NCBI Conserved Domain Search

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

667-783

3.58e-08

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: 57.44 E-value: 3.58e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  667 VEMQRTAIQEREKQfRLQSTRGNLLLEQERQRNFEKQREERAGVEKLQSQLRQEQ-QRWERERARqqqELElagaRLQER 745
Cdd:pfam17380  383 LQMERQQKNERVRQ-ELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREvRRLEEERAR---EME----RVRLE 454

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1907186219  746 EGEARQMRQRLDQErtELERQRQAYQHDLERlREAQRA 783
Cdd:pfam17380  455 EQERQQQVERLRQQ--EEERKRKKLELEKEK-RDRKRA 489

Smc

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

658-781

4.96e-08

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 4.96e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  658 AVIAQQDSYVEMQRTAIQEREKQFRLQSTRgnlLLEQERQRNFEKQREERAGVEKLQsqLRQEQQRWERERARQQQELEL 737
Cdd:COG1196    267 AELEELRLELEELELELEEAQAEEYELLAE---LARLEQDIARLEERRRELEERLEE--LEEELAELEEELEELEEELEE 341

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907186219  738 AGARLQEREGEARQMRQRLDQERTELERQRQAYQHDLERLREAQ 781
Cdd:COG1196    342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385

ROM1

COG5422

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

74-296

1.89e-07

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

Pssm-ID: 227709 [Multi-domain] Cd Length: 1175 Bit Score: 55.28 E-value: 1.89e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219   74 DAHEFEAESWSLSVDLAYAKKQKKEVVKRQDVLYELMQTEAHHVRTLKIMLKVYSRALQEELQFSGQA----VSRLFPCA 149
Cdd:COG5422    457 DKFDEEKNLWTLSVPKEVWESLPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWIKPLEESNIIPENArrnfIKHVFANI 536

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  150 DDLLDMHSHFLARLkeRRQEFLEEgsdrnyVIQKIGDVLVQQFSgetgermkeKYAVFCS-GHNDAVGQYKLLLQQS--K 226
Cdd:COG5422    537 NEIYAVNSKLLKAL--TNRQCLSP------IVNGIADIFLDYVP---------KFEPFIKyGASQPYAKYEFEREKSvnP 599

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  227 KFQNLIKKIGNFSIVRRLGVQECILLVTQRITKYPVLVERIIQNTEAGTEDYKDLSQALSLIKDIISQVD 296
Cdd:COG5422    600 NFARFDHEVERLDESRKLELDGYLTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVIDMLREFLSRLN 669

SMC_prok_B

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

668-784

5.26e-06

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

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 5.26e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  668 EMQRTAIQEREKQFRLQSTRGNL--LLEQERQRNFEKQREER--AGVEKLQSQLRQEQQRWERERARQQQELELAGAR-- 741
Cdd:TIGR02168  685 KIEELEEKIAELEKALAELRKELeeLEEELEQLRKELEELSRqiSALRKDLARLEAEVEQLEERIAQLSKELTELEAEie 764

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907186219  742 -LQEREGEARQMRQRLDQERTELERQRQAYQHDLERLREAQRAV 784
Cdd:TIGR02168  765 eLEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808

mukB

chromosome partition protein MukB;

663-779

1.04e-05

chromosome partition protein MukB;

Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 1.04e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  663 QDSYVEMQRTAIQEREKQFRLQSTRGNLL-LEQ--ERQRNFEKQREERAGVEKLQSQLRQEQQRWERERARQQQELELAG 739
Cdd:PRK04863   495 WDVARELLRRLREQRHLAEQLQQLRMRLSeLEQrlRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESV 574

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1907186219  740 ARLQEREGEARQMRQRLDQERTELERQR---QAYQHDLERLRE 779
Cdd:PRK04863   575 SEARERRMALRQQLEQLQARIQRLAARApawLAAQDALARLRE 617

smart00233

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

384-440

2.84e-04

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

Pssm-ID: 214574 [Multi-domain] Cd Length: 102 Bit Score: 40.99 E-value: 2.84e-04

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907186219   384 SKPPVISLQKLIVREVAN----EEKAMFLISasMQGPEMYEMYTSSKEDRNIWMAHIRRAV 440
Cdd:smart00233   43 KPKGSIDLSGCTVREAPDpdssKKPHCFEIK--TSDRKTLLLQAESEEEREKWVEALRKAI 101

PRK13729

conjugal transfer pilus assembly protein TraB; Provisional

740-892

1.54e-03

conjugal transfer pilus assembly protein TraB; Provisional

Pssm-ID: 184281 [Multi-domain] Cd Length: 475 Bit Score: 42.12 E-value: 1.54e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  740 ARLQEREGEARQMRQRLDQERTEL---ERQRQAYQHDLERLREAQRAVdrererlellrrfKKQNTVPGALPPEVLAE-- 814
Cdd:PRK13729    69 HATTEMQVTAAQMQKQYEEIRRELdvlNKQRGDDQRRIEKLGQDNAAL-------------AEQVKALGANPVTATGEpv 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  815 AQPASHPPSFNGDGLEGHSAPAKAPgtQGSAMLHGTGP----DNVERPEVARWDSAPPesrpaksdvpiqllsaTNQIQR 890
Cdd:PRK13729   136 PQMPASPPGPEGEPQPGNTPVSFPP--QGSVAVPPPTAfypgNGVTPPPQVTYQSVPV----------------PNRIQR 197


                   ..
gi 1907186219  891 QT 892
Cdd:PRK13729   198 KT 199

Name

Accession

Description

Interval

E-value

PH_ARHGEF18

cd15794

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

337-455

4.67e-61

Pssm-ID: 275437 Cd Length: 119 Bit Score: 203.60 E-value: 4.67e-61

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  337 QRQLHLEGALCWKSTSGRLKDVLAVLLTDVLLLLQEKDQKYVFASVDSKPPVISLQKLIVREVANEEKAMFLISASMQGP 416
Cdd:cd15794      1 RRQLLLEGMLYWKAASGRLKDILALLLTDVLLLLQEKDQKYVFASVDSKPPVISLQKLIVREVANEEKAMFLISASLNGP 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1907186219  417 EMYEMYTSSKEDRNIWMAHIRRAVESCPDEEEDVFSEAE 455
Cdd:cd15794     81 EMYEIHTNSKEDRNTWMAHIRRAVESCPDEEEGLFSEPE 119

