPRTSRTLLLLAKAVQSIGNLGLqlGQGKEQWMAP 264

                          250       260
                   ....*....|....*....|...
gi 1137509602  586 MNEFLEMEWGSMQQFLYEISNMD 608
Cdd:cd05135    265 LHPFILQSVARVKDFLDRLIDID 287
RasGAP_p120GAP cd05391
Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates ...
 348-632 1.50e-31

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: 126.83  E-value: 1.50e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  348 ILPMELYKEFAEYITNnyrtlcavlEPLLSVKSKEEV--------AYALVHILQSTGKAKDFLSDMAMCEVDRfMDREHL 419
Cdd:cd05391      4 IMPEEEYSELKELILQ---------KELHVVYALAHVcgqdrtllASILLRIFRHEKLESLLLRTLNDREISM-EDEATT 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  420 IFRENTLATKAIEEYLKLIGHRYLKDAIGEFIRALYESEENCEVDPMRTPPSvlADHQANLRMCCELALC---KIVNSHC 496
Cdd:cd05391     74 LFRATTLASTLMEQYMKATATPFVHHALKDTILKILESKQSCELNPSKLEKN--EDVNTNLEHLLNILSElveKIFMAAE 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  497 VFPRELKDVFASWRVRCAERGRED--IADRLISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLASFS 574
Cdd:cd05391    152 ILPPTLRYIYGCLQKSVQQKWPTNttVRTRVVSGFVFLRLICPAILNPRMFNIISETPSPTAARTLTLVAKSLQNLANLV 231

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1137509602  575 KFSGKEDHMCFMNEFLEMEWGSMQQFLYEISNM-DTGSNVGGFEGyiDLGRELSMLHSL 632
Cdd:cd05391    232 EFGAKEPYMEGVNPFIKKNKERMIMFLDELGNVpELPDTTEHSRT--DLSRDLAALHEI 288
RasGAP_Neurofibromin cd05130
Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the ...
 383-635 8.86e-30

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: 121.66  E-value: 8.86e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  383 EVAYALVHILQSTGKAKDFLSDMAMCEVDrFMDREHLIFRENTLATKAIEEYLKLIGHRYLKDAIGEFIRALYESEE--N 460
Cdd:cd05130     41 ELARVLVTLFDSKHLLYQLLWNMFSKEVE-LADSMQTLFRGNSLASKIMTFCFKVYGATYLQSLLEPLLRTMITSSEwvS 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  461 CEVDPMRTPPS-VLADHQANLRMCCELALCKIVNSHCVFPRELKDV-FASWRVRCAeRGREDIADRLiSSSLFLRFLCPA 538
Cdd:cd05130    120 YEVDPTRLEGNeNLEENQRNLLQLTEKFFHAIISSSDEFPPQLRSVcHCLYQVVSH-RFPNSGLGAV-GSAIFLRFINPA 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  539 IMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLASFSKFSgKEDHMCFMNEFLEMEWGSMQQFLYEISNMdtGSNVGGFEG 618
Cdd:cd05130    198 IVSPYEYGILDREPPPRVKRGLKLMSKILQNIANHVLFT-KEAHMLPFNDFLRNHFEAGRRFFSSIASD--CGAVDGPSS 274

                          250       260
                   ....*....|....*....|.
gi 1137509602  619 ----YIDLGRELSmLHSLLWE 635
Cdd:cd05130    275 kylsFINDANVLA-LHRLLWN 294
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
 401-572 4.65e-29

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: 115.85  E-value: 4.65e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  401 FLSDMAMCEVDRFMDREHLiFRENTLATKAIEEYLKL-IGHRYLKDAIGEFIRALYESEE-NCEVDPMR----------- 467
Cdd:pfam00616    1 LISELIEEEIESSDNPNDL-LRGNSLVSKLLETYNRRpRGQEYLKKVLGPLVRKIIEDEDlDLESDPRKiyeslinqeel 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  468 --------------------TPPSVLADHQANLRMCCELALCKIVNSHCVFPREL----KDVFASWRVRCAERGREDIAd 523
Cdd:pfam00616   80 ktgrsdlprdvspeeaiedpEVRQIFEDNLQKLRELADEFLDAIYSSLNQLPYGIryicKQLYELLEEKFPDASEEEIL- 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1137509602  524 RLISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLAS 572
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVDHQISPKQRRNLTLIAKVLQNLAN 207
RasGAP_RASA2 cd05394
Ras-GTPase Activating Domain of RASA2; RASA2 (or GAP1(m)) is a member of the GAP1 family of ...
 379-606 8.39e-28

