NCBI Conserved Domain Search

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

2466-2642

1.42e-05

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 1.42e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2466 IVHLHELLSMLQGVVLQQDSYIEDQK-LVLTEKVLTRSASRPSSLieQEKQRSLEKQRQDLANLQKQQA--QHLEEKRRR 2542
Cdd:COG4717     70 LKELKELEEELKEAEEKEEEYAELQEeLEELEEELEELEAELEEL--REELEKLEKLLQLLPLYQELEAleAELAELPER 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2543 EREWEAREQELRDREAKLAEREETVRRRQQDLER--------DREELQQKKGTYQCDLERLRAAQ---KQLEREQEQLRR 2611
Cdd:COG4717    148 LEELEERLEELRELEEELEELEAELAELQEELEElleqlslaTEEELQDLAEELEELQQRLAELEeelEEAQEELEELEE 227

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1720424479 2612 DTERLSQRQMDQNLCQVSNKHGRLMRIPSFL 2642
Cdd:COG4717    228 ELEQLENELEAAALEERLKEARLLLLIAAAL 258

PRK12704

phosphodiesterase; Provisional

2553-2623

5.45e-05

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 5.45e-05

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720424479 2553 LRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAAQKQLEREQEQLRRDTERLSQRQMDQ 2623
Cdd:PRK12704    84 LQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEE 154

SMC_prok_B

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

2455-2610

5.84e-05

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

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 5.84e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2455 LKRNSEQVVQSIVHLHELLSMLQGVVLQQDSYIED--QKLVLTEKVLTRSASRPSSLIEQEK--QRSLEKQRQDLANLQK 2530
Cdd:TIGR02168  794 LKEELKALREALDELRAELTLLNEEAANLRERLESleRRIAATERRLEDLEEQIEELSEDIEslAAEIEELEELIEELES 873

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2531 QQAQHLEEKRRREREWEAreqeLRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAaqkQLEREQEQLR 2610
Cdd:TIGR02168  874 ELEALLNERASLEEALAL----LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV---RIDNLQERLS 946

DUF5401

pfam17380

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

2482-2623

1.79e-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: 47.04 E-value: 1.79e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2482 QQDSYIEDQKLVLTEKVLTRSASRPSSLIEQEKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEAREQELRDREAKla 2561
Cdd:pfam17380  355 QEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEA-- 432

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720424479 2562 eREETVRRRQQDLERDREELQQKKGTYQCDLERLRaaQKQLEREQEQLRRDTERLSQRQMDQ 2623
Cdd:pfam17380  433 -RQREVRRLEEERAREMERVRLEEQERQQQVERLR--QQEEERKRKKLELEKEKRDRKRAEE 491

smart00109

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

1733-1779

3.96e-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: 37.45 E-value: 3.96e-03

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1720424479  1733 HTFSPIPIVGPISCSQCMKP--FTNKDAYTCAGCGAFVHKGCRENLAS-C 1779
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSiwGSFKQGLRCSECKVKCHKKCADKVPKaC 50

ATP-synt_Fo_b

cd06503

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...

2560-2623

9.06e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.

Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 38.96 E-value: 9.06e-03

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720424479 2560 LAEREETVRRRQQDLERDREELQQKKGTYQcdlERLRAAQKQLEREQEQLRRDTERLSQRQMDQ 2623
Cdd:cd06503     28 LDEREEKIAESLEEAEKAKEEAEELLAEYE---EKLAEARAEAQEIIEEARKEAEKIKEEILAE 88

Name

Accession

Description

Interval

E-value

PH_AKAP13

cd13392

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

2172-2274

3.81e-62

Pssm-ID: 275427 Cd Length: 103 Bit Score: 207.45 E-value: 3.81e-62

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2172 LVRDGSVFLKSTTGRLKEVQAVLLTDILVFLQEKDQKYVFASLDHKSTVISLKKLIVREVAHEEKGLFLISMGVKDPEMV 2251
Cdd:cd13392      1 LVRDGPVSLKNTAGRLKEVQAVLLSDVLVFLQEKDQKYVFASLDQKSTVISLKKLIVREVAHEEKGLFLISMGIADPEMV 80

                           90       100
                   ....*....|....*....|...
gi 1720424479 2252 EVHASSREERNSWIQIIQDTINS 2274
Cdd:cd13392     81 EVHASSKEERNSWMQIIQDTINT 103

PH_16

pfam17838

PH domain;

2156-2273

1.96e-51

PH domain;

Pssm-ID: 436083 Cd Length: 127 Bit Score: 177.98 E-value: 1.96e-51

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2156 MKSGQMFAKEDLRRKKLVRDGSVFLKSTTGRLKEVQAVLLTDILVFLQEKDQKYVFASL-------DHK--STVISLKKL 2226
Cdd:pfam17838    1 HPLGEEFKKLDLTTRKLIHEGPLTWRNSKGKLVEVHALLLEDILVLLQEKDQKLVLACLstgsenvDQKtqSPIISLKKL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1720424479 2227 IVREVAHEEKGLFLISMGVKDPEMVEVHASSREERNSWIQIIQDTIN 2273
Cdd:pfam17838   81 IVREVATDKKAFFLISTSPSDPQMYELHASTKSERNTWTKLIQDAIE 127