RhoGEF

cd00160

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

102-296

2.10e-45

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: 161.31 E-value: 2.10e-45

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  102 RQDVLYELMQTEAHHVRTLKIMLKVYSRALQEELQ-FSGQAVSRLFPCADDLLDMHSHFLARLKERRQEfleegSDRNYv 180
Cdd:cd00160      1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKELLpLSPEEVELLFGNIEEIYEFHRIFLKSLEERVEE-----WDKSG- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  181 iQKIGDVLVQQFSgetgerMKEKYAVFCSGHNDAVGQYKLLLQQSKKFQNLIKKIGnfSIVRRLGVQECILLVTQRITKY 260
Cdd:cd00160     75 -PRIGDVFLKLAP------FFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAE--SECGRLKLESLLLKPVQRLTKY 145

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1907186219  261 PVLVERIIQNTEAGTEDYKDLSQALSLIKDIISQVD 296
Cdd:cd00160    146 PLLLKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181

RhoGEF

smart00325

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

105-297

1.70e-42

Pssm-ID: 214619 [Multi-domain] Cd Length: 180 Bit Score: 153.23 E-value: 1.70e-42

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219   105 VLYELMQTEAHHVRTLKIMLKVYSRALQEELQ-FSGQAVSRLFPCADDLLDMHSHFLARLKERRQEFLEEGsdrnyviQK 183
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPLKKELKlLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSV-------ER 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219   184 IGDVLVQQfsgetgERMKEKYAVFCSGHNDAVgqyKLL--LQQSKKFQNLIKKIGNFSIVRRLGVQECILLVTQRITKYP 261
Cdd:smart00325   74 IGDVFLKL------EEFFKIYSEYCSNHPDAL---ELLkkLKKNPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYP 144

                           170       180       190
                    ....*....|....*....|....*....|....*.
gi 1907186219   262 VLVERIIQNTEAGTEDYKDLSQALSLIKDIISQVDA 297
Cdd:smart00325  145 LLLKELLKHTPEDHEDREDLKKALKAIKELANQVNE 180

PH_p190RhoGEF

cd14680

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

343-440

1.82e-40

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: 144.37 E-value: 1.82e-40

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  343 EGALCWKSTSGRLKDVLAVLLTDVLLLLQEKDQKYVFASVDSKPPVISLQKLIVREVANEEKAMFLISASMQGPEMYEMY 422
Cdd:cd14680      4 EGLVYWKTATGRFKDILALLLTDVLLFLQEKDQKYIFAAVDQKPPVICLQKLIVREVANEERGMFLISASSAGPEMYEIH 83

                           90
                   ....*....|....*...
gi 1907186219  423 TSSKEDRNIWMAHIRRAV 440
Cdd:cd14680     84 TSSKEERNNWMRLIQEAV 101

PH_ARHGEF2

cd13393

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

337-455

1.04e-36

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: 134.24 E-value: 1.04e-36

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  337 QRQLHLEGALCWKSTSGRLKDVLAVLLTDVLLLLQEKDQKYVFASVDsKPPVISLQKLIVREVANEEKAMFLISASmqGP 416
Cdd:cd13393      1 RRKLIHDGCLLWKTASGRFKDVQVLLMTDVLVFLQEKDQKYIFPTLD-KPAVISLQNLIVRDIANQEKGMFLISAA--PP 77

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1907186219  417 EMYEMYTSSKEDRNIWMAHIRRAVESCPDEEEDVFSEAE 455
Cdd:cd13393     78 EMYEVHAASRDDRNTWMRLIQQTVKTCPSREEFPLIETE 116

RhoGEF

pfam00621

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

105-296

1.80e-36

Pssm-ID: 459876 [Multi-domain] Cd Length: 176 Bit Score: 135.89 E-value: 1.80e-36

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  105 VLYELMQTEAHHVRTLKIMLKVYSRALQEELQFSGQAVSRLFPCADDLLDMHshflarlkerRQEFLEEGSDRNYVIQKI 184
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEIKTIFSNIEEIYELH----------RQLLLEELLKEWISIQRI 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  185 GDVLVQQFSGetgermKEKYAVFCSGHNDAVGQYKLLLQQSKKFQNLIKKIGNFSIVRRLGVQECILLVTQRITKYPVLV 264
Cdd:pfam00621   71 GDIFLKFAPG------FKVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLL 144

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1907186219  265 ERIIQNTEAGTEDYKDLSQALSLIKDIISQVD 296
Cdd:pfam00621  145 KELLKHTPPDHPDYEDLKKALEAIKEVAKQIN 176

PH_ARHGEF2_18_like

cd15789

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

340-440

3.87e-34

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: 126.42 E-value: 3.87e-34

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  340 LHLEGALCWKSTSGRLKDVLAVLLTDVLLLLQEKDQKYVFASVDSKPPVISLQKLIVREVANEEKAMFLISASMqgPEMY 419
Cdd:cd15789      1 LKFEGTAWLKQARGKTKDVLVVVLTDVLFFLQEKDQKYVFVSPDNKAGVVSLQKLLVREKAGQEKRMFLISASP--DGMP 78

                           90       100
                   ....*....|....*....|....
gi 1907186219  420 EMYTSSKE---DRNIWMAHIRRAV 440
Cdd:cd15789     79 EMYELKVQkpkDKNTWIQTIRQAV 102

PH_16

pfam17838

PH domain;

323-441

6.50e-33

PH domain;

Pssm-ID: 436083 Cd Length: 127 Bit Score: 123.67 E-value: 6.50e-33

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  323 LKNGLTFRKEDMLQQRQLHlEGALCWKSTSGRLKDVLAVLLTDVLLLLQEKDQKYVFAS-------VDSK--PPVISLQK 393
Cdd:pfam17838    1 HPLGEEFKKLDLTTRKLIH-EGPLTWRNSKGKLVEVHALLLEDILVLLQEKDQKLVLAClstgsenVDQKtqSPIISLKK 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1907186219  394 LIVREVANEEKAMFLISASMQGPEMYEMYTSSKEDRNIWMAHIRRAVE 441
Cdd:pfam17838   80 LIVREVATDKKAFFLISTSPSDPQMYELHASTKSERNTWTKLIQDAIE 127