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: 114.61  E-value: 8.39e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  379 KSKEEVAYALVHILQSTGKAKDFLSDMAMCEVDRFMDrEHLIFRENTLATKAIEEYLKLIGHRYLKDAIGEFIRALYESE 458
Cdd:cd05394     33 RDKYDAVLPLVRLLLHHNKLVPFVAAVAALDLKDTQE-ANTIFRGNSLATRCLDEMMKIVGKHYLKVTLKPVLDEICESP 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  459 ENCEVDPMRTPPSVLAD-HQANLRMCCELALCKIVNSHCVFPRELKDVFASWRVRCAERGRED--IADRLISSSLFLRFL 535
Cdd:cd05394    112 KPCEIDPIKLKEGDNVEnNKENLRYYVDKVFFSIVKSSMSCPTLMCDVFRSLRHLAVKRFPNDphVQYSAVSSFVFLRFF 191

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1137509602  536 CPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLASFSKFSG------KEDHMC-FMNEFLEMEW-GSMQQFLYEISN 606
Cdd:cd05394    192 AVAVVSPHTFQLRPHHPDAQTSRTLTLISKTIQTLGSWGSLSKsklssfKETFMCdFFKMFQEEKYiEKVKKFLDEISS 270
PH_RASAL3 cd13374
RAS protein activator like-3 Pleckstrin homology (PH) domain; RASAL3 is thought to be a Ras ...
 135-228 8.37e-27

RAS protein activator like-3 Pleckstrin homology (PH) domain; RASAL3 is thought to be a Ras GTPase-activating protein. It is involved in positive regulation of Ras GTPase activity and of small GTPase mediated signal transduction as well as negative regulation of Ras protein signal transduction. It contains a PH domain, a C2 domain, and a Ras-GAP domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270177  Cd Length: 146  Bit Score: 107.41  E-value: 8.37e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  135 SHESLLSPSSAAEaLDLTLDEDAVIKPVHSSILGQEYCFEVTTLSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVD 214
Cdd:cd13374     50 ALGSRESLATISE-LDLGAERDVRVWPLHPSLLGEPHCFQVTWPGGSRCFSCRSAAERDRWIEDLRRSFQPHQDNVEREE 128

                           90
                   ....*....|....
gi 1137509602  215 NVLKLWIIEARDLP 228
Cdd:cd13374    129 TWLSVWVHEAKGLP 142
RasGAP_RASA4 cd05395
Ras-GTPase Activating Domain of RASA4; Ras GTPase activating-like 4 protein (RASAL4), also ...
 368-583 2.41e-22

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: 98.79  E-value: 2.41e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  368 LCAVLEPLLSVKSKEEVAYALVHILQSTGKAKDFLSDMAMCEVDRFMDREHLiFRENTLATKAIEEYLKLIGHRYLKDAI 447
Cdd:cd05395     27 LISLIDETTTAECRQEVATNLVKLFLGQGLAKEFLDLLFQLELDKTTEPNTL-FRSNSLASKSMESFLKVAGMQYLHSVL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  448 GEFIRALYESEENCEVDP---------------MRTPPSVLADHQANLRMCCELALCKIVNSHCVFPRELKDVFASWRVR 512
Cdd:cd05395    106 GPTINRVFEEKKYVELDPskveikdvgcsglhrIQTESEVIEQSAQLLQSYLGELLSAISKSVKYCPAVIRATFRQLFKR 185

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1137509602  513 CAERGREDIADRL----ISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLASFSKFSG--KEDHM 583
Cdd:cd05395    186 VQERFPENQHQNVkfiaVTSFLCLRFFSPAIMSPKLFHLREKHADARTSRTLLLLAKAVQNVGNMDTLASraKEAWM 262
RasGAP_GAPA cd05132
Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to ...
 439-690 6.01e-19

