NCBI Conserved Domain Search

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

1013-1152

3.88e-06

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

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 3.88e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  1013 GPDPPHRDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLF-----------KCQEETTQKLVLEYQ--ARLEEGEE 1079
Cdd:TIGR02168  664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELeeleeeleqlrKELEELSRQISALRKdlARLEAEVE 743

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568914241  1080 RLRRQQEDKDIQMKGIISRLMSVEEELKKDHAEMQAAVDSKQKI---IDAQEKRIASLDAANARLMSALTQLKERY 1152
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeaqIEQLKEELKALREALDELRAELTLLNEEA 819

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

1025-1153

1.21e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 1.21e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241 1025 KEELSQAEKDLAVLQDKLRISTKKLEEYETlfkcQEETTQKLVLEYQARLEEGEERLRRQQEDKDiQMKGIISRLMSVEE 1104
Cdd:COG4372    51 REELEQAREELEQLEEELEQARSELEQLEE----ELEELNEQLQAAQAELAQAQEELESLQEEAE-ELQEELEELQKERQ 125

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568914241 1105 ELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYS 1153
Cdd:COG4372   126 DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174

PRK03918

DNA double-strand break repair ATPase Rad50;

1025-1150

3.74e-05

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 3.74e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241 1025 KEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVlEYQARLEEGEERLRRQQEDKDI--QMKGIISRLMSV 1102
Cdd:PRK03918  306 LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK-ELEKRLEELEERHELYEEAKAKkeELERLKKRLTGL 384

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568914241 1103 E-EELKKdhaEMQAAVDSKQKIIDAQEK---RIASLDAANARLMSALTQLKE 1150
Cdd:PRK03918  385 TpEKLEK---ELEELEKAKEEIEEEISKitaRIGELKKEIKELKKAIEELKK 433

Name

Accession

Description

Interval

E-value

DUF3498

pfam12004

Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...

639-1152

0e+00

Pssm-ID: 463427 [Multi-domain] Cd Length: 511 Bit Score: 674.94 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241   639 LRDVHTALSTPGSGQLPG--TNDLASTPGSGSSSVSAGLQKMVIENDLsGLIDFTRLPSPTPENKDLFFVTRSSGVQPSP 716
Cdd:pfam12004    1 LRDITTALTNPTPIQQQLrrFSEHSSSPPVPGRSISSGLQKMFEDPDD-GLSDFTRLPSPTPENKDLFFVTRPPLLQPSP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241   717 ARSSSYSEANEPDLQMANGSKSLSMVDLQDARTLDGEAgSPVGPDALPADGQVPATQLLAG---WPARAAPVSLAGLATV 793
Cdd:pfam12004   80 ARSSSYSDANEPDQQLPNGNKSLSMVDLQDSRSLQGSP-SPPLHDAPLNLSQAGSQASVGLrpaWAARTSQGNPQSAPQV 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241   794 RRAVPTPTTPGTSEgapgrPQLLAPLSFQNPVYQMAAGLPLSPRGLG--DSGSEGHSSLSSHSNSEELAAAAK----LGS 867
Cdd:pfam12004  159 RRPLQTPVTQGTRP-----QQLLAPLSFQNPVYHMAAGLPVSPRGLGspDSSSETHSSFSSHSNSEDLSSAAAnkksGPS 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241   868 FSTAAEELARRPGELARRQMSLTEKGGQPTVPRQNSAGPQRRIDQPPPPPPPPPPAPRGRtppTLLSTLQYPRPSSGTLA 947
Cdd:pfam12004  234 NSSYSEDFARRSTEFTRRQLSLTELQHQPAVPRQNSAGPQRRIDQQGLGGPPLTRGRTPP---SLLNSASYPRPSSGSLM 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241   948 SASPDWagPGTRLRQQSSSSKGDSPELKPRAMHKQGPSPVSPNALD---RTAAWLLTMNAQLLEDEGLGPDpphrdrlrS 1024
Cdd:pfam12004  311 SSSPDW--PPARLRQQSSSSKGDSPETKQRTQHQQVPSPVNPSTLSpveRTAAWVLNMNGQYEEEESSGPE--------S 380

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  1025 KEELSQAEK---DLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVLEYQARLEEGEERLRRQQEDKDIQMKGIISRLMS 1101
Cdd:pfam12004  381 REELKQAEKyeqEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMA 460

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568914241  1102 VEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERY 1152
Cdd:pfam12004  461 VEEELKKDHAEMQAVIDSKQKIIDAQEKRIASLDAANARLMSALTQLKERY 511

RasGAP_DAB2IP

cd05136

Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...

326-649

0e+00

Pssm-ID: 213338 Cd Length: 324 Bit Score: 616.90 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  326 RYQTVSILPMEMYKEFAEHITNHYLGLCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCgDNEHLIF 405
Cdd:cd05136     1 RYQSVDILPLEVYKEFLEYLTNNYLDLCEVLEPVLSVKAKEELATALVHILQSTGKAKEFLTDLVMAEVDRL-DDEHLIF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  406 RENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCS-SADLPEHQGNLKMCCELAFCKIINSYCVFPR 484
Cdd:cd05136    80 RGNTLATKAMEAYLKLVGQKYLQETLGEFIRALYESEEDCEVDPSKCPpSASLSRNQANLRRSVELAWCKILSSHCVFPR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  485 ELKEVFASWRQECSSRGRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGSKE 564
Cdd:cd05136   160 ELREVFSSWRERLEERGREDIADRLISASLFLRFLCPAILSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  565 EYMSFMNQFLEHEWTNMQRFLLEISNPETLSNTAGFEGYIDLGRELSSLHSLLWEAVSQLDQSVVSKLGPLPRILRDVHT 644
Cdd:cd05136   240 EYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITE 319


                  ....*
gi 568914241  645 ALSTP 649
Cdd:cd05136   320 ALRNP 324

PH_DAB2IP

cd13376

DOC-2/Disabled homolog 2-interacting protein Pleckstrin homology (PH) domain; DAB2IP (also ...

68-254

4.06e-115

Pssm-ID: 270179 Cd Length: 182 Bit Score: 355.17 E-value: 4.06e-115

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241   68 VTGFLSRRLKGSIKRTKSQPKLDRNHSFRHILPGFRSAaaaaaDNERSHLMPRLKESRSHESLLSPSSAVEALDLSMEEE 147
Cdd:cd13376     1 VTGFLSRRLKGSIKRTKSQPKLDRNSSFRHILPGFRSV-----DNERSHLMPRLKESRSHESLLSPSSAVEALDLSMEEE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  148 VIIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRVEHILKLWVIEAKDLPAKKKYLCE 227
Cdd:cd13376    76 VVIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRVENMLKLWIIEAKDLPAKKKYLCE 155

                         170       180
                  ....*....|....*....|....*..
gi 568914241  228 LCLDDVLYARTTSKLKTDNVFWGEHFE 254
Cdd:cd13376   156 LCLDDVLYARTTCKLKTDNVFWGEHFE 182

RasGAP

smart00323

GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...

