NCBI Conserved Domain Search

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

1191-1302

4.51e-05

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 4.51e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1191 QEKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCD 1270
Cdd:COG1196   238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317

                          90       100       110
                  ....*....|....*....|....*....|..
gi 568948645 1271 LERLRAAQKQLEREQEQLRRDTERLSQRQMDQ 1302
Cdd:COG1196   318 LEELEEELAELEEELEELEEELEELEEELEEA 349

PRK12704

phosphodiesterase; Provisional

1232-1302

4.83e-05

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 4.83e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568948645 1232 LRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAAQKQLEREQEQLRRDTERLSQRQMDQ 1302
Cdd:PRK12704   84 LQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEE 154

SMC_prok_B

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

1134-1289

8.92e-05

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

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 8.92e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  1134 LKRNSEQVVQSIVHLHELLSMLQGVVLQQDSYIED--QKLVLTEKVLTRSASRPSSLIEQEK--QRSLEKQRQDLANLQK 1209
Cdd:TIGR02168  794 LKEELKALREALDELRAELTLLNEEAANLRERLESleRRIAATERRLEDLEEQIEELSEDIEslAAEIEELEELIEELES 873

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  1210 QQAQHLEEKRRREREWEAreqeLRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAaqkQLEREQEQLR 1289
Cdd:TIGR02168  874 ELEALLNERASLEEALAL----LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV---RIDNLQERLS 946

DUF5401

pfam17380

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

1161-1302

1.29e-04

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

Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.66 E-value: 1.29e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  1161 QQDSYIEDQKLVLTEKVLTRSASRPSSLIEQEKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEAREQELRDREAKla 1240
Cdd:pfam17380  355 QEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEA-- 432

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568948645  1241 eREETVRRRQQDLERDREELQQKKGTYQCDLERLRaaQKQLEREQEQLRRDTERLSQRQMDQ 1302
Cdd:pfam17380  433 -RQREVRRLEEERAREMERVRLEEQERQQQVERLR--QQEEERKRKKLELEKEKRDRKRAEE 491

YhaN

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

944-1298

1.49e-03

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.49e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  944 IQIIQDTINSLNRDEDE---GIPSENEEEKKLLDTKARELKEQLQQKDQQILLLLEEKEMIFRDMTECSTPLPedcspth 1020
Cdd:COG4717   165 LEELEAELAELQEELEElleQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE------- 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1021 sprvlfRSNTEEALKGGPLMKSAINEVEILQSLVSGSLGGTLGQSISSPVEQEVMAAPISLPRRAETFGGfdcHQMNASK 1100
Cdd:COG4717   238 ------AAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG---KEAEELQ 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1101 GGEKEEGDDGQDLRRTESDSGLKKGGNGNLVFMLKRNSEQVVQSIVHLHELLSMLQgvvLQQdsyIEDQKLVLTEKVLTR 1180
Cdd:COG4717   309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ---LEE---LEQEIAALLAEAGVE 382

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1181 SASRPSSLIEQEKQRslEKQRQDLANLQKQQAQHLEEKRRREREWEareqelrdrEAKLAEREETVRRRQQDLERDREEL 1260
Cdd:COG4717   383 DEEELRAALEQAEEY--QELKEELEELEEQLEELLGELEELLEALD---------EEELEEELEELEEELEELEEELEEL 451

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 568948645 1261 QQKKGtyqcdleRLRAAQKQLEREQE--QLRRDTERLSQR 1298
Cdd:COG4717   452 REELA-------ELEAELEQLEEDGElaELLQELEELKAE 484

smart00109

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...

411-457

1.61e-03

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.

Pssm-ID: 197519 Cd Length: 50 Bit Score: 37.83 E-value: 1.61e-03

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 568948645    411 HTFSPIPIVGPISCSQCMKP--FTNKDAYTCAGCGAFVHKGCRENLAS-C 457
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSiwGSFKQGLRCSECKVKCHKKCADKVPKaC 50

Name

Accession

Description

Interval

E-value

PH_AKAP13

cd13392

A-kinase anchoring protein 13 Pleckstrin homology (PH) domain; The Rho-specific GEF activity ...

851-953

1.22e-60

Pssm-ID: 275427 Cd Length: 103 Bit Score: 202.45 E-value: 1.22e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  851 LVRDGSVFLKSTTGRLKEVQAVLLTDILVFLQEKDQKYVFASLDHKSTVISLKKLIVREVAHEEKGLFLISMGVKDPEMV 930
Cdd:cd13392     1 LVRDGPVSLKNTAGRLKEVQAVLLSDVLVFLQEKDQKYVFASLDQKSTVISLKKLIVREVAHEEKGLFLISMGIADPEMV 80

                          90       100
                  ....*....|....*....|...
gi 568948645  931 EVHASSREERNSWIQIIQDTINS 953
Cdd:cd13392    81 EVHASSKEERNSWMQIIQDTINT 103

PH_16

pfam17838

PH domain;

835-952

5.58e-50

PH domain;

Pssm-ID: 436083 Cd Length: 127 Bit Score: 172.97 E-value: 5.58e-50

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645   835 MKSGQMFAKEDLRRKKLVRDGSVFLKSTTGRLKEVQAVLLTDILVFLQEKDQKYVFASL-------DHK--STVISLKKL 905
Cdd:pfam17838    1 HPLGEEFKKLDLTTRKLIHEGPLTWRNSKGKLVEVHALLLEDILVLLQEKDQKLVLACLstgsenvDQKtqSPIISLKKL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 568948645   906 IVREVAHEEKGLFLISMGVKDPEMVEVHASSREERNSWIQIIQDTIN 952
Cdd:pfam17838   81 IVREVATDKKAFFLISTSPSDPQMYELHASTKSERNTWTKLIQDAIE 127

RhoGEF

cd00160

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...

614-808

7.52e-46

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.

Pssm-ID: 238091 [Multi-domain] Cd Length: 181 Bit Score: 163.24 E-value: 7.52e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  614 RQEVIYELMQTELHHIRTLKIMSDVYSRGMMTDLL-FEQQMVEKLFPCLDELISIHSQFFQRILERKKESLVDKSeknfl 692
Cdd:cd00160     1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLpLSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWDKSGP----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  693 ikRIGDVLVSQFSgesaerLKKTYGKFCGQHNQSVNYFKDLYTKDKRFQAFVKKKMSSSvvRRLGIPECILLVTQRITKY 772
Cdd:cd00160    76 --RIGDVFLKLAP------FFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAESEC--GRLKLESLLLKPVQRLTKY 145

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 568948645  773 PVLFQRILQCTKDNEVEQEDLTQSLSLVKDVIGAVD 808
Cdd:cd00160   146 PLLLKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181

PH_ARHGEF18

cd15794

Rho guanine nucleotide exchange factor 18 Pleckstrin homology (PH) domain; ARHGEF18, also ...

