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Conserved domains on  [gi|1958759726|ref|XP_038960144|]
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disabled homolog 2-interacting protein isoform X1 [Rattus norvegicus]

Protein Classification

RASAL2/DAB2IP family protein( domain architecture ID 11686133)

RASAL2/DAB2IP family protein similar to Homo sapien Ras GTPase-activating protein nGAP (RASAL2/NGAP) and disabled homolog 2-interacting protein (DAB2IP/AIP1)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
 646-1159 0e+00

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


:

Pssm-ID: 463427 [Multi-domain]  Cd Length: 511  Bit Score: 672.62  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  646 LRDVHTALSTPGSGQLPG--TNDLASTPGSGSSSVSAGLQKMVIENDLsGLIDFTRLPSPTPENKDLFFVTRSSGVQPSP 723
Cdd:pfam12004    1 LRDITTALTNPTPIQQQLrrFSEHSSSPPVPGRSISSGLQKMFEDPDD-GLSDFTRLPSPTPENKDLFFVTRPPLLQPSP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  724 ARSSSYSEANEPDLQMANGSKSLSMVDLQDARTLDGEAgSPVGPEALPADGQVPATQLVAG---WPARAAPVSLAGLATV 800
Cdd:pfam12004   80 ARSSSYSDANEPDQQLPNGNKSLSMVDLQDSRSLQGSP-SPPLHDAPLNLSQAGSQASVGLrpaWAARTSQGNPQSAPQV 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  801 RRAVPTPTTPGTSEgapgrPQLLAPLSFQNPVYQMAAGLPLSPRGLG--DSGSEGHSSLSSHSNSEELAAAAK----LGS 874
Cdd:pfam12004  159 RRPLQTPVTQGTRP-----QQLLAPLSFQNPVYHMAAGLPVSPRGLGspDSSSETHSSFSSHSNSEDLSSAAAnkksGPS 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  875 FSTAAEELARRPGELARRQMSLTEKGGQPTVPRQNSAGPQRRIDQPPPPPPPPPPAPRGRtppTMLSTLQYPRPSSGTLA 954
Cdd:pfam12004  234 NSSYSEDFARRSTEFTRRQLSLTELQHQPAVPRQNSAGPQRRIDQQGLGGPPLTRGRTPP---SLLNSASYPRPSSGSLM 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  955 SASPDWagPGTRLRQQSSSSKGDSPELKPRALHKQGPSPVSPNALD---RTAAWLLTMNAQLLEDEGLGPDpphrdrlrS 1031
Cdd:pfam12004  311 SSSPDW--PPARLRQQSSSSKGDSPETKQRTQHQQVPSPVNPSTLSpveRTAAWVLNMNGQYEEEESSGPE--------S 380

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1032 KEELSQAEK---DLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVLEYQARLEEGEERLRRQQEDKDVQMKGIISRLMS 1108
Cdd:pfam12004  381 REELKQAEKyeqEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMA 460

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958759726 1109 VEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERY 1159
Cdd:pfam12004  461 VEEELKKDHAEMQAVIDSKQKIIDAQEKRIASLDAANARLMSALTQLKERY 511
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
 333-656 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: 615.75  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  333 RYQTITILPMEMYKEFAEHITNHYLGLCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCgDNEHLIF 412
Cdd:cd05136      1 RYQSVDILPLEVYKEFLEYLTNNYLDLCEVLEPVLSVKAKEELATALVHILQSTGKAKEFLTDLVMAEVDRL-DDEHLIF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  413 RENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCSA-ADLPEHQGNLKMCCELAFCKIINSYCVFPR 491
Cdd:cd05136     80 RGNTLATKAMEAYLKLVGQKYLQETLGEFIRALYESEEDCEVDPSKCPPsASLSRNQANLRRSVELAWCKILSSHCVFPR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  492 ELKEVFASWRQECSSRGRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGSKE 571
Cdd:cd05136    160 ELREVFSSWRERLEERGREDIADRLISASLFLRFLCPAILSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  572 EYMSFMNQFLEHEWTNMQRFLLEISNPETLSNTAGFEGYIDLGRELSSLHSLLWEAVSQLDQSIVSKLGPLPRILRDVHT 651
Cdd:cd05136    240 EYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITE 319


                   ....*
gi 1958759726  652 ALSTP 656
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 ...
 75-261 1.20e-114

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 cd13376:

Pssm-ID: 473070  Cd Length: 182  Bit Score: 354.01  E-value: 1.20e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726   75 VTGFLSRRLKGSIKRTKSQPKLDRNHSFRHILPGFRSAataaaDNERSHLMPRLKESRSHESLLSPSSAVEALDLSMEEE 154
Cdd:cd13376      1 VTGFLSRRLKGSIKRTKSQPKLDRNSSFRHILPGFRSV-----DNERSHLMPRLKESRSHESLLSPSSAVEALDLSMEEE 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  155 VLIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRVEHILKLWVIEAKDLPAKKKYLCE 234
Cdd:cd13376     76 VVIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRVENMLKLWIIEAKDLPAKKKYLCE 155

                          170       180
                   ....*....|....*....|....*..
gi 1958759726  235 LCLDDVLYARTTGKLKTDNVFWGEHFE 261
Cdd:cd13376    156 LCLDDVLYARTTCKLKTDNVFWGEHFE 182
C2_SynGAP_like cd04013
C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and ...
 203-342 2.55e-78

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: 253.77  E-value: 2.55e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  203 PNKDNSRRVEHILKLWVIEAKDLPAKKKYLCELCLDDVLYARTTGKLKTDNVFWGEHFEFHNLPPLRTVTVHLYRETDKK 282
Cdd:cd04013      1 PNRDNSRRTENSLKLWIIEAKGLPPKKRYYCELCLDKTLYARTTSKLKTDTLFWGEHFEFSNLPPVSVITVNLYRESDKK 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958759726  283 KKKERNSYLGLVSLPAASVAGRQFVEKWYPVVTPNP------KGGKGPGPMIRIKARYQTITILPM 342
Cdd:cd04013     81 KKKDKSQLIGTVNIPVTDVSSRQFVEKWYPVSTPKGngksggKEGKGESPSIRIKARYQSTRVLPL 146
 
Name Accession Description Interval E-value
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
 646-1159 0e+00

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


Pssm-ID: 463427 [Multi-domain]  Cd Length: 511  Bit Score: 672.62  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  646 LRDVHTALSTPGSGQLPG--TNDLASTPGSGSSSVSAGLQKMVIENDLsGLIDFTRLPSPTPENKDLFFVTRSSGVQPSP 723
Cdd:pfam12004    1 LRDITTALTNPTPIQQQLrrFSEHSSSPPVPGRSISSGLQKMFEDPDD-GLSDFTRLPSPTPENKDLFFVTRPPLLQPSP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  724 ARSSSYSEANEPDLQMANGSKSLSMVDLQDARTLDGEAgSPVGPEALPADGQVPATQLVAG---WPARAAPVSLAGLATV 800
Cdd:pfam12004   80 ARSSSYSDANEPDQQLPNGNKSLSMVDLQDSRSLQGSP-SPPLHDAPLNLSQAGSQASVGLrpaWAARTSQGNPQSAPQV 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  801 RRAVPTPTTPGTSEgapgrPQLLAPLSFQNPVYQMAAGLPLSPRGLG--DSGSEGHSSLSSHSNSEELAAAAK----LGS 874
Cdd:pfam12004  159 RRPLQTPVTQGTRP-----QQLLAPLSFQNPVYHMAAGLPVSPRGLGspDSSSETHSSFSSHSNSEDLSSAAAnkksGPS 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  875 FSTAAEELARRPGELARRQMSLTEKGGQPTVPRQNSAGPQRRIDQPPPPPPPPPPAPRGRtppTMLSTLQYPRPSSGTLA 954
Cdd:pfam12004  234 NSSYSEDFARRSTEFTRRQLSLTELQHQPAVPRQNSAGPQRRIDQQGLGGPPLTRGRTPP---SLLNSASYPRPSSGSLM 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  955 SASPDWagPGTRLRQQSSSSKGDSPELKPRALHKQGPSPVSPNALD---RTAAWLLTMNAQLLEDEGLGPDpphrdrlrS 1031
Cdd:pfam12004  311 SSSPDW--PPARLRQQSSSSKGDSPETKQRTQHQQVPSPVNPSTLSpveRTAAWVLNMNGQYEEEESSGPE--------S 380

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1032 KEELSQAEK---DLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVLEYQARLEEGEERLRRQQEDKDVQMKGIISRLMS 1108
Cdd:pfam12004  381 REELKQAEKyeqEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMA 460

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958759726 1109 VEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERY 1159
Cdd:pfam12004  461 VEEELKKDHAEMQAVIDSKQKIIDAQEKRIASLDAANARLMSALTQLKERY 511
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
 333-656 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: 615.75  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  333 RYQTITILPMEMYKEFAEHITNHYLGLCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCgDNEHLIF 412
Cdd:cd05136      1 RYQSVDILPLEVYKEFLEYLTNNYLDLCEVLEPVLSVKAKEELATALVHILQSTGKAKEFLTDLVMAEVDRL-DDEHLIF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  413 RENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCSA-ADLPEHQGNLKMCCELAFCKIINSYCVFPR 491
Cdd:cd05136     80 RGNTLATKAMEAYLKLVGQKYLQETLGEFIRALYESEEDCEVDPSKCPPsASLSRNQANLRRSVELAWCKILSSHCVFPR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  492 ELKEVFASWRQECSSRGRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGSKE 571
Cdd:cd05136    160 ELREVFSSWRERLEERGREDIADRLISASLFLRFLCPAILSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  572 EYMSFMNQFLEHEWTNMQRFLLEISNPETLSNTAGFEGYIDLGRELSSLHSLLWEAVSQLDQSIVSKLGPLPRILRDVHT 651
Cdd:cd05136    240 EYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITE 319