PH_RhoGEF

cd13329

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

340-440

3.27e-29

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: 112.36 E-value: 3.27e-29

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  340 LHlEGALCWKSTSGRLKDVLAVLLTDVLLLLQEKDQKYV--------FASVDSKPPVISLQKLIVREVANEEKAMFLISA 411
Cdd:cd13329      2 IH-EGPLTWKVARGKLIEVHVLLLEDLLVLLQKQDDKYLlklhltgsFDSKDTKSPVIKLSTLLVREVATDKKAFFLIST 80

                           90       100
                   ....*....|....*....|....*....
gi 1907186219  412 SMQGPEMYEMYTSSKEDRNIWMAHIRRAV 440
Cdd:cd13329     81 SKNGPQMYELVANSSSERKTWIKHISDAV 109

PH_AKAP13

cd13392

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

343-442

3.54e-29

A-kinase anchoring protein 13 Pleckstrin homology (PH) domain; The Rho-specific GEF activity of AKAP13 (also called Brx-1, AKAP-Lbc, and proto-Lbc) mediates signaling downstream of G-protein coupled receptors and Toll-like receptor 2. It plays a role in cell growth, cell development and actin fiber formation. Protein kinase A (PKA) binds and phosphorylates AKAP13, regulating its Rho-GEF activity. Alternative splicing of this gene in humans has at least 3 transcript variants encoding different isoforms (i.e. proto-/onco-Lymphoid blast crisis, Lbc and breast cancer nuclear receptor-binding auxiliary protein, Brx) containing a dbl oncogene homology (DH) domain and PH domain which are required for full transforming activity. The DH domain is associated with guanine nucleotide exchange activation while the PH domain has multiple functions including determine protein sub-cellular localisation via phosphoinositide interactions, while others bind protein partners. Other ligands include protein kinase C which is bound by the PH domain of AKAP13, serving to activate protein kinase D and mobilize a cardiac hypertrophy signaling pathway. 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: 275427 Cd Length: 103 Bit Score: 112.31 E-value: 3.54e-29

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  343 EGALCWKSTSGRLKDVLAVLLTDVLLLLQEKDQKYVFASVDSKPPVISLQKLIVREVANEEKAMFLISASMQGPEMYEMY 422
Cdd:cd13392      4 DGPVSLKNTAGRLKEVQAVLLSDVLVFLQEKDQKYVFASLDQKSTVISLKKLIVREVAHEEKGLFLISMGIADPEMVEVH 83

                           90       100
                   ....*....|....*....|
gi 1907186219  423 TSSKEDRNIWMAHIRRAVES 442
Cdd:cd13392     84 ASSKEERNSWMQIIQDTINT 103

PH_PRG

cd13391

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

329-440

3.29e-13

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: 67.75 E-value: 3.29e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  329 FRKEDMLQQRQLHlEGALCWKSTSGRLKDVLAVLLTDVLLLLQEKDQKYVF--------ASVDSK---PPVISLQKLIVR 397
Cdd:cd13391     18 FKNLDLTTRRMIH-EGPLTWRISKDKTLDLHVLLLEDLLVLLQKQDEKLVLkchsktavGSSDSKqtfSPVLKLNSVLIR 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1907186219  398 EVANEEKAMFLISASMQGPEMYEMYTSSKEDRNIWMAHIRRAV 440
Cdd:cd13391     97 SVATDKRALFIICTSKLGPQIYELVALTSSEKNTWMELLEEAV 139

PH_LARG

cd13390

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

329-438

2.69e-10

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: 59.23 E-value: 2.69e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  329 FRKEDMLQQRQLHlEGALCWKSTSGRLKDVLAVLLTDVLLLLQEKDQKYVF--------ASVDSK---PPVISLQKLIVR 397
Cdd:cd13390     16 LRNLDLTKRKMIH-EGPLTWKVNRDKTIDLYTLLLEDILVLLQKQDDRLVLrchskilaSTADSKhtfSPVIKLNTVLVR 94

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1907186219  398 EVANEEKAMFLISASMQGPEMYEMYTSSKEDRNIWMAHIRR 438
Cdd:cd13390     95 QVATDNKAFFVISMSENGAQIYELVAQTVSEKTVWQDLITR 135

DUF5401

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

667-783

3.58e-08

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: 57.44 E-value: 3.58e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  667 VEMQRTAIQEREKQfRLQSTRGNLLLEQERQRNFEKQREERAGVEKLQSQLRQEQ-QRWERERARqqqELElagaRLQER 745
Cdd:pfam17380  383 LQMERQQKNERVRQ-ELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREvRRLEEERAR---EME----RVRLE 454

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1907186219  746 EGEARQMRQRLDQErtELERQRQAYQHDLERlREAQRA 783
Cdd:pfam17380  455 EQERQQQVERLRQQ--EEERKRKKLELEKEK-RDRKRA 489

Smc

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

658-781

4.96e-08

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 4.96e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  658 AVIAQQDSYVEMQRTAIQEREKQFRLQSTRgnlLLEQERQRNFEKQREERAGVEKLQsqLRQEQQRWERERARQQQELEL 737
Cdd:COG1196    267 AELEELRLELEELELELEEAQAEEYELLAE---LARLEQDIARLEERRRELEERLEE--LEEELAELEEELEELEEELEE 341

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907186219  738 AGARLQEREGEARQMRQRLDQERTELERQRQAYQHDLERLREAQ 781
Cdd:COG1196    342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385

DUF5401

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

660-781

6.18e-08

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: 56.67 E-value: 6.18e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  660 IAQQDSYVEMQRtaIQEREKQFRLQSTRGNLLLEQERQRNFEKQREEragvekLQSQLRQEQQRWERERARQQQELELAG 739
Cdd:pfam17380  353 IRQEERKRELER--IRQEEIAMEISRMRELERLQMERQQKNERVRQE------LEAARKVKILEEERQRKIQQQKVEMEQ 424

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1907186219  740 ARLQEREGEARQMRqRLDQERT-ELERQRQ---AYQHDLERLREAQ 781
Cdd:pfam17380  425 IRAEQEEARQREVR-RLEEERArEMERVRLeeqERQQQVERLRQQE 469