RhoGEF

cd00160

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

1935-2129

9.76e-49

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: 172.48 E-value: 9.76e-49

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 1935 RQEVIYELMQTELHHIRTLKIMSDVYSRGMMTDLL-FEQQMVEKLFPCLDELISIHSQFFQRILERKKESLVDKSeknfl 2013
Cdd:cd00160      1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLpLSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWDKSGP----- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2014 ikRIGDVLVSQFSgesaerLKKTYGKFCGQHNQSVNYFKDLYTKDKRFQAFVKKKMSSSvvRRLGIPECILLVTQRITKY 2093
Cdd:cd00160     76 --RIGDVFLKLAP------FFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAESEC--GRLKLESLLLKPVQRLTKY 145

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1720424479 2094 PVLFQRILQCTKDNEVEQEDLTQSLSLVKDVIGAVD 2129
Cdd:cd00160    146 PLLLKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181

RhoGEF

smart00325

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

1938-2129

4.56e-45

Pssm-ID: 214619 [Multi-domain] Cd Length: 180 Bit Score: 161.70 E-value: 4.56e-45

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479  1938 VIYELMQTELHHIRTLKIMSDVYSRGM-MTDLLFEQQMVEKLFPCLDELISIHSQFFQRILERKKESLVDKseknfliKR 2016
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLkKELKLLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSV-------ER 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479  2017 IGDVLVSQfsgesaERLKKTYGKFCGQHNQSVNYFKDLyTKDKRFQAFVKKKMSSSVVRRLGIPECILLVTQRITKYPVL 2096
Cdd:smart00325   74 IGDVFLKL------EEFFKIYSEYCSNHPDALELLKKL-KKNPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLL 146

                           170       180       190
                    ....*....|....*....|....*....|...
gi 1720424479  2097 FQRILQCTKDNEVEQEDLTQSLSLVKDVIGAVD 2129
Cdd:smart00325  147 LKELLKHTPEDHEDREDLKKALKAIKELANQVN 179

PH_ARHGEF18

cd15794

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

2169-2288

9.04e-44

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: 155.83 E-value: 9.04e-44

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2169 RKKLVRDGSVFLKSTTGRLKEVQAVLLTDILVFLQEKDQKYVFASLDHKSTVISLKKLIVREVAHEEKGLFLISMGVKDP 2248
Cdd:cd15794      1 RRQLLLEGMLYWKAASGRLKDILALLLTDVLLLLQEKDQKYVFASVDSKPPVISLQKLIVREVANEEKAMFLISASLNGP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1720424479 2249 EMVEVHASSREERNSWIQIIQDTINSLNrDEDEGIPSENE 2288
Cdd:cd15794     81 EMYEIHTNSKEDRNTWMAHIRRAVESCP-DEEEGLFSEPE 119

PH_p190RhoGEF

cd14680

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

2172-2272

1.39e-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: 151.69 E-value: 1.39e-42

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2172 LVRDGSVFLKSTTGRLKEVQAVLLTDILVFLQEKDQKYVFASLDHKSTVISLKKLIVREVAHEEKGLFLISMGVKDPEMV 2251
Cdd:cd14680      1 LLHEGLVYWKTATGRFKDILALLLTDVLLFLQEKDQKYIFAAVDQKPPVICLQKLIVREVANEERGMFLISASSAGPEMY 80

                           90       100
                   ....*....|....*....|.
gi 1720424479 2252 EVHASSREERNSWIQIIQDTI 2272
Cdd:cd14680     81 EIHTSSKEERNNWMRLIQEAV 101

PH_ARHGEF2

cd13393

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

2169-2280

1.23e-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: 146.57 E-value: 1.23e-40

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2169 RKKLVRDGSVFLKSTTGRLKEVQAVLLTDILVFLQEKDQKYVFASLDhKSTVISLKKLIVREVAHEEKGLFLISmgVKDP 2248
Cdd:cd13393      1 RRKLIHDGCLLWKTASGRFKDVQVLLMTDVLVFLQEKDQKYIFPTLD-KPAVISLQNLIVRDIANQEKGMFLIS--AAPP 77

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1720424479 2249 EMVEVHASSREERNSWIQIIQDTINSLNRDED 2280
Cdd:cd13393     78 EMYEVHAASRDDRNTWMRLIQQTVKTCPSREE 109

PH_RhoGEF

cd13329

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

2172-2272

5.54e-40

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: 144.33 E-value: 5.54e-40

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2172 LVRDGSVFLKSTTGRLKEVQAVLLTDILVFLQEKDQKYV--------FASLDHKSTVISLKKLIVREVAHEEKGLFLISM 2243
Cdd:cd13329      1 LIHEGPLTWKVARGKLIEVHVLLLEDLLVLLQKQDDKYLlklhltgsFDSKDTKSPVIKLSTLLVREVATDKKAFFLIST 80

                           90       100
                   ....*....|....*....|....*....
gi 1720424479 2244 GVKDPEMVEVHASSREERNSWIQIIQDTI 2272
Cdd:cd13329     81 SKNGPQMYELVANSSSERKTWIKHISDAV 109

RhoGEF

pfam00621

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

1938-2129

8.18e-36

Pssm-ID: 459876 [Multi-domain] Cd Length: 176 Bit Score: 135.12 E-value: 8.18e-36

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 1938 VIYELMQTELHHIRTLKIMSDVYSRGMMTDLLFEQQMVEKLFPCLDELISIHSQFFqrilerkkesLVDKSEKNFLIKRI 2017
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEIKTIFSNIEEIYELHRQLL----------LEELLKEWISIQRI 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2018 GDVLVSQFSGesaerlKKTYGKFCGQHNQSVNYFKDLYTKDKRFQAFVKKKMSSSVVRRLGIPECILLVTQRITKYPVLF 2097
Cdd:pfam00621   71 GDIFLKFAPG------FKVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLL 144