321-639

9.01e-113

Pssm-ID: 214617 Cd Length: 344 Bit Score: 355.08 E-value: 9.01e-113

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241    321 IRIKARYQTVSILPMEMYKEFAEHITNHYLG-LCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCgD 399
Cdd:smart00323    9 LRLKTVYTTDFILPSEYYEELLELLLFSLDLsLASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRALIDPEVERT-D 87

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241    400 NEHLIFRENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCSSADLPEHQGNLKMCCELAFCKIINSY 479
Cdd:smart00323   88 DPNTIFRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEGEDLETNLENLLQYVERLFDAIINSS 167

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241    480 CVFPRELKEVFASWRQECSSR-GRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFA 558
Cdd:smart00323  168 DRLPYGLRDICKQLRQAAEKRfPDADVIYKAVSSFVFLRFFCPAIVSPKLFNLVDEHPDPTTRRTLTLIAKVLQNLANLS 247

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241    559 KFGSKEEYMSFMNQFLEHEWTNMQRFLLEISNPETLSNTAGFEGYIDLGRELSSLHSLLWEAVSQLDQsVVSKLGPLPRI 638
Cdd:smart00323  248 EFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEILVDKVSDSTTISGRELSLLHSLLLENGDALKR-ELNNEDPLGKL 326


                    .
gi 568914241    639 L 639
Cdd:smart00323  327 L 327

PH_SynGAP

cd13375

Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain; SynGAP is a member of ...

60-254

5.37e-103

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: 322.80 E-value: 5.37e-103

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241   60 PSAstPFRVT-GFLSRRLKGSIKRTKSQPKLDRNHSFRHILPGFRSAaaaaaDNERSHLMPRLKESRSHESLLSPSSAVE 138
Cdd:cd13375     1 PTA--PFRPSqGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSA-----DHDRARLMQSFKESHSHESLLSPSSAAE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  139 ALDLSMEEEVIIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRVEHILKLWVIEAKDL 218
Cdd:cd13375    74 ALDLNLDEDSIIKPVHSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEAREL 153

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 568914241  219 PAKKKYLCELCLDDVLYARTTSKLKTDNVFWGEHFE 254
Cdd:cd13375   154 PPKKRYYCELCLDDMLYARTTSKPRTDTVFWGEHFE 189

C2_SynGAP_like

cd04013

C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and ...

196-335

4.29e-80

Pssm-ID: 175980 [Multi-domain] Cd Length: 146 Bit Score: 258.78 E-value: 4.29e-80

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  196 PNKDNSRRVEHILKLWVIEAKDLPAKKKYLCELCLDDVLYARTTSKLKTDNVFWGEHFEFHNLPPLRTVTVHLYRETDKK 275
Cdd:cd04013     1 PNRDNSRRTENSLKLWIIEAKGLPPKKRYYCELCLDKTLYARTTSKLKTDTLFWGEHFEFSNLPPVSVITVNLYRESDKK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568914241  276 KKKERNSYLGLVSLPAASVAGRQFVEKWYPVVTPNP------KGGKGPGPMIRIKARYQTVSILPM 335
Cdd:cd04013    81 KKKDKSQLIGTVNIPVTDVSSRQFVEKWYPVSTPKGngksggKEGKGESPSIRIKARYQSTRVLPL 146

RasGAP

cd04519

Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...

338-590

2.16e-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: 247.02 E-value: 2.16e-74

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  338 YKEFAEHITNHYLGLCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCgDNEHLIFRENTLATKAIEE 417
Cdd:cd04519     3 YRLLSLLLTESPLALLRELSQVLPVKDKEEVATALLRIFESRGLALEFLRYLVRSEVKNT-KNPNTLFRGNSLATKLLDQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  418 YLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCSSADLPEHQGNLKMCCELAFCKIINSYCVFPRELKEVFASWRQEC 497
Cdd:cd04519    82 YMKLVGQEYLKETLSPLIREILESKESCEIDTKLPVGEDLEENLENLLELVNKLVDRILSSLDRLPPELRYVFKILREFL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  498 SSR--GRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGSKEEYMSFMNQFLE 575
Cdd:cd04519   162 AERfpEEPDEAYQAVSGFLFLRFICPAIVSPELFGLVPDEPSEQARRNLTLISKVLQSLANGVEFGDKEPFMKPLNDFIK 241

                         250
                  ....*....|....*
gi 568914241  576 HEWTNMQRFLLEISN 590
Cdd:cd04519   242 SNKPKLKQFLDELSS 256

PH_nGAP

cd13373

Neuronal growth-associated proteins Pleckstrin homology (PH) domain; nGAP (also called RASAL2 ...

65-210

2.71e-61

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: 205.35 E-value: 2.71e-61

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241   65 PFRVTGFLSRRLKGSIKRTKSQPKLDRNHSFRhiLPGFRSAaaaaadNERSHLMPRLKESRSHESLLSPSSAVEALDLSM 144
Cdd:cd13373     1 PFKVSGFFSKRLKGSIKRTKSQSKLDRNTSFR--LPSLRSA------DDRSRGLPKLKESRSHESLLSPGSAVEALDLGR 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568914241  145 EEEVIIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRVEHILKL 210
Cdd:cd13373    73 EEKVSVKPLHSSILGQDFCFEVTYSSGSKCFSCSSAAERDKWMENLRRTVQPNKDNCRRAENVLRL 138

PH_RasSynGAP-like

cd13262

Synaptic Ras-GTPase activating protein family Pleckstrin homology (PH) domain; The RasSynGAP ...

68-204

2.04e-58

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: 196.88 E-value: 2.04e-58

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241   68 VTGFLSRRLKGSIKRTKSQPKLDRNHSFRhiLPGFRSAaaaaadneRSHLMPRLKESRSHESLLSPSSAveALDLSMEEE 147
Cdd:cd13262     1 ASGFFSRRLKGPLKRTKSVTKLERKSSKR--LPRTRLA--------RAPAGPRLRGSRSHESLLSSSSA--ALDLSADED 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568914241  148 VIIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRV 204
Cdd:cd13262    69 VVIRPLHSSILGRKHCFQVTTSEGTRCFSCRSAAERDRWIEDLRRAAQPNKDNCRRT 125

RasGAP_CLA2_BUD2

cd05137

Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein ...

324-575

1.69e-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: 1.69e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  324 KARYQTVSILPMEMYKEFAEHITNHYLGLCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVD-------- 395
Cdd:cd05137     1 KVRLDENVVLPSKNYKPLEELLHNFDLGLTLQIAELVPGDKLERLSEILLDIFQASGREDEWFMALVEDEIDgidkstsk 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  396 -----RCGDNEH-LIFRENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCSSA-------DLPEHQG 462
Cdd:cd05137    81 nkdmgKSSNNEAnLLFRGNSLLTKSLEKYMRRIGKEYLEKSIGDVIRKICEENKDCEVDPSRVKESdsiekeeDLEENWE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  463 NLKMCCELAFCKIINSYCVFPRELKEVFASWRQECSSRGRPDISE-RL--ISASLFLRFLCPAIMSPSLFNLLQEYPDDR 539
Cdd:cd05137   161 NLISLTEEIWNSIYITSNDCPPELRKILKHIRAKVEDRYGDFLRTvTLnsVSGFLFLRFFCPAILNPKLFGLLKDHPRPR 240

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 568914241  540 TARTLTLIAKVTQNLANFAKFGSKEEYMSFMNQFLE 575
Cdd:cd05137   241 AQRTLTLIAKVLQNLANLTTFGQKEPWMEPMNEFLT 276

RasGAP_GAP1_like

cd05128

Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras ...