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: 90.10  E-value: 6.01e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  439 GHRYLKDAIGEFIRALYESEE-NCEVDPMR-----------------------TPPSVLADH------QANLRMCCELA- 487
Cdd:cd05132     67 GQSYLKTVLADRINDLISLKDlNLEINPLKvyeqmindieldtglpsnlprgiTPEEAAENPavqniiEPRLEMLEEITn 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  488 --LCKIVNSHCVFP----------RELKdvfaswRVRCAERGREDIADrLISSSLFLRFLCPAIMSPSLFNLTQEYPGER 555
Cdd:cd05132    147 sfLEAIINSLDEVPygirwickqiRSLT------RRKFPDASDETICS-LIGGFFLLRFINPAIVSPQAYMLVDGKPSDN 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  556 TSRTLTLIAKVVQNLASFSKFSgKEDHMCFMNEFLEMEWGSMQQFLYEISNMDTGSNVGGFEGYIDLGR----------E 625
Cdd:cd05132    220 TRRTLTLIAKLLQNLANKPSYS-KEPYMAPLQPFVEENKERLNKFLNDLCEVDDFYESLELDQYIALSKkdlsinitlnE 298

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1137509602  626 LSMLHSLLWEVMAQLSKDAILKLGPLPRLLNdisvalrnpqlhrQASHQPDRQQDRLLTRPAFNR 690
Cdd:cd05132    299 IYNTHSLLVKHLAELAPDHNDHLRLILQELG-------------PAPPQVPRKENRTIELPLYSR 350
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 217-314 1.03e-12

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 65.55  E-value: 1.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  217 LKLWIIEARDLPAKKR-----YYCELCLDDMLYARTTSKPRTDTVFWGEHFEFNNL-PAIRSLRLHLYketDKKRRKeKS 290
Cdd:cd00030      1 LRVTVIEARNLPAKDLngksdPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLdPESDTLTVEVW---DKDRFS-KD 76

                           90       100
                   ....*....|....*....|....*
gi 1137509602  291 TYLGLVSIPISSITGR-QFVEQWYP 314
Cdd:cd00030     77 DFLGEVEIPLSELLDSgKEGELWLP 101
C2_Ras_p21A1 cd08400
C2 domain present in RAS p21 protein activator 1 (RasA1); RasA1 is a GAP1 (GTPase activating ...
 217-343 1.93e-12

C2 domain present in RAS p21 protein activator 1 (RasA1); RasA1 is a GAP1 (GTPase activating protein 1), a Ras-specific GAP member, which suppresses Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. RasA1 contains a C2 domain, a Ras-GAP domain, a pleckstrin homology (PH)-like domain, a SH3 domain, and 2 SH2 domains. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology.


Pssm-ID: 176045 [Multi-domain]  Cd Length: 126  Bit Score: 65.47  E-value: 1.93e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  217 LKLWIIEARDLPAKK--RYYCELCLDDMLYARTTSKPRTDTVfWGEHFEFNNLPA-IRSLRLHLYKetdkKRRKEKSTYL 293
Cdd:cd08400      6 LQLNVLEAHKLPVKHvpHPYCVISLNEVKVARTKVREGPNPV-WSEEFVFDDLPPdVNSFTISLSN----KAKRSKDSEI 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1137509602  294 GLVSIPISSITGRQFVEQWYPVIqPSALAKGGSVGsgkvinaSIRLKSRY 343
Cdd:cd08400     81 AEVTVQLSKLQNGQETDEWYPLS-SASPLKGGEWG-------SLRIRARY 122
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 216-312 7.95e-11

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 60.19  E-value: 7.95e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602   216 VLKLWIIEARDLPAKKRY-----YCELCLDDMLY--ARTTSKPRTDTVFWGEHFEFN-NLPAIRSLRLHLYketDKKRRK 287
Cdd:smart00239    1 TLTVKIISARNLPPKDKGgksdpYVKVSLDGDPKekKKTKVVKNTLNPVWNETFEFEvPPPELAELEIEVY---DKDRFG 77

                            90       100
                    ....*....|....*....|....*
gi 1137509602   288 eKSTYLGLVSIPISSITGRQFVEQW 312
Cdd:smart00239   78 -RDDFIGQVTIPLSDLLLGGRHEKL 101
C2A_RasGAP cd08383
C2 domain (first repeat) of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ...
 217-343 1.62e-10

C2 domain (first repeat) of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. The proteins here all contain either a single C2 domain or two tandem C2 domains, a Ras-GAP domain, and a pleckstrin homology (PH)-like domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology.