848-967

1.79e-43

Rho guanine nucleotide exchange factor 18 Pleckstrin homology (PH) domain; ARHGEF18, also called p114RhoGEF, is a key regulator of RhoA-Rock2 signaling that is crucial for maintenance of polarity in the vertebrate retinal epithelium, and consequently is essential for cellular differentiation, morphology and eventually organ function. ARHGEF18 contains Dbl-homology (DH) and pleckstrin-homology (PH) domains which bind and catalyze the exchange of GDP for GTP on RhoA. 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: 275437 Cd Length: 119 Bit Score: 153.91 E-value: 1.79e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  848 RKKLVRDGSVFLKSTTGRLKEVQAVLLTDILVFLQEKDQKYVFASLDHKSTVISLKKLIVREVAHEEKGLFLISMGVKDP 927
Cdd:cd15794     1 RRQLLLEGMLYWKAASGRLKDILALLLTDVLLLLQEKDQKYVFASVDSKPPVISLQKLIVREVANEEKAMFLISASLNGP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 568948645  928 EMVEVHASSREERNSWIQIIQDTINSLNrDEDEGIPSENE 967
Cdd:cd15794    81 EMYEIHTNSKEDRNTWMAHIRRAVESCP-DEEEGLFSEPE 119

RhoGEF

smart00325

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...

617-808

1.95e-42

Pssm-ID: 214619 [Multi-domain] Cd Length: 180 Bit Score: 153.61 E-value: 1.95e-42

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645    617 VIYELMQTELHHIRTLKIMSDVYSRGM-MTDLLFEQQMVEKLFPCLDELISIHSQFFQRILERKKESLVDKseknfliKR 695
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLkKELKLLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSV-------ER 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645    696 IGDVLVSQfsgesaERLKKTYGKFCGQHNQSVNYFKDLyTKDKRFQAFVKKKMSSSVVRRLGIPECILLVTQRITKYPVL 775
Cdd:smart00325   74 IGDVFLKL------EEFFKIYSEYCSNHPDALELLKKL-KKNPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLL 146

                           170       180       190
                    ....*....|....*....|....*....|...
gi 568948645    776 FQRILQCTKDNEVEQEDLTQSLSLVKDVIGAVD 808
Cdd:smart00325  147 LKELLKHTPEDHEDREDLKKALKAIKELANQVN 179

PH_p190RhoGEF

cd14680

Rho guanine nucleotide exchange factor Pleckstrin homology domain; p190RhoGEF (also called ...

851-951

2.58e-42

Rho guanine nucleotide exchange factor Pleckstrin homology domain; p190RhoGEF (also called RIP2 or ARHGEF28) belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. In addition to the Dbl homology (DH)-PH domain, p190RhoGEF contains an N-terminal C1 (Protein kinase C conserved region 1) domain. The DH-PH domains bind and catalyze the exchange of GDP for GTP on RhoA. 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: 275430 Cd Length: 101 Bit Score: 150.15 E-value: 2.58e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  851 LVRDGSVFLKSTTGRLKEVQAVLLTDILVFLQEKDQKYVFASLDHKSTVISLKKLIVREVAHEEKGLFLISMGVKDPEMV 930
Cdd:cd14680     1 LLHEGLVYWKTATGRFKDILALLLTDVLLFLQEKDQKYIFAAVDQKPPVICLQKLIVREVANEERGMFLISASSAGPEMY 80

                          90       100
                  ....*....|....*....|.
gi 568948645  931 EVHASSREERNSWIQIIQDTI 951
Cdd:cd14680    81 EIHTSSKEERNNWMRLIQEAV 101

PH_ARHGEF2

cd13393

Rho guanine nucleotide exchange factor 2 Pleckstrin homology (PH) domain; ARHGEF2, also called ...

848-959

4.62e-40

Rho guanine nucleotide exchange factor 2 Pleckstrin homology (PH) domain; ARHGEF2, also called GEF-H1, acts as guanine nucleotide exchange factor (GEF) for RhoA GTPases. It is thought to play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. ARHGEF2 contains a C1 domain followed by Dbl-homology (DH) and pleckstrin-homology (PH) domains which bind and catalyze the exchange of GDP for GTP on RhoA. 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: 275428 Cd Length: 116 Bit Score: 144.25 E-value: 4.62e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  848 RKKLVRDGSVFLKSTTGRLKEVQAVLLTDILVFLQEKDQKYVFASLDhKSTVISLKKLIVREVAHEEKGLFLISmgVKDP 927
Cdd:cd13393     1 RRKLIHDGCLLWKTASGRFKDVQVLLMTDVLVFLQEKDQKYIFPTLD-KPAVISLQNLIVRDIANQEKGMFLIS--AAPP 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 568948645  928 EMVEVHASSREERNSWIQIIQDTINSLNRDED 959
Cdd:cd13393    78 EMYEVHAASRDDRNTWMRLIQQTVKTCPSREE 109

PH_RhoGEF

cd13329

Rho guanine nucleotide exchange factor Pleckstrin homology domain; RhoGEFs belongs to ...

851-951

2.66e-39

Rho guanine nucleotide exchange factor Pleckstrin homology domain; RhoGEFs belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. The members here all contain Dbl homology (DH)-PH domains. In addition some members contain N-terminal C1 (Protein kinase C conserved region 1) domains, PDZ (also called DHR/Dlg homologous regions) domains, ANK (ankyrin) domains, and RGS (Regulator of G-protein signalling) domains or C-terminal ATP-synthase B subunit. The DH-PH domains bind and catalyze the exchange of GDP for GTP on RhoA. RhoGEF2/Rho guanine nucleotide exchange factor 2, p114RhoGEF/p114 Rho guanine nucleotide exchange factor, p115RhoGEF, p190RhoGEF, PRG/PDZ Rho guanine nucleotide exchange factor, RhoGEF 11, RhoGEF 12, RhoGEF 18, AKAP13/A-kinase anchoring protein 13, and LARG/Leukemia-associated Rho guanine nucleotide exchange factor are included in this CD. 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: 275411 Cd Length: 109 Bit Score: 141.63 E-value: 2.66e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  851 LVRDGSVFLKSTTGRLKEVQAVLLTDILVFLQEKDQKYV--------FASLDHKSTVISLKKLIVREVAHEEKGLFLISM 922
Cdd:cd13329     1 LIHEGPLTWKVARGKLIEVHVLLLEDLLVLLQKQDDKYLlklhltgsFDSKDTKSPVIKLSTLLVREVATDKKAFFLIST 80

                          90       100
                  ....*....|....*....|....*....
gi 568948645  923 GVKDPEMVEVHASSREERNSWIQIIQDTI 951
Cdd:cd13329    81 SKNGPQMYELVANSSSERKTWIKHISDAV 109

RhoGEF

pfam00621

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...