351-591

1.27e-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: 180.14 E-value: 1.27e-50

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  351 GLCAALEPILSAKtKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCGDnEHLIFRENTLATKAIEEYLKLVGQKYLQDA 430
Cdd:cd05128    22 SAVYLLEELVKVD-KDDVARPLVRIFLHHGQIVPLLRALASREISKTQD-PNTLFRGNSLASKCMDEFMKLVGMQYLHET 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  431 LGEFIKALYESDENCEVDPSKCSSADLPE-HQGNLKMCCELAFCKIINSYCVFPRELKEVFASWRQECSSR--GRPDISE 507
Cdd:cd05128   100 LKPVIDEIFSEKKSCEIDPSKLKDGEVLEtNLANLRGYVERVFKAITSSARRCPTLMCEIFSDLRESAAQRfpDNEDVPY 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  508 RLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGS----KEEYMS-FMNQFL-EHEWTNM 581
Cdd:cd05128   180 TAVSGFIFLRFFAPAILNPKLFGLREEHPDPQTARTLTLISKTIQTLGNLGSSSSglgvKEAYMSpLYERFTdEQHVDAV 259

                         250
                  ....*....|
gi 568914241  582 QRFLLEISNP 591
Cdd:cd05128   260 KKFLDRISSV 269

RasGAP_Neurofibromin_like

cd05392

Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins ...

334-630

2.78e-46

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: 169.00 E-value: 2.78e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  334 PMEMYKEFAEHITNHYLGLCAALEpILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCgDNEHLIFRENTLATK 413
Cdd:cd05392     2 KSEAYDELLELLIEDPQLLLAIAE-VCPSSEVDLLAQSLLNLFETRNRLLPLISWLIEDEISHT-SRAADLFRRNSVATR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  414 AIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCSSADLPEHQGNLKMCCELAFCKIINSYCVFPRELKEVFASW 493
Cdd:cd05392    80 LLTLYAKSVGNKYLRKVLRPLLTEIVDNKDYFEVEKIKPDDENLEENADLLMKYAQMLLDSITDSVDQLPPSFRYICNTI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  494 RQECSSRgRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGSKEEYMSFMNQF 573
Cdd:cd05392   160 YESVSKK-FPDAALIAVGGFLFLRFICPAIVSPESENLLDPPPTPEARRSLILIAKVLQNIANGVLFSLKEPYLESLNEF 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568914241  574 LEHEWTNMQRFLLEISNPETLSNTAGFEGYIDLGRELSSLHSLLWEAVSQLDQSVVS 630
Cdd:cd05392   239 LKKNSDRIQQFLSEVSTIPPTDPIFDESDEEPITADLRYLHKFLYLHFLEIRKEVLK 295

RasGAP_p120GAP

cd05391

Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates ...

332-616

3.06e-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: 160.73 E-value: 3.06e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  332 ILPMEMYKEFAEHITNHYLGLCAALEPiLSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRcGDNEHLIFRENTLA 411
Cdd:cd05391     4 IMPEEEYSELKELILQKELHVVYALAH-VCGQDRTLLASILLRIFRHEKLESLLLRTLNDREISM-EDEATTLFRATTLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  412 TKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCSSADlpEHQGNLKMCCELAFC---KIINSYCVFPRELKE 488
Cdd:cd05391    82 STLMEQYMKATATPFVHHALKDTILKILESKQSCELNPSKLEKNE--DVNTNLEHLLNILSElveKIFMAAEILPPTLRY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  489 VFaSWRQECSSRGRPD---ISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGSKEE 565
Cdd:cd05391   160 IY-GCLQKSVQQKWPTnttVRTRVVSGFVFLRLICPAILNPRMFNIISETPSPTAARTLTLVAKSLQNLANLVEFGAKEP 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568914241  566 YMSFMNQFLEHEWTNMQRFLLEISN-PETLSNTAGFEGyiDLGRELSSLHSL 616
Cdd:cd05391   239 YMEGVNPFIKKNKERMIMFLDELGNvPELPDTTEHSRT--DLSRDLAALHEI 288

RasGAP_RASA3

cd05134

Ras-GTPase Activating Domain of RASA3; RASA3 (or GAP1_IP4BP) is a member of the GAP1 family ...

363-590

7.71e-39

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: 145.94 E-value: 7.71e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  363 KTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCGDnEHLIFRENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESD 442
Cdd:cd05134    33 REKQEAAIPLVRLFLHYGKIVPFISAIASAEVNRTQD-PNTIFRGNSLTSKCIDETMKLAGMHYLQVTLKPIIDEICQEH 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  443 ENCEVDPSKCS-SADLPEHQGNLKMCCELAFCKIINSYCVFPRELKEVFASWRQECSSR--GRPDISERLISASLFLRFL 519
Cdd:cd05134   112 KPCEIDPVKLKdGENLENNRENLRQYVDRIFRVITKSGVSCPTVMCDIFFSLRESAAKRfqVDPDVRYTAVSSFIFLRFF 191

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568914241  520 CPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGS---KEEYM-SFMNQFLEHEWTN-MQRFLLEISN 590
Cdd:cd05134   192 APAILSPNLFQLTPHHPDPQTSRTLTLISKTIQTLGSLSKSKSanfKESYMaAFYDYFNEQKYADaVKNFLDLISS 267

RasGAP_Neurofibromin

cd05130

Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the ...

367-619

1.09e-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: 133.22 E-value: 1.09e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  367 EMASALVHILQSTGKVKDFLTDLMMSEVDRCGDNEHLiFRENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDE--N 444
Cdd:cd05130    41 ELARVLVTLFDSKHLLYQLLWNMFSKEVELADSMQTL-FRGNSLASKIMTFCFKVYGATYLQSLLEPLLRTMITSSEwvS 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  445 CEVDPSKC-SSADLPEHQGNLKMCCELAFCKIINSYCVFPRELKEVFASWRQECSSRGrPDISERLISASLFLRFLCPAI 523
Cdd:cd05130   120 YEVDPTRLeGNENLEENQRNLLQLTEKFFHAIISSSDEFPPQLRSVCHCLYQVVSHRF-PNSGLGAVGSAIFLRFINPAI 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  524 MSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFgSKEEYMSFMNQFLEHEWTNMQRFLLEI-SNPETLSNTAG-FE 601
Cdd:cd05130   199 VSPYEYGILDREPPPRVKRGLKLMSKILQNIANHVLF-TKEAHMLPFNDFLRNHFEAGRRFFSSIaSDCGAVDGPSSkYL 277

                         250
                  ....*....|....*...
gi 568914241  602 GYIDLGrELSSLHSLLWE 619
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 ...

117-219

5.08e-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: 119.35 E-value: 5.08e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  117 LMPRLKESRSHESLL------SPSSAVEA---------LDLSMEEEVIIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAA 181
Cdd:cd13374    25 LLKRLKEKKKAKAEStgtgrdGPPSALGSreslatiseLDLGAERDVRVWPLHPSLLGEPHCFQVTWPGGSRCFSCRSAA 104

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568914241  182 ERDKWMENLRRAVHPNKDNSRRVEHILKLWVIEAKDLP 219
Cdd:cd13374   105 ERDRWIEDLRRSFQPHQDNVEREETWLSVWVHEAKGLP 142

RasGAP_RASAL

cd05135

Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like ...