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1720424479 2098 QRILQCTKDNEVEQEDLTQSLSLVKDVIGAVD 2129
Cdd:pfam00621  145 KELLKHTPPDHPDYEDLKKALEAIKEVAKQIN 176

PH_ARHGEF2_18_like

cd15789

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

2172-2269

3.77e-30

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: 116.02 E-value: 3.77e-30

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2172 LVRDGSVFLKSTTGRLKEVQAVLLTDILVFLQEKDQKYVFASLDHKSTVISLKKLIVREVAHEEKGLFLISmgVKDPEMV 2251
Cdd:cd15789      1 LKFEGTAWLKQARGKTKDVLVVVLTDVLFFLQEKDQKYVFVSPDNKAGVVSLQKLLVREKAGQEKRMFLIS--ASPDGMP 78

                           90       100
                   ....*....|....*....|.
gi 1720424479 2252 EVHASSRE---ERNSWIQIIQ 2269
Cdd:cd15789     79 EMYELKVQkpkDKNTWIQTIR 99

C1_AKAP13

cd20878

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

1729-1785

3.96e-30

Pssm-ID: 410428 Cd Length: 60 Bit Score: 114.36 E-value: 3.96e-30

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720424479 1729 TLNGHTFSPIPIVGPISCSQCMKPFTNKDAYTCAGCGAFVHKGCRENLASCAKVKMK 1785
Cdd:cd20878      4 TLNGHVFSPVSSVGPTQCYHCSKPLNTKDAFLCANCNVQVHKGCRESLPVCAKVKMK 60

C1_p190RhoGEF-like

cd20815

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

1731-1782

7.00e-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: 73.61 E-value: 7.00e-16

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720424479 1731 NGHTFSPIPIVGPISCSQCMKPFTNKDAYTCAGCGAFVHK-GCRENLASCAKV 1782
Cdd:cd20815      2 NTHQFVPVSFSNSTKCDVCSKPLTNKPALQCENCSVNVHDsSCKDQLADCTKF 54

PH_p115RhoGEF

cd14679

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

2162-2275

8.81e-13

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: 67.56 E-value: 8.81e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2162 FAKEDLRRKKLVRDGSVFLKSTTGRLKEVQAVLLTDILVFLQEKDQKYVF--------ASLDHK---STVISLKKLIVRE 2230
Cdd:cd14679      1 FKNIDITKKKLVHEGPLTWRVTKDKAIEVHVLLLDDLLVLLQKQDERLVLkchsrtttPTPDGKqmlSPIIKLNSAMTRE 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1720424479 2231 VAHEEKGLFLISMGVKDPEMVEVHASSREERNSWIQIIQDTINSL 2275
Cdd:cd14679     81 VATDRKAFYVIFTWEQGAQIYELVAQTVSERKNWCALISETAGLL 125

PH_PRG

cd13391

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

2162-2273

1.72e-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: 66.98 E-value: 1.72e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2162 FAKEDLRRKKLVRDGSVFLKSTTGRLKEVQAVLLTDILVFLQEKDQKYVF--------ASLDHKST---VISLKKLIVRE 2230
Cdd:cd13391     18 FKNLDLTTRRMIHEGPLTWRISKDKTLDLHVLLLEDLLVLLQKQDEKLVLkchsktavGSSDSKQTfspVLKLNSVLIRS 97

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1720424479 2231 VAHEEKGLFLISMGVKDPEMVEVHASSREERNSWIQIIQDTIN 2273
Cdd:cd13391     98 VATDKRALFIICTSKLGPQIYELVALTSSEKNTWMELLEEAVR 140

PH_LARG

cd13390

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

2166-2268

4.09e-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: 65.78 E-value: 4.09e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2166 DLRRKKLVRDGSVFLKSTTGRLKEVQAVLLTDILVFLQEKDQKYVF--------ASLDHKST---VISLKKLIVREVAHE 2234
Cdd:cd13390     20 DLTKRKMIHEGPLTWKVNRDKTIDLYTLLLEDILVLLQKQDDRLVLrchskilaSTADSKHTfspVIKLNTVLVRQVATD 99

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1720424479 2235 EKGLFLISMGVKDPEMVEVHASSREERNSWIQII 2268
Cdd:cd13390    100 NKAFFVISMSENGAQIYELVAQTVSEKTVWQDLI 133

C1_p190RhoGEF

cd20876

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

1730-1781

4.04e-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: 60.53 E-value: 4.04e-11

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720424479 1730 LNGHTFSPIPIVGPISCSQCMKPFTNKDAYTCAGCGAFVHKGCRENLASCAK 1781
Cdd:cd20876      5 SNGHQFVTGSFSGPTLCVVCDKPVTGKELLQCSNCTVNVHKGCKESAPPCTK 56

C1_ARHGEF2

cd20877

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

1731-1788

1.08e-10

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: 59.21 E-value: 1.08e-10

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720424479 1731 NGHTFSPIPIVGPISCSQCMKPFTNKDAYTCAGCGAFVHKGCRENLASCAKVKMKQPK 1788
Cdd:cd20877      4 NGHLFTTITVSGTTMCSACNKSITAKEALICPTCNVTIHNRCKDTLPNCTKVKQKQQK 61

smart00233

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

2172-2273

2.04e-08

Pssm-ID: 214574 [Multi-domain] Cd Length: 102 Bit Score: 54.09 E-value: 2.04e-08

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479  2172 LVRDGSVFLKSTTGRL--KEVQAVLLTDILVFLQEKDQKYVFasldHKSTVISLKKLIVREVAH----EEKGLFLISMGv 2245
Cdd:smart00233    1 VIKEGWLYKKSGGGKKswKKRYFVLFNSTLLYYKSKKDKKSY----KPKGSIDLSGCTVREAPDpdssKKPHCFEIKTS- 75