617-808

7.71e-34

Pssm-ID: 459876 [Multi-domain] Cd Length: 176 Bit Score: 128.57 E-value: 7.71e-34

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645   617 VIYELMQTELHHIRTLKIMSDVYSRGMMTDLLFEQQMVEKLFPCLDELISIHSQFFqrilerkkesLVDKSEKNFLIKRI 696
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEIKTIFSNIEEIYELHRQLL----------LEELLKEWISIQRI 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645   697 GDVLVSQFSGesaerlKKTYGKFCGQHNQSVNYFKDLYTKDKRFQAFVKKKMSSSVVRRLGIPECILLVTQRITKYPVLF 776
Cdd:pfam00621   71 GDIFLKFAPG------FKVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLL 144

                          170       180       190
                   ....*....|....*....|....*....|..
gi 568948645   777 QRILQCTKDNEVEQEDLTQSLSLVKDVIGAVD 808
Cdd:pfam00621  145 KELLKHTPPDHPDYEDLKKALEAIKEVAKQIN 176

C1_AKAP13

cd20878

protein kinase C conserved region 1 (C1 domain) found in A-kinase anchor protein 13 (AKAP-13) ...

407-463

6.40e-31

Pssm-ID: 410428 Cd Length: 60 Bit Score: 115.90 E-value: 6.40e-31

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568948645  407 TLNGHTFSPIPIVGPISCSQCMKPFTNKDAYTCAGCGAFVHKGCRENLASCAKVKMK 463
Cdd:cd20878     4 TLNGHVFSPVSSVGPTQCYHCSKPLNTKDAFLCANCNVQVHKGCRESLPVCAKVKMK 60

PH_ARHGEF2_18_like

cd15789

rho guanine nucleotide exchange factor; RhoGEFs belongs to regulator of G-protein signaling ...

851-948

1.12e-29

rho guanine nucleotide exchange factor; RhoGEFs belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. The members here all contain Dbl homology (DH)-PH domains. In addition some members contain N-terminal C1 (Protein kinase C conserved region 1) domains, PDZ (also called DHR/Dlg homologous regions) domains, ANK (ankyrin) domains, and RGS (Regulator of G-protein signalling) domains or C-terminal ATP-synthase B subunit. The DH-PH domains bind and catalyze the exchange of GDP for GTP on RhoA. RhoGEF2/Rho guanine nucleotide exchange factor 2, p114RhoGEF/p114 Rho guanine nucleotide exchange factor, p115RhoGEF, p190RhoGEF, PRG/PDZ Rho guanine nucleotide exchange factor, RhoGEF 11, RhoGEF 12, RhoGEF 18, AKAP13/A-kinase anchoring protein 13, and LARG/Leukemia-associated Rho guanine nucleotide exchange factor are included in this CD. 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: 275432 Cd Length: 102 Bit Score: 114.09 E-value: 1.12e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  851 LVRDGSVFLKSTTGRLKEVQAVLLTDILVFLQEKDQKYVFASLDHKSTVISLKKLIVREVAHEEKGLFLISmgVKDPEMV 930
Cdd:cd15789     1 LKFEGTAWLKQARGKTKDVLVVVLTDVLFFLQEKDQKYVFVSPDNKAGVVSLQKLLVREKAGQEKRMFLIS--ASPDGMP 78

                          90       100
                  ....*....|....*....|.
gi 568948645  931 EVHASSRE---ERNSWIQIIQ 948
Cdd:cd15789    79 EMYELKVQkpkDKNTWIQTIR 99

C1_p190RhoGEF-like

cd20815

protein kinase C conserved region 1 (C1 domain) found in the 190 kDa guanine nucleotide ...

409-460

1.36e-16

protein kinase C conserved region 1 (C1 domain) found in the 190 kDa guanine nucleotide exchange factor (p190RhoGEF)-like family; The p190RhoGEF-like protein family includes p190RhoGEF, Rho guanine nucleotide exchange factor 2 (ARHGEF2), A-kinase anchor protein 13 (AKAP-13) and similar proteins. p190RhoGEF is a brain-enriched, RhoA-specific guanine nucleotide exchange factor that regulates signaling pathways downstream of integrins and growth factor receptors. It is involved in axonal branching, synapse formation and dendritic morphogenesis, as well as in focal adhesion formation, cell motility and B-lymphocytes activation. ARHGEF2 acts as a guanine nucleotide exchange factor (GEF) that activates Rho-GTPases by promoting the exchange of GDP for GTP. It is thought to play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. AKAP-13 is a scaffold protein that plays an important role in assembling signaling complexes downstream of several types of G protein-coupled receptors. It activates RhoA in response to signaling via G protein-coupled receptors via its function as Rho guanine nucleotide exchange factor. It may also activate other Rho family members. AKAP-13 plays a role in cell growth, cell development and actin fiber formation. Members of this family share a common domain architecture containing C1, RhoGEF or Dbl-homologous (DH), and Pleckstrin Homology (PH) domains. Some members may contain additional domains such as the DUF5401 domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

Pssm-ID: 410365 Cd Length: 54 Bit Score: 75.15 E-value: 1.36e-16

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568948645  409 NGHTFSPIPIVGPISCSQCMKPFTNKDAYTCAGCGAFVHK-GCRENLASCAKV 460
Cdd:cd20815     2 NTHQFVPVSFSNSTKCDVCSKPLTNKPALQCENCSVNVHDsSCKDQLADCTKF 54

PH_p115RhoGEF

cd14679

Rho guanine nucleotide exchange factor Pleckstrin homology domain; p115RhoGEF (also called LSC, ...

841-954

1.01e-12

Rho guanine nucleotide exchange factor Pleckstrin homology domain; p115RhoGEF (also called LSC, GEF1 or LBCL2) belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. In addition to the Dbl homology (DH)-PH domain, p115RhoGEF contains an N-terminal RGS (Regulator of G-protein signalling) domain. The DH-PH domains bind and catalyze the exchange of GDP for GTP on RhoA. 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: 275429 Cd Length: 125 Bit Score: 66.40 E-value: 1.01e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  841 FAKEDLRRKKLVRDGSVFLKSTTGRLKEVQAVLLTDILVFLQEKDQKYVF--------ASLDHK---STVISLKKLIVRE 909
Cdd:cd14679     1 FKNIDITKKKLVHEGPLTWRVTKDKAIEVHVLLLDDLLVLLQKQDERLVLkchsrtttPTPDGKqmlSPIIKLNSAMTRE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 568948645  910 VAHEEKGLFLISMGVKDPEMVEVHASSREERNSWIQIIQDTINSL 954
Cdd:cd14679    81 VATDRKAFYVIFTWEQGAQIYELVAQTVSERKNWCALISETAGLL 125

PH_PRG

cd13391

PDZ Rho guanine nucleotide exchange factor Pleckstrin homology (PH) domain; PRG (also called ...