Smc

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

660-783

6.35e-08

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 6.35e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  660 IAQQDSYVEMQRTAIQEREKQFRLQSTRGNLLLEQ----ERQRNFEKQREERAGVEKLqsQLRQEQQRWERERARQQQEL 735
Cdd:COG1196    262 LAELEAELEELRLELEELELELEEAQAEEYELLAElarlEQDIARLEERRRELEERLE--ELEEELAELEEELEELEEEL 339

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1907186219  736 ELAGARLQEREGEARQMRQRLDQERTELERQRQAYQHDLERLREAQRA 783
Cdd:COG1196    340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

PH_p115RhoGEF

cd14679

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

329-440

1.65e-07

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: 51.00 E-value: 1.65e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  329 FRKEDMLQQRQLHlEGALCWKSTSGRLKDVLAVLLTDVLLLLQEKDQKYVF--------ASVDSK---PPVISLQKLIVR 397
Cdd:cd14679      1 FKNIDITKKKLVH-EGPLTWRVTKDKAIEVHVLLLDDLLVLLQKQDERLVLkchsrtttPTPDGKqmlSPIIKLNSAMTR 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1907186219  398 EVANEEKAMFLISASMQGPEMYEMYTSSKEDRNIWMAHIRRAV 440
Cdd:cd14679     80 EVATDRKAFYVIFTWEQGAQIYELVAQTVSERKNWCALISETA 122

ROM1

COG5422

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

74-296

1.89e-07

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

Pssm-ID: 227709 [Multi-domain] Cd Length: 1175 Bit Score: 55.28 E-value: 1.89e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219   74 DAHEFEAESWSLSVDLAYAKKQKKEVVKRQDVLYELMQTEAHHVRTLKIMLKVYSRALQEELQFSGQA----VSRLFPCA 149
Cdd:COG5422    457 DKFDEEKNLWTLSVPKEVWESLPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWIKPLEESNIIPENArrnfIKHVFANI 536

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  150 DDLLDMHSHFLARLkeRRQEFLEEgsdrnyVIQKIGDVLVQQFSgetgermkeKYAVFCS-GHNDAVGQYKLLLQQS--K 226
Cdd:COG5422    537 NEIYAVNSKLLKAL--TNRQCLSP------IVNGIADIFLDYVP---------KFEPFIKyGASQPYAKYEFEREKSvnP 599

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  227 KFQNLIKKIGNFSIVRRLGVQECILLVTQRITKYPVLVERIIQNTEAGTEDYKDLSQALSLIKDIISQVD 296
Cdd:COG5422    600 NFARFDHEVERLDESRKLELDGYLTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVIDMLREFLSRLN 669

Smc

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

662-785

3.33e-07

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 3.33e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  662 QQDSYVEMQRTAIQEREKQFRLQSTRGNLLLEQERQRNFEKQREE----RAGVEKLQSQLRQEQQRWERERARQQQELEL 737
Cdd:COG1196    311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEaeaeLAEAEEALLEAEAELAEAEEELEELAEELLE 390

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1907186219  738 AGARLQEREGEARQMRQRLDQERTELERQRQAYQHDLERLREAQRAVD 785
Cdd:COG1196    391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438

Smc

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

658-863

6.79e-07

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 6.79e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  658 AVIAQQDSYVEMQRTAIQEREKQFRLQSTRGNLLLEQERQRNFEKQREERAgVEKLQSQLRQEQQRweRERARQQQELEL 737
Cdd:COG1196    359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE-EALLERLERLEEEL--EELEEALAELEE 435

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  738 AGARLQEREGEARQMRQRLDQERTELERQRQAYQHDLERLREAQRAVDRERERLELLRRFKKQNTVPGALPPEVLAEAQP 817
Cdd:COG1196    436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1907186219  818 ASHPPSFNGDGLEGHSAPAKAPGTQGSAMLHGTGPDNVERPEVARW 863
Cdd:COG1196    516 LAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAA 561

YhaN

COG4717

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

661-784

3.02e-06

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 3.02e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  661 AQQDSYVEMQRTAIQEREKQFRLQSTRGNLLLEQERQRNFEKQREERAGVEKLQSQLRQEQQRWERERARQQQELELAgA 740
Cdd:COG4717     85 EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE-E 163

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1907186219  741 RLQEREGEARQMRQRLDQERTEL-ERQRQAYQHDLERLREAQRAV 784
Cdd:COG4717    164 ELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRL 208

DUF4670

pfam15709

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...

676-782

3.19e-06

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.

Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.11 E-value: 3.19e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  676 EREKQFRLQSTRGNLllEQERQRNFEKQREERAgvEKLQSQLRQEQQR---------WERERARQQQELELAGARLQERE 746
Cdd:pfam15709  341 ERAEMRRLEVERKRR--EQEEQRRLQQEQLERA--EKMREELELEQQRrfeeirlrkQRLEEERQRQEEEERKQRLQLQA 416

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1907186219  747 GEARQMRQRLDQERTELERQRQAYQHDLERLREAQR 782
Cdd:pfam15709  417 AQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQ 452

DUF5401

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

659-782

4.14e-06

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: 50.89 E-value: 4.14e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  659 VIAQQDSYVEMQRTAIQEREKQFRLQSTRGNLLLEQERQRNFEKQREERAGVEKLQSQLRQEQQRWERERARqqqelELA 738
Cdd:pfam17380  277 IVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERER-----ELE 351

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907186219  739 GARLQEREGEARQMRQrlDQERTELERQRQAYQHDLERLREAQR 782
Cdd:pfam17380  352 RIRQEERKRELERIRQ--EEIAMEISRMRELERLQMERQQKNER 393

Smc

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

661-787

4.25e-06

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 4.25e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  661 AQQDSYVEMQRTAIQEREKQFRLQSTRGNLLLEQERQRNFEKQREERAGVEKLQSQLRQEQQRWERERARQQQELELAGA 740
Cdd:COG1196    286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1907186219  741 RLQEREGEARQMRQRLDQERTELERQRQAYQHDLERLREAQRAVDRE 787
Cdd:COG1196    366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412