                            90       100
                    ....*....|....*....|....*...
gi 1720424479  2246 kDPEMVEVHASSREERNSWIQIIQDTIN 2273
Cdd:smart00233   76 -DRKTLLLQAESEEEREKWVEALRKAIA 102

C1_ARHGEF18-like

cd20879

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

1731-1780

9.25e-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: 50.58 E-value: 9.25e-08

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720424479 1731 NGHTFSPIPIVGPISCSQCMKPFTNKDAYTCAGCGAFVHKGCRENLASCA 1780
Cdd:cd20879      2 NGHQLVPGTFSSCATCSLCSKPLQNRNGLQCLNCAVNVHKNCKTLLTECS 51

C1_dGM13116p-like

cd20831

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

1731-1781

8.64e-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: 8.64e-07

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720424479 1731 NGHTFSPIPIVGPISCSQCMKPFT---NKDAYTCAGCGAFVHKGCRENLAS-CAK 1781
Cdd:cd20831      4 NDHTFVATHFKGGPSCAVCNKLIPgrfGKQGYQCRDCGLICHKRCHVKVEThCPS 58

cd00029

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

1733-1778

1.50e-06

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: 47.13 E-value: 1.50e-06

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1720424479 1733 HTFSPIPIVGPISCSQCMKPFTN--KDAYTCAGCGAFVHKGCRENLAS 1778
Cdd:cd00029      1 HRFVPTTFSSPTFCDVCGKLIWGlfKQGLKCSDCGLVCHKKCLDKAPS 48

ROM1

COG5422

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

1907-2207

1.53e-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: 54.13 E-value: 1.53e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 1907 DSKQLEAESWSRTVDSKFLKQQKKDVVKRQEVIYELMQTELHHIRTLKIMSDVYSRGMMTDLLF----EQQMVEKLFPCL 1982
Cdd:COG5422    457 DKFDEEKNLWTLSVPKEVWESLPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWIKPLEESNIIpenaRRNFIKHVFANI 536

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 1983 DELISIHSQFfqrilerkKESLVDKSEKNFLIKRIGDV------LVSQFSGESAERLkktYGKFCGQHNQSVNYfkdlyt 2056
Cdd:COG5422    537 NEIYAVNSKL--------LKALTNRQCLSPIVNGIADIfldyvpKFEPFIKYGASQP---YAKYEFEREKSVNP------ 599

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2057 kdkRFQAFVKKKMSSSVVRRLGIPECILLVTQRITKYPVLFQRILQCTKDNEVEQEDLTQSLSLVKDVIGAVDSKVASYE 2136
Cdd:COG5422    600 ---NFARFDHEVERLDESRKLELDGYLTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVIDMLREFLSRLNFESGKAE 676

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720424479 2137 KKVRLGEIYTKTDSKSiMRMKSGQMFAKEDLRRKKLVRDGSVfLKSTTGRLKEVQAVLLTDILVFLQEKDQ 2207
Cdd:COG5422    677 NRGDLFHLNQQLLFKP-EYVNLGLNDEYRKIIFKGVLKRKAK-SKTDGSLRGDIQFFLLDNMLLFCKAKAV 745

pfam00169

PH domain; PH stands for pleckstrin homology.

2172-2272

7.20e-06

PH domain; PH stands for pleckstrin homology.

Pssm-ID: 459697 [Multi-domain] Cd Length: 105 Bit Score: 47.17 E-value: 7.20e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2172 LVRDGSVFLKSTT--GRLKEVQAVLLTDILVFLQEKDQKYVFAsldhKSTVISLKKLIVREVAHEEKG----LFLISMGV 2245
Cdd:pfam00169    1 VVKEGWLLKKGGGkkKSWKKRYFVLFDGSLLYYKDDKSGKSKE----PKGSISLSGCEVVEVVASDSPkrkfCFELRTGE 76

                           90       100
                   ....*....|....*....|....*...
gi 1720424479 2246 KDP-EMVEVHASSREERNSWIQIIQDTI 2272
Cdd:pfam00169   77 RTGkRTYLLQAESEEERKDWIKAIQSAI 104

YhaN

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

2466-2642

1.42e-05

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 1.42e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2466 IVHLHELLSMLQGVVLQQDSYIEDQK-LVLTEKVLTRSASRPSSLieQEKQRSLEKQRQDLANLQKQQA--QHLEEKRRR 2542
Cdd:COG4717     70 LKELKELEEELKEAEEKEEEYAELQEeLEELEEELEELEAELEEL--REELEKLEKLLQLLPLYQELEAleAELAELPER 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2543 EREWEAREQELRDREAKLAEREETVRRRQQDLER--------DREELQQKKGTYQCDLERLRAAQ---KQLEREQEQLRR 2611
Cdd:COG4717    148 LEELEERLEELRELEEELEELEAELAELQEELEElleqlslaTEEELQDLAEELEELQQRLAELEeelEEAQEELEELEE 227

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1720424479 2612 DTERLSQRQMDQNLCQVSNKHGRLMRIPSFL 2642
Cdd:COG4717    228 ELEQLENELEAAALEERLKEARLLLLIAAAL 258

PRK12704

phosphodiesterase; Provisional

2553-2623

5.45e-05

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 5.45e-05

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720424479 2553 LRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAAQKQLEREQEQLRRDTERLSQRQMDQ 2623
Cdd:PRK12704    84 LQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEE 154