841-952

1.19e-12

PDZ Rho guanine nucleotide exchange factor Pleckstrin homology (PH) domain; PRG (also called RhoGEF11) belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. RhoGEFs activate Rho GTPases regulating cytoskeletal structure, gene transcription, and cell migration. PRG contains an N-terminal PDZ domain, a regulators of G-protein signaling-like (RGSL) domain, a linker region, and a C-terminal Dbl-homology (DH) and pleckstrin-homology (PH) domains which bind and catalyze the exchange of GDP for GTP on RhoA. As is the case in p115-RhoGEF, it is thought that the PRG activated by relieving autoinhibition caused by the linker region. 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: 275426 Cd Length: 142 Bit Score: 66.59 E-value: 1.19e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  841 FAKEDLRRKKLVRDGSVFLKSTTGRLKEVQAVLLTDILVFLQEKDQKYVF--------ASLDHKST---VISLKKLIVRE 909
Cdd:cd13391    18 FKNLDLTTRRMIHEGPLTWRISKDKTLDLHVLLLEDLLVLLQKQDEKLVLkchsktavGSSDSKQTfspVLKLNSVLIRS 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568948645  910 VAHEEKGLFLISMGVKDPEMVEVHASSREERNSWIQIIQDTIN 952
Cdd:cd13391    98 VATDKRALFIICTSKLGPQIYELVALTSSEKNTWMELLEEAVR 140

PH_LARG

cd13390

Leukemia-associated Rho guanine nucleotide exchange factor Pleckstrin homology (PH) domain; ...

845-947

5.45e-12

Leukemia-associated Rho guanine nucleotide exchange factor Pleckstrin homology (PH) domain; LARG (also called RhoGEF12) belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. RhoGEFs activate Rho GTPases regulating cytoskeletal structure, gene transcription, and cell migration. LARG contains a N-terminal extension, followed by Dbl homology (DH)-PH domains which bind and catalyze the exchange of GDP for GTP on RhoA in addition to a RGS domain. The active site of RhoA adopts two distinct GDP-excluding conformations among the four unique complexes in the asymmetric unit. The LARG PH domain also contains a potential protein-docking site. LARG forms a homotetramer via its DH domains. 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: 275425 Cd Length: 138 Bit Score: 64.62 E-value: 5.45e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  845 DLRRKKLVRDGSVFLKSTTGRLKEVQAVLLTDILVFLQEKDQKYVF--------ASLDHKST---VISLKKLIVREVAHE 913
Cdd:cd13390    20 DLTKRKMIHEGPLTWKVNRDKTIDLYTLLLEDILVLLQKQDDRLVLrchskilaSTADSKHTfspVIKLNTVLVRQVATD 99

                          90       100       110
                  ....*....|....*....|....*....|....
gi 568948645  914 EKGLFLISMGVKDPEMVEVHASSREERNSWIQII 947
Cdd:cd13390   100 NKAFFVISMSENGAQIYELVAQTVSEKTVWQDLI 133

C1_p190RhoGEF

cd20876

protein kinase C conserved region 1 (C1 domain) found in 190 kDa guanine nucleotide exchange ...

408-459

1.40e-11

protein kinase C conserved region 1 (C1 domain) found in 190 kDa guanine nucleotide exchange factor (p190RhoGEF) and similar proteins; p190RhoGEF, also called Rho guanine nucleotide exchange factor (RGNEF), Rho guanine nucleotide exchange factor 28 (ARHGEF28), or RIP2, is a brain-enriched, RhoA-specific guanine nucleotide exchange factor that regulates signaling pathways downstream of integrins and growth factor receptors. It is involved in axonal branching, synapse formation and dendritic morphogenesis, as well as in focal adhesion formation, cell motility and B-lymphocytes activation. In addition to the Dbl homology (DH)-PH domain, p190RhoGEF contains an N-terminal C1 (Protein kinase C conserved region 1) domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

Pssm-ID: 410426 Cd Length: 61 Bit Score: 60.91 E-value: 1.40e-11

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568948645  408 LNGHTFSPIPIVGPISCSQCMKPFTNKDAYTCAGCGAFVHKGCRENLASCAK 459
Cdd:cd20876     5 SNGHQFVTGSFSGPTLCVVCDKPVTGKELLQCSNCTVNVHKGCKESAPPCTK 56

C1_ARHGEF2

cd20877

protein kinase C conserved region 1 (C1 domain) found in Rho guanine nucleotide exchange ...

409-466

1.92e-11

protein kinase C conserved region 1 (C1 domain) found in Rho guanine nucleotide exchange factor 2 (ARHGEF2) and similar proteins; ARHGEF2, also called guanine nucleotide exchange factor H1 (GEF-H1), microtubule-regulated Rho-GEF, or proliferating cell nucleolar antigen p40, acts as guanine nucleotide exchange factor (GEF) that activates Rho-GTPases by promoting the exchange of GDP for GTP. It is thought to play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. ARHGEF2 may be involved in epithelial barrier permeability, cell motility and polarization, dendritic spine morphology, antigen presentation, leukemic cell differentiation, cell cycle regulation, innate immune response, and cancer. It contains a C1 domain followed by Dbl-homology (DH) and pleckstrin-homology (PH) domains which bind and catalyze the exchange of GDP for GTP on RhoA. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

Pssm-ID: 410427 Cd Length: 61 Bit Score: 60.75 E-value: 1.92e-11

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568948645  409 NGHTFSPIPIVGPISCSQCMKPFTNKDAYTCAGCGAFVHKGCRENLASCAKVKMKQPK 466
Cdd:cd20877     4 NGHLFTTITVSGTTMCSACNKSITAKEALICPTCNVTIHNRCKDTLPNCTKVKQKQQK 61

C1_ARHGEF18-like

cd20879

protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine ...