Pssm-ID: 176029 [Multi-domain]  Cd Length: 117  Bit Score: 59.59  E-value: 1.62e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  217 LKLWIIEARDLPAKK--RYYCELCLDDMLYARTTSKPRTDTvFWGEHFEFNNLPA-IRSLRLHLY-KETDKKRRKeksty 292
Cdd:cd08383      2 LRLRILEAKNLPSKGtrDPYCTVSLDQVEVARTKTVEKLNP-FWGEEFVFDDPPPdVTFFTLSFYnKDKRSKDRD----- 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1137509602  293 LGLVSIPISSITGRQFVEQWYPVIqpSALAKGGSVGsgkvinaSIRLKSRY 343
Cdd:cd08383     76 IVIGKVALSKLDLGQGKDEWFPLT--PVDPDSEVQG-------SVRLRARY 117
C2 pfam00168
C2 domain;
215-315 1.74e-09

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 56.56  E-value: 1.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  215 NVLKLWIIEARDLPAKKRY-----YCELCL-DDMLYARTTSKPRTDTVFWGEHFEFN-NLPAIRSLRLHLYketDKkRRK 287
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGNgtsdpYVKVYLlDGKQKKKTKVVKNTLNPVWNETFTFSvPDPENAVLEIEVY---DY-DRF 76

                           90       100
                   ....*....|....*....|....*...
gi 1137509602  288 EKSTYLGLVSIPISSITGRQFVEQWYPV 315
Cdd:pfam00168   77 GRDDFIGEVRIPLSELDSGEGLDGWYPL 104
RasGAP_IQGAP_like cd05127
Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family ...
 409-658 3.26e-07

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: 54.13  E-value: 3.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  409 EVDRFMDREHLIFRENTLATKAIEEYLK-LIGHRYLKDAIGEFIRALYESEE-NCEVDP------------MRT------ 468
Cdd:cd05127     21 EIESKVSLPEDIVTGNPTVIKLVVNYNRgPRGQKYLRELLGPVVKEILDDDDlDLETDPvdiykawinqeeSRTgepskl 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  469 PPSV--------------LADHQANLRMCCELALCKIVNSHCVFP-------RELKDvfaSWRVRCAERGREDIAdRLIS 527
Cdd:cd05127    101 PYDVtreqalkdpevrkrLIEHLEKLRAITDKFLTAITESLDKMPygmryiaKVLKE---ALREKFPDAPEEEIL-KIVG 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  528 SSLFLRFLCPAIMSPSLFNLTQEYPGERTS----RTLTLIAKVVQNLASFSKFSGKEDHMCFMNEFLEMEWGSMQQFLYE 603
Cdd:cd05127    177 NLLYYRYMNPAIVAPEAFDIIDLSVGGQLSplqrRNLGSIAKVLQQAASGKLFGGENPYLSPLNPYISESHEKFKKFFLE 256

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1137509602  604 IS---------NMDTGSNVGGFEG---YIDLgRELSMLHSLLWEVMAQLSKD------AILK-LGPLPRLLNDI 658
Cdd:cd05127    257 ACtvpeaeehfNIDEYSDLTMLTKptiYISL-QEIFATHKLLLEHQDEIAPDpddplrELLDdLGPAPTIESLL 329
RasGAP_IQGAP2 cd05131
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a ...
 468-645 5.53e-07

Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a member of the IQGAP family that contains a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeat, a single WW domain, four IQ motifs which mediate interactions with calmodulin, and a Ras-GTPase-activating protein (GAP)-related domain that binds Rho family GTPases. IQGAP2 and IQGAP3 play important roles in the regulation of the cytoskeleton for axon outgrowth in hippocampal neurons and are thought to stay in a common regulatory pathway. The results of RNA interference studies indicated that IQGAP3 partially compensates functions of IQGAP2, but has lesser ability than IQGAP2 to promote axon outgrowth in hippocampal neuron. Moreover, IQGAP2 is required for the cadherin-mediated cell-to-cell adhesion in Xenopus laevis embryos.


