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Conserved domains on  [gi|4557779|ref|NP_000252|]
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myocilin precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OLF super family cl02549
Olfactomedin-like domain;
246-502 1.99e-143

Olfactomedin-like domain;


The actual alignment was detected with superfamily member smart00284:

Pssm-ID: 470611  Cd Length: 255  Bit Score: 411.92  E-value: 1.99e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779     246 GELVWVGEPLTLRTAETitGKYGVWMRDPKPTYPYtQETTWRIDTVGTDVRQVFEYDLISQFMQGYPSKVHILPRPLEST 325
Cdd:smart00284   1 GGLAGISKPVTLQTSWK--GKSGAWMKDPLWNTTK-KSLYWYMPLNTRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGT 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779     326 GAVVYSGSLYFQGAESRTVIRYELNTETVKAEKEIPGAGYHGQFPYSWGGYTDIDLAVDEAGLWVIYSTDEAKGAIVLSK 405
Cdd:smart00284  78 GVVVYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISK 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779     406 LNPENLELEQTWETNIRKQSVANAFIICGTLYTVSSYTSADATVNFAYDTGTGISKTLTIPFKNRYKYSSMIDYNPLEKK 485
Cdd:smart00284 158 LNPATLTIENTWITTYNKRSASNAFMICGILYVTRSLGSKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPNDRK 237

                          250
                   ....*....|....*..
gi 4557779     486 LFAWDNLNMVTYDIKLS 502
Cdd:smart00284 238 LYAWNNGHLVHYDIALK 254
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
71-196 1.35e-07

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


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.54  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779    71 IHNLQRDSSTQRLDLEATKARLSSLESLLHQLTLDqaarPQETQEGLQRELGTLRRERDQLETQTRELETAYSNLLRDKS 150
Cdd:COG4913  340 LEQLEREIERLERELEERERRRARLEALLAALGLP----LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR 415

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 4557779   151 VLEEEKKRLRQENENLARRLESSSQEVARLRRGQCPQTRDTARAVP 196
Cdd:COG4913  416 DLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELP 461
 
Name Accession Description Interval E-value
OLF smart00284
Olfactomedin-like domains;
246-502 1.99e-143

Olfactomedin-like domains;


Pssm-ID: 128580  Cd Length: 255  Bit Score: 411.92  E-value: 1.99e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779     246 GELVWVGEPLTLRTAETitGKYGVWMRDPKPTYPYtQETTWRIDTVGTDVRQVFEYDLISQFMQGYPSKVHILPRPLEST 325
Cdd:smart00284   1 GGLAGISKPVTLQTSWK--GKSGAWMKDPLWNTTK-KSLYWYMPLNTRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGT 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779     326 GAVVYSGSLYFQGAESRTVIRYELNTETVKAEKEIPGAGYHGQFPYSWGGYTDIDLAVDEAGLWVIYSTDEAKGAIVLSK 405
Cdd:smart00284  78 GVVVYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISK 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779     406 LNPENLELEQTWETNIRKQSVANAFIICGTLYTVSSYTSADATVNFAYDTGTGISKTLTIPFKNRYKYSSMIDYNPLEKK 485
Cdd:smart00284 158 LNPATLTIENTWITTYNKRSASNAFMICGILYVTRSLGSKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPNDRK 237

                          250
                   ....*....|....*..
gi 4557779     486 LFAWDNLNMVTYDIKLS 502
Cdd:smart00284 238 LYAWNNGHLVHYDIALK 254
OLF pfam02191
Olfactomedin-like domain;
248-501 9.22e-125

Olfactomedin-like domain;


Pssm-ID: 460482  Cd Length: 246  Bit Score: 364.16  E-value: 9.22e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779    248 LVWVGEPLTLRTAEtitGKYGVWMRDPKPTYpytqETTWRIDTvGTDVRQVFEYDLISQFMQGYPSKVHILPRPLESTGA 327
Cdd:pfam02191   1 LVSVSKPVTVKLSG---GKYGAWMKDPLPPS----DKIYVTDR-GTSGNTLREYASLDDFKNGSPSKKYKLPYPWQGTGH 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779    328 VVYSGSLYFQGAESRTVIRYELNTETVKAEKEIPGAGYHGQFPYSWGGYTDIDLAVDEAGLWVIYSTDEAKGAIVLSKLN 407
Cdd:pfam02191  73 VVYNGSLYYNKYNSRNIVKYDLTTRTVAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779    408 PENLELEQTWETNIRKQSVANAFIICGTLYTVSSYTSADATVNFAYDTGTGISKTLTIPFKNRYKYSSMIDYNPLEKKLF 487
Cdd:pfam02191 153 PETLEVEQTWNTSYPKRSAGNAFMVCGVLYAVRSVNTRREEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLY 232

                         250
                  ....*....|....
gi 4557779    488 AWDNLNMVTYDIKL 501
Cdd:pfam02191 233 AWDDGYQVTYPVTF 246
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
71-196 1.35e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.54  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779    71 IHNLQRDSSTQRLDLEATKARLSSLESLLHQLTLDqaarPQETQEGLQRELGTLRRERDQLETQTRELETAYSNLLRDKS 150
Cdd:COG4913  340 LEQLEREIERLERELEERERRRARLEALLAALGLP----LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR 415

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 4557779   151 VLEEEKKRLRQENENLARRLESSSQEVARLRRGQCPQTRDTARAVP 196
Cdd:COG4913  416 DLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELP 461
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 71-171 1.07e-05

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 44.94  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779     71 IHNLQRDSSTQRLDLEATKARLSSLESLLHQltldQAARPQETQEGLQRE----------LGTLRRERDQLETQTREL-- 138
Cdd:pfam07926   3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEK----QAEIAREAQQNYERElvlhaedikaLQALREELNELKAEIAELka 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 4557779    139 --ETAYSNLLRDKSVLEEEKKRLRQENENLARRLE 171
Cdd:pfam07926  79 eaESAKAELEESEESWEEQKKELEKELSELEKRIE 113
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 71-184 2.29e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.37  E-value: 2.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779      71 IHNLQRDSSTQRLDLEATKARLSSLESLLHQLtldqaarpQETQEGLQRELGTLRRERDQLETQTRELETAYSNLLRDKS 150
Cdd:TIGR02169  303 IASLERSIAEKERELEDAEERLAKLEAEIDKL--------LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE 374

                           90