409-458

1.68e-08

protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine nucleotide exchange factor 18 (ARHGEF18)-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate ARHGEF18, which is also called 114 kDa Rho-specific guanine nucleotide exchange factor (p114-Rho-GEF), p114RhoGEF, or septin-associated RhoGEF (SA-RhoGEF). ARHGEF18 acts as guanine nucleotide exchange factor (GEF) for RhoA GTPases. Its activation induces formation of actin stress fibers. ARHGEF18 also acts as a GEF for RAC1, inducing production of reactive oxygen species (ROS). Members of this family contain C1, RhoGEF or Dbl-homologous (DH), and Pleckstrin Homology (PH) domains, as well as a DUF5401 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

Pssm-ID: 410429 Cd Length: 53 Bit Score: 52.12 E-value: 1.68e-08

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568948645  409 NGHTFSPIPIVGPISCSQCMKPFTNKDAYTCAGCGAFVHKGCRENLASCA 458
Cdd:cd20879     2 NGHQLVPGTFSSCATCSLCSKPLQNRNGLQCLNCAVNVHKNCKTLLTECS 51

smart00233

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

851-952

4.24e-08

Pssm-ID: 214574 [Multi-domain] Cd Length: 102 Bit Score: 52.55 E-value: 4.24e-08

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645    851 LVRDGSVFLKSTTGRL--KEVQAVLLTDILVFLQEKDQKYVFasldHKSTVISLKKLIVREVAH----EEKGLFLISMGv 924
Cdd:smart00233    1 VIKEGWLYKKSGGGKKswKKRYFVLFNSTLLYYKSKKDKKSY----KPKGSIDLSGCTVREAPDpdssKKPHCFEIKTS- 75

                            90       100
                    ....*....|....*....|....*...
gi 568948645    925 kDPEMVEVHASSREERNSWIQIIQDTIN 952
Cdd:smart00233   76 -DRKTLLLQAESEEEREKWVEALRKAIA 102

C1_dGM13116p-like

cd20831

protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and ...

409-459

4.06e-07

protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and similar proteins; This group contains uncharacterized proteins including Drosophila melanogaster GM13116p and Caenorhabditis elegans hypothetical protein R11G1.4, both of which contain C2 (a calcium-binding domain) and C1 domains. This model describes the C1 domain, a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

Pssm-ID: 410381 Cd Length: 58 Bit Score: 48.11 E-value: 4.06e-07

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568948645  409 NGHTFSPIPIVGPISCSQCMKPFT---NKDAYTCAGCGAFVHKGCRENLAS-CAK 459
Cdd:cd20831     4 NDHTFVATHFKGGPSCAVCNKLIPgrfGKQGYQCRDCGLICHKRCHVKVEThCPS 58

cd00029

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...

411-457

6.54e-07

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.

Pssm-ID: 410341 Cd Length: 50 Bit Score: 47.51 E-value: 6.54e-07

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568948645  411 HTFSPIPIVGPISCSQCMKPFTN--KDAYTCAGCGAFVHKGCRENLAS-C 457
Cdd:cd00029     1 HRFVPTTFSSPTFCDVCGKLIWGlfKQGLKCSDCGLVCHKKCLDKAPSpC 50

ROM1

COG5422

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...

586-886

2.91e-06

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];

Pssm-ID: 227709 [Multi-domain] Cd Length: 1175 Bit Score: 52.20 E-value: 2.91e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  586 DSKQLEAESWSRTVDSKFLKQQKKDVVKRQEVIYELMQTELHHIRTLKIMSDVYSRGMMTDLLF----EQQMVEKLFPCL 661
Cdd:COG5422   457 DKFDEEKNLWTLSVPKEVWESLPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWIKPLEESNIIpenaRRNFIKHVFANI 536

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  662 DELISIHSQFfqrilerkKESLVDKSEKNFLIKRIGDV------LVSQFSGESAERLkktYGKFCGQHNQSVNYfkdlyt 735
Cdd:COG5422   537 NEIYAVNSKL--------LKALTNRQCLSPIVNGIADIfldyvpKFEPFIKYGASQP---YAKYEFEREKSVNP------ 599

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  736 kdkRFQAFVKKKMSSSVVRRLGIPECILLVTQRITKYPVLFQRILQCTKDNEVEQEDLTQSLSLVKDVIGAVDSKVASYE 815
Cdd:COG5422   600 ---NFARFDHEVERLDESRKLELDGYLTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVIDMLREFLSRLNFESGKAE 676

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568948645  816 KKVRLGEIYTKTDSKSiMRMKSGQMFAKEDLRRKKLVRDGSVfLKSTTGRLKEVQAVLLTDILVFLQEKDQ 886
Cdd:COG5422   677 NRGDLFHLNQQLLFKP-EYVNLGLNDEYRKIIFKGVLKRKAK-SKTDGSLRGDIQFFLLDNMLLFCKAKAV 745

pfam00169

PH domain; PH stands for pleckstrin homology.

851-951

2.20e-05

PH domain; PH stands for pleckstrin homology.

Pssm-ID: 459697 [Multi-domain] Cd Length: 105 Bit Score: 44.86 E-value: 2.20e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645   851 LVRDGSVFLKSTT--GRLKEVQAVLLTDILVFLQEKDQKYVFAsldhKSTVISLKKLIVREVAHEEKG----LFLISMGV 924
Cdd:pfam00169    1 VVKEGWLLKKGGGkkKSWKKRYFVLFDGSLLYYKDDKSGKSKE----PKGSISLSGCEVVEVVASDSPkrkfCFELRTGE 76

                           90       100
                   ....*....|....*....|....*...
gi 568948645   925 KDP-EMVEVHASSREERNSWIQIIQDTI 951
Cdd:pfam00169   77 RTGkRTYLLQAESEEERKDWIKAIQSAI 104

Smc

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

1191-1302

4.51e-05

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 4.51e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1191 QEKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCD 1270
Cdd:COG1196   238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317

                          90       100       110
                  ....*....|....*....|....*....|..
gi 568948645 1271 LERLRAAQKQLEREQEQLRRDTERLSQRQMDQ 1302
Cdd:COG1196   318 LEELEEELAELEEELEELEEELEELEEELEEA 349

Smc

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

1134-1302

4.55e-05

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 4.55e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1134 LKRNSEQVVQSIVHLHELLSMLQgvvlQQDSYIEDQKLVLTEKVLTRSASRPSsliEQEKQRSLEKQRQDLANLQKQQAQ 1213
Cdd:COG1196   293 LLAELARLEQDIARLEERRRELE----ERLEELEEELAELEEELEELEEELEE---LEEELEEAEEELEEAEAELAEAEE 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1214 HLEEKRRREREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQkkgtyqcDLERLRAAQKQLEREQEQLRRDTE 1293
Cdd:COG1196   366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-------RLERLEEELEELEEALAELEEEEE 438


                  ....*....
gi 568948645 1294 RLSQRQMDQ 1302
Cdd:COG1196   439 EEEEALEEA 447

PRK12704

phosphodiesterase; Provisional

1232-1302

4.83e-05

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 4.83e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568948645 1232 LRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAAQKQLEREQEQLRRDTERLSQRQMDQ 1302
Cdd:PRK12704   84 LQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEE 154