SMC_prok_B

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

2455-2610

5.84e-05

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 5.84e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2455 LKRNSEQVVQSIVHLHELLSMLQGVVLQQDSYIED--QKLVLTEKVLTRSASRPSSLIEQEK--QRSLEKQRQDLANLQK 2530
Cdd:TIGR02168  794 LKEELKALREALDELRAELTLLNEEAANLRERLESleRRIAATERRLEDLEEQIEELSEDIEslAAEIEELEELIEELES 873

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2531 QQAQHLEEKRRREREWEAreqeLRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAaqkQLEREQEQLR 2610
Cdd:TIGR02168  874 ELEALLNERASLEEALAL----LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV---RIDNLQERLS 946

YhaN

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

2512-2620

6.03e-05

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 6.03e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2512 QEKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQcD 2591
Cdd:COG4717     52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP-L 130

                           90       100
                   ....*....|....*....|....*....
gi 1720424479 2592 LERLRAAQKQLEREQEQLRRDTERLSQRQ 2620
Cdd:COG4717    131 YQELEALEAELAELPERLEELEERLEELR 159

Smc

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

2510-2623

6.14e-05

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 6.14e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2510 IEQEKQRSLEKQRQDLANLQKQQAQHLEekrrrereweareqeLRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQ 2589
Cdd:COG1196    300 LEQDIARLEERRRELEERLEELEEELAE---------------LEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1720424479 2590 CDLERLRAAQKQLEREQEQLRRDTERLSQRQMDQ 2623
Cdd:COG1196    365 EALLEAEAELAEAEEELEELAEELLEALRAAAEL 398

Smc

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

2455-2623

6.57e-05

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 6.57e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2455 LKRNSEQVVQSIVHLHELLSMLQgvvlQQDSYIEDQKLVLTEKVLTRSASRPSsliEQEKQRSLEKQRQDLANLQKQQAQ 2534
Cdd:COG1196    293 LLAELARLEQDIARLEERRRELE----ERLEELEEELAELEEELEELEEELEE---LEEELEEAEEELEEAEAELAEAEE 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2535 HLEEKRRREREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQkkgtyqcDLERLRAAQKQLEREQEQLRRDTE 2614
Cdd:COG1196    366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-------RLERLEEELEELEEALAELEEEEE 438


                   ....*....
gi 1720424479 2615 RLSQRQMDQ 2623
Cdd:COG1196    439 EEEEALEEA 447

Smc

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

2512-2623

8.05e-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: 8.05e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2512 QEKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCD 2591
Cdd:COG1196    238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1720424479 2592 LERLRAAQKQLEREQEQLRRDTERLSQRQMDQ 2623
Cdd:COG1196    318 LEELEEELAELEEELEELEEELEELEEELEEA 349

YhaN

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

2265-2619

1.17e-04

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 1.17e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2265 IQIIQDTINSLNRDEDE---GIPSENEEEKKLLDTKARELKEQLQQKDQQILLLLEEKEMIFRDMTECSTPLpedcspth 2341
Cdd:COG4717    165 LEELEAELAELQEELEElleQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-------- 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2342 sprvlFRSNTEEALKGGPLMKSAINEVEILQSLVSGSLGGTLGQSISSPVEQEVMAAPISLPRRAETFGGfdcHQMNASK 2421
Cdd:COG4717    237 -----EAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG---KEAEELQ 308

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2422 GGEKEEGDDGQDLRRTESDSGLKKGGNGNLVFMLKRNSEQVVQSIVHLHELLSMLQgvvLQQdsyIEDQKLVLTEKVLTR 2501
Cdd:COG4717    309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ---LEE---LEQEIAALLAEAGVE 382

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2502 SASRPSSLIEQEKQRslEKQRQDLANLQKQQAQHLEEKRRREREWEareqelrdrEAKLAEREETVRRRQQDLERDREEL 2581
Cdd:COG4717    383 DEEELRAALEQAEEY--QELKEELEELEEQLEELLGELEELLEALD---------EEELEEELEELEEELEELEEELEEL 451

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1720424479 2582 QQKKGtyqcdleRLRAAQKQLEREQE--QLRRDTERLSQR 2619
Cdd:COG4717    452 REELA-------ELEAELEQLEEDGElaELLQELEELKAE 484

SMC_prok_B

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

2469-2629

1.55e-04

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 1.55e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2469 LHELLSMLQGVVLQQDSYIED---QKLVLTEKV--LTRSASRPSSLIEQEKQRsLEKQRQDLANLQKQQAQHLEEKRRRE 2543
Cdd:TIGR02168  279 LEEEIEELQKELYALANEISRleqQKQILRERLanLERQLEELEAQLEELESK-LDELAEELAELEEKLEELKEELESLE 357

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2544 REWEAREQELRDREAKLAEREETVRRrqqdLERDREELQQKKGTYQCDLERLRAAQKQLEREQEQLRRDTERLSQRQMDQ 2623
Cdd:TIGR02168  358 AELEELEAELEELESRLEELEEQLET----LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433


                   ....*.
gi 1720424479 2624 NLCQVS 2629
Cdd:TIGR02168  434 ELKELQ 439

Smc

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

2511-2623

1.58e-04

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 1.58e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2511 EQEKQRSLEKQRQDLANLQKQQAQHleekrrrEREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKgtyqc 2590
Cdd:COG1196    220 EELKELEAELLLLKLRELEAELEEL-------EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ----- 287

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1720424479 2591 dlERLRAAQKQLEREQEQLRRDTERLSQRQMDQ 2623
Cdd:COG1196    288 --AEEYELLAELARLEQDIARLEERRRELEERL 318