Pssm-ID: 213333 [Multi-domain]  Cd Length: 359  Bit Score: 53.46  E-value: 5.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  468 TPPSVLADHQA---NLRMCCELALCKIVNSHCVFPRELKDVFASWRVRCAER---GREDIADRLISSSLFLRFLCPAIMS 541
Cdd:cd05131    121 THPEVVNKLESsiqSLRSVTDKVLGSIFSSLDLIPYGMRYIAKVLKNSLHEKfpdATEDELLKIVGNLLYYRYMNPAIVA 200

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  542 PSLFNLTQEYPG----ERTSRTLTLIAKVVQNLASFSKFSGKEDHMCFMNEFLEMEWGSMQQFLYEISNM---DTGSNVG 614
Cdd:cd05131    201 PDGFDIIDMTAGgqihSEQRRNLGSVAKVLQHAASNKLFEGENAHLSSMNSYLSQTYQKFRKFFQAACDVpepEEKFNID 280

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1137509602  615 GFEGYIDLGR--------ELSMLHSLLWEvmaqlSKDAI 645
Cdd:cd05131    281 EYSDMVTLSKpviyisieEIINTHSLLLE-----HQDAI 314
C2A_RasA2_RasA3 cd08401
C2 domain first repeat present in RasA2 and RasA3; RasA2 and RasA3 are GAP1s (GTPase ...
 216-318 2.31e-06

C2 domain first repeat present in RasA2 and RasA3; RasA2 and RasA3 are GAP1s (GTPase activating protein 1s ), Ras-specific GAP members, which suppresses Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. RasA2 and RasA3 are both inositol 1,3,4,5-tetrakisphosphate-binding proteins and contain an N-terminal C2 domain, a Ras-GAP domain, a pleckstrin-homology (PH) domain which localizes it to the plasma membrane, and Bruton's Tyrosine Kinase (BTK) a zinc binding domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176046 [Multi-domain]  Cd Length: 121  Bit Score: 48.20  E-value: 2.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  216 VLKLWIIEARDLPAKKR------YYCELCLDDMLYARTTSKPRTDTVFWGEHFEFNNLPAIRSLRLHLYkETDKKRRkek 289
Cdd:cd08401      1 SLKIKIGEAKNLPPRSGpnkmrdCYCTVNLDQEEVFRTKTVEKSLCPFFGEDFYFEIPRTFRHLSFYIY-DRDVLRR--- 76

                           90       100
                   ....*....|....*....|....*....
gi 1137509602  290 STYLGLVSIPISSITGRQFVEQWYPvIQP 318
Cdd:cd08401     77 DSVIGKVAIKKEDLHKYYGKDTWFP-LQP 104
C2A_MCTP_PRT_plant cd04022
C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 221-314 2.59e-06

C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); plant subset; MCTPs are involved in Ca2+ signaling at the membrane. Plant-MCTPs are composed of a variable N-terminal sequence, four C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-II topology.


Pssm-ID: 175989 [Multi-domain]  Cd Length: 127  Bit Score: 48.10  E-value: 2.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  221 IIEARDLPAKKRY-----YCELCLDDMLYaRTTSKPRTDTVFWGEHFEFN--NLPAIRSLRLHLYKEtDKKRRKEKSTYL 293
Cdd:cd04022      6 VVDAQDLMPKDGQgsssaYVELDFDGQKK-RTRTKPKDLNPVWNEKLVFNvsDPSRLSNLVLEVYVY-NDRRSGRRRSFL 83

                           90       100
                   ....*....|....*....|..
gi 1137509602  294 GLVSIPISSITGRQ-FVEQWYP 314
Cdd:cd04022     84 GRVRISGTSFVPPSeAVVQRYP 105
RasGAP_IQGAP1 cd05133
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a ...
 479-658 4.22e-06

Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a homodimeric protein that is widely expressed among vertebrate cell types from early embryogenesis. Mammalian IQGAP1 protein is the best characterized member of the IQGAP family, and contains several protein-interacting domains. Human IQGAP1 is most similar to mouse Iqgap1 (94% identity) and has 62% identity to human IQGAP2. IQGAP1 binds and cross-links actin filaments in vitro and has been implicated in Ca2+/calmodulin signaling, E-cadherin-dependent cell adhesion, cell motility, and invasion. Yeast IQGAP homologs have a role in the recruitment of actin filaments, are components of the spindle pole body, and are required for actomyosin ring assembly and cytokinesis. Furthermore, IQGAP1 over-expression has also been detected in gastric and colorectal carcinomas and gastric cancer cell lines.