YhaN

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

1145-1321

5.79e-05

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 5.79e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1145 IVHLHELLSMLQGVVLQQDSYIEDQK-LVLTEKVLTRSASRPSSLieQEKQRSLEKQRQDLANLQKQQA--QHLEEKRRR 1221
Cdd:COG4717    70 LKELKELEEELKEAEEKEEEYAELQEeLEELEEELEELEAELEEL--REELEKLEKLLQLLPLYQELEAleAELAELPER 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1222 EREWEAREQELRDREAKLAEREETVRRRQQDLER--------DREELQQKKGTYQCDLERLRAAQ---KQLEREQEQLRR 1290
Cdd:COG4717   148 LEELEERLEELRELEEELEELEAELAELQEELEElleqlslaTEEELQDLAEELEELQQRLAELEeelEEAQEELEELEE 227

                         170       180       190
                  ....*....|....*....|....*....|.
gi 568948645 1291 DTERLSQRQMDQNLCQVSNKHGRLMRIPSFL 1321
Cdd:COG4717   228 ELEQLENELEAAALEERLKEARLLLLIAAAL 258

SMC_prok_B

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

1134-1289

8.92e-05

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 8.92e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  1134 LKRNSEQVVQSIVHLHELLSMLQGVVLQQDSYIED--QKLVLTEKVLTRSASRPSSLIEQEK--QRSLEKQRQDLANLQK 1209
Cdd:TIGR02168  794 LKEELKALREALDELRAELTLLNEEAANLRERLESleRRIAATERRLEDLEEQIEELSEDIEslAAEIEELEELIEELES 873

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  1210 QQAQHLEEKRRREREWEAreqeLRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAaqkQLEREQEQLR 1289
Cdd:TIGR02168  874 ELEALLNERASLEEALAL----LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV---RIDNLQERLS 946

YhaN

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

1191-1299

9.82e-05

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 9.82e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1191 QEKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQcD 1270
Cdd:COG4717    52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP-L 130

                          90       100
                  ....*....|....*....|....*....
gi 568948645 1271 LERLRAAQKQLEREQEQLRRDTERLSQRQ 1299
Cdd:COG4717   131 YQELEALEAELAELPERLEELEERLEELR 159

DUF5401

pfam17380

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

1161-1302

1.29e-04

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

Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.66 E-value: 1.29e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  1161 QQDSYIEDQKLVLTEKVLTRSASRPSSLIEQEKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEAREQELRDREAKla 1240
Cdd:pfam17380  355 QEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEA-- 432

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568948645  1241 eREETVRRRQQDLERDREELQQKKGTYQCDLERLRaaQKQLEREQEQLRRDTERLSQRQMDQ 1302
Cdd:pfam17380  433 -RQREVRRLEEERAREMERVRLEEQERQQQVERLR--QQEEERKRKKLELEKEKRDRKRAEE 491

Smc

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

1190-1302

1.30e-04

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 1.30e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1190 EQEKQRSLEKQRQDLANLQKQQAQHleekrrrEREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKgtyqc 1269
Cdd:COG1196   220 EELKELEAELLLLKLRELEAELEEL-------EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ----- 287

                          90       100       110
                  ....*....|....*....|....*....|...
gi 568948645 1270 dlERLRAAQKQLEREQEQLRRDTERLSQRQMDQ 1302
Cdd:COG1196   288 --AEEYELLAELARLEQDIARLEERRRELEERL 318

COG4913

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

1139-1299

2.43e-04

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 2.43e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1139 EQVVQSIVHLHELLSMLQGVVLQQDSYIEDQKLVLTEKVLTRSASRPSSLIEQEKQ-----RSLEKQR-----QDLANLQ 1208
Cdd:COG4913   265 AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAlreelDELEAQIrgnggDRLEQLE 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1209 KQQAQHLEEKRRREREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAAQKQLEREQEQL 1288
Cdd:COG4913   345 REIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL 424

                         170
                  ....*....|.
gi 568948645 1289 RRDTERLSQRQ 1299
Cdd:COG4913   425 EAEIASLERRK 435

SMC_prok_B

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

1148-1308

2.72e-04

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 2.72e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  1148 LHELLSMLQGVVLQQDSYIED---QKLVLTEKV--LTRSASRPSSLIEQEKQRsLEKQRQDLANLQKQQAQHLEEKRRRE 1222
Cdd:TIGR02168  279 LEEEIEELQKELYALANEISRleqQKQILRERLanLERQLEELEAQLEELESK-LDELAEELAELEEKLEELKEELESLE 357

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  1223 REWEAREQELRDREAKLAEREETVRRrqqdLERDREELQQKKGTYQCDLERLRAAQKQLEREQEQLRRDTERLSQRQMDQ 1302
Cdd:TIGR02168  358 AELEELEAELEELESRLEELEEQLET----LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433


                   ....*.
gi 568948645  1303 NLCQVS 1308
Cdd:TIGR02168  434 ELKELQ 439

C1_MgcRacGAP

cd20821

protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ...

411-454

2.93e-04

protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and similar proteins; MgcRacGAP, also called Rac GTPase-activating protein 1 (RACGAP1) or protein CYK4, plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling; and ii) after phosphorylation by aurora B, MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain an N-terminal C1 domain, and a C-terminal RhoGAP domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

Pssm-ID: 410371 Cd Length: 55 Bit Score: 40.08 E-value: 2.93e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568948645  411 HTFSPIPIVGPISCSQCMKPFT-NKDAYTCAGCGAFVHKGCRENL 454
Cdd:cd20821     3 HRFVSKTVIKPETCVVCGKRIKfGKKALKCKDCRVVCHPDCKDKL 47

SMC_prok_B

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

1134-1303

3.06e-04

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 3.06e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  1134 LKRNSEQVVQSIVHLHELLSMLQGVVLQQDSYIEDQKLVLTEKVLTRSASRPSSLIEQEKQRSLEKQRQDLANLQKQQAQ 1213
Cdd:TIGR02168  717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  1214 HLEEKRRREREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAAQKQLEREQEQLRRDTE 1293
Cdd:TIGR02168  797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876

                          170
                   ....*....|
gi 568948645  1294 RLSQRQMDQN 1303
Cdd:TIGR02168  877 ALLNERASLE 886

Smc

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

1191-1302

6.16e-04

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 6.16e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1191 QEKQRSLEKQRQDLANLQKQQAQhLEEKRrreREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQcd 1270
Cdd:COG1196   277 EELELELEEAQAEEYELLAELAR-LEQDI---ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE-- 350

                          90       100       110
                  ....*....|....*....|....*....|..
gi 568948645 1271 lERLRAAQKQLEREQEQLRRDTERLSQRQMDQ 1302
Cdd:COG1196   351 -EELEEAEAELAEAEEALLEAEAELAEAEEEL 381

DUF5401

pfam17380

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

1161-1300

6.71e-04

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

Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 6.71e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  1161 QQDSY--IEDQKLVLTEKVLTRSASRPSSLIEQEKQRSLEKQRQ--------DLANLQKQQAQHLEEKRRREREWEAREQ 1230
Cdd:pfam17380  289 QQEKFekMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQaaiyaeqeRMAMERERELERIRQEERKRELERIRQE 368

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  1231 ELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAAQKQLeREQEQLRRDTERLSQRQM 1300
Cdd:pfam17380  369 EIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQK-VEMEQIRAEQEEARQREV 437

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

1194-1328

1.23e-03

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

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 1.23e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1194 QRSLEKQRQDLANLQKQQAQhleekrrrereweareqeLRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLER 1273
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAE------------------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568948645 1274 LRAAQKQLEREQEQLRRDTERlsQRQMDQNLCQVSNKHGRLMRiPSFLPNSDEFS 1328
Cdd:COG4942    81 LEAELAELEKEIAELRAELEA--QKEELAELLRALYRLGRQPP-LALLLSPEDFL 132

Zwint

pfam15556

ZW10 interactor; This family of proteins is found in eukaryotes. Proteins in this family are ...