DUF5401

pfam17380

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

2482-2623

1.79e-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: 47.04 E-value: 1.79e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2482 QQDSYIEDQKLVLTEKVLTRSASRPSSLIEQEKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEAREQELRDREAKla 2561
Cdd:pfam17380  355 QEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEA-- 432

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720424479 2562 eREETVRRRQQDLERDREELQQKKGTYQCDLERLRaaQKQLEREQEQLRRDTERLSQRQMDQ 2623
Cdd:pfam17380  433 -RQREVRRLEEERAREMERVRLEEQERQQQVERLR--QQEEERKRKKLELEKEKRDRKRAEE 491

COG4913

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

2460-2620

2.89e-04

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 2.89e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2460 EQVVQSIVHLHELLSMLQGVVLQQDSYIEDQKLVLTEKVLTRSASRPSSLIEQEKQ-----RSLEKQR-----QDLANLQ 2529
Cdd:COG4913    265 AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAlreelDELEAQIrgnggDRLEQLE 344

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2530 KQQAQHLEEKRRREREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAAQKQLEREQEQL 2609
Cdd:COG4913    345 REIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL 424

                          170
                   ....*....|.
gi 1720424479 2610 RRDTERLSQRQ 2620
Cdd:COG4913    425 EAEIASLERRK 435

SMC_prok_B

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

2455-2624

3.15e-04

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 3.15e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2455 LKRNSEQVVQSIVHLHELLSMLQGVVLQQDSYIEDQKLVLTEKVLTRSASRPSSLIEQEKQRSLEKQRQDLANLQKQQAQ 2534
Cdd:TIGR02168  717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2535 HLEEKRRREREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAAQKQLEREQEQLRRDTE 2614
Cdd:TIGR02168  797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876

                          170
                   ....*....|
gi 1720424479 2615 RLSQRQMDQN 2624
Cdd:TIGR02168  877 ALLNERASLE 886

FliJ

COG2882

Flagellar biosynthesis chaperone FliJ [Cell motility];

2511-2622

3.91e-04

Flagellar biosynthesis chaperone FliJ [Cell motility];

Pssm-ID: 442129 [Multi-domain] Cd Length: 142 Bit Score: 42.97 E-value: 3.91e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2511 EQEKQRSLEKQRQDLANLQKQQAQhleekrrrereWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKgtyqc 2590
Cdd:COG2882     35 AEEQLEQLEQYREEYEQRLQQKLQ-----------QGLSAAQLRNYQQFIARLDEAIEQQQQQVAQAEQQVEQAR----- 98

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1720424479 2591 dlERLRAAQKQL-------EREQEQLRRDTERLSQRQMD 2622
Cdd:COG2882     99 --QAWLEARQERkaleklkERRREEERQEENRREQKELD 135

YhaN

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

2455-2611

4.83e-04

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 4.83e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2455 LKRNSEQVVQSIVHLHELLSMLQGVVLQQDSYIEDQKLVLTEKVLTRSASRPSSLIEQ-----EKQRSLEKQRQDLANLQ 2529
Cdd:COG4717     97 LEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERleelrELEEELEELEAELAELQ 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2530 KQQAQHLEEKRRREreweareqelRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLERLRaAQKQLEREQEQL 2609
Cdd:COG4717    177 EELEELLEQLSLAT----------EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE-NELEAAALEERL 245


                   ..
gi 1720424479 2610 RR 2611
Cdd:COG4717    246 KE 247

C1_MgcRacGAP

cd20821

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

1733-1776

6.69e-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: 39.70 E-value: 6.69e-04

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1720424479 1733 HTFSPIPIVGPISCSQCMKPFT-NKDAYTCAGCGAFVHKGCRENL 1776
Cdd:cd20821      3 HRFVSKTVIKPETCVVCGKRIKfGKKALKCKDCRVVCHPDCKDKL 47

EnvC

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

2515-2649

7.09e-04

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: 44.75 E-value: 7.09e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2515 QRSLEKQRQDLANLQKQQAQhleekrrrereweareqeLRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLER 2594
Cdd:COG4942     19 ADAAAEAEAELEQLQQEIAE------------------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720424479 2595 LRAAQKQLEREQEQLRRDTERlsQRQMDQNLCQVSNKHGRLMRiPSFLPNSDEFS 2649
Cdd:COG4942     81 LEAELAELEKEIAELRAELEA--QKEELAELLRALYRLGRQPP-LALLLSPEDFL 132

DUF4659

pfam15558

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...

2489-2624

8.37e-04

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.

Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 44.26 E-value: 8.37e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2489 DQKLVltEKVLTRsasrpssliEQEKQRSLEKQRQdlANLQKQQAQHLEEKRRREREWEAREQELRDREAKLAEREETVR 2568
Cdd:pfam15558    6 DRKIA--ALMLAR---------HKEEQRMRELQQQ--AALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKA 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720424479 2569 RRQQDLERDREelQQKKGTYQCD-----------------LERLRAAQKQLEREQEQLRRDTERLSQRQMDQN 2624
Cdd:pfam15558   73 RLGREERRRAD--RREKQVIEKEsrwreqaedqenqrqekLERARQEAEQRKQCQEQRLKEKEEELQALREQN 143

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

2512-2638

9.21e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 9.21e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2512 QEKQRSLEKQRQDLANLQKQQAQhleekrrrereweareqelrdREAKLAEREETVRRRQQDLERDREELQQKKGtyqcD 2591
Cdd:COG4372     55 EQAREELEQLEEELEQARSELEQ---------------------LEEELEELNEQLQAAQAELAQAQEELESLQE----E 109