Smc

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

694-783

4.66e-06

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 4.66e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  694 QERQRNFEKQREERAGVEKLQSQLRQEQQRWERERARQQQELELAGARLQEREGE---ARQMRQRLDQERTELERQRQAY 770
Cdd:COG1196    249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDiarLEERRRELEERLEELEEELAEL 328

                           90
                   ....*....|...
gi 1907186219  771 QHDLERLREAQRA 783
Cdd:COG1196    329 EEELEELEEELEE 341

SMC_prok_B

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

668-784

5.26e-06

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 5.26e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  668 EMQRTAIQEREKQFRLQSTRGNL--LLEQERQRNFEKQREER--AGVEKLQSQLRQEQQRWERERARQQQELELAGAR-- 741
Cdd:TIGR02168  685 KIEELEEKIAELEKALAELRKELeeLEEELEQLRKELEELSRqiSALRKDLARLEAEVEQLEERIAQLSKELTELEAEie 764

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907186219  742 -LQEREGEARQMRQRLDQERTELERQRQAYQHDLERLREAQRAV 784
Cdd:TIGR02168  765 eLEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808

YhaN

COG4717

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

641-807

7.94e-06

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 7.94e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  641 ELVHRVQTLSQLLLSLQAVIAQQDSYVEMQRTAIQEREKQFRLQSTRGNLLLEQERQRNFEKQREERAGVEKLQSQLRQE 720
Cdd:COG4717     92 ELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  721 QQRWERERARQQQELELAgarLQEREGEARQMRQRLDQERTELERQRQAYQHDLERLREAQRAVDRERERLELLRRFKKQ 800
Cdd:COG4717    172 LAELQEELEELLEQLSLA---TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248


                   ....*..
gi 1907186219  801 NTVPGAL 807
Cdd:COG4717    249 RLLLLIA 255

mukB

chromosome partition protein MukB;

663-779

1.04e-05

chromosome partition protein MukB;

Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 1.04e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  663 QDSYVEMQRTAIQEREKQFRLQSTRGNLL-LEQ--ERQRNFEKQREERAGVEKLQSQLRQEQQRWERERARQQQELELAG 739
Cdd:PRK04863   495 WDVARELLRRLREQRHLAEQLQQLRMRLSeLEQrlRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESV 574

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1907186219  740 ARLQEREGEARQMRQRLDQERTELERQR---QAYQHDLERLRE 779
Cdd:PRK04863   575 SEARERRMALRQQLEQLQARIQRLAARApawLAAQDALARLRE 617

Smc

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

668-783

1.39e-05

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 1.39e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  668 EMQRTAIQEREKQFRLQSTRGNLLLEQERQRNFEKQREERAG-----VEKLQSQLRQEQQRWERERARQQQELELAG--A 740
Cdd:COG1196    324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEalleaEAELAEAEEELEELAEELLEALRAAAELAAqlE 403

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1907186219  741 RLQEREGEARQMRQRLDQERTELERQRQAYQHDLERLREAQRA 783
Cdd:COG1196    404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446

COG4913

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

670-777

5.17e-05

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 5.17e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  670 QRTAIQEREKQFRLQSTRGNLLLEQERQRNFEKQREERAGVEKLQSQLRQEQQRWERERARQQQELELAGARLQE----R 745
Cdd:COG4913    260 LAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdR 339

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1907186219  746 EGEARQMRQRLDQERTELERQRQAYQHDLERL 777
Cdd:COG4913    340 LEQLEREIERLERELEERERRRARLEALLAAL 371

EnvC

COG4942

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

694-782

5.62e-05

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: 46.68 E-value: 5.62e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  694 QERQRNFEKQREERAGVEKLQSQLRQEQQRWERERARQQQELELAGARLQEREGEARQMRQRLDQ---ERTELERQRQAY 770
Cdd:COG4942     23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekEIAELRAELEAQ 102

                           90
                   ....*....|...
gi 1907186219  771 QHDL-ERLREAQR 782
Cdd:COG4942    103 KEELaELLRALYR 115

HlpA

COG2825

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...

711-779

8.53e-05

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];

Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 44.06 E-value: 8.53e-05

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907186219  711 EKLQSQLRQEQQRWERERARQQQELELAGARLQEREG-----EARQMRQRLDQERTELERQRQAYQHDLERLRE 779
Cdd:COG2825     42 KAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEAAtlseeERQKKERELQKKQQELQRKQQEAQQDLQKRQQ 115

DUF5401

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

662-782

8.76e-05

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: 8.76e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  662 QQDSYVEMQRTAI-QEREKQFRLQSTRGNLL-LEQERQRNFEKQ-----REERAGVEKLQS--QLRQEQQRWERERARQQ 732
Cdd:pfam17380  289 QQEKFEKMEQERLrQEKEEKAREVERRRKLEeAEKARQAEMDRQaaiyaEQERMAMEREREleRIRQEERKRELERIRQE 368

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907186219  733 qELELAGARLQEREGEARQMRQRLDQERTELERQRQAYQHDLERLREAQR 782
Cdd:pfam17380  369 -EIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQ 417

EnvC

COG4942

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

692-808

1.28e-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: 45.53 E-value: 1.28e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  692 LEQERQRNFEKQREERAGVEKLQSQLRQEQQRWERERARQQQELelagARLQEREGEARQMRQRLDQERTELERQRQAYQ 771
Cdd:COG4942    144 LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEER----AALEALKAERQKLLARLEKELAELAAELAELQ 219

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907186219  772 HDLERLREAQRAVDRERERLELLRRFKKQNTVPGALP 808
Cdd:COG4942    220 QEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256

Smc

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

673-784

1.39e-04

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 1.39e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  673 AIQEREKQFRLQSTRGNLLLEQERQRNFEKQREERAGVEKLQSQLRQEQQRWERERARQQQELELAGARLQEREGEARQM 752
Cdd:COG1196    658 AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1907186219  753 RQRLDQERTELERQRQAYQHDLERLREAQRAV 784
Cdd:COG1196    738 LEELLEEEELLEEEALEELPEPPDLEELEREL 769

pfam00169

PH domain; PH stands for pleckstrin homology.

376-441

1.58e-04

PH domain; PH stands for pleckstrin homology.