1242-1314

1.41e-03

ZW10 interactor; This family of proteins is found in eukaryotes. Proteins in this family are typically between 127 and 281 amino acids in length.

Pssm-ID: 464766 [Multi-domain] Cd Length: 252 Bit Score: 42.27 E-value: 1.41e-03

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568948645  1242 REETVRRRQQDLERDREELQQKKgtyQCDLERLRAAQKQLEREQEQ-LRRDTE-----RLSQRQMDQNLCQVSNKHGRL 1314
Cdd:pfam15556   92 KMEEAQRKRAQLQEALEQLQAKK---QMAMEKLRTAQKQWQLQQEKhLQHLAEvsaevRERQTGTQQELERLYQELGTL 167

COG4913

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

1191-1299

1.46e-03

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.46e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1191 QEKQRSLEKQRQDLANlQKQQAQHLEEKRRREREWEAREQELRDREAKLA-------------EREETVRRRQQDLERDR 1257
Cdd:COG4913   630 EERLEALEAELDALQE-RREALQRLAEYSWDEIDVASAEREIAELEAELErldassddlaaleEQLEELEAELEELEEEL 708

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568948645 1258 EELQQKKGtyqcdleRLRAAQKQLEREQEQLRRDTERLSQRQ 1299
Cdd:COG4913   709 DELKGEIG-------RLEKELEQAEEELDELQDRLEAAEDLA 743

YhaN

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

944-1298

1.49e-03

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.49e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  944 IQIIQDTINSLNRDEDE---GIPSENEEEKKLLDTKARELKEQLQQKDQQILLLLEEKEMIFRDMTECSTPLPedcspth 1020
Cdd:COG4717   165 LEELEAELAELQEELEElleQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE------- 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1021 sprvlfRSNTEEALKGGPLMKSAINEVEILQSLVSGSLGGTLGQSISSPVEQEVMAAPISLPRRAETFGGfdcHQMNASK 1100
Cdd:COG4717   238 ------AAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG---KEAEELQ 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1101 GGEKEEGDDGQDLRRTESDSGLKKGGNGNLVFMLKRNSEQVVQSIVHLHELLSMLQgvvLQQdsyIEDQKLVLTEKVLTR 1180
Cdd:COG4717   309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ---LEE---LEQEIAALLAEAGVE 382

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1181 SASRPSSLIEQEKQRslEKQRQDLANLQKQQAQHLEEKRRREREWEareqelrdrEAKLAEREETVRRRQQDLERDREEL 1260
Cdd:COG4717   383 DEEELRAALEQAEEY--QELKEELEELEEQLEELLGELEELLEALD---------EEELEEELEELEEELEELEEELEEL 451

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 568948645 1261 QQKKGtyqcdleRLRAAQKQLEREQE--QLRRDTERLSQR 1298
Cdd:COG4717   452 REELA-------ELEAELEQLEEDGElaELLQELEELKAE 484

YhaN

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

1134-1290

1.52e-03

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 1.52e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1134 LKRNSEQVVQSIVHLHELLSMLQGVVLQQDSYIEDQKLVLTEKVLTRSASRPSSLIEQ-----EKQRSLEKQRQDLANLQ 1208
Cdd:COG4717    97 LEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERleelrELEEELEELEAELAELQ 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1209 KQQAQHLEEKRRREreweareqelRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLERLRaAQKQLEREQEQL 1288
Cdd:COG4717   177 EELEELLEQLSLAT----------EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE-NELEAAALEERL 245


                  ..
gi 568948645 1289 RR 1290
Cdd:COG4717   246 KE 247

C1_VAV

cd20810

protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function ...

411-457

1.56e-03

protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and as scaffold proteins, and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

Pssm-ID: 410360 Cd Length: 52 Bit Score: 38.01 E-value: 1.56e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568948645  411 HTFSPipivgPISCSQCMK----PFtnKDAYTCAGCGAFVHKGCRENLASC 457
Cdd:cd20810     8 TTFKE-----PTTCSVCKKllkgLF--FQGYKCSVCGAAVHKECIAKVKRC 51

smart00109

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...

411-457

1.61e-03

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.

Pssm-ID: 197519 Cd Length: 50 Bit Score: 37.83 E-value: 1.61e-03

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 568948645    411 HTFSPIPIVGPISCSQCMKP--FTNKDAYTCAGCGAFVHKGCRENLAS-C 457
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSiwGSFKQGLRCSECKVKCHKKCADKVPKaC 50

C1_ScPKC1-like_rpt1

cd20822

first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae ...

409-457

1.88e-03

first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae protein kinase C-like 1 (ScPKC1) and similar proteins; ScPKC1 is required for cell growth and for the G2 to M transition of the cell division cycle. It mediates a protein kinase cascade, activating BCK1 which itself activates MKK1/MKK2. The family also includes Schizosaccharomyces pombe PKC1 and PKC2, which are involved in the control of cell shape and act as targets of the inhibitor staurosporine. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

Pssm-ID: 410372 Cd Length: 52 Bit Score: 37.65 E-value: 1.88e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568948645  409 NGHTFSPIPIVGPISCSQCMKPFTNKdAYTCAGCGAFVHKGCREN-LASC 457
Cdd:cd20822     1 RGHKFVQKQFYQIMRCAVCGEFLVNA-GYQCEDCKYTCHKKCYEKvVTKC 49

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

1191-1290

2.09e-03

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

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 2.09e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1191 QEKQRSLEKQrqdLANLQKQQAQHLEEKRRREREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKgtyqcd 1270
Cdd:COG4942    19 ADAAAEAEAE---LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE------ 89

                          90       100
                  ....*....|....*....|
gi 568948645 1271 lERLRAAQKQLEREQEQLRR 1290
Cdd:COG4942    90 -KEIAELRAELEAQKEELAE 108

Smc

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

1190-1299

2.49e-03

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 2.49e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1190 EQEKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQC 1269
Cdd:COG1196   258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337

                          90       100       110
                  ....*....|....*....|....*....|
gi 568948645 1270 DLERLRAAQKQLEREQEQLRRDTERLSQRQ 1299
Cdd:COG1196   338 ELEELEEELEEAEEELEEAEAELAEAEEAL 367

Smc

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

1190-1299

3.05e-03

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 3.05e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1190 EQEKQRSLEKQRQDLANLQKQQAQHLEEKRRRereweAR-EQELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQ 1268
Cdd:COG1196   388 LLEALRAAAELAAQLEELEEAEEALLERLERL-----EEeLEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568948645 1269 CDLERLRAAQKQLEREQEQLRRDTERLSQRQ 1299
Cdd:COG1196   463 ELLAELLEEAALLEAALAELLEELAEAAARL 493

Golgin_A5

pfam09787

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...