354-585

8.79e-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: 120.30 E-value: 8.79e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  354 AALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCGDNEHLiFRENTLATKAIEEYLKLVGQKYLQDALGE 433
Cdd:cd05135    29 AMLEEVTTGESRQDVATKLVKIFLGQGLVVPFLDYLNTREVGRTTDPNTL-FRSNSLASKSMEQFMKVVGMPYLHEVLKP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  434 FIKALYESDENCEVDPSK--------------CSSADLPEH-----QGNLKMCCElafcKIINSYCVFPRELKEVFASWR 494
Cdd:cd05135   108 VINRIFEEKKYVELDPCKidlnrtrrisfkgsLSEAQVRESslellQGYLGSIID----AIVGSVDQCPPVMRVAFKQLH 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  495 QECSSR----GRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANF-AKFGS-KEEYMS 568
Cdd:cd05135   184 KRVEERfpeaEHQDVKYLAISGFLFLRFFAPAILTPKLFQLREQHADPRTSRTLLLLAKAVQSIGNLgLQLGQgKEQWMA 263

                         250
                  ....*....|....*..
gi 568914241  569 FMNQFLEHEWTNMQRFL 585
Cdd:cd05135   264 PLHPFILQSVARVKDFL 280

RasGAP_RASA2

cd05394

Ras-GTPase Activating Domain of RASA2; RASA2 (or GAP1(m)) is a member of the GAP1 family of ...

372-592

3.16e-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: 118.46 E-value: 3.16e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  372 LVHILQSTGKVKDFLTDLMMSEVDRCGDnEHLIFRENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSK 451
Cdd:cd05394    42 LVRLLLHHNKLVPFVAAVAALDLKDTQE-ANTIFRGNSLATRCLDEMMKIVGKHYLKVTLKPVLDEICESPKPCEIDPIK 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  452 CSSADLPE-HQGNLKMCCELAFCKIINSYCVFPRELKEVFASWRQECSSR--GRPDISERLISASLFLRFLCPAIMSPSL 528
Cdd:cd05394   121 LKEGDNVEnNKENLRYYVDKVFFSIVKSSMSCPTLMCDVFRSLRHLAVKRfpNDPHVQYSAVSSFVFLRFFAVAVVSPHT 200

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568914241  529 FNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGS------KEEYM-SFMNQFLEHEWT-NMQRFLLEISNPE 592
Cdd:cd05394   201 FQLRPHHPDAQTSRTLTLISKTIQTLGSWGSLSKsklssfKETFMcDFFKMFQEEKYIeKVKKFLDEISSTE 272

RasGAP

pfam00616

GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...

385-556

7.14e-29

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

Pssm-ID: 459871 Cd Length: 207 Bit Score: 115.08 E-value: 7.14e-29

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241   385 FLTDLMMSEVDRCgDNEHLIFRENTLATKAIEEYLKL-VGQKYLQDALGEFIKALYESDE-NCEVDPSK----------- 451
Cdd:pfam00616    1 LISELIEEEIESS-DNPNDLLRGNSLVSKLLETYNRRpRGQEYLKKVLGPLVRKIIEDEDlDLESDPRKiyeslinqeel 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241   452 -CSSADLP-------------------EHQGNLKMCCELAFCKIINSYCVFPREL----KEVFASWRQECssrgrPDISE 507
Cdd:pfam00616   80 kTGRSDLPrdvspeeaiedpevrqifeDNLQKLRELADEFLDAIYSSLNQLPYGIryicKQLYELLEEKF-----PDASE 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568914241   508 R----LISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLAN 556
Cdd:pfam00616  155 EeilnAIGGFLFLRFFCPAIVNPDLFGLVDHQISPKQRRNLTLIAKVLQNLAN 207

RasGAP_RASA4

cd05395

Ras-GTPase Activating Domain of RASA4; Ras GTPase activating-like 4 protein (RASAL4), also ...

352-592

2.78e-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: 2.78e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  352 LCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCGDNEHLiFRENTLATKAIEEYLKLVGQKYLQDAL 431
Cdd:cd05395    27 LISLIDETTTAECRQEVATNLVKLFLGQGLAKEFLDLLFQLELDKTTEPNTL-FRSNSLASKSMESFLKVAGMQYLHSVL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  432 GEFIKALYESDENCEVDPSK-------CSSADLPEHQGN--------LKMCCELAFCKIINSYCVFPRELKEVFASWRQE 496
Cdd:cd05395   106 GPTINRVFEEKKYVELDPSKveikdvgCSGLHRIQTESEvieqsaqlLQSYLGELLSAISKSVKYCPAVIRATFRQLFKR 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  497 CSSRgRPDISER-----LISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGS--KEEYMSF 569
Cdd:cd05395   186 VQER-FPENQHQnvkfiAVTSFLCLRFFSPAIMSPKLFHLREKHADARTSRTLLLLAKAVQNVGNMDTLASraKEAWMAP 264

                         250       260
                  ....*....|....*....|...
gi 568914241  570 MNQFLEHEWTNMQRFLLEISNPE 592
Cdd:cd05395   265 LQPAIQQGVAQLKDFITKLVDIE 287

RasGAP_GAPA

cd05132

Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to ...

406-636

7.80e-25

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: 107.44 E-value: 7.80e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  406 RENTLATKAIEEYLKLV-GQKYLQDALGEFIKALYE-SDENCEVDPSKC-------------------------SSADLP 458
Cdd:cd05132    49 RANTAVSRMMTTYTRRGpGQSYLKTVLADRINDLISlKDLNLEINPLKVyeqmindieldtglpsnlprgitpeEAAENP 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  459 EHQG----NLKMCCELA---FCKIINSYCVFPRELKEVFASWRQECSSRgRPDISER----LISASLFLRFLCPAIMSPS 527
Cdd:cd05132   129 AVQNiiepRLEMLEEITnsfLEAIINSLDEVPYGIRWICKQIRSLTRRK-FPDASDEticsLIGGFFLLRFINPAIVSPQ 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  528 LFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFgSKEEYMSFMNQFLEHEWTNMQRFLLEISNPETLSNTAGFEGYIDLG 607
Cdd:cd05132   208 AYMLVDGKPSDNTRRTLTLIAKLLQNLANKPSY-SKEPYMAPLQPFVEENKERLNKFLNDLCEVDDFYESLELDQYIALS 286

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 568914241  608 R----------ELSSLHSLLWEAVSQLDQS-------VVSKLGPLP 636
Cdd:cd05132   287 KkdlsinitlnEIYNTHSLLVKHLAELAPDhndhlrlILQELGPAP 332

C2A_RasGAP

cd08383

C2 domain (first repeat) of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ...

208-327

1.31e-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: 62.67 E-value: 1.31e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  208 LKLWVIEAKDLPAKKK---YlCELCLDDVLYARTTSKLKTdNVFWGEHFEFHNLPPL---RTVTVHLYretdKKKKKERN 281
Cdd:cd08383     2 LRLRILEAKNLPSKGTrdpY-CTVSLDQVEVARTKTVEKL-NPFWGEEFVFDDPPPDvtfFTLSFYNK----DKRSKDRD 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568914241  282 SYLGLVSLpaASVAGRQFVEKWYPVVTPNPKGGKgPGpMIRIKARY 327
Cdd:cd08383    76 IVIGKVAL--SKLDLGQGKDEWFPLTPVDPDSEV-QG-SVRLRARY 117

cd00030

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...