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1720424479 2592 LERLRAAQKQLEREQEQLRRDTERLSQRQmDQNLCQVSNKHGRLMRI 2638
Cdd:COG4372    110 AEELQEELEELQKERQDLEQQRKQLEAQI-AELQSEIAEREEELKEL 155

FliJ

pfam02050

Flagellar FliJ protein;

2512-2622

9.60e-04

Flagellar FliJ protein;

Pssm-ID: 426581 [Multi-domain] Cd Length: 123 Bit Score: 41.50 E-value: 9.60e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2512 QEKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEAREqeLRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCD 2591
Cdd:pfam02050    8 AEAQRELQQAEEKLEELQQYRAEYQQQLSGAGQGISAAE--LRNYQAFISQLDEAIAQQQQELAQAEAQVEKAREEWQEA 85

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1720424479 2592 LERLRAAQKQLEREQEQLRRDTERLSQRQMD 2622
Cdd:pfam02050   86 RQERKSLEKLREREKKEERKEQNRREQKQLD 116

Smc

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

2512-2623

9.63e-04

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 9.63e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2512 QEKQRSLEKQRQDLANLQKQQAQhLEEKRrreREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQcd 2591
Cdd:COG1196    277 EELELELEEAQAEEYELLAELAR-LEQDI---ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE-- 350

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1720424479 2592 lERLRAAQKQLEREQEQLRRDTERLSQRQMDQ 2623
Cdd:COG1196    351 -EELEEAEAELAEAEEALLEAEAELAEAEEEL 381

DUF5401

pfam17380

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

2482-2621

9.84e-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: 44.73 E-value: 9.84e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2482 QQDSY--IEDQKLVLTEKVLTRSASRPSSLIEQEKQRSLEKQRQ--------DLANLQKQQAQHLEEKRRREREWEAREQ 2551
Cdd:pfam17380  289 QQEKFekMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQaaiyaeqeRMAMERERELERIRQEERKRELERIRQE 368

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2552 ELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQCDLERLRAAQKQLeREQEQLRRDTERLSQRQM 2621
Cdd:pfam17380  369 EIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQK-VEMEQIRAEQEEARQREV 437

COG4913

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

2512-2620

1.07e-03

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.07e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2512 QEKQRSLEKQRQDLANlQKQQAQHLEEKRRREREWEAREQELRDREAKLA-------------EREETVRRRQQDLERDR 2578
Cdd:COG4913    630 EERLEALEAELDALQE-RREALQRLAEYSWDEIDVASAEREIAELEAELErldassddlaaleEQLEELEAELEELEEEL 708

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1720424479 2579 EELQQKKGtyqcdleRLRAAQKQLEREQEQLRRDTERLSQRQ 2620
Cdd:COG4913    709 DELKGEIG-------RLEKELEQAEEELDELQDRLEAAEDLA 743

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

2512-2637

1.14e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 1.14e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2512 QEKQRSLEKQRQDLANLQK---QQAQHLEEKRRREREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKGTY 2588
Cdd:COG4372     62 EQLEEELEQARSELEQLEEeleELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAEL 141

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1720424479 2589 QCDLERLRAAQKQLEREQEQLRRDTERLSQRQMDQNLCQVSNKHGRLMR 2637
Cdd:COG4372    142 QSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190

EnvC

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

2512-2611

1.80e-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: 43.21 E-value: 1.80e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2512 QEKQRSLEKQrqdLANLQKQQAQHLEEKRRREREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKgtyqcd 2591
Cdd:COG4942     19 ADAAAEAEAE---LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE------ 89

                           90       100
                   ....*....|....*....|
gi 1720424479 2592 lERLRAAQKQLEREQEQLRR 2611
Cdd:COG4942     90 -KEIAELRAELEAQKEELAE 108

TPH

pfam13868

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

2510-2637

1.89e-03

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

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 1.89e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2510 IEQEKQRSLEKQRQDLANLQKQQAQHleekrrrereweareQELR--------DREAKLAEREETVRRRQQ--DLERDRE 2579
Cdd:pfam13868  178 IEEEKEREIARLRAQQEKAQDEKAER---------------DELRaklyqeeqERKERQKEREEAEKKARQrqELQQARE 242

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720424479 2580 E-LQQKKGTYQCDLERLRAAQKQLEREQEQLRRDTERLSQRQMDQNLcqvsnKHGRLMR 2637
Cdd:pfam13868  243 EqIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRL-----EHRRELE 296

Golgin_A5

pfam09787

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

2510-2620

1.94e-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: 42.82 E-value: 1.94e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2510 IEQEKQRSLEKQRQDL-ANLQKQQAQHLEEKRRREREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKGTY 2588
Cdd:pfam09787   58 LLREEIQKLRGQIQQLrTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATL 137

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1720424479 2589 QcdlERLRAAQKQLEREQEQLRRDTERLSQRQ 2620
Cdd:pfam09787  138 Q---SRIKDREAEIEKLRNQLTSKSQSSSSQS 166

Zwint

pfam15556

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

2563-2635

2.13e-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: 42.66 E-value: 2.13e-03

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720424479 2563 REETVRRRQQDLERDREELQQKKgtyQCDLERLRAAQKQLEREQEQ-LRRDTE-----RLSQRQMDQNLCQVSNKHGRL 2635
Cdd:pfam15556   92 KMEEAQRKRAQLQEALEQLQAKK---QMAMEKLRTAQKQWQLQQEKhLQHLAEvsaevRERQTGTQQELERLYQELGTL 167