                   ....*
gi 1958759726  652 ALSTP 656
Cdd:cd05136    320 ALRNP 324
PH_DAB2IP cd13376
DOC-2/Disabled homolog 2-interacting protein Pleckstrin homology (PH) domain; DAB2IP (also ...
 75-261 1.20e-114

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: 354.01  E-value: 1.20e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726   75 VTGFLSRRLKGSIKRTKSQPKLDRNHSFRHILPGFRSAataaaDNERSHLMPRLKESRSHESLLSPSSAVEALDLSMEEE 154
Cdd:cd13376      1 VTGFLSRRLKGSIKRTKSQPKLDRNSSFRHILPGFRSV-----DNERSHLMPRLKESRSHESLLSPSSAVEALDLSMEEE 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  155 VLIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRVEHILKLWVIEAKDLPAKKKYLCE 234
Cdd:cd13376     76 VVIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRVENMLKLWIIEAKDLPAKKKYLCE 155

                          170       180
                   ....*....|....*....|....*..
gi 1958759726  235 LCLDDVLYARTTGKLKTDNVFWGEHFE 261
Cdd:cd13376    156 LCLDDVLYARTTCKLKTDNVFWGEHFE 182
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
 328-646 4.70e-113

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: 356.23  E-value: 4.70e-113
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726   328 IRIKARYQTITILPMEMYKEFAEHITNHYLG-LCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCgD 406
Cdd:smart00323    9 LRLKTVYTTDFILPSEYYEELLELLLFSLDLsLASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRALIDPEVERT-D 87

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726   407 NEHLIFRENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCSAADLPEHQGNLKMCCELAFCKIINSY 486
Cdd:smart00323   88 DPNTIFRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEGEDLETNLENLLQYVERLFDAIINSS 167

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726   487 CVFPRELKEVFASWRQECSSR-GRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFA 565
Cdd:smart00323  168 DRLPYGLRDICKQLRQAAEKRfPDADVIYKAVSSFVFLRFFCPAIVSPKLFNLVDEHPDPTTRRTLTLIAKVLQNLANLS 247

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726   566 KFGSKEEYMSFMNQFLEHEWTNMQRFLLEISNPETLSNTAGFEGYIDLGRELSSLHSLLWEAVSQLDQSIvSKLGPLPRI 645
Cdd:smart00323  248 EFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEILVDKVSDSTTISGRELSLLHSLLLENGDALKREL-NNEDPLGKL 326


                    .
gi 1958759726   646 L 646
Cdd:smart00323  327 L 327
C2_SynGAP_like cd04013
C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and ...
 203-342 2.55e-78

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: 253.77  E-value: 2.55e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  203 PNKDNSRRVEHILKLWVIEAKDLPAKKKYLCELCLDDVLYARTTGKLKTDNVFWGEHFEFHNLPPLRTVTVHLYRETDKK 282
Cdd:cd04013      1 PNRDNSRRTENSLKLWIIEAKGLPPKKRYYCELCLDKTLYARTTSKLKTDTLFWGEHFEFSNLPPVSVITVNLYRESDKK 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958759726  283 KKKERNSYLGLVSLPAASVAGRQFVEKWYPVVTPNP------KGGKGPGPMIRIKARYQTITILPM 342
Cdd:cd04013     81 KKKDKSQLIGTVNIPVTDVSSRQFVEKWYPVSTPKGngksggKEGKGESPSIRIKARYQSTRVLPL 146
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
 392-563 2.38e-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: 116.62  E-value: 2.38e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  392 FLTDLMMSEVDRCgDNEHLIFRENTLATKAIEEYLKL-VGQKYLQDALGEFIKALYESDE-NCEVDPSK----------- 458
Cdd:pfam00616    1 LISELIEEEIESS-DNPNDLLRGNSLVSKLLETYNRRpRGQEYLKKVLGPLVRKIIEDEDlDLESDPRKiyeslinqeel 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  459 -------------CSAADLPE-------HQGNLKMCCELAFCKIINSYCVFPREL----KEVFASWRQECssrgrPDISE 514
Cdd:pfam00616   80 ktgrsdlprdvspEEAIEDPEvrqifedNLQKLRELADEFLDAIYSSLNQLPYGIryicKQLYELLEEKF-----PDASE 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958759726  515 R----LISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLAN 563
Cdd:pfam00616  155 EeilnAIGGFLFLRFFCPAIVNPDLFGLVDHQISPKQRRNLTLIAKVLQNLAN 207
C2 pfam00168
C2 domain;
213-313 1.81e-08

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 53.48  E-value: 1.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  213 HILKLWVIEAKDLPAKKK------YlCELCLDDVLY-ARTTGKLKTDNVFWGEHFEFH-NLPPLRTVTVHLYretDKKKK 284
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGngtsdpY-VKVYLLDGKQkKKTKVVKNTLNPVWNETFTFSvPDPENAVLEIEVY---DYDRF 76

                           90       100
                   ....*....|....*....|....*....
gi 1958759726  285 KeRNSYLGLVSLPAASVAGRQFVEKWYPV 313
Cdd:pfam00168   77 G-RDDFIGEVRIPLSELDSGEGLDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 214-310 1.94e-08

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: 53.26  E-value: 1.94e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726   214 ILKLWVIEAKDLPAKKKYL-----CELCLDDVLY--ARTTGKLKTDNVFWGEHFEFH-NLPPLRTVTVHLYretDKKKKK 285
Cdd:smart00239    1 TLTVKIISARNLPPKDKGGksdpyVKVSLDGDPKekKKTKVVKNTLNPVWNETFEFEvPPPELAELEIEVY---DKDRFG 77

                            90       100
                    ....*....|....*....|....*
gi 1958759726   286 eRNSYLGLVSLPAASVAGRQFVEKW 310
Cdd:smart00239   78 -RDDFIGQVTIPLSDLLLGGRHEKL 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1020-1159 7.89e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 7.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1020 GPDPPHRDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLF-----------KCQEETTQKLVLEYQ--ARLEEGEE 1086
Cdd:TIGR02168  664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELeeleeeleqlrKELEELSRQISALRKdlARLEAEVE 743

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958759726 1087 RLRRQQEDKDVQMKGIISRLMSVEEELKKDHAEMQAAVDSKQKI---IDAQEKRIASLDAANARLMSALTQLKERY 1159
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeaqIEQLKEELKALREALDELRAELTLLNEEA 819
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 149-202 9.52e-06

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: 45.62  E-value: 9.52e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1958759726   149 LSMEEEVLIKPVHSSILGQDYCFEVTTSSG-SKCFSCRSAAERDKWMENLRRAVH 202
Cdd:smart00233   48 IDLSGCTVREAPDPDSSKKPHCFEIKTSDRkTLLLQAESEEEREKWVEALRKAIA 102
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1010-1164 1.63e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1010 NAQLLEDEGLgpdppHRDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETlfkcQEETTQKLVLEYQARLEEGEERLR 1089
Cdd:COG1196    228 ELLLLKLREL-----EAELEELEAELEELEAELEELEAELAELEAELEELRL----ELEELELELEEAQAEEYELLAELA 298

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958759726 1090 RQQEDKDVQMKGIIsRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYSMRAR 1164
Cdd:COG1196    299 RLEQDIARLEERRR-ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1032-1157 5.85e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 5.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1032 KEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVlEYQARLEEGEERLRRQQE--DKDVQMKGIISRLMSV 1109
Cdd:PRK03918   306 LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK-ELEKRLEELEERHELYEEakAKKEELERLKKRLTGL 384

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958759726 1110 E-EELKKdhaEMQAAVDSKQKIIDAQEK---RIASLDAANARLMSALTQLKE 1157
Cdd:PRK03918   385 TpEKLEK---ELEELEKAKEEIEEEISKitaRIGELKKEIKELKKAIEELKK 433
rad4 TIGR00605
DNA repair protein rad4; All proteins in this family for which functions are known are ...
 41-222 1.60e-03

DNA repair protein rad4; All proteins in this family for which functions are known are involved in targeting nucleotide excision repair to specific regions of the genome.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273170 [Multi-domain]  Cd Length: 713  Bit Score: 42.56  E-value: 1.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726   41 RESPQERPGSRRSLPGSLSEKSPSmEPSAATPFRVTGFLSRRLKGSI-KRTKSQPK-LDRNHSFRH----ILPGFrsaAT 114
Cdd:TIGR00605  269 RGSILENLNVPTRLVFSDFLLSVS-KGHNDPEISSEGFVPKLSACNAnQRLIMSCEsADRTSRFRMkkdpSLPGF---SA 344

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  115 AAADNERSHLMPRLKESRSHESLLSPSSAVEALDLSMEEEVLIKPVHSSILGQDY-CFEVTTSSGSKCFscrsAAERDKW 193
Cdd:TIGR00605  345 YSDMDKSPIFTCEEGDKFIDRWITYVDFWVEVFIEQEEKWVCVDAVHSGVVPKGVtCFEPATLMMTYVF----AYDRDGY 420

                          170       180
                   ....*....|....*....|....*....
gi 1958759726  194 MENLRRAVHPNKDNSRRVEHILKLWVIEA 222
Cdd:TIGR00605  421 VKDVTRRYCDQWSTKVRKRRVEKADFGET 449
 
Name Accession Description Interval E-value
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
 646-1159 0e+00