Pssm-ID: 213335  Cd Length: 380  Bit Score: 50.81  E-value: 4.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  479 NLRMCCELALCKIVNSHCVFPRELKDVFASWRVRCAER---GREDIADRLISSSLFLRFLCPAIMSPSLFNLTQEYPGER 555
Cdd:cd05133    135 NMRMVTDKFLSAIISSVDKIPYGMRFIAKVLKDTLHEKfpdAGEDELLKIVGNLLYYRYMNPAIVAPDAFDIIDLSAGGQ 214

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  556 TS----RTLTLIAKVVQNLASFSKFSGKEDHMCFMNEFLEMEWGSMQQFLY---EISNMDTGSNVGGFEG---------Y 619
Cdd:cd05133    215 LTtdqrRNLGSIAKMLQHAASNKMFLGDNAHLSPINEYLSQSYQKFRRFFQaacDVPELEDKFNVDEYSDlvtltkpviY 294

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1137509602  620 IDLGrELSMLHSLLWEvmaqlSKDAILKL--GPLPRLLNDI 658
Cdd:cd05133    295 ISIG-EIINTHTLLLD-----HQDAIAPEhnDPIHELLDDL 329
C2A_C2C_Synaptotagmin_like cd08391
C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a ...
 216-334 4.22e-06

C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains either the first or third repeat in Synaptotagmin-like proteins with a type-I topology.


Pssm-ID: 176037 [Multi-domain]  Cd Length: 121  Bit Score: 47.29  E-value: 4.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  216 VLKLWIIEARDLPAKKRY-----------YCELCLDDMLYARTTSKPRTDTVfWGEHFEF--NNLPAiRSLRLHLY-KET 281
Cdd:cd08391      2 VLRIHVIEAQDLVAKDKFvgglvkgksdpYVIVRVGAQTFKSKVIKENLNPK-WNEVYEAvvDEVPG-QELEIELFdEDP 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1137509602  282 DKkrrkekSTYLGLVSIPISSITGRQFVEQWYPVIqpsalakggSVGSGKVIN 334
Cdd:cd08391     80 DK------DDFLGRLSIDLGSVEKKGFIDEWLPLE---------DVKSGRLHL 117
RasGAP_IQGAP3 cd12207
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 3; This family ...
 519-658 8.14e-06

Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 3; This family represents the IQ motif containing GTPase activating protein 3 (IQGAP3), which associates with Ras GTP-binding proteins. 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: 213346 [Multi-domain]  Cd Length: 350  Bit Score: 49.83  E-value: 8.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  519 EDIADRLISSSLFLRFLCPAIMSPSLFNLTQE------YPGERtsRTLTLIAKVVQNLASFSKFSGKEDHMCFMNEFLEM 592
Cdd:cd12207    178 EDEVYKVVGNLLYYRFMNPAVVAPDGFDIVDCsaggalQPEQR--RMLGSVAKVLQHAAANKHFQGDSEHLQALNQYLEE 255

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1137509602  593 EWGSMQQFLY---------EISNMDTGS---NVGGFEGYIDLGrELSMLHSLLWEVMAQLSKDailKLGPLPRLLNDI 658
Cdd:cd12207    256 THVKFRKFILqaccvpepeERFNVDEYSemvAVAKPVIYITVG-ELINTHKLLLEHQDSIAPD---HSDPLHELLEDL 329
C2A_Synaptotagmin-like cd04024
C2 domain first repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
 216-332 2.04e-05

C2 domain first repeat present in Synaptotagmin-like proteins; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 175990 [Multi-domain]  Cd Length: 128  Bit Score: 45.49  E-value: 2.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  216 VLKLWIIEARDLPAKKRY-------YCELCLDDmlyarttSKPRTDTVF------WGEHFEFNNLPAIRSLrLHLyKETD 282
Cdd:cd04024      2 VLRVHVVEAKDLAAKDRSgkgksdpYAILSVGA-------QRFKTQTIPntlnpkWNYWCEFPIFSAQNQL-LKL-ILWD 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1137509602  283 KKRRKEKStYLGLVSIPISSITGRQFVEQ---WYPViqPSALAKGGSVGSGKV 332
Cdd:cd04024     73 KDRFAGKD-YLGEFDIALEEVFADGKTGQsdkWITL--KSTRPGKTSVVSGEI 122
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 82-204 5.05e-05