Pssm-ID: 459697 [Multi-domain] Cd Length: 105 Bit Score: 41.78 E-value: 1.58e-04

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907186219  376 KYVFASVDSKP-PVISLQKLIVREVANEEKA----MF-LISASMQGPEMYEMYTSSKEDRNIWMAHIRRAVE 441
Cdd:pfam00169   34 KDDKSGKSKEPkGSISLSGCEVVEVVASDSPkrkfCFeLRTGERTGKRTYLLQAESEEERKDWIKAIQSAIR 105

TPH

pfam13868

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

673-779

1.75e-04

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: 44.91 E-value: 1.75e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  673 AIQEREKQFRLQSTRGNLLLEQERQRNFEKQREE---RAGVEKLQSQLRQEQQRWERERARQQQELELAGARLQEREGEA 749
Cdd:pfam13868  227 AEKKARQRQELQQAREEQIELKERRLAEEAEREEeefERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQR 306

                           90       100       110
                   ....*....|....*....|....*....|
gi 1907186219  750 RQMRQRLDQERTELERQRQAYQHDLERLRE 779
Cdd:pfam13868  307 AAEREEELEEGERLREEEAERRERIEEERQ 336

Smc

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

638-783

1.92e-04

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 1.92e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  638 LELELVHRVQTLSQLLLSLQAVIAQQDSYVEMQRTAIQEREKQFRLQSTRGNLLLEQERQRNFEKQREERAgvekLQSQL 717
Cdd:COG1196    321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA----LRAAA 396

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907186219  718 RQEQQrwERERARQQQELELAGARLQEREGEARQMRQRLDQERTELERQRQAYQHDLERLREAQRA 783
Cdd:COG1196    397 ELAAQ--LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460

COG4913

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

658-785

2.13e-04

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.13e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  658 AVIAQQDSYVEMQRTAIQEREKQFRLQSTRgnllleqERQRNFEKQREERAGVEKLQSQLRQEqqrwereraRQQQELEL 737
Cdd:COG4913    229 ALVEHFDDLERAHEALEDAREQIELLEPIR-------ELAERYAAARERLAELEYLRAALRLW---------FAQRRLEL 292

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1907186219  738 AGARLQEREGEArqmrQRLDQERTELERQRQAYQHDLERLREAQRAVD 785
Cdd:COG4913    293 LEAELEELRAEL----ARLEAELERLEARLDALREELDELEAQIRGNG 336

smart00233

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

384-440

2.84e-04

Pssm-ID: 214574 [Multi-domain] Cd Length: 102 Bit Score: 40.99 E-value: 2.84e-04

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907186219   384 SKPPVISLQKLIVREVAN----EEKAMFLISasMQGPEMYEMYTSSKEDRNIWMAHIRRAV 440
Cdd:smart00233   43 KPKGSIDLSGCTVREAPDpdssKKPHCFEIK--TSDRKTLLLQAESEEEREKWVEALRKAI 101

SMC_prok_A

TIGR02169

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

667-782

4.12e-04

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

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 4.12e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  667 VEMQRTAIQEREKQFRLQStrgnllLEQERQRNFEKQREERAGVEKLQSQLRQEQQR---WERERARQQQELELAGARLQ 743
Cdd:TIGR02169  301 AEIASLERSIAEKERELED------AEERLAKLEAEIDKLLAEIEELEREIEEERKRrdkLTEEYAELKEELEDLRAELE 374

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1907186219  744 EREGEARQMRQRLDQERTELE---RQRQAYQHDLERLREAQR 782
Cdd:TIGR02169  375 EVDKEFAETRDELKDYREKLEklkREINELKRELDRLQEELQ 416

PRK12704

phosphodiesterase; Provisional

674-777

4.88e-04

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 4.88e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  674 IQEREKQfrLQSTRGNLLLE-----QERQRNFEKQ-REERAGVEKLQSQLRQEQQRWERErarqQQELELAGARLQEREG 747
Cdd:PRK12704    44 LEEAKKE--AEAIKKEALLEakeeiHKLRNEFEKElRERRNELQKLEKRLLQKEENLDRK----LELLEKREEELEKKEK 117

                           90       100       110
                   ....*....|....*....|....*....|
gi 1907186219  748 EARQMRQRLDQERTELERQRQAYQHDLERL 777
Cdd:PRK12704   118 ELEQKQQELEKKEEELEELIEEQLQELERI 147

HAUS5

pfam14817

HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. ...

687-782

4.90e-04

HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.

Pssm-ID: 464332 [Multi-domain] Cd Length: 643 Bit Score: 43.88 E-value: 4.90e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  687 RGNLLL---------EQERQRNFEKQREERAGVEKLQ---SQLRQEQQRWERERARQQQELELAgarLQEREgEARQ--- 751
Cdd:pfam14817   54 RGNLLWygglqdkgkAESRQSAAARRLELQKEIERLRaeiSRLDKQLEARELELSREEAERERA---LDEIS-DSRHrql 129

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1907186219  752 ----MRQRLDQERTELERQRQAYQHDLERLREAQR 782
Cdd:pfam14817  130 lleaYDQQCEEARKILAEDHQRLQGQLQQLRDAAR 164

SMC_prok_B

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

660-783

4.93e-04

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 4.93e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  660 IAQQDSYVEMQRTAIQEREKQFR-LQSTRGNLLLEQER-QRNFEKQREERAGVEKLQSQLRQEQQRWERERARQQQEL-- 735
Cdd:TIGR02168  262 LQELEEKLEELRLEVSELEEEIEeLQKELYALANEISRlEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELae 341

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  736 ------------ELAGARLQEREGEARQMRQRLDQERTELERQRQAYqHDLERLREAQRA 783
Cdd:TIGR02168  342 leekleelkeelESLEAELEELEAELEELESRLEELEEQLETLRSKV-AQLELQIASLNN 400

MAP7

pfam05672

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...

676-777

5.59e-04

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.

Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 41.56 E-value: 5.59e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  676 EREKQFRLQSTRGNLLLEQERQRNFEKQR----EERAGVEKLQSQLRQEQQRWERERARQQQELELAGARLQEREGEARQ 751
Cdd:pfam05672   28 EREEQERLEKEEEERLRKEELRRRAEEERarreEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEEAE 107

                           90       100
                   ....*....|....*....|....*.
gi 1907186219  752 MRQRLDQERTELERQRQAYQHDLERL 777
Cdd:pfam05672  108 AKAREEAERQRQEREKIMQQEEQERL 133

CusB_dom_1

pfam00529

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...

661-783

6.80e-04

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.

Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 43.18 E-value: 6.80e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  661 AQQDSYVEMQRTAIQEREKQFRLQSTRGnlLLEQERQRNFEKQREERAGVEKLQSQLRQEQQRWERER------ARQQQE 734
Cdd:pfam00529   65 AQLAKAQAQVARLQAELDRLQALESELA--ISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRvlapigGISRES 142

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1907186219  735 LELAGARLQEREGEARQMRQRLDQERTELERQRQAYQHDLERLREAQRA 783
Cdd:pfam00529  143 LVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQL 191

SMC_prok_B

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

668-782

6.98e-04

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 6.98e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  668 EMQRTAIQEREKQFRLQSTRGNLLLEQERQRNfEKQREERAGVEKLQSQL-RQEQQRWERERARQQQELELAGARLQERE 746
Cdd:TIGR02168  368 EELESRLEELEEQLETLRSKVAQLELQIASLN-NEIERLEARLERLEDRReRLQQEIEELLKKLEEAELKELQAELEELE 446

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1907186219  747 GEARQMRQRLDQERTELERQRQAYQHDLERLREAQR 782
Cdd:TIGR02168  447 EELEELQEELERLEEALEELREELEEAEQALDAAER 482

COG4913

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

668-787

7.53e-04

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 7.53e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  668 EMQRTAIQEREKQFRLQSTRGNLLLEQERQRNFEKQREERAgvEKLQSQLRQEQQRWERERARQQQELELAG-------A 740
Cdd:COG4913    303 ELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL--EREIERLERELEERERRRARLEALLAALGlplpasaE 380

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1907186219  741 RLQEREGEARQMRQRLDQERTELERQRQAYQHDLERLREAQRAVDRE 787
Cdd:COG4913    381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427

SMC_prok_B

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

668-780

1.11e-03

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 1.11e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  668 EMQRTAIQEREKQFRLQSTRGNLLLEQERQRNFEKQREERAG-VEKLQSQLRQEQQrwerERARQQQELELAGARLQERE 746
Cdd:TIGR02168  811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEdIESLAAEIEELEE----LIEELESELEALLNERASLE 886

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907186219  747 GEARQMRQRLDQERTEL---ERQRQAYQHDLERLREA 780
Cdd:TIGR02168  887 EALALLRSELEELSEELrelESKRSELRRELEELREK 923

mukB

chromosome partition protein MukB;

658-781

1.13e-03

chromosome partition protein MukB;

Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.13e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  658 AVIAQQDSYVEMQR--TAIQEREK--QFRLQSTRGNLLLEQERQRNFEKQREERAGVEKLQSQLRQeqqrwererarQQQ 733
Cdd:PRK04863   301 QLAAEQYRLVEMARelAELNEAESdlEQDYQAASDHLNLVQTALRQQEKIERYQADLEELEERLEE-----------QNE 369

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907186219  734 ELELAGARLQEREGEARQMRQRLDQERTEL--------ERQRQA--YQHDLERLREAQ 781
Cdd:PRK04863   370 VVEEADEQQEENEARAEAAEEEVDELKSQLadyqqaldVQQTRAiqYQQAVQALERAK 427

SMC_prok_B

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

670-780

1.19e-03

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 1.19e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  670 QRTAIQEREKQFRLQstrgnllleQERQRNFEKQREE-RAGVEKLQSQLRQEQQRWERERaRQQQELELAGARLQEREGE 748
Cdd:TIGR02168  675 RRREIEELEEKIEEL---------EEKIAELEKALAElRKELEELEEELEQLRKELEELS-RQISALRKDLARLEAEVEQ 744

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1907186219  749 ARQMRQRLDQERTELERQRQAYQHDLERLREA 780
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAEEE 776

Smc

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

668-780

1.23e-03

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 1.23e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  668 EMQRTAIQEREKQFRLQSTRGNLLLEQERQRNFEKQREERAGVEKLQSQLRQEQQRWERERARQQQELELAGARLQEREG 747
Cdd:COG1196    652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907186219  748 EARQMRQRLDQERTELERQ-----------RQAYQHDLERLREA 780
Cdd:COG1196    732 AEREELLEELLEEEELLEEealeelpeppdLEELERELERLERE 775

fliH

PRK06800

flagellar assembly protein H; Validated

693-763

1.31e-03

flagellar assembly protein H; Validated

Pssm-ID: 180700 Cd Length: 228 Bit Score: 41.40 E-value: 1.31e-03

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907186219  693 EQERQRNFEKQREERAGVEKLQSQLRQEQQRWERERARQQQELELAGARLQEREGEARQMRQRLDQERTEL 763
Cdd:PRK06800    33 EEEIQKDHEELLAQQKSLHKELNQLRQEQQKLERERQQLLADREQFQEHVQQQMKEIEAARQQFQKEQQET 103

YqiK

COG2268

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];

692-784

1.32e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];

Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.55 E-value: 1.32e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  692 LEQERQRNFEKQREERAGVEKLQSQLRQEQqrwERERARQQQELELAGARLQ---EREGEARQMRQRLDQERTELERQRQ 768
Cdd:COG2268    228 LEQEREIETARIAEAEAELAKKKAEERREA---ETARAEAEAAYEIAEANAErevQRQLEIAEREREIELQEKEAEREEA 304

                           90
                   ....*....|....*.
gi 1907186219  769 AYQHDLERLREAQRAV 784
Cdd:COG2268    305 ELEADVRKPAEAEKQA 320

DUF5401

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

668-778

1.37e-03

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: 42.80 E-value: 1.37e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  668 EMQRTAIQEREKQFRLQSTRGNLLLEQERQRNFEKQREERAGVEKLQSQLrQEQQRWERERARQQQELElagARLQEREG 747
Cdd:pfam17380  447 EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI-LEKELEERKQAMIEEERK---RKLLEKEM 522