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


Pssm-ID: 463427 [Multi-domain]  Cd Length: 511  Bit Score: 672.62  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  646 LRDVHTALSTPGSGQLPG--TNDLASTPGSGSSSVSAGLQKMVIENDLsGLIDFTRLPSPTPENKDLFFVTRSSGVQPSP 723
Cdd:pfam12004    1 LRDITTALTNPTPIQQQLrrFSEHSSSPPVPGRSISSGLQKMFEDPDD-GLSDFTRLPSPTPENKDLFFVTRPPLLQPSP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  724 ARSSSYSEANEPDLQMANGSKSLSMVDLQDARTLDGEAgSPVGPEALPADGQVPATQLVAG---WPARAAPVSLAGLATV 800
Cdd:pfam12004   80 ARSSSYSDANEPDQQLPNGNKSLSMVDLQDSRSLQGSP-SPPLHDAPLNLSQAGSQASVGLrpaWAARTSQGNPQSAPQV 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  801 RRAVPTPTTPGTSEgapgrPQLLAPLSFQNPVYQMAAGLPLSPRGLG--DSGSEGHSSLSSHSNSEELAAAAK----LGS 874
Cdd:pfam12004  159 RRPLQTPVTQGTRP-----QQLLAPLSFQNPVYHMAAGLPVSPRGLGspDSSSETHSSFSSHSNSEDLSSAAAnkksGPS 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  875 FSTAAEELARRPGELARRQMSLTEKGGQPTVPRQNSAGPQRRIDQPPPPPPPPPPAPRGRtppTMLSTLQYPRPSSGTLA 954
Cdd:pfam12004  234 NSSYSEDFARRSTEFTRRQLSLTELQHQPAVPRQNSAGPQRRIDQQGLGGPPLTRGRTPP---SLLNSASYPRPSSGSLM 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  955 SASPDWagPGTRLRQQSSSSKGDSPELKPRALHKQGPSPVSPNALD---RTAAWLLTMNAQLLEDEGLGPDpphrdrlrS 1031
Cdd:pfam12004  311 SSSPDW--PPARLRQQSSSSKGDSPETKQRTQHQQVPSPVNPSTLSpveRTAAWVLNMNGQYEEEESSGPE--------S 380

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1032 KEELSQAEK---DLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVLEYQARLEEGEERLRRQQEDKDVQMKGIISRLMS 1108
Cdd:pfam12004  381 REELKQAEKyeqEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMA 460

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958759726 1109 VEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERY 1159
Cdd:pfam12004  461 VEEELKKDHAEMQAVIDSKQKIIDAQEKRIASLDAANARLMSALTQLKERY 511
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
 333-656 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: 615.75  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  333 RYQTITILPMEMYKEFAEHITNHYLGLCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCgDNEHLIF 412
Cdd:cd05136      1 RYQSVDILPLEVYKEFLEYLTNNYLDLCEVLEPVLSVKAKEELATALVHILQSTGKAKEFLTDLVMAEVDRL-DDEHLIF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  413 RENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCSA-ADLPEHQGNLKMCCELAFCKIINSYCVFPR 491
Cdd:cd05136     80 RGNTLATKAMEAYLKLVGQKYLQETLGEFIRALYESEEDCEVDPSKCPPsASLSRNQANLRRSVELAWCKILSSHCVFPR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  492 ELKEVFASWRQECSSRGRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGSKE 571
Cdd:cd05136    160 ELREVFSSWRERLEERGREDIADRLISASLFLRFLCPAILSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  572 EYMSFMNQFLEHEWTNMQRFLLEISNPETLSNTAGFEGYIDLGRELSSLHSLLWEAVSQLDQSIVSKLGPLPRILRDVHT 651
Cdd:cd05136    240 EYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITE 319


                   ....*
gi 1958759726  652 ALSTP 656
Cdd:cd05136    320 ALRNP 324
PH_DAB2IP cd13376
DOC-2/Disabled homolog 2-interacting protein Pleckstrin homology (PH) domain; DAB2IP (also ...
 75-261 1.20e-114

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: 354.01  E-value: 1.20e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726   75 VTGFLSRRLKGSIKRTKSQPKLDRNHSFRHILPGFRSAataaaDNERSHLMPRLKESRSHESLLSPSSAVEALDLSMEEE 154
Cdd:cd13376      1 VTGFLSRRLKGSIKRTKSQPKLDRNSSFRHILPGFRSV-----DNERSHLMPRLKESRSHESLLSPSSAVEALDLSMEEE 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  155 VLIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRVEHILKLWVIEAKDLPAKKKYLCE 234
Cdd:cd13376     76 VVIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRVENMLKLWIIEAKDLPAKKKYLCE 155

                          170       180
                   ....*....|....*....|....*..
gi 1958759726  235 LCLDDVLYARTTGKLKTDNVFWGEHFE 261
Cdd:cd13376    156 LCLDDVLYARTTCKLKTDNVFWGEHFE 182
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
 328-646 4.70e-113

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: 356.23  E-value: 4.70e-113
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726   328 IRIKARYQTITILPMEMYKEFAEHITNHYLG-LCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCgD 406
Cdd:smart00323    9 LRLKTVYTTDFILPSEYYEELLELLLFSLDLsLASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRALIDPEVERT-D 87

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726   407 NEHLIFRENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCSAADLPEHQGNLKMCCELAFCKIINSY 486
Cdd:smart00323   88 DPNTIFRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEGEDLETNLENLLQYVERLFDAIINSS 167

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726   487 CVFPRELKEVFASWRQECSSR-GRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFA 565
Cdd:smart00323  168 DRLPYGLRDICKQLRQAAEKRfPDADVIYKAVSSFVFLRFFCPAIVSPKLFNLVDEHPDPTTRRTLTLIAKVLQNLANLS 247

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726   566 KFGSKEEYMSFMNQFLEHEWTNMQRFLLEISNPETLSNTAGFEGYIDLGRELSSLHSLLWEAVSQLDQSIvSKLGPLPRI 645
Cdd:smart00323  248 EFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEILVDKVSDSTTISGRELSLLHSLLLENGDALKREL-NNEDPLGKL 326


                    .
gi 1958759726   646 L 646
Cdd:smart00323  327 L 327
PH_SynGAP cd13375
Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain; SynGAP is a member of ...
 70-261 1.86e-102

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: 321.65  E-value: 1.86e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726   70 ATPFRVT-GFLSRRLKGSIKRTKSQPKLDRNHSFRHILPGFRSAataaaDNERSHLMPRLKESRSHESLLSPSSAVEALD 148
Cdd:cd13375      2 TAPFRPSqGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSA-----DHDRARLMQSFKESHSHESLLSPSSAAEALD 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  149 LSMEEEVLIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRVEHILKLWVIEAKDLPAK 228
Cdd:cd13375     77 LNLDEDSIIKPVHSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPK 156

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1958759726  229 KKYLCELCLDDVLYARTTGKLKTDNVFWGEHFE 261
Cdd:cd13375    157 KRYYCELCLDDMLYARTTSKPRTDTVFWGEHFE 189
C2_SynGAP_like cd04013
C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and ...
 203-342 2.55e-78

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: 253.77  E-value: 2.55e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  203 PNKDNSRRVEHILKLWVIEAKDLPAKKKYLCELCLDDVLYARTTGKLKTDNVFWGEHFEFHNLPPLRTVTVHLYRETDKK 282
Cdd:cd04013      1 PNRDNSRRTENSLKLWIIEAKGLPPKKRYYCELCLDKTLYARTTSKLKTDTLFWGEHFEFSNLPPVSVITVNLYRESDKK 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958759726  283 KKKERNSYLGLVSLPAASVAGRQFVEKWYPVVTPNP------KGGKGPGPMIRIKARYQTITILPM 342
Cdd:cd04013     81 KKKDKSQLIGTVNIPVTDVSSRQFVEKWYPVSTPKGngksggKEGKGESPSIRIKARYQSTRVLPL 146
RasGAP cd04519
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...
 345-597 1.73e-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: 247.40  E-value: 1.73e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  345 YKEFAEHITNHYLGLCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCgDNEHLIFRENTLATKAIEE 424
Cdd:cd04519      3 YRLLSLLLTESPLALLRELSQVLPVKDKEEVATALLRIFESRGLALEFLRYLVRSEVKNT-KNPNTLFRGNSLATKLLDQ 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  425 YLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCSAADLPEHQGNLKMCCELAFCKIINSYCVFPRELKEVFASWRQEC 504
Cdd:cd04519     82 YMKLVGQEYLKETLSPLIREILESKESCEIDTKLPVGEDLEENLENLLELVNKLVDRILSSLDRLPPELRYVFKILREFL 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  505 SSR--GRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGSKEEYMSFMNQFLE 582
Cdd:cd04519    162 AERfpEEPDEAYQAVSGFLFLRFICPAIVSPELFGLVPDEPSEQARRNLTLISKVLQSLANGVEFGDKEPFMKPLNDFIK 241

                          250
                   ....*....|....*
gi 1958759726  583 HEWTNMQRFLLEISN 597
Cdd:cd04519    242 SNKPKLKQFLDELSS 256
PH_nGAP cd13373
Neuronal growth-associated proteins Pleckstrin homology (PH) domain; nGAP (also called RASAL2 ...
 72-217 7.29e-62

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: 207.27  E-value: 7.29e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726   72 PFRVTGFLSRRLKGSIKRTKSQPKLDRNHSFRhiLPGFRSAataaadNERSHLMPRLKESRSHESLLSPSSAVEALDLSM 151
Cdd:cd13373      1 PFKVSGFFSKRLKGSIKRTKSQSKLDRNTSFR--LPSLRSA------DDRSRGLPKLKESRSHESLLSPGSAVEALDLGR 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958759726  152 EEEVLIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRVEHILKL 217
Cdd:cd13373     73 EEKVSVKPLHSSILGQDFCFEVTYSSGSKCFSCSSAAERDKWMENLRRTVQPNKDNCRRAENVLRL 138
PH_RasSynGAP-like cd13262
Synaptic Ras-GTPase activating protein family Pleckstrin homology (PH) domain; The RasSynGAP ...
 75-211 8.35e-59

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: 197.65  E-value: 8.35e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726   75 VTGFLSRRLKGSIKRTKSQPKLDRNHSFRhiLPGFRSAataaadneRSHLMPRLKESRSHESLLSPSSAveALDLSMEEE 154
Cdd:cd13262      1 ASGFFSRRLKGPLKRTKSVTKLERKSSKR--LPRTRLA--------RAPAGPRLRGSRSHESLLSSSSA--ALDLSADED 68