208-305

5.10e-11

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: 60.54 E-value: 5.10e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  208 LKLWVIEAKDLPAKKK-----YLCELCLDDVLYARTTSKLKTDNVFWGEHFEFHNLPPL-RTVTVHLYretDKKKKKeRN 281
Cdd:cd00030     1 LRVTVIEARNLPAKDLngksdPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLDPEsDTLTVEVW---DKDRFS-KD 76

                          90       100
                  ....*....|....*....|....*
gi 568914241  282 SYLGLVSLPAASVAGR-QFVEKWYP 305
Cdd:cd00030    77 DFLGEVEIPLSELLDSgKEGELWLP 101

C2_Ras_p21A1

cd08400

C2 domain present in RAS p21 protein activator 1 (RasA1); RasA1 is a GAP1 (GTPase activating ...

208-327

1.05e-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: 1.05e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  208 LKLWVIEAKDLPAKK---KYlCELCLDDVLYARTTSKLKTDNVfWGEHFEFHNLPP-LRTVTVHLYretdKKKKKERNSY 283
Cdd:cd08400     6 LQLNVLEAHKLPVKHvphPY-CVISLNEVKVARTKVREGPNPV-WSEEFVFDDLPPdVNSFTISLS----NKAKRSKDSE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568914241  284 LGLVSLPAASVAGRQFVEKWYPVVTPNPKGGKGPGpMIRIKARY 327
Cdd:cd08400    80 IAEVTVQLSKLQNGQETDEWYPLSSASPLKGGEWG-SLRIRARY 122

smart00239

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...

207-303

3.62e-09

Pssm-ID: 214577 [Multi-domain] Cd Length: 101 Bit Score: 55.19 E-value: 3.62e-09

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241    207 ILKLWVIEAKDLPAKKKYL-----CELCLDDVLY--ARTTSKLKTDNVFWGEHFEFH-NLPPLRTVTVHLYretDKKKKK 278
Cdd:smart00239    1 TLTVKIISARNLPPKDKGGksdpyVKVSLDGDPKekKKTKVVKNTLNPVWNETFEFEvPPPELAELEIEVY---DKDRFG 77

                            90       100
                    ....*....|....*....|....*
gi 568914241    279 eRNSYLGLVSLPAASVAGRQFVEKW 303
Cdd:smart00239   78 -RDDFIGQVTIPLSDLLLGGRHEKL 101

pfam00168

C2 domain;

206-306

8.68e-09

C2 domain;

Pssm-ID: 425499 [Multi-domain] Cd Length: 104 Bit Score: 54.25 E-value: 8.68e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241   206 HILKLWVIEAKDLPAKKK------YlCELCLDDVLY-ARTTSKLKTDNVFWGEHFEFH-NLPPLRTVTVHLYretDKKKK 277
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGngtsdpY-VKVYLLDGKQkKKTKVVKNTLNPVWNETFTFSvPDPENAVLEIEVY---DYDRF 76

                           90       100
                   ....*....|....*....|....*....
gi 568914241   278 KeRNSYLGLVSLPAASVAGRQFVEKWYPV 306
Cdd:pfam00168   77 G-RDDFIGEVRIPLSELDSGEGLDGWYPL 104

RasGAP_IQGAP2

cd05131

Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a ...

412-660

2.04e-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: 54.62 E-value: 2.04e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  412 TKAIEEYLKLVGQkyLQDALGEFIKALYE-SDENCEVDPSkcSSADLPEHQGNLKMCCELAFCKIINSYCVFPRELKEVF 490
Cdd:cd05131    87 TNPVEVYKAWVNQ--LETATGEASKLPYDvTTEQALTHPE--VVNKLESSIQSLRSVTDKVLGSIFSSLDLIPYGMRYIA 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  491 ASWRQECSSRgRPDISE----RLISASLFLRFLCPAIMSPSLFNLL------QEYPDDRtaRTLTLIAKVTQNLANFAKF 560
Cdd:cd05131   163 KVLKNSLHEK-FPDATEdellKIVGNLLYYRYMNPAIVAPDGFDIIdmtaggQIHSEQR--RNLGSVAKVLQHAASNKLF 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  561 GSKEEYMSFMNQFLEHEWTNMQRFL---LEISNPETLSNTAGFEGYIDLGR--------ELSSLHSLLWE---AVSQlDQ 626
Cdd:cd05131   240 EGENAHLSSMNSYLSQTYQKFRKFFqaaCDVPEPEEKFNIDEYSDMVTLSKpviyisieEIINTHSLLLEhqdAIAP-DQ 318

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 568914241  627 S-----VVSKLGPLPrilrDVHTALstpGSGQLpGTNDL 660
Cdd:cd05131   319 NdllheLLKDLGEVP----DVESFL---GEGTV-DPNDP 349

smart00233

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...

142-195

2.67e-06

Pssm-ID: 214574 [Multi-domain] Cd Length: 102 Bit Score: 47.16 E-value: 2.67e-06

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 568914241    142 LSMEEEVIIKPVHSSILGQDYCFEVTTSSG-SKCFSCRSAAERDKWMENLRRAVH 195
Cdd:smart00233   48 IDLSGCTVREAPDPDSSKKPHCFEIKTSDRkTLLLQAESEEEREKWVEALRKAIA 102

RasGAP_IQGAP_like

cd05127

Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family ...

514-641

3.68e-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: 3.68e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  514 LFLRFLCPAIMSPSLFNLLQEYPDDRTA----RTLTLIAKVTQNLANFAKFGSKEEYMSFMNQFLEHEWTNMQRFLLEIS 589
Cdd:cd05127   179 LYYRYMNPAIVAPEAFDIIDLSVGGQLSplqrRNLGSIAKVLQQAASGKLFGGENPYLSPLNPYISESHEKFKKFFLEAC 258

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568914241  590 NPETLSNTAGFEGYIDLG-----------RELSSLHSLLWEavsQLDQSVVSKLGPLPRILRD 641
Cdd:cd05127   259 TVPEAEEHFNIDEYSDLTmltkptiyislQEIFATHKLLLE---HQDEIAPDPDDPLRELLDD 318

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

1013-1152

3.88e-06

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 3.88e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  1013 GPDPPHRDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLF-----------KCQEETTQKLVLEYQ--ARLEEGEE 1079
Cdd:TIGR02168  664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELeeleeeleqlrKELEELSRQISALRKdlARLEAEVE 743

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568914241  1080 RLRRQQEDKDIQMKGIISRLMSVEEELKKDHAEMQAAVDSKQKI---IDAQEKRIASLDAANARLMSALTQLKERY 1152
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeaqIEQLKEELKALREALDELRAELTLLNEEA 819

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

1025-1153

1.21e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 1.21e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241 1025 KEELSQAEKDLAVLQDKLRISTKKLEEYETlfkcQEETTQKLVLEYQARLEEGEERLRRQQEDKDiQMKGIISRLMSVEE 1104
Cdd:COG4372    51 REELEQAREELEQLEEELEQARSELEQLEE----ELEELNEQLQAAQAELAQAQEELESLQEEAE-ELQEELEELQKERQ 125

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568914241 1105 ELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYS 1153
Cdd:COG4372   126 DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174

C2A_C2C_Synaptotagmin_like

cd08391

C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a ...