EnvC

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

2444-2619

2.16e-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: 43.21 E-value: 2.16e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2444 KKGGNGNLVFMLkrNSEQVVQSIVHLHellsMLQGVVLQQDSYIEDQKLVLTEkvltrsasrpssliEQEKQRSLEKQRQ 2523
Cdd:COG4942    115 RLGRQPPLALLL--SPEDFLDAVRRLQ----YLKYLAPARREQAEELRADLAE--------------LAALRAELEAERA 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2524 DLANLQKQQAQhleekrrrereweareqELRDREAKLAEREETVRRRQQDLERDREELQQkkgtyqcdlerLRAAQKQLE 2603
Cdd:COG4942    175 ELEALLAELEE-----------------ERAALEALKAERQKLLARLEKELAELAAELAE-----------LQQEAEELE 226

                          170
                   ....*....|....*.
gi 1720424479 2604 REQEQLRRDTERLSQR 2619
Cdd:COG4942    227 ALIARLEAEAAAAAER 242

C1_VAV

cd20810

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

1733-1779

2.39e-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: 2.39e-03

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720424479 1733 HTFSPipivgPISCSQCMK----PFtnKDAYTCAGCGAFVHKGCRENLASC 1779
Cdd:cd20810      8 TTFKE-----PTTCSVCKKllkgLF--FQGYKCSVCGAAVHKECIAKVKRC 51

C1_ScPKC1-like_rpt1

cd20822

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

1731-1779

2.97e-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: 38.04 E-value: 2.97e-03

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720424479 1731 NGHTFSPIPIVGPISCSQCMKPFTNKdAYTCAGCGAFVHKGCREN-LASC 1779
Cdd:cd20822      1 RGHKFVQKQFYQIMRCAVCGEFLVNA-GYQCEDCKYTCHKKCYEKvVTKC 49

mukB

PRK04863

chromosome partition protein MukB;

2513-2619

3.07e-03

chromosome partition protein MukB;

Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 3.07e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2513 EKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKG---TYQ 2589
Cdd:PRK04863   530 RQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPawlAAQ 609

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720424479 2590 CDLERLRAA---------------QKQLERE-------------QEQLRRDTERLSQR 2619
Cdd:PRK04863   610 DALARLREQsgeefedsqdvteymQQLLEREreltverdelaarKQALDEEIERLSQP 667

EnvC

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

2510-2623

3.36e-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: 42.44 E-value: 3.36e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2510 IEQEKQRSLEKQRQDLANLQKQQAQhleekrrrereweareqeLRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQ 2589
Cdd:COG4942    144 LAPARREQAEELRADLAELAALRAE------------------LEAERAELEALLAELEEERAALEALKAERQKLLARLE 205

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1720424479 2590 CDLERLRAAQKQLEREQEQLRRDTERLSQRQMDQ 2623
Cdd:COG4942    206 KELAELAAELAELQQEAEELEALIARLEAEAAAA 239

smart00109

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

1733-1779

3.96e-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: 37.45 E-value: 3.96e-03

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1720424479  1733 HTFSPIPIVGPISCSQCMKP--FTNKDAYTCAGCGAFVHKGCRENLAS-C 1779
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSiwGSFKQGLRCSECKVKCHKKCADKVPKaC 50

Smc

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

2511-2620

4.25e-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: 4.25e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2511 EQEKQRSLEKQRQDLANLQKQQAQHLEEKRRRereweAR-EQELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQ 2589
Cdd:COG1196    388 LLEALRAAAELAAQLEELEEAEEALLERLERL-----EEeLEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1720424479 2590 CDLERLRAAQKQLEREQEQLRRDTERLSQRQ 2620
Cdd:COG1196    463 ELLAELLEEAALLEAALAELLEELAEAAARL 493

Smc

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

2511-2620

4.82e-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: 4.82e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2511 EQEKQRSLEKQRQDLANLQKQQAQHLEEKRRREREWEAREQELRDREAKLAEREETVRRRQQDLERDREELQQKKGTYQC 2590
Cdd:COG1196    258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337

                           90       100       110
                   ....*....|....*....|....*....|
gi 1720424479 2591 DLERLRAAQKQLEREQEQLRRDTERLSQRQ 2620
Cdd:COG1196    338 ELEELEEELEEAEEELEEAEAELAEAEEAL 367

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

2512-2620

5.47e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 5.47e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2512 QEKQRSLEKQRQDLANLQKQQAQhleekrrrereweaREQELRDREAKLAEREETVRRRQQDLERDREELQQKKGTyqcd 2591
Cdd:COG4372     41 DKLQEELEQLREELEQAREELEQ--------------LEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE---- 102

                           90       100
                   ....*....|....*....|....*....
gi 1720424479 2592 LERLRAAQKQLEREQEQLRRDTERLSQRQ 2620
Cdd:COG4372    103 LESLQEEAEELQEELEELQKERQDLEQQR 131

TPH

pfam13868

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

2511-2625

5.80e-03

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.44 E-value: 5.80e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720424479 2511 EQEKQRSLEKQRQDLANLQKQQAQHleekrrrerewearEQELRDREAKLAERE-ETVRRRQQDLER----DREELQQKK 2585
Cdd:pfam13868  223 EREEAEKKARQRQELQQAREEQIEL--------------KERRLAEEAEREEEEfERMLRKQAEDEEieqeEAEKRRMKR 288

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1720424479 2586 GTYQCDLERL---RAAQKQLEREQEQLRRDTERLSQRQMDQNL 2625
Cdd:pfam13868  289 LEHRRELEKQieeREEQRAAEREEELEEGERLREEEAERRERI 331

EnvC