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958759726  155 VLIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRV 211
Cdd:cd13262     69 VVIRPLHSSILGRKHCFQVTTSEGTRCFSCRSAAERDRWIEDLRRAAQPNKDNCRRT 125
RasGAP_CLA2_BUD2 cd05137
Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein ...
 331-582 1.74e-55

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: 197.02  E-value: 1.74e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  331 KARYQTITILPMEMYKEFAEHITNHYLGLCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVD-------- 402
Cdd:cd05137      1 KVRLDENVVLPSKNYKPLEELLHNFDLGLTLQIAELVPGDKLERLSEILLDIFQASGREDEWFMALVEDEIDgidkstsk 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  403 -----RCGDNEH-LIFRENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCSAA-------DLPEHQG 469
Cdd:cd05137     81 nkdmgKSSNNEAnLLFRGNSLLTKSLEKYMRRIGKEYLEKSIGDVIRKICEENKDCEVDPSRVKESdsiekeeDLEENWE 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  470 NLKMCCELAFCKIINSYCVFPRELKEVFASWRQECSSRGRPDISE-RL--ISASLFLRFLCPAIMSPSLFNLLQEYPDDR 546
Cdd:cd05137    161 NLISLTEEIWNSIYITSNDCPPELRKILKHIRAKVEDRYGDFLRTvTLnsVSGFLFLRFFCPAILNPKLFGLLKDHPRPR 240

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1958759726  547 TARTLTLIAKVTQNLANFAKFGSKEEYMSFMNQFLE 582
Cdd:cd05137    241 AQRTLTLIAKVLQNLANLTTFGQKEPWMEPMNEFLT 276
RasGAP_GAP1_like cd05128
Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras ...
 358-598 3.85e-50

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: 178.60  E-value: 3.85e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  358 GLCAALEPILSAKtKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCGDnEHLIFRENTLATKAIEEYLKLVGQKYLQDA 437
Cdd:cd05128     22 SAVYLLEELVKVD-KDDVARPLVRIFLHHGQIVPLLRALASREISKTQD-PNTLFRGNSLASKCMDEFMKLVGMQYLHET 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  438 LGEFIKALYESDENCEVDPSKCSAADLPE-HQGNLKMCCELAFCKIINSYCVFPRELKEVFASWRQECSSR--GRPDISE 514
Cdd:cd05128    100 LKPVIDEIFSEKKSCEIDPSKLKDGEVLEtNLANLRGYVERVFKAITSSARRCPTLMCEIFSDLRESAAQRfpDNEDVPY 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  515 RLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGS----KEEYMS-FMNQFL-EHEWTNM 588
Cdd:cd05128    180 TAVSGFIFLRFFAPAILNPKLFGLREEHPDPQTARTLTLISKTIQTLGNLGSSSSglgvKEAYMSpLYERFTdEQHVDAV 259

                          250
                   ....*....|
gi 1958759726  589 QRFLLEISNP 598
Cdd:cd05128    260 KKFLDRISSV 269
RasGAP_Neurofibromin_like cd05392
Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins ...
 341-637 1.57e-45

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: 167.08  E-value: 1.57e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  341 PMEMYKEFAEHITNHYLGLCAALEpILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCgDNEHLIFRENTLATK 420
Cdd:cd05392      2 KSEAYDELLELLIEDPQLLLAIAE-VCPSSEVDLLAQSLLNLFETRNRLLPLISWLIEDEISHT-SRAADLFRRNSVATR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  421 AIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCSAADLPEHQGNLKMCCELAFCKIINSYCVFPRELKEVFASW 500
Cdd:cd05392     80 LLTLYAKSVGNKYLRKVLRPLLTEIVDNKDYFEVEKIKPDDENLEENADLLMKYAQMLLDSITDSVDQLPPSFRYICNTI 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  501 RQECSSRgRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGSKEEYMSFMNQF 580
Cdd:cd05392    160 YESVSKK-FPDAALIAVGGFLFLRFICPAIVSPESENLLDPPPTPEARRSLILIAKVLQNIANGVLFSLKEPYLESLNEF 238

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958759726  581 LEHEWTNMQRFLLEISNPETLSNTAGFEGYIDLGRELSSLHSLLWEAVSQLDQSIVS 637
Cdd:cd05392    239 LKKNSDRIQQFLSEVSTIPPTDPIFDESDEEPITADLRYLHKFLYLHFLEIRKEVLK 295
RasGAP_p120GAP cd05391
Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates ...
 339-646 2.38e-43

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: 161.12  E-value: 2.38e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  339 ILPMEMYKEFAEHITNHYLGLCAALEPiLSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRcGDNEHLIFRENTLA 418
Cdd:cd05391      4 IMPEEEYSELKELILQKELHVVYALAH-VCGQDRTLLASILLRIFRHEKLESLLLRTLNDREISM-EDEATTLFRATTLA 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  419 TKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCSAADlpEHQGNLKMCCELAFC---KIINSYCVFPRELKE 495
Cdd:cd05391     82 STLMEQYMKATATPFVHHALKDTILKILESKQSCELNPSKLEKNE--DVNTNLEHLLNILSElveKIFMAAEILPPTLRY 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  496 VFaSWRQECSSRGRPD---ISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGSKEE 572
Cdd:cd05391    160 IY-GCLQKSVQQKWPTnttVRTRVVSGFVFLRLICPAILNPRMFNIISETPSPTAARTLTLVAKSLQNLANLVEFGAKEP 238

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958759726  573 YMSFMNQFLEHEWTNMQRFLLEISN-PETLSNTAGFEGyiDLGRELSSLHSLLWEAVSQLdQSIVSKLGPLPRIL 646
Cdd:cd05391    239 YMEGVNPFIKKNKERMIMFLDELGNvPELPDTTEHSRT--DLSRDLAALHEICVAHSDEL-RTLSNERGALKKLL 310
RasGAP_RASA3 cd05134
Ras-GTPase Activating Domain of RASA3; RASA3 (or GAP1_IP4BP) is a member of the GAP1 family ...
 370-597 1.27e-38

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: 145.55  E-value: 1.27e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  370 KTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCGDnEHLIFRENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESD 449
Cdd:cd05134     33 REKQEAAIPLVRLFLHYGKIVPFISAIASAEVNRTQD-PNTIFRGNSLTSKCIDETMKLAGMHYLQVTLKPIIDEICQEH 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  450 ENCEVDPSKCS-AADLPEHQGNLKMCCELAFCKIINSYCVFPRELKEVFASWRQECSSR--GRPDISERLISASLFLRFL 526
Cdd:cd05134    112 KPCEIDPVKLKdGENLENNRENLRQYVDRIFRVITKSGVSCPTVMCDIFFSLRESAAKRfqVDPDVRYTAVSSFIFLRFF 191

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958759726  527 CPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGS---KEEYM-SFMNQFLEHEWTN-MQRFLLEISN 597
Cdd:cd05134    192 APAILSPNLFQLTPHHPDPQTSRTLTLISKTIQTLGSLSKSKSanfKESYMaAFYDYFNEQKYADaVKNFLDLISS 267
RasGAP_Neurofibromin cd05130
Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the ...
 374-626 3.80e-33

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: 131.29  E-value: 3.80e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  374 EMASALVHILQSTGKVKDFLTDLMMSEVDRCGDNEHLiFRENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDE--N 451
Cdd:cd05130     41 ELARVLVTLFDSKHLLYQLLWNMFSKEVELADSMQTL-FRGNSLASKIMTFCFKVYGATYLQSLLEPLLRTMITSSEwvS 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  452 CEVDPSKC-SAADLPEHQGNLKMCCELAFCKIINSYCVFPRELKEVFASWRQECSSRGrPDISERLISASLFLRFLCPAI 530
Cdd:cd05130    120 YEVDPTRLeGNENLEENQRNLLQLTEKFFHAIISSSDEFPPQLRSVCHCLYQVVSHRF-PNSGLGAVGSAIFLRFINPAI 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  531 MSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFgSKEEYMSFMNQFLEHEWTNMQRFLLEI-SNPETLSNTAG-FE 608
Cdd:cd05130    199 VSPYEYGILDREPPPRVKRGLKLMSKILQNIANHVLF-TKEAHMLPFNDFLRNHFEAGRRFFSSIaSDCGAVDGPSSkYL 277

                          250
                   ....*....|....*...
gi 1958759726  609 GYIDLGrELSSLHSLLWE 626
Cdd:cd05130    278 SFINDA-NVLALHRLLWN 294
PH_RASAL3 cd13374
RAS protein activator like-3 Pleckstrin homology (PH) domain; RASAL3 is thought to be a Ras ...
 66-226 1.98e-31

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: 120.50  E-value: 1.98e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726   66 EPSAATPFRVtgflsRRLKGSIKRTKSQPKldrnhsfrhilpGFRSAATAAADNERSHLmprlkESRSHESLLSpssave 145
Cdd:cd13374     10 EPEAAGPNQG-----HNVRGLLKRLKEKKK------------AKAESTGTGRDGPPSAL-----GSRESLATIS------ 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  146 ALDLSMEEEVLIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRVEHILKLWVIEAKDL 225
Cdd:cd13374     62 ELDLGAERDVRVWPLHPSLLGEPHCFQVTWPGGSRCFSCRSAAERDRWIEDLRRSFQPHQDNVEREETWLSVWVHEAKGL 141


                   .
gi 1958759726  226 P 226
Cdd:cd13374    142 P 142
RasGAP_RASAL cd05135
Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like ...
 361-592 5.40e-30