206-305

1.22e-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: 45.75 E-value: 1.22e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  206 HILKLWVIEAKDLPAKKKYLCEL--------CLDDVLYARTTSKLKTDNV--FWGEHFEF--HNLPPLrTVTVHLYretD 273
Cdd:cd08391     1 GVLRIHVIEAQDLVAKDKFVGGLvkgksdpyVIVRVGAQTFKSKVIKENLnpKWNEVYEAvvDEVPGQ-ELEIELF---D 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 568914241  274 KKKKKErnSYLGLVSLPAASVAGRQFVEKWYP 305
Cdd:cd08391    77 EDPDKD--DFLGRLSIDLGSVEKKGFIDEWLP 106

Smc

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

1003-1157

1.37e-05

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 1.37e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241 1003 NAQLLEDEGLgpdppHRDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETlfkcQEETTQKLVLEYQARLEEGEERLR 1082
Cdd:COG1196   228 ELLLLKLREL-----EAELEELEAELEELEAELEELEAELAELEAELEELRL----ELEELELELEEAQAEEYELLAELA 298

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568914241 1083 RQQEDKDIQMKGIIsRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYSMQAR 1157
Cdd:COG1196   299 RLEQDIARLEERRR-ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

C2A_MCTP_PRT_plant

cd04022

C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...

212-305

1.37e-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: 45.79 E-value: 1.37e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  212 VIEAKDLPAKKKY-----LCELCLDDVLYaRTTSKLKTDNVFWGEHFEF--HNLPPLRTVTVHLYRETDKKKKKeRNSYL 284
Cdd:cd04022     6 VVDAQDLMPKDGQgsssaYVELDFDGQKK-RTRTKPKDLNPVWNEKLVFnvSDPSRLSNLVLEVYVYNDRRSGR-RRSFL 83

                          90       100
                  ....*....|....*....|..
gi 568914241  285 GLVSLPAASVAGRQ-FVEKWYP 305
Cdd:cd04022    84 GRVRISGTSFVPPSeAVVQRYP 105

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

1023-1156

3.06e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 3.06e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241 1023 RSKEELSQAEKDLAVLQDKLRISTKKLEEYETLfkcQEETTQKLvleyqARLEEGEERLRRQQEdkdiQMKGIISRLMSV 1102
Cdd:COG4372    63 QLEEELEQARSELEQLEEELEELNEQLQAAQAE---LAQAQEEL-----ESLQEEAEELQEELE----ELQKERQDLEQQ 130

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568914241 1103 EEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYSMQA 1156
Cdd:COG4372   131 RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA 184

RasGAP_IQGAP1

cd05133

Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a ...

503-606

3.20e-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: 3.20e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  503 PDISE----RLISASLFLRFLCPAIMSPSLFNLL------QEYPDDRtaRTLTLIAKVTQNLANFAKFGSKEEYMSFMNQ 572
Cdd:cd05133   174 PDAGEdellKIVGNLLYYRYMNPAIVAPDAFDIIdlsaggQLTTDQR--RNLGSIAKMLQHAASNKMFLGDNAHLSPINE 251

                          90       100       110
                  ....*....|....*....|....*....|....
gi 568914241  573 FLEHEWTNMQRFLLEISNPETLSNTAGFEGYIDL 606
Cdd:cd05133   252 YLSQSYQKFRRFFQAACDVPELEDKFNVDEYSDL 285

Smc

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

1025-1150

3.45e-05

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 3.45e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241 1025 KEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVLEyQARLEEGEERLRRQQEDKDIQMKGIISRLMSVEE 1104
Cdd:COG1196   273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER-LEELEEELAELEEELEELEEELEELEEELEEAEE 351

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568914241 1105 ELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKE 1150
Cdd:COG1196   352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397

PRK03918

DNA double-strand break repair ATPase Rad50;

1025-1150

3.74e-05

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 3.74e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241 1025 KEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVlEYQARLEEGEERLRRQQEDKDI--QMKGIISRLMSV 1102
Cdd:PRK03918  306 LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK-ELEKRLEELEERHELYEEAKAKkeELERLKKRLTGL 384

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568914241 1103 E-EELKKdhaEMQAAVDSKQKIIDAQEK---RIASLDAANARLMSALTQLKE 1150
Cdd:PRK03918  385 TpEKLEK---ELEELEKAKEEIEEEISKitaRIGELKKEIKELKKAIEELKK 433

DR0291

COG1579

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

1020-1151

3.78e-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: 46.46 E-value: 3.78e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241 1020 DRLRSK-----EELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQE---ETTQKLVLEYQARLEEG------------EE 1079
Cdd:COG1579    20 DRLEHRlkelpAELAELEDELAALEARLEAAKTELEDLEKEIKRLEleiEEVEARIKKYEEQLGNVrnnkeyealqkeIE 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568914241 1080 RLRRQQEDKDIQMKGIISRLmsveEELKKDHAEMQAAVDSKQKIIDAQEKRiasLDAANARLMSALTQLKER 1151
Cdd:COG1579   100 SLKRRISDLEDEILELMERI----EELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAE 164

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

1020-1158

4.59e-05

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 4.59e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  1020 DRLRS-KEELSQAEKDLAVLQDKLRISTKKLEEYETLF----------KCQEETTQKLVLEYQARLEEGEERLRRQQE-- 1086
Cdd:TIGR02168  232 LRLEElREELEELQEELKEAEEELEELTAELQELEEKLeelrlevselEEEIEELQKELYALANEISRLEQQKQILRErl 311

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568914241  1087 ---DKDIQMK-GIISRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYSMQARN 1158
Cdd:TIGR02168  312 anlERQLEELeAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387

RasGAP_IQGAP3

cd12207

Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 3; This family ...

514-651

6.71e-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: 46.36 E-value: 6.71e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  514 LFLRFLCPAIMSPSLFNLLQE------YPDDRtaRTLTLIAKVTQNLANFAKFGSKEEYMSFMNQFLEHEWTNMQRFLLE 587
Cdd:cd12207   189 LYYRFMNPAVVAPDGFDIVDCsaggalQPEQR--RMLGSVAKVLQHAAANKHFQGDSEHLQALNQYLEETHVKFRKFILQ 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  588 ---ISNPETLSNTAGFEG---------YIDLGrELSSLHSLLWEAVSQL--DQS-----VVSKLGPLPRILRDVHTALST 648
Cdd:cd12207   267 accVPEPEERFNVDEYSEmvavakpviYITVG-ELINTHKLLLEHQDSIapDHSdplheLLEDLGEVPTVQSLIGESWAD 345


                  ...
gi 568914241  649 PGS 651
Cdd:cd12207   346 LGD 348

C2A_Rasal1_RasA4

cd04054

C2 domain first repeat present in RasA1 and RasA4; Rasal1 and RasA4 are both members of GAP1 ...