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 43.69  E-value: 5.05e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602    82 QSFLSRRLKGSIKRAKSqpkldrtssfRHMILprfrsadqeRTRLMQSFKESHSHESllspSSAAEALDLtlDEDAVIKP 161
Cdd:smart00233    4 EGWLYKKSGGGKKSWKK----------RYFVL---------FNSTLLYYKSKKDKKS----YKPKGSIDL--SGCTVREA 58

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 1137509602   162 VHSSILGQEYCFEVTTLSG-TKCFACRSAAERDKWIENLQRAVK 204
Cdd:smart00233   59 PDPDSSKKPHCFEIKTSDRkTLLLQAESEEEREKWVEALRKAIA 102
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1185-1283 1.22e-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: 46.60  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602 1185 KLKEYSKSMDESRMDRVKEYEEEIHSLKERLIMSHRKLEEYERRMLSQEQQTSKI---LSQYQSRLDDSERRLRQQQVEK 1261
Cdd:TIGR02169  273 LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLeaeIDKLLAEIEELEREIEEERKRR 352

                           90       100
                   ....*....|....*....|..
gi 1137509602 1262 DsQIKGIINRLMAVEDELRVSA 1283
Cdd:TIGR02169  353 D-KLTEEYAELKEELEDLRAEL 373
C2_fungal_Inn1p-like cd08681
C2 domain found in fungal Ingression 1 (Inn1) proteins; Saccharomyces cerevisiae Inn1 ...
 221-315 1.34e-03

C2 domain found in fungal Ingression 1 (Inn1) proteins; Saccharomyces cerevisiae Inn1 associates with the contractile actomyosin ring at the end of mitosis and is needed for cytokinesis. The C2 domain of Inn1, located at the N-terminus, is required for ingression of the plasma membrane. The C-terminus is relatively unstructured and contains eight PXXP motifs that are thought to mediate interaction of Inn1 with other proteins with SH3 domains in the cytokinesis proteins Hof1 (an F-BAR protein) and Cyk3 (whose overexpression can restore primary septum formation in Inn1Delta cells) as well as recruiting Inn1 to the bud-neck by binding to Cyk3. Inn1 and Cyk3 appear to cooperate in activating chitin synthase Chs2 for primary septum formation, which allows coordination of actomyosin ring contraction with ingression of the cleavage furrow. It is thought that the C2 domain of Inn1 helps to preserve the link between the actomyosin ring and the plasma membrane, contributing both to membrane ingression, as well as to stability of the contracting ring. Additionally, Inn1 might induce curvature of the plasma membrane adjacent to the contracting ring, thereby promoting ingression of the membrane. It has been shown that the C2 domain of human synaptotagmin induces curvature in target membranes and thereby contributes to fusion of these membranes with synaptic vesicles. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176063 [Multi-domain]  Cd Length: 118  Bit Score: 39.92  E-value: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  221 IIEARDLPAKKRY-----YCELCLDDMlyarttsKPRTDTVF-------WGEHFEFNNLPAI-RSLRLHLYKETdkkrrK 287
Cdd:cd08681      7 VLKARNLPNKRKLdkqdpYCVLRIGGV-------TKKTKTDFrggqhpeWDEELRFEITEDKkPILKVAVFDDD-----K 74

                           90       100
                   ....*....|....*....|....*...
gi 1137509602  288 EKSTYLGLVSIPISSITGRQFVEQWYPV 315
Cdd:cd08681     75 RKPDLIGDTEVDLSPALKEGEFDDWYEL 102
PHA03247 PHA03247
large tegument protein UL36; Provisional
 993-1183 1.84e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602  993 TATGTGTPTSVATPPSTVHPVRHGSVAPPPPQRLKSQLSISPG----------------ATSTPPKAR-------PQSRN 1049
Cdd:PHA03247  2817 ALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGgdvrrrppsrspaakpAAPARPPVRrlarpavSRSTE 2896