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: 121.07  E-value: 5.40e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  361 AALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCGDNEHLiFRENTLATKAIEEYLKLVGQKYLQDALGE 440
Cdd:cd05135     29 AMLEEVTTGESRQDVATKLVKIFLGQGLVVPFLDYLNTREVGRTTDPNTL-FRSNSLASKSMEQFMKVVGMPYLHEVLKP 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  441 FIKALYESDENCEVDPSK--------------CSAADLPEH-----QGNLKMCCElafcKIINSYCVFPRELKEVFASWR 501
Cdd:cd05135    108 VINRIFEEKKYVELDPCKidlnrtrrisfkgsLSEAQVRESslellQGYLGSIID----AIVGSVDQCPPVMRVAFKQLH 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  502 QECSSR----GRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANF-AKFGS-KEEYMS 575
Cdd:cd05135    184 KRVEERfpeaEHQDVKYLAISGFLFLRFFAPAILTPKLFQLREQHADPRTSRTLLLLAKAVQSIGNLgLQLGQgKEQWMA 263

                          250
                   ....*....|....*..
gi 1958759726  576 FMNQFLEHEWTNMQRFL 592
Cdd:cd05135    264 PLHPFILQSVARVKDFL 280
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
 392-563 2.38e-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: 116.62  E-value: 2.38e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  392 FLTDLMMSEVDRCgDNEHLIFRENTLATKAIEEYLKL-VGQKYLQDALGEFIKALYESDE-NCEVDPSK----------- 458
Cdd:pfam00616    1 LISELIEEEIESS-DNPNDLLRGNSLVSKLLETYNRRpRGQEYLKKVLGPLVRKIIEDEDlDLESDPRKiyeslinqeel 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  459 -------------CSAADLPE-------HQGNLKMCCELAFCKIINSYCVFPREL----KEVFASWRQECssrgrPDISE 514
Cdd:pfam00616   80 ktgrsdlprdvspEEAIEDPEvrqifedNLQKLRELADEFLDAIYSSLNQLPYGIryicKQLYELLEEKF-----PDASE 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958759726  515 R----LISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLAN 563
Cdd:pfam00616  155 EeilnAIGGFLFLRFFCPAIVNPDLFGLVDHQISPKQRRNLTLIAKVLQNLAN 207
RasGAP_RASA2 cd05394
Ras-GTPase Activating Domain of RASA2; RASA2 (or GAP1(m)) is a member of the GAP1 family of ...
 379-599 4.16e-29

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: 118.07  E-value: 4.16e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  379 LVHILQSTGKVKDFLTDLMMSEVDRCGDnEHLIFRENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSK 458
Cdd:cd05394     42 LVRLLLHHNKLVPFVAAVAALDLKDTQE-ANTIFRGNSLATRCLDEMMKIVGKHYLKVTLKPVLDEICESPKPCEIDPIK 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  459 CSAADLPE-HQGNLKMCCELAFCKIINSYCVFPRELKEVFASWRQECSSR--GRPDISERLISASLFLRFLCPAIMSPSL 535
Cdd:cd05394    121 LKEGDNVEnNKENLRYYVDKVFFSIVKSSMSCPTLMCDVFRSLRHLAVKRfpNDPHVQYSAVSSFVFLRFFAVAVVSPHT 200

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958759726  536 FNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGS------KEEYM-SFMNQFLEHEWT-NMQRFLLEISNPE 599
Cdd:cd05394    201 FQLRPHHPDAQTSRTLTLISKTIQTLGSWGSLSKsklssfKETFMcDFFKMFQEEKYIeKVKKFLDEISSTE 272
RasGAP_GAPA cd05132
Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to ...
 413-643 7.11e-26

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: 110.52  E-value: 7.11e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  413 RENTLATKAIEEYLKLV-GQKYLQDALGEFIKALYE-SDENCEVDPSKC-------------------------SAADLP 465
Cdd:cd05132     49 RANTAVSRMMTTYTRRGpGQSYLKTVLADRINDLISlKDLNLEINPLKVyeqmindieldtglpsnlprgitpeEAAENP 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  466 EHQG----NLKMCCELA---FCKIINSYCVFPRELKEVFASWRQECSSRgRPDISER----LISASLFLRFLCPAIMSPS 534
Cdd:cd05132    129 AVQNiiepRLEMLEEITnsfLEAIINSLDEVPYGIRWICKQIRSLTRRK-FPDASDEticsLIGGFFLLRFINPAIVSPQ 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  535 LFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFgSKEEYMSFMNQFLEHEWTNMQRFLLEISNPETLSNTAGFEGYIDLG 614
Cdd:cd05132    208 AYMLVDGKPSDNTRRTLTLIAKLLQNLANKPSY-SKEPYMAPLQPFVEENKERLNKFLNDLCEVDDFYESLELDQYIALS 286

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1958759726  615 R----------ELSSLHSLLWEAVSQLDQS-------IVSKLGPLP 643
Cdd:cd05132    287 KkdlsinitlnEIYNTHSLLVKHLAELAPDhndhlrlILQELGPAP 332
RasGAP_RASA4 cd05395
Ras-GTPase Activating Domain of RASA4; Ras GTPase activating-like 4 protein (RASAL4), also ...
 359-599 2.72e-25

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: 107.26  E-value: 2.72e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  359 LCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCGDNEHLiFRENTLATKAIEEYLKLVGQKYLQDAL 438
Cdd:cd05395     27 LISLIDETTTAECRQEVATNLVKLFLGQGLAKEFLDLLFQLELDKTTEPNTL-FRSNSLASKSMESFLKVAGMQYLHSVL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  439 GEFIKALYESDENCEVDPSK-------CSAADLPEHQGN--------LKMCCELAFCKIINSYCVFPRELKEVFASWRQE 503
Cdd:cd05395    106 GPTINRVFEEKKYVELDPSKveikdvgCSGLHRIQTESEvieqsaqlLQSYLGELLSAISKSVKYCPAVIRATFRQLFKR 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  504 CSSRgRPDISER-----LISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGS--KEEYMSF 576
Cdd:cd05395    186 VQER-FPENQHQnvkfiAVTSFLCLRFFSPAIMSPKLFHLREKHADARTSRTLLLLAKAVQNVGNMDTLASraKEAWMAP 264

                          250       260
                   ....*....|....*....|...
gi 1958759726  577 MNQFLEHEWTNMQRFLLEISNPE 599
Cdd:cd05395    265 LQPAIQQGVAQLKDFITKLVDIE 287
C2A_RasGAP cd08383
C2 domain (first repeat) of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ...
 215-334 2.73e-11

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: 61.90  E-value: 2.73e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  215 LKLWVIEAKDLPAKKK---YlCELCLDDVLYARTTGKLKTdNVFWGEHFEFHNLPPL---RTVTVHLYretdKKKKKERN 288
Cdd:cd08383      2 LRLRILEAKNLPSKGTrdpY-CTVSLDQVEVARTKTVEKL-NPFWGEEFVFDDPPPDvtfFTLSFYNK----DKRSKDRD 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958759726  289 SYLGLVSLpaASVAGRQFVEKWYPVVTPNPKGGKgPGpMIRIKARY 334
Cdd:cd08383     76 IVIGKVAL--SKLDLGQGKDEWFPLTPVDPDSEV-QG-SVRLRARY 117
C2_Ras_p21A1 cd08400
C2 domain present in RAS p21 protein activator 1 (RasA1); RasA1 is a GAP1 (GTPase activating ...
 215-334 1.07e-10

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: 60.46  E-value: 1.07e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  215 LKLWVIEAKDLPAKK---KYlCELCLDDVLYARTtgKLKTD-NVFWGEHFEFHNLPP-LRTVTVHLYretdKKKKKERNS 289
Cdd:cd08400      6 LQLNVLEAHKLPVKHvphPY-CVISLNEVKVART--KVREGpNPVWSEEFVFDDLPPdVNSFTISLS----NKAKRSKDS 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1958759726  290 YLGLVSLPAASVAGRQFVEKWYPVVTPNPKGGKGPGpMIRIKARY 334
Cdd:cd08400     79 EIAEVTVQLSKLQNGQETDEWYPLSSASPLKGGEWG-SLRIRARY 122
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 215-312 2.08e-10

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: 58.62  E-value: 2.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  215 LKLWVIEAKDLPAKKK-----YLCELCLDDVLYARTTGKLKTDNVFWGEHFEFHNLPPL-RTVTVHLYretDKKKKKeRN 288
Cdd:cd00030      1 LRVTVIEARNLPAKDLngksdPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLDPEsDTLTVEVW---DKDRFS-KD 76

                           90       100
                   ....*....|....*....|....*
gi 1958759726  289 SYLGLVSLPAASVAGR-QFVEKWYP 312
Cdd:cd00030     77 DFLGEVEIPLSELLDSgKEGELWLP 101
C2 pfam00168
C2 domain;
213-313 1.81e-08

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 53.48  E-value: 1.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  213 HILKLWVIEAKDLPAKKK------YlCELCLDDVLY-ARTTGKLKTDNVFWGEHFEFH-NLPPLRTVTVHLYretDKKKK 284
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGngtsdpY-VKVYLLDGKQkKKTKVVKNTLNPVWNETFTFSvPDPENAVLEIEVY---DYDRF 76

                           90       100
                   ....*....|....*....|....*....
gi 1958759726  285 KeRNSYLGLVSLPAASVAGRQFVEKWYPV 313
Cdd:pfam00168   77 G-RDDFIGEVRIPLSELDSGEGLDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 214-310 1.94e-08

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: 53.26  E-value: 1.94e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726   214 ILKLWVIEAKDLPAKKKYL-----CELCLDDVLY--ARTTGKLKTDNVFWGEHFEFH-NLPPLRTVTVHLYretDKKKKK 285
Cdd:smart00239    1 TLTVKIISARNLPPKDKGGksdpyVKVSLDGDPKekKKTKVVKNTLNPVWNETFEFEvPPPELAELEIEVY---DKDRFG 77