212-303

3.17e-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: 41.73 E-value: 3.17e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  212 VIEAKDLPAK-----KKYLCELCLDDVLYARTTSKLKTDNVFWGEHFEFHNLPPLRTVTVHLYREtdkkKKKERNSYLGL 286
Cdd:cd04054     6 IVEGKNLPAKditgsSDPYCIVKVDNEVIIRTATVWKTLNPFWGEEYTVHLPPGFHTVSFYVLDE----DTLSRDDVIGK 81

                          90
                  ....*....|....*...
gi 568914241  287 VSLPAASVAGR-QFVEKW 303
Cdd:cd04054    82 VSLTREVISAHpRGIDGW 99

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

1024-1150

4.90e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 4.90e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241 1024 SKEELSQAEKDLAVLQDKLRISTKKLEEYET--------LFKCQEE--TTQKLVLEYQARLEEGEERLRRQQEdkdiQMK 1093
Cdd:COG4372    29 LSEQLRKALFELDKLQEELEQLREELEQAREeleqleeeLEQARSEleQLEEELEELNEQLQAAQAELAQAQE----ELE 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568914241 1094 GIISRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKE 1150
Cdd:COG4372   105 SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

1019-1143

8.77e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 8.77e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241 1019 RDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVLEYQaRLEEGEERLRRQQEDKDIQMKGIISR 1098
Cdd:COG4372    73 SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ-DLEQQRKQLEAQIAELQSEIAEREEE 151

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568914241 1099 LMSVEEELKKDHAEMQAAVDSKQKIIDAQ-EKRIASL-DAANARLMS 1143
Cdd:COG4372   152 LKELEEQLESLQEELAALEQELQALSEAEaEQALDELlKEANRNAEK 198

Smc

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

1025-1151

9.65e-04

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 9.65e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241 1025 KEELSQAEKDLAVLQDKLRisTKKLEEYETlfkcQEETTQKLVLEYQARLEEGEERLRRQQEDkdiqmkgiISRLMSVEE 1104
Cdd:COG1196   219 KEELKELEAELLLLKLREL--EAELEELEA----ELEELEAELEELEAELAELEAELEELRLE--------LEELELELE 284

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568914241 1105 ELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKER 1151
Cdd:COG1196   285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331

DR0291

COG1579

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

1019-1151

9.68e-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: 42.22 E-value: 9.68e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241 1019 RDRL-RSKEELSQAEKDLAVLQDKLRISTKKLEEYETLfkcQEE-TTQKlvlEYQARLEEgEERLRRQQEDKDIQMKGII 1096
Cdd:COG1579    44 EARLeAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ---LGNvRNNK---EYEALQKE-IESLKRRISDLEDEILELM 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568914241 1097 SRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKER 1151
Cdd:COG1579   117 ERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171

RasGAP_RAP6

cd05129

Ras-GTPase Activating Domain of Rab5-activating protein 6; Rab5-activating protein 6 (RAP6) is ...

418-632

1.12e-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: 42.71 E-value: 1.12e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  418 YLKLVGQKYLQDALGEFIKALYESDE-NCEVDPSKC-------------SSADLPEHQGNLKMCCE------LAFCKII- 476
Cdd:cd05129   104 ELLFSAKLYLTAALHKPIMQVLVDDEiFLETDPQKAlcrfspaeqekrfGEEGTPEQQRKLQQYRAeflsrlVALVNKFi 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  477 -----NSYCvFPRELKE-VFASWRQECSSRGRPDISERLISASL-FLRFLCPAIMSPSLFNLLQEYPDDRTAR-TLTLIA 548
Cdd:cd05129   184 sslrqSVYC-FPQSLRWiVRQLRKILTRSGDDEEAEARALCTDLlFTNFICPAIVNPEQYGIISDAPISEVARhNLMQVA 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  549 KVTQNLAnFAKFGSKE-EYMSFMNQFLEHEWTNMQRFLLE----------ISNPETLSNTAGFEGYIDLGRELSSLHSLL 617
Cdd:cd05129   263 QILQVLA-LTEFESPDpRLKELLSKFDKDCVSAFLDVVIVgravetpppsSSALLEGSRTAVLITESDLATLVEFLRSVK 341

                         250
                  ....*....|....*
gi 568914241  618 WEAVSQLDQSVVSKL 632
Cdd:cd05129   342 TGDEEKEDQMALDNL 356

YhaN

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

1033-1161

1.14e-03

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.14e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241 1033 KDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVlEYQARLEEGEERLRRQqeDKDIQMKGIISRLMSVEEELKKDHAE 1112
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELE-ELEAELEELREELEKL--EKLLQLLPLYQELEALEAELAELPER 147

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568914241 1113 MQAAVDSKQKIIDAQEkRIASLDAANARLMSALTQLKERYSMQARNGVS 1161
Cdd:COG4717   148 LEELEERLEELRELEE-ELEELEAELAELQEELEELLEQLSLATEEELQ 195

C2A_RasA2_RasA3

cd08401

C2 domain first repeat present in RasA2 and RasA3; RasA2 and RasA3 are GAP1s (GTPase ...

210-306

1.17e-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: 40.11 E-value: 1.17e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  210 LWVI-EAKDLPAKKK------YLCELCLDDVLYARTTSKLKTDNVFWGEHFEFHNLPPLRTVTVHLYretdKKKKKERNS 282
Cdd:cd08401     3 KIKIgEAKNLPPRSGpnkmrdCYCTVNLDQEEVFRTKTVEKSLCPFFGEDFYFEIPRTFRHLSFYIY----DRDVLRRDS 78

                          90       100
                  ....*....|....*....|....
gi 568914241  283 YLGLVSLPAASVAGRQFVEKWYPV 306
Cdd:cd08401    79 VIGKVAIKKEDLHKYYGKDTWFPL 102

Caldesmon

pfam02029

Caldesmon;

959-1174

1.39e-03

Caldesmon;

Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.55 E-value: 1.39e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241   959 RLRQ-QSSSSKGDSPELKPRAMHKQGPS-----PVSPNALDRTAAWLLTMnaQLLEDeglgpdpphRDRLRSKEELS-QA 1031
Cdd:pfam02029   19 RRRQkEEEEPSGQVTESVEPNEHNSYEEdselkPSGQGGLDEEEAFLDRT--AKREE---------RRQKRLQEALErQK 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  1032 EKDLAVLQDKLRISTKK----LEEYET----------LFKCQEETTQKLVLEYQARL---------EEGEERLRRQQEDK 1088
Cdd:pfam02029   88 EFDPTIADEKESVAERKenneEEENSSwekeekrdsrLGRYKEEETEIREKEYQENKwstevrqaeEEGEEEEDKSEEAE 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  1089 DIQmkgiisRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYSMQARNGVSPTNPTKL 1168
Cdd:pfam02029  168 EVP------TENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAE 241


                   ....*.
gi 568914241  1169 QITENG 1174
Cdd:pfam02029  242 VFLEAE 247

YhaN

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

1026-1141

1.40e-03

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 1.40e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241 1026 EELSQAEKDLAVLQDKLRISTKKLEEYETLfkcqEETTQKLvleyQARLEEGEERLRRQQEDKDIQMKGIISRLMSVEEE 1105
Cdd:COG4717   132 QELEALEAELAELPERLEELEERLEELREL----EEELEEL----EAELAELQEELEELLEQLSLATEEELQDLAEELEE 203