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602 1050 LLLQSPESSFGGRQNSPQQQQQQQHQLSVKQSDSPAPGLPHQSSSARDSQGAPQGGNGETTDTPTKSTKQPQQQSQQQPP 1129
Cdd:PHA03247  2897 SFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPR 2976

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1137509602 1130 PQQHLLKPTVNKQGSqSPATLTPTPNERTVAWVSNMP-HLSAD------IEILRSSSNLED 1183
Cdd:PHA03247  2977 FRVPQPAPSREAPAS-STPPLTGHSLSRVSSWASSLAlHEETDpppvslKQTLWPPDDTED 3036
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1185-1296 2.34e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602 1185 KLKEYSKSMDESRmDRVKEYEEEIHSLKE--RLIMSHRKLEEYERRMLSQEQQTSKILSQYQSRLDDSERRLRQQQvEKD 1262
Cdd:PRK03918   260 KIRELEERIEELK-KEIEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE-EKE 337

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1137509602 1263 SQIKGIINRLMAVEDEL-----RVSAIPEIKPRMFREQE 1296
Cdd:PRK03918   338 ERLEELKKKLKELEKRLeeleeRHELYEEAKAKKEELER 376
C2_PKC_epsilon cd04014
C2 domain in Protein Kinase C (PKC) epsilon; A single C2 domain is found in PKC epsilon. The ...
 217-263 2.39e-03

C2 domain in Protein Kinase C (PKC) epsilon; A single C2 domain is found in PKC epsilon. The PKC family of serine/threonine kinases regulates apoptosis, proliferation, migration, motility, chemo-resistance, and differentiation. There are 3 groups: group 1 (alpha, betaI, beta II, gamma) which require phospholipids and calcium, group 2 (delta, epsilon, theta, eta) which do not require calcium for activation, and group 3 (xi, iota/lambda) which are atypical and can be activated in the absence of diacylglycerol and calcium. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-II topology.


Pssm-ID: 175981 [Multi-domain]  Cd Length: 132  Bit Score: 39.56  E-value: 2.39e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1137509602  217 LKLWIIEARDL-PAK--KRY------------YCELCLDDMLYARTTSKPRTDTVFWGEHFE 263
Cdd:cd04014      6 LKIKICEAVDLkPTDwsTRHavpkkgsqlldpYVSIDVDDTHIGKTSTKPKTNSPVWNEEFT 67
PRK12704 PRK12704
phosphodiesterase; Provisional
 1183-1299 2.72e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 2.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602 1183 DLKLKEYSKSMDESRMDRVKEYEEEIHSLKERLIMSHR----KLEEYERRMLSQEQQTSK---ILSQYQSRLDDSERRLR 1255
Cdd:PRK12704    41 KRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRerrnELQKLEKRLLQKEENLDRkleLLEKREEELEKKEKELE 120

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1137509602 1256 QQQVEKDSQIKGIINRLMAVEDEL-RVSAI--PEIKPRMFREQEEDS 1299
Cdd:PRK12704   121 QKQQELEKKEEELEELIEEQLQELeRISGLtaEEAKEILLEKVEEEA 167
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 1178-1266 4.98e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.35  E-value: 4.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602 1178 SSNLEDL--KLKEYSKSMDESRmDRVKEYEEEIHSLKERLIMSHRKLEEYERRMLS-QEQQTSKILSQYQSRLDDSERRL 1254
Cdd:PRK00409   515 KEKLNELiaSLEELERELEQKA-EEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEeAEKEAQQAIKEAKKEADEIIKEL 593

                           90
                   ....*....|..
gi 1137509602 1255 RQQQVEKDSQIK 1266
Cdd:PRK00409   594 RQLQKGGYASVK 605
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1195-1299 7.16e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 7.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137509602 1195 ESRMDRVKEYEEEIHSLKERLIMSHRKLEEYERRMLSQEQQTSKILSQYQSRLDDSERRLRQQQVEKDSQIKGIINRLMA 1274
Cdd:COG4717    145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224

                           90       100
                   ....*....|....*....|....*
gi 1137509602 1275 VEDELRvsaipEIKPRMFREQEEDS 1299
Cdd:COG4717    225 LEEELE-----QLENELEAAALEER 244
 
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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