                            90       100
                    ....*....|....*....|....*
gi 1958759726   286 eRNSYLGLVSLPAASVAGRQFVEKW 310
Cdd:smart00239   78 -RDDFIGQVTIPLSDLLLGGRHEKL 101
RasGAP_IQGAP2 cd05131
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a ...
 419-667 1.45e-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: 55.00  E-value: 1.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  419 TKAIEEYLKLVGQkyLQDALGEFIKALYE-SDENCEVDPSkcSAADLPEHQGNLKMCCELAFCKIINSYCVFPRELKEVF 497
Cdd:cd05131     87 TNPVEVYKAWVNQ--LETATGEASKLPYDvTTEQALTHPE--VVNKLESSIQSLRSVTDKVLGSIFSSLDLIPYGMRYIA 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  498 ASWRQECSSRgRPDISE----RLISASLFLRFLCPAIMSPSLFNLL------QEYPDDRtaRTLTLIAKVTQNLANFAKF 567
Cdd:cd05131    163 KVLKNSLHEK-FPDATEdellKIVGNLLYYRYMNPAIVAPDGFDIIdmtaggQIHSEQR--RNLGSVAKVLQHAASNKLF 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  568 GSKEEYMSFMNQFLEHEWTNMQRFL---LEISNPETLSNTAGFEGYIDLGR--------ELSSLHSLLWE---AVSQlDQ 633
Cdd:cd05131    240 EGENAHLSSMNSYLSQTYQKFRKFFqaaCDVPEPEEKFNIDEYSDMVTLSKpviyisieEIINTHSLLLEhqdAIAP-DQ 318

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1958759726  634 S-----IVSKLGPLPrilrDVHTALstpGSGQLpGTNDL 667
Cdd:cd05131    319 NdllheLLKDLGEVP----DVESFL---GEGTV-DPNDP 349
RasGAP_IQGAP_like cd05127
Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family ...
 521-645 4.54e-06

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: 50.28  E-value: 4.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  521 LFLRFLCPAIMSPSLFNLLQEYPDDRTA----RTLTLIAKVTQNLANFAKFGSKEEYMSFMNQFLEHEWTNMQRFLLEIS 596
Cdd:cd05127    179 LYYRYMNPAIVAPEAFDIIDLSVGGQLSplqrRNLGSIAKVLQQAASGKLFGGENPYLSPLNPYISESHEKFKKFFLEAC 258

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958759726  597 NPETLSNTAGFEGYIDLG-----------RELSSLHSLLWEAVSQL--DQS-----IVSKLGPLPRI 645
Cdd:cd05127    259 TVPEAEEHFNIDEYSDLTmltkptiyislQEIFATHKLLLEHQDEIapDPDdplreLLDDLGPAPTI 325
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1020-1159 7.89e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 7.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1020 GPDPPHRDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLF-----------KCQEETTQKLVLEYQ--ARLEEGEE 1086
Cdd:TIGR02168  664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELeeleeeleqlrKELEELSRQISALRKdlARLEAEVE 743

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958759726 1087 RLRRQQEDKDVQMKGIISRLMSVEEELKKDHAEMQAAVDSKQKI---IDAQEKRIASLDAANARLMSALTQLKERY 1159
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeaqIEQLKEELKALREALDELRAELTLLNEEA 819
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 149-202 9.52e-06

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: 45.62  E-value: 9.52e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1958759726   149 LSMEEEVLIKPVHSSILGQDYCFEVTTSSG-SKCFSCRSAAERDKWMENLRRAVH 202
Cdd:smart00233   48 IDLSGCTVREAPDPDSSKKPHCFEIKTSDRkTLLLQAESEEEREKWVEALRKAIA 102
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1010-1164 1.63e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1010 NAQLLEDEGLgpdppHRDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETlfkcQEETTQKLVLEYQARLEEGEERLR 1089
Cdd:COG1196    228 ELLLLKLREL-----EAELEELEAELEELEAELEELEAELAELEAELEELRL----ELEELELELEEAQAEEYELLAELA 298

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958759726 1090 RQQEDKDVQMKGIIsRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYSMRAR 1164
Cdd:COG1196    299 RLEQDIARLEERRR-ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1032-1160 2.41e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.97  E-value: 2.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1032 KEELSQAEKDLAVLQDKLRISTKKLEEYETlfkcQEETTQKLVLEYQARLEEGEERLRRQQEDKDvQMKGIISRLMSVEE 1111
Cdd:COG4372     51 REELEQAREELEQLEEELEQARSELEQLEE----ELEELNEQLQAAQAELAQAQEELESLQEEAE-ELQEELEELQKERQ 125

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1958759726 1112 ELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYS 1160
Cdd:COG4372    126 DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1032-1157 2.46e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 2.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1032 KEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVLEyQARLEEGEERLRRQQEDKDVQMKGIISRLMSVEE 1111
Cdd:COG1196    273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER-LEELEEELAELEEELEELEEELEELEEELEEAEE 351

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958759726 1112 ELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKE 1157
Cdd:COG1196    352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
RasGAP_IQGAP1 cd05133
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a ...
 510-613 3.55e-05

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: 47.73  E-value: 3.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  510 PDISE----RLISASLFLRFLCPAIMSPSLFNLL------QEYPDDRtaRTLTLIAKVTQNLANFAKFGSKEEYMSFMNQ 579
Cdd:cd05133    174 PDAGEdellKIVGNLLYYRYMNPAIVAPDAFDIIdlsaggQLTTDQR--RNLGSIAKMLQHAASNKMFLGDNAHLSPINE 251

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1958759726  580 FLEHEWTNMQRFLLEISNPETLSNTAGFEGYIDL 613
Cdd:cd05133    252 YLSQSYQKFRRFFQAACDVPELEDKFNVDEYSDL 285
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1027-1159 3.56e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.13  E-value: 3.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1027 DRLRS-KEELSQAEKDLAVLQDKLRISTKKLEEYETLF----------KCQEETTQKLVLEYQARLEEGEERLRRQQE-- 1093
Cdd:TIGR02168  232 LRLEElREELEELQEELKEAEEELEELTAELQELEEKLeelrlevselEEEIEELQKELYALANEISRLEQQKQILRErl 311

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1094 ----DKDVQMKGIISRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERY 1159
Cdd:TIGR02168  312 anleRQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
C2A_MCTP_PRT_plant cd04022
C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
 219-312 3.59e-05

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: 44.64  E-value: 3.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  219 VIEAKDLPAKKKY-----LCELCLDDVLYaRTTGKLKTDNVFWGEHFEF--HNLPPLRTVTVHLYRETDKKKKKeRNSYL 291
Cdd:cd04022      6 VVDAQDLMPKDGQgsssaYVELDFDGQKK-RTRTKPKDLNPVWNEKLVFnvSDPSRLSNLVLEVYVYNDRRSGR-RRSFL 83

                           90       100
                   ....*....|....*....|..
gi 1958759726  292 GLVSLPAASVAGRQ-FVEKWYP 312
Cdd:cd04022     84 GRVRISGTSFVPPSeAVVQRYP 105
C2A_C2C_Synaptotagmin_like cd08391
C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a ...
 213-312 4.90e-05

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: 43.82  E-value: 4.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  213 HILKLWVIEAKDLPAKKKYL-----------CELCLDDVLYaRTTGKLKTDNVFWGEHFEF--HNLPPLrTVTVHLYret 279
Cdd:cd08391      1 GVLRIHVIEAQDLVAKDKFVgglvkgksdpyVIVRVGAQTF-KSKVIKENLNPKWNEVYEAvvDEVPGQ-ELEIELF--- 75

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958759726  280 DKKKKKErnSYLGLVSLPAASVAGRQFVEKWYP 312
Cdd:cd08391     76 DEDPDKD--DFLGRLSIDLGSVEKKGFIDEWLP 106
RasGAP_IQGAP3 cd12207
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 3; This family ...
 521-658 5.72e-05

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: 46.75  E-value: 5.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  521 LFLRFLCPAIMSPSLFNLLQE------YPDDRtaRTLTLIAKVTQNLANFAKFGSKEEYMSFMNQFLEHEWTNMQRFLLE 594
Cdd:cd12207    189 LYYRFMNPAVVAPDGFDIVDCsaggalQPEQR--RMLGSVAKVLQHAAANKHFQGDSEHLQALNQYLEETHVKFRKFILQ 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  595 ---ISNPETLSNTAGFEG---------YIDLGrELSSLHSLLWEAVSQL--DQS-----IVSKLGPLPRILRDVHTALST 655
Cdd:cd12207    267 accVPEPEERFNVDEYSEmvavakpviYITVG-ELINTHKLLLEHQDSIapDHSdplheLLEDLGEVPTVQSLIGESWAD 345


                   ...
gi 1958759726  656 PGS 658
Cdd:cd12207    346 LGD 348
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1032-1157 5.85e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 5.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1032 KEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVlEYQARLEEGEERLRRQQE--DKDVQMKGIISRLMSV 1109
Cdd:PRK03918   306 LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK-ELEKRLEELEERHELYEEakAKKEELERLKKRLTGL 384

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958759726 1110 E-EELKKdhaEMQAAVDSKQKIIDAQEK---RIASLDAANARLMSALTQLKE 1157
Cdd:PRK03918   385 TpEKLEK---ELEELEKAKEEIEEEISKitaRIGELKKEIKELKKAIEELKK 433
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1027-1158 7.14e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 45.69  E-value: 7.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1027 DRLRSK-----EELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQE---ETTQKLVLEYQARLE---------------E 1083
Cdd:COG1579     20 DRLEHRlkelpAELAELEDELAALEARLEAAKTELEDLEKEIKRLEleiEEVEARIKKYEEQLGnvrnnkeyealqkeiE 99

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958759726 1084 GEERLRRQQEDKdvqmkgiISRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRiasLDAANARLMSALTQLKER 1158
Cdd:COG1579    100 SLKRRISDLEDE-------ILELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAE 164
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1026-1157 7.17e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.37  E-value: 7.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1026 RDRLRSKEELSQAEKDLAVLQDKLrisTKKLEEYETLFKCQEETTQKLVlEYQARLEEGEERLRRQQ--------EDKDV 1097
Cdd:TIGR02169  730 QEEEKLKERLEELEEDLSSLEQEI---ENVKSELKELEARIEELEEDLH-KLEEALNDLEARLSHSRipeiqaelSKLEE 805