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568914241 1106 LKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARL 1141
Cdd:COG4717   204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239

YhaN

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

999-1152

2.10e-03

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.10e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  999 LLTMNAQLLEDEGLGPDPPHRDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLFkcQEETTQKLVLEYQARLEEGE 1078
Cdd:COG4717   368 LEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL--DEEELEEELEELEEELEELE 445

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568914241 1079 ERLRRQQEDKdIQMKGIISRLMSvEEELkkdhAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERY 1152
Cdd:COG4717   446 EELEELREEL-AELEAELEQLEE-DGEL----AELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513

SMC_prok_A

TIGR02169

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

999-1155

2.25e-03

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

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 2.25e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241   999 LLTMNAQLLEDEGL---GPDPPHRDRLRSKEELSQAEKdlavLQDKLristKKLE-EYETLFKCQEETtQKLVLEYQARL 1074
Cdd:TIGR02169  641 MVTLEGELFEKSGAmtgGSRAPRGGILFSRSEPAELQR----LRERL----EGLKrELSSLQSELRRI-ENRLDELSQEL 711

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  1075 EEGEERLRRQQedKDIQM-KGIISRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYS 1153
Cdd:TIGR02169  712 SDASRKIGEIE--KEIEQlEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS 789


                   ..
gi 568914241  1154 MQ 1155
Cdd:TIGR02169  790 HS 791

SMC_prok_A

TIGR02169

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

1023-1172

2.49e-03

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 2.49e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  1023 RSKEELSQAEKDLAVLQ----------DKLRISTKKLEEYETLFKCQEETTQKLVL-EYQARLEEGE------ERLRRQQ 1085
Cdd:TIGR02169  174 KALEELEEVEENIERLDliidekrqqlERLRREREKAERYQALLKEKREYEGYELLkEKEALERQKEaierqlASLEEEL 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  1086 EDKDIQMKGIISRLMSVEEELKKDHAEMQAAVDSKQKIIdaqEKRIASLDAANARLMSALTQLK---ERYSMQARNGVSP 1162
Cdd:TIGR02169  254 EKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRV---KEKIGELEAEIASLERSIAEKErelEDAEERLAKLEAE 330

                          170
                   ....*....|
gi 568914241  1163 TNPTKLQITE 1172
Cdd:TIGR02169  331 IDKLLAEIEE 340

C2_plant_PLD

cd04015

C2 domain present in plant phospholipase D (PLD); PLD hydrolyzes terminal phosphodiester bonds ...

284-327

2.52e-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: 2.52e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568914241  284 LGLVSLPAASVAGRQFVEKWYPVVTPNPKGGKgPGPMIRIKARY 327
Cdd:cd04015   115 IGRAYIPVEDLLSGEPVEGWLPILDSNGKPPK-PGAKIRVSLQF 157

Smc

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

1019-1151

3.11e-03

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 3.11e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241 1019 RDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVLEYQARLEEGEERLRRQQEDKDIQMkgiisR 1098
Cdd:COG1196   316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL-----E 390

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568914241 1099 LMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKER 1151
Cdd:COG1196   391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443

GOLGA2L5

pfam15070

Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ...

992-1114

3.30e-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: 41.59 E-value: 3.30e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241   992 LDRTAAWLLTMNAQLLEDEGLGPDPPHRDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLfkCQEETTQKLVLEYQ 1071
Cdd:pfam15070   55 LETSLAELKNQAAVPPAEEEQPPAGPSEEEQRLQEEAEQLQKELEALAGQLQAQVQDNEQLSRL--NQEQEQRLLELERA 132

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 568914241  1072 ARLEeGEERLRRQQEDKDIQM-KGIISRLMSVEEELKKDHAEMQ 1114
Cdd:pfam15070  133 AERW-GEQAEDRKQILEDMQSdRATISRALSQNRELKEQLAELQ 175

CwlO1

COG3883

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

1025-1151

3.50e-03

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 3.50e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241 1025 KEELSQAEKDLAVLQDKLRISTKKLEEYETlfkcQEETTQKLVLEYQARLEEGEE----RLRRQQED------------- 1087
Cdd:COG3883    36 QAELDALQAELEELNEEYNELQAELEALQA----EIDKLQAEIAEAEAEIEERREelgeRARALYRSggsvsyldvllgs 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568914241 1088 KDI---------------QMKGIISRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKER 1151
Cdd:COG3883   112 ESFsdfldrlsalskiadADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

1003-1152

3.58e-03

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 3.58e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  1003 NAQLLEDEglgpdpphRDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKL--VLEYQAR----LEE 1076
Cdd:TIGR02168  322 EAQLEELE--------SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELeeQLETLRSkvaqLEL 393

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568914241  1077 GEERLRRQQEDKDIQMKGIISRLMSVEEELKKDHAEMQ-AAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERY 1152
Cdd:TIGR02168  394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEELERLEEALEELREEL 470

HEC1

COG5185

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...

1023-1151

4.50e-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: 41.10 E-value: 4.50e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241 1023 RSKEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVleyqarlEEGEERLRRQQEDKDIQMKGIISRLMSV 1102
Cdd:COG5185   374 KSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAA-------DRQIEELQRQIEQATSSNEEVSKLLNEL 446

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568914241 1103 EEELKKDHAEMQaaVDSKQKIIDAQEKRIASLDAANARLMSALTQLKER 1151
Cdd:COG5185   447 ISELNKVMREAD--EESQSRLEEAYDEINRSVRSKKEDLNEELTQIESR 493

cd00821

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...

142-190

4.97e-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: 4.97e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568914241  142 LSMEEEVIIKPVHSSilGQDYCFEVTTSSGSK-CFSCRSAAERDKWMENL 190
Cdd:cd00821    45 IPLSGILEVEEVSPK--ERPHCFELVTPDGRTyYLQADSEEERQEWLKAL 92

RNase_Y_N

pfam12072

RNase Y N-terminal region;

1020-1113

5.58e-03

RNase Y N-terminal region;

Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 39.48 E-value: 5.58e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241  1020 DRLRSKEE--------LSQAEKDLAVLQDKLRISTKKLEEyetlfkcQEETTQKLVLEYQARLEE--GeerlRRQQEDKD 1089
Cdd:pfam12072   85 RRLLQKEEtldrkdesLEKKEESLEKKEKELEAQQQQLEE-------KEEELEELIEEQRQELERisG----LTSEEAKE 153

                           90       100
                   ....*....|....*....|....
gi 568914241  1090 IQMKgiisrlmSVEEELKKDHAEM 1113
Cdd:pfam12072  154 ILLD-------EVEEELRHEAAVM 170

COG4913

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

1025-1151

7.18e-03

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 7.18e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914241 1025 KEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEEttQKLVLEYQARLEEGEERLRRQQEDKDIqmkgiISRLMSVEE 1104
Cdd:COG4913   623 EEELAEAEERLEALEAELDALQERREALQRLAEYSWD--EIDVASAEREIAELEAELERLDASSDD-----LAALEEQLE 695

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568914241 1105 ELKKDHAEMQAAvdskqkiIDAQEKRIASLDAANARLMSALTQLKER 1151
Cdd:COG4913   696 ELEAELEELEEE-------LDELKGEIGRLEKELEQAEEELDELQDR 735

YhaN