1189-1299

3.08e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.

Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.28 E-value: 3.08e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  1189 IEQEKQRSLEKQRQDL-ANLQKQQAQHLEEKRRREREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKGTY 1267
Cdd:pfam09787   58 LLREEIQKLRGQIQQLrTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATL 137

                           90       100       110
                   ....*....|....*....|....*....|..
gi 568948645  1268 QcdlERLRAAQKQLEREQEQLRRDTERLSQRQ 1299
Cdd:pfam09787  138 Q---SRIKDREAEIEKLRNQLTSKSQSSSSQS 166

mukB

PRK04863

chromosome partition protein MukB;

1192-1298

3.31e-03

chromosome partition protein MukB;

Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 3.31e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1192 EKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKG---TYQ 1268
Cdd:PRK04863  530 RQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPawlAAQ 609

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568948645 1269 CDLERLRAA---------------QKQLERE-------------QEQLRRDTERLSQR 1298
Cdd:PRK04863  610 DALARLREQsgeefedsqdvteymQQLLEREreltverdelaarKQALDEEIERLSQP 667

FliJ

COG2882

Flagellar biosynthesis chaperone FliJ [Cell motility];

1190-1301

3.37e-03

Flagellar biosynthesis chaperone FliJ [Cell motility];

Pssm-ID: 442129 [Multi-domain] Cd Length: 142 Bit Score: 39.50 E-value: 3.37e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1190 EQEKQRSLEKQRQDLANLQKQQAQhleekrrrereWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQC 1269
Cdd:COG2882    35 AEEQLEQLEQYREEYEQRLQQKLQ-----------QGLSAAQLRNYQQFIARLDEAIEQQQQQVAQAEQQVEQARQAWLE 103

                          90       100       110
                  ....*....|....*....|....*....|..
gi 568948645 1270 DLERLRAAQKQLEREQEQLRRDTERLSQRQMD 1301
Cdd:COG2882   104 ARQERKALEKLKERRREEERQEENRREQKELD 135

C1_ScPKC1-like_rpt2

cd20823

second protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae ...

411-450

4.50e-03

second protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae protein kinase C-like 1 (ScPKC1) and similar proteins; ScPKC1 is required for cell growth and for the G2 to M transition of the cell division cycle. It mediates a protein kinase cascade, activating BCK1 which itself activates MKK1/MKK2. The family also includes Schizosaccharomyces pombe PKC1 and PKC2, which are involved in the control of cell shape and act as targets of the inhibitor staurosporine. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.

Pssm-ID: 410373 Cd Length: 59 Bit Score: 36.90 E-value: 4.50e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568948645  411 HTFSPIPIVGPISCSQC--MKPFTNKDAYTCAGCGAFVHKGC 450
Cdd:cd20823     5 HRFEPFTNLGANWCCHCgqMLPLGRKQIRKCTECGKTAHAQC 46

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

1189-1302

5.02e-03

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

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 5.02e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1189 IEQEKQRSLEKQRQDLANLQKQQAQhleekrrrereweareqeLRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQ 1268
Cdd:COG4942   144 LAPARREQAEELRADLAELAALRAE------------------LEAERAELEALLAELEEERAALEALKAERQKLLARLE 205

                          90       100       110
                  ....*....|....*....|....*....|....
gi 568948645 1269 CDLERLRAAQKQLEREQEQLRRDTERLSQRQMDQ 1302
Cdd:COG4942   206 KELAELAAELAELQQEAEELEALIARLEAEAAAA 239

MukB

COG3096

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...

1236-1314

5.42e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.48 E-value: 5.42e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1236 EAKLAEREETVRRrQQDLERDREELQQKKG---TYQCDLERLRAAQK-QLEREQEQLRRDTERlsQRQMDQNLCQVSNKH 1311
Cdd:COG3096   518 RAQLAELEQRLRQ-QQNAERLLEEFCQRIGqqlDAAEELEELLAELEaQLEELEEQAAEAVEQ--RSELRQQLEQLRARI 594


                  ...
gi 568948645 1312 GRL 1314
Cdd:COG3096   595 KEL 597

Smc

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

1190-1299

5.42e-03

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 5.42e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1190 EQEKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKGTyqc 1269
Cdd:COG1196   251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE--- 327

                          90       100       110
                  ....*....|....*....|....*....|
gi 568948645 1270 DLERLRAAQKQLEREQEQLRRDTERLSQRQ 1299
Cdd:COG1196   328 LEEELEELEEELEELEEELEEAEEELEEAE 357

CwlO1

COG3883

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

1232-1303

5.44e-03

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 5.44e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568948645 1232 LRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAAQKQLEREQEQLRRDTERLSQRQMDQN 1303
Cdd:COG3883   145 LEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216

FliJ

pfam02050

Flagellar FliJ protein;

1191-1301

5.65e-03

Flagellar FliJ protein;

Pssm-ID: 426581 [Multi-domain] Cd Length: 123 Bit Score: 38.42 E-value: 5.65e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645  1191 QEKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEAREqeLRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCD 1270
Cdd:pfam02050    8 AEAQRELQQAEEKLEELQQYRAEYQQQLSGAGQGISAAE--LRNYQAFISQLDEAIAQQQQELAQAEAQVEKAREEWQEA 85

                           90       100       110
                   ....*....|....*....|....*....|.
gi 568948645  1271 LERLRAAQKQLEREQEQLRRDTERLSQRQMD 1301
Cdd:pfam02050   86 RQERKSLEKLREREKKEERKEQNRREQKQLD 116

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

1191-1316

6.05e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 6.05e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948645 1191 QEKQRSLEKQRQDLANLQK---QQAQHLEEKRRREREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKGTY 1267
Cdd:COG4372    62 EQLEEELEQARSELEQLEEeleELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAEL 141

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568948645 1268 QCDLERLRAAQKQLEREQEQLRRDTERLSQRQMDQNLCQVSNKHGRLMR 1316
Cdd:COG4372   142 QSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190

EnvC