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958759726 1098 QMKGIISRLMSVEEELKKDHAEMQAAVDSKQ----KIIDAQEKRI---ASLDAANARLMSALTQLKE 1157
Cdd:TIGR02169  806 EVSRIEARLREIEQKLNRLTLEKEYLEKEIQelqeQRIDLKEQIKsieKEIENLNGKKEELEEELEE 872
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1030-1163 1.04e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 1.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1030 RSKEELSQAEKDLAVLQDKLRISTKKLEEYETLfkcQEETTQKLvleyqARLEEGEERLRRQQEdkdvQMKGIISRLMSV 1109
Cdd:COG4372     63 QLEEELEQARSELEQLEEELEELNEQLQAAQAE---LAQAQEEL-----ESLQEEAEELQEELE----ELQKERQDLEQQ 130

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958759726 1110 EEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYSMRA 1163
Cdd:COG4372    131 RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA 184
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1032-1159 6.78e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.60  E-value: 6.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1032 KEELSQAEKDLAVLQDKLRISTKKL------EEYETLFKcqEETTQKLvleYQARLEEGEERLRRQQEDKDVQMKGIISR 1105
Cdd:COG1579     58 EKEIKRLELEIEEVEARIKKYEEQLgnvrnnKEYEALQK--EIESLKR---RISDLEDEILELMERIEELEEELAELEAE 132

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958759726 1106 LMSVEEELKKDHAEMQAAV-DSKQKIIDAQEKRIASLDAANARLMSALTQLKERY 1159
Cdd:COG1579    133 LAELEAELEEKKAELDEELaELEAELEELEAEREELAAKIPPELLALYERIRKRK 187
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1031-1157 7.17e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 7.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1031 SKEELSQAEKDLAVLQDKLRISTKKLEEYET-LFKCQEE--TTQKLVLEYQARLEEGEERLRRQQEDKDV---QMKGIIS 1104
Cdd:COG4372     29 LSEQLRKALFELDKLQEELEQLREELEQAREeLEQLEEEleQARSELEQLEEELEELNEQLQAAQAELAQaqeELESLQE 108

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958759726 1105 RLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKE 1157
Cdd:COG4372    109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
C2A_Rasal1_RasA4 cd04054
C2 domain first repeat present in RasA1 and RasA4; Rasal1 and RasA4 are both members of GAP1 ...
 219-310 7.74e-04

C2 domain first repeat present in RasA1 and RasA4; Rasal1 and RasA4 are both members of GAP1 (GTPase activating protein 1). Rasal1 responds to repetitive Ca2+ signals by associating with the plasma membrane and deactivating Ras. RasA4 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. Both of these proteins contains two C2 domains, a Ras-GAP domain, a plextrin homology (PH)-like domain, and a Bruton's Tyrosine Kinase (BTK) 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: 176018 [Multi-domain]  Cd Length: 121  Bit Score: 40.58  E-value: 7.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  219 VIEAKDLPAK-----KKYLCELCLDDVLYARTTGKLKTDNVFWGEHFEFHNLPPLRTVTVHLYREtdkkKKKERNSYLGL 293
Cdd:cd04054      6 IVEGKNLPAKditgsSDPYCIVKVDNEVIIRTATVWKTLNPFWGEEYTVHLPPGFHTVSFYVLDE----DTLSRDDVIGK 81

                           90
                   ....*....|....*...
gi 1958759726  294 VSLPAASVAGR-QFVEKW 310
Cdd:cd04054     82 VSLTREVISAHpRGIDGW 99
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1030-1179 1.01e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1030 RSKEELSQAEKDLAVLQ----------DKLRISTKKLEEYETLFKCQEETTQKLVL-EYQARLEEGE------ERLRRQQ 1092
Cdd:TIGR02169  174 KALEELEEVEENIERLDliidekrqqlERLRREREKAERYQALLKEKREYEGYELLkEKEALERQKEaierqlASLEEEL 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1093 EDKDVQMKGIISRLMSVEEELKKDHAEMQAAVDSKQKIIdaqEKRIASLDAANARLMSALTQLK---ERYSMRARNGVSP 1169
Cdd:TIGR02169  254 EKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRV---KEKIGELEAEIASLERSIAEKErelEDAEERLAKLEAE 330

                          170
                   ....*....|
gi 1958759726 1170 TNPTKLQITE 1179
Cdd:TIGR02169  331 IDKLLAEIEE 340
PRK12704 PRK12704
phosphodiesterase; Provisional
 1037-1159 1.18e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1037 QAEKDLAVLQDKLRISTKKlEEYETLFKCQEETTQKLvleyQARLEEGEERLRRQQED---KDVQMKGIISRLMSVEEEL 1113
Cdd:PRK12704    52 EAIKKEALLEAKEEIHKLR-NEFEKELRERRNELQKL----EKRLLQKEENLDRKLELlekREEELEKKEKELEQKQQEL 126

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958759726 1114 KKDHAEMQAAVDSKQKIIdaqeKRIASLDAANARLMsALTQLKERY 1159
Cdd:PRK12704   127 EKKEEELEELIEEQLQEL----ERISGLTAEEAKEI-LLEKVEEEA 167
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1032-1158 1.29e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1032 KEELSQAEKDLAVLQDKLRisTKKLEEYETlfkcQEETTQKLVLEYQARLEEGEERLRRQQEDkdvqmkgiISRLMSVEE 1111
Cdd:COG1196    219 KEELKELEAELLLLKLREL--EAELEELEA----ELEELEAELEELEAELAELEAELEELRLE--------LEELELELE 284

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1958759726 1112 ELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKER 1158
Cdd:COG1196    285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
Caldesmon pfam02029
Caldesmon;
966-1181 1.29e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 42.93  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  966 RLRQ-QSSSSKGDSPELKPRALHKQGPS-----PVSPNALDRTAAWLLTMnaQLLEDeglgpdpphRDRLRSKEELS-QA 1038
Cdd:pfam02029   19 RRRQkEEEEPSGQVTESVEPNEHNSYEEdselkPSGQGGLDEEEAFLDRT--AKREE---------RRQKRLQEALErQK 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1039 EKDLAVLQDKLRISTKK----LEEYET----------LFKCQEETTQKLVLEYQARL---------EEGEERLRRQQEDK 1095
Cdd:pfam02029   88 EFDPTIADEKESVAERKenneEEENSSwekeekrdsrLGRYKEEETEIREKEYQENKwstevrqaeEEGEEEEDKSEEAE 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1096 DVQmkgiisRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYSMRARNGVSPTNPTKL 1175
Cdd:pfam02029  168 EVP------TENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAE 241


                   ....*.
gi 1958759726 1176 QITENG 1181
Cdd:pfam02029  242 VFLEAE 247
rad4 TIGR00605
DNA repair protein rad4; All proteins in this family for which functions are known are ...
 41-222 1.60e-03

DNA repair protein rad4; All proteins in this family for which functions are known are involved in targeting nucleotide excision repair to specific regions of the genome.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273170 [Multi-domain]  Cd Length: 713  Bit Score: 42.56  E-value: 1.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726   41 RESPQERPGSRRSLPGSLSEKSPSmEPSAATPFRVTGFLSRRLKGSI-KRTKSQPK-LDRNHSFRH----ILPGFrsaAT 114
Cdd:TIGR00605  269 RGSILENLNVPTRLVFSDFLLSVS-KGHNDPEISSEGFVPKLSACNAnQRLIMSCEsADRTSRFRMkkdpSLPGF---SA 344

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  115 AAADNERSHLMPRLKESRSHESLLSPSSAVEALDLSMEEEVLIKPVHSSILGQDY-CFEVTTSSGSKCFscrsAAERDKW 193
Cdd:TIGR00605  345 YSDMDKSPIFTCEEGDKFIDRWITYVDFWVEVFIEQEEKWVCVDAVHSGVVPKGVtCFEPATLMMTYVF----AYDRDGY 420

                          170       180
                   ....*....|....*....|....*....
gi 1958759726  194 MENLRRAVHPNKDNSRRVEHILKLWVIEA 222
Cdd:TIGR00605  421 VKDVTRRYCDQWSTKVRKRRVEKADFGET 449
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1026-1150 1.65e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 1.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1026 RDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVLEYQaRLEEGEERLRRQQEDKDVQMKGIISR 1105
Cdd:COG4372     73 SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ-DLEQQRKQLEAQIAELQSEIAEREEE 151

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1958759726 1106 LMSVEEELKKDHAEMQAAVDSKQKIIDAQ-EKRIASL-DAANARLMS 1150
Cdd:COG4372    152 LKELEEQLESLQEELAALEQELQALSEAEaEQALDELlKEANRNAEK 198
GOLGA2L5 pfam15070
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ...
 999-1121 1.97e-03

Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.