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1907186219  748 EARQMRQRLDQERTELERQRQAYQHDLERLR 778
Cdd:pfam17380  523 EERQKAIYEEERRREAEEERRKQQEMEERRR 553

PRK13729

conjugal transfer pilus assembly protein TraB; Provisional

740-892

1.54e-03

conjugal transfer pilus assembly protein TraB; Provisional

Pssm-ID: 184281 [Multi-domain] Cd Length: 475 Bit Score: 42.12 E-value: 1.54e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  740 ARLQEREGEARQMRQRLDQERTEL---ERQRQAYQHDLERLREAQRAVdrererlellrrfKKQNTVPGALPPEVLAE-- 814
Cdd:PRK13729    69 HATTEMQVTAAQMQKQYEEIRRELdvlNKQRGDDQRRIEKLGQDNAAL-------------AEQVKALGANPVTATGEpv 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  815 AQPASHPPSFNGDGLEGHSAPAKAPgtQGSAMLHGTGP----DNVERPEVARWDSAPPesrpaksdvpiqllsaTNQIQR 890
Cdd:PRK13729   136 PQMPASPPGPEGEPQPGNTPVSFPP--QGSVAVPPPTAfypgNGVTPPPQVTYQSVPV----------------PNRIQR 197


                   ..
gi 1907186219  891 QT 892
Cdd:PRK13729   198 KT 199

CCDC158

pfam15921

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...

660-785

1.84e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.

Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 1.84e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  660 IAQQDSYVEMQRTAIQEREKQFRLQ--STRGNLLLEQERQRN----FEKQREE-RAGVEKLQSQLRQEQQRWERERARQQ 732
Cdd:pfam15921  269 IEQLISEHEVEITGLTEKASSARSQanSIQSQLEIIQEQARNqnsmYMRQLSDlESTVSQLRSELREAKRMYEDKIEELE 348

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907186219  733 QELELAGARLQEregeARQMRQRLDQERTELERQRQAYQHDLERlREAQRAVD 785
Cdd:pfam15921  349 KQLVLANSELTE----ARTERDQFSQESGNLDDQLQKLLADLHK-REKELSLE 396

COG4913

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

667-780

1.86e-03

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.86e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  667 VEMQRTAIQEREKQfRLQSTRGNLLLEQ-ERQRnfEKQREERAGVEKLQSQLRQEQQRWERERARQQQELELAGARLQER 745
Cdd:COG4913    663 VASAEREIAELEAE-LERLDASSDDLAAlEEQL--EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907186219  746 EGEA---------------------RQMRQRLDQERTELERQRQAYQHDLERLREA 780
Cdd:COG4913    740 EDLArlelralleerfaaalgdaveRELRENLEERIDALRARLNRAEEELERAMRA 795

DUF5401

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

663-782

1.93e-03

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: 42.03 E-value: 1.93e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  663 QDSYVEMQRT-AIQEREKQFRLQstrgnlLLEQERQRNFEKQREERAGVEKLQSQLRQEQQRWERERA------RQQQEL 735
Cdd:pfam17380  416 QQQKVEMEQIrAEQEEARQREVR------RLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLelekekRDRKRA 489

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907186219  736 ELAGARLQEREGEARQM------RQRLDQERTELERQRQAYQHDLERLREAQR 782
Cdd:pfam17380  490 EEQRRKILEKELEERKQamieeeRKRKLLEKEMEERQKAIYEEERRREAEEER 542

mukB

chromosome partition protein MukB;

662-786

1.99e-03

chromosome partition protein MukB;

Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 1.99e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  662 QQDSYVEMQRTAIQEREKQFRLQSTRGNLLLEQERQR-----NFEKQREERAGVEKLQSQLRQEQQRWEReRARQQQELE 736
Cdd:PRK04863   531 QQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLeslseSVSEARERRMALRQQLEQLQARIQRLAA-RAPAWLAAQ 609

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907186219  737 LAGARLQEREGEARQMRQRLDQER-TELERQRQAYQHDlERLREAQRAVDR 786
Cdd:PRK04863   610 DALARLREQSGEEFEDSQDVTEYMqQLLERERELTVER-DELAARKQALDE 659

DUF4670

pfam15709

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...

667-783

2.58e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.

Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.48 E-value: 2.58e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  667 VEMQRtaiQEREKQFRLQ------STRGNLLLEQERQRNFE-----KQREEragvEKLQSQLRQEQQRW-----ERERAR 730
Cdd:pfam15709  350 VERKR---REQEEQRRLQqeqlerAEKMREELELEQQRRFEeirlrKQRLE----EERQRQEEEERKQRlqlqaAQERAR 422

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907186219  731 QQQE------LELAGARLQE--REGEARQMRQRLDQERTELERQR---QAYQHDLERLREAQRA 783
Cdd:pfam15709  423 QQQEefrrklQELQRKKQQEeaERAEAEKQRQKELEMQLAEEQKRlmeMAEEERLEYQRQKQEA 486

TPH

pfam13868

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

660-783

3.19e-03

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.06 E-value: 3.19e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  660 IAQQDSYVEMQRTAIQERE---KQFRLQSTRGNLLLEQERQRNFEKQREERAGVEKLQSQLRQEQQRWERERARQQQELE 736
Cdd:pfam13868  136 NEEQAEWKELEKEEEREEDeriLEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQ 215

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1907186219  737 LAGARLQEREGEARQMRQRLdqertELERQRQAYQHDLERLREAQRA 783
Cdd:pfam13868  216 ERKERQKEREEAEKKARQRQ-----ELQQAREEQIELKERRLAEEAE 257

Smc

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

682-781

3.44e-03

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 3.44e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907186219  682 RLQSTRGNL------LLEQERQRN-FEKQRE--ERAgvEKLQSQLRQEQQRW--------ERERARQQQELELAGARLQE 744
Cdd:COG1196    180 KLEATEENLerlediLGELERQLEpLERQAEkaERY--RELKEELKELEAELlllklrelEAELEELEAELEELEAELEE 257

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1907186219  745 REGEARQM---RQRLDQERTELERQRQAYQHDLERLREAQ 781
Cdd:COG1196    258 LEAELAELeaeLEELRLELEELELELEEAQAEEYELLAEL 297

SMC_prok_B