Pssm-ID: 464485 [Multi-domain]  Cd Length: 521  Bit Score: 42.36  E-value: 1.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  999 LDRTAAWLLTMNAQLLEDEGLGPDPPHRDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLfkCQEETTQKLVLEYQ 1078
Cdd:pfam15070   55 LETSLAELKNQAAVPPAEEEQPPAGPSEEEQRLQEEAEQLQKELEALAGQLQAQVQDNEQLSRL--NQEQEQRLLELERA 132

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1958759726 1079 ARLEeGEERLRRQQEDKDVQM-KGIISRLMSVEEELKKDHAEMQ 1121
Cdd:pfam15070  133 AERW-GEQAEDRKQILEDMQSdRATISRALSQNRELKEQLAELQ 175
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1033-1148 2.15e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 2.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1033 EELSQAEKDLAVLQDKLRISTKKLEEYETLfkcqEETTQKLvleyQARLEEGEERLRRQQEDKDVQMKGIISRLMSVEEE 1112
Cdd:COG4717    132 QELEALEAELAELPERLEELEERLEELREL----EEELEEL----EAELAELQEELEELLEQLSLATEEELQDLAEELEE 203

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958759726 1113 LKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARL 1148
Cdd:COG4717    204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1040-1168 2.44e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 2.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1040 KDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVlEYQARLEEGEERLRRQQEDKDVQMkgIISRLMSVEEELKKDHAE 1119
Cdd:COG4717     71 KELKELEEELKEAEEKEEEYAELQEELEELEEELE-ELEAELEELREELEKLEKLLQLLP--LYQELEALEAELAELPER 147

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1958759726 1120 MQAAVDSKQKIIDAQEkRIASLDAANARLMSALTQLKERYSMRARNGVS 1168
Cdd:COG4717    148 LEELEERLEELRELEE-ELEELEAELAELQEELEELLEQLSLATEEELQ 195
C2_plant_PLD cd04015
C2 domain present in plant phospholipase D (PLD); PLD hydrolyzes terminal phosphodiester bonds ...
 291-334 2.53e-03

C2 domain present in plant phospholipase D (PLD); PLD hydrolyzes terminal phosphodiester bonds in diester glycerophospholipids resulting in the degradation of phospholipids. In vitro PLD transfers phosphatidic acid to primary alcohols. In plants PLD plays a role in germination, seedling growth, phosphatidylinositol metabolism, and changes in phospholipid composition. There is a single Ca(2+)/phospholipid-binding C2 domain in PLD. 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: 175982 [Multi-domain]  Cd Length: 158  Bit Score: 39.98  E-value: 2.53e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958759726  291 LGLVSLPAASVAGRQFVEKWYPVVTPNPKGGKgPGPMIRIKARY 334
Cdd:cd04015    115 IGRAYIPVEDLLSGEPVEGWLPILDSNGKPPK-PGAKIRVSLQF 157
C2A_RasA2_RasA3 cd08401
C2 domain first repeat present in RasA2 and RasA3; RasA2 and RasA3 are GAP1s (GTPase ...
 217-313 2.58e-03

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: 38.96  E-value: 2.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  217 LWVI-EAKDLPAKKK------YLCELCLDDVLYARTTGKLKTDNVFWGEHFEFHNLPPLRTVTVHLYretdKKKKKERNS 289
Cdd:cd08401      3 KIKIgEAKNLPPRSGpnkmrdCYCTVNLDQEEVFRTKTVEKSLCPFFGEDFYFEIPRTFRHLSFYIY----DRDVLRRDS 78

                           90       100
                   ....*....|....*....|....
gi 1958759726  290 YLGLVSLPAASVAGRQFVEKWYPV 313
Cdd:cd08401     79 VIGKVAIKKEDLHKYYGKDTWFPL 102
RasGAP_RAP6 cd05129
Ras-GTPase Activating Domain of Rab5-activating protein 6; Rab5-activating protein 6 (RAP6) is ...
 425-580 2.61e-03

Ras-GTPase Activating Domain of Rab5-activating protein 6; Rab5-activating protein 6 (RAP6) is an endosomal protein with a role in the regulation of receptor-mediated endocytosis. RAP6 contains a Vps9 domain, which is involved in the activation of Rab5, and a Ras GAP domain (RGD). Rab5 is a small GTPase required for the control of the endocytic route, and its activity is regulated by guanine nucleotide exchange factor, such as Rabex5, and GAPs, such as RN-tre. Human Rap6 protein is localized on the plasma membrane and on the endosome. RAP6 binds to Rab5 and Ras through the Vps9 and RGD domains, respectively.


Pssm-ID: 213331  Cd Length: 365  Bit Score: 41.56  E-value: 2.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  425 YLKLVGQKYLQDALGEFIKALYESDE-NCEVDPSKCSAA-------------DLPEHQGNLKMCCE------LAFCKII- 483
Cdd:cd05129    104 ELLFSAKLYLTAALHKPIMQVLVDDEiFLETDPQKALCRfspaeqekrfgeeGTPEQQRKLQQYRAeflsrlVALVNKFi 183

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726  484 -----NSYCvFPRELKE-VFASWRQECSSRGRPDISERLISASL-FLRFLCPAIMSPSLFNLLQEYPDDRTAR-TLTLIA 555
Cdd:cd05129    184 sslrqSVYC-FPQSLRWiVRQLRKILTRSGDDEEAEARALCTDLlFTNFICPAIVNPEQYGIISDAPISEVARhNLMQVA 262

                          170       180
                   ....*....|....*....|....*.
gi 1958759726  556 KVTQNLAnFAKFGSKE-EYMSFMNQF 580
Cdd:cd05129    263 QILQVLA-LTEFESPDpRLKELLSKF 287
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1006-1159 3.10e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 3.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1006 LLTMNAQLLEDEGLGPDPPHRDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLFkcQEETTQKLVLEYQARLEEGE 1085
Cdd:COG4717    368 LEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL--DEEELEEELEELEEELEELE 445

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958759726 1086 ERLRRQQEdkdvQMKGIISRLmsveEELKKDH--AEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERY 1159
Cdd:COG4717    446 EELEELRE----ELAELEAEL----EQLEEDGelAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1026-1158 3.61e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 3.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1026 RDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVLEYQARLEEGEERLRRQQEDKDVQMkgiisR 1105
Cdd:COG1196    316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL-----E 390

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958759726 1106 LMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKER 1158
Cdd:COG1196    391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 149-197 4.23e-03

Pleckstrin homology (PH) 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: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 37.52  E-value: 4.23e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958759726  149 LSMEEEVLIKPVHSSilGQDYCFEVTTSSGSK-CFSCRSAAERDKWMENL 197
Cdd:cd00821     45 IPLSGILEVEEVSPK--ERPHCFELVTPDGRTyYLQADSEEERQEWLKAL 92
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 1030-1158 5.60e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 40.71  E-value: 5.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1030 RSKEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVleyqarlEEGEERLRRQQEDKDVQMKGIISRLMSV 1109
Cdd:COG5185    374 KSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAA-------DRQIEELQRQIEQATSSNEEVSKLLNEL 446

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1958759726 1110 EEELKKDHAEMQaaVDSKQKIIDAQEKRIASLDAANARLMSALTQLKER 1158
Cdd:COG5185    447 ISELNKVMREAD--EESQSRLEEAYDEINRSVRSKKEDLNEELTQIESR 493
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1032-1158 6.63e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 6.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1032 KEELSQAEKDLAVLQDKLRISTKKLEEYETlfkcQEETTQKLVLEYQARLEEGEE----RLRRQQEDKDV---------- 1097
Cdd:COG3883     36 QAELDALQAELEELNEEYNELQAELEALQA----EIDKLQAEIAEAEAEIEERREelgeRARALYRSGGSvsyldvllgs 111

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958759726 1098 ------------------QMKGIISRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKER 1158
Cdd:COG3883    112 esfsdfldrlsalskiadADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1006-1161 7.72e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 7.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1006 LLTMNAQLLEDEGL---GPDPPHRDRLRSKEELSQA----------EKDLAVLQDKLRISTKKLEEYETLFKCQEETTQK 1072
Cdd:TIGR02169  641 MVTLEGELFEKSGAmtgGSRAPRGGILFSRSEPAELqrlrerleglKRELSSLQSELRRIENRLDELSQELSDASRKIGE 720

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1073 LVLEYQaRLEEGEERLRRQQEDKDVQMKgiisrlmSVEEELKKDHAEMqaavdskqkiiDAQEKRIASLDAANARLMSAL 1152
Cdd:TIGR02169  721 IEKEIE-QLEQEEEKLKERLEELEEDLS-------SLEQEIENVKSEL-----------KELEARIEELEEDLHKLEEAL 781


                   ....*....
gi 1958759726 1153 TQLKERYSM 1161
Cdd:TIGR02169  782 NDLEARLSH 790
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1010-1159 7.79e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 7.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958759726 1010 NAQLLEDEglgpdpphRDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKL--VLEYQAR----LEE 1083
Cdd:TIGR02168  322 EAQLEELE--------SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELeeQLETLRSkvaqLEL 393

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958759726 1084 GEERLRRQQEDKDVQMKGIISRLMSVEEELKKDHAEMQ-AAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERY 1159
Cdd:TIGR02168  394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
PH_RASA1 cd13260
RAS p21 protein activator (GTPase activating protein) 1 Pleckstrin homology (PH) domain; RASA1 ...
 147-199 8.54e-03

RAS p21 protein activator (GTPase activating protein) 1 Pleckstrin homology (PH) domain; RASA1 (also called RasGap1 or p120) is a member of the RasGAP family of GTPase-activating proteins. RASA1 contains N-terminal SH2-SH3-SH2 domains, followed by two C2 domains, a PH domain, a RasGAP domain, and a BTK domain. Splice variants lack the N-terminal domains. It is a cytosolic vertebrate protein that acts as a suppressor of RAS via its C-terminal GAP domain function, enhancing the weak intrinsic GTPase activity of RAS proteins resulting in the inactive GDP-bound form of RAS, allowing control of cellular proliferation and differentiation. Additionally, it is involved in mitogenic signal transmission towards downstream interacting partners through its N-terminal SH2-SH3-SH2 domains. RASA1 interacts with a number of proteins including: G3BP1, SOCS3, ANXA6, Huntingtin, KHDRBS1, Src, EPHB3, EPH receptor B2, Insulin-like growth factor 1 receptor, PTK2B, DOK1, PDGFRB, HCK, Caveolin 2, DNAJA3, HRAS, GNB2L1 and NCK1. 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: 270080  Cd Length: 103  Bit Score: 36.94  E-value: 8.54e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958759726  147 LDLSmeeEVLIKPVHSSILGQDYCFEVTTSSGSKC----FSCRSAAERDKWMENLRR 199
Cdd:cd13260     48 IDLS---YCSLYPVHDSLFGRPNCFQIVVRALNEStityLCADTAELAQEWMRALRA 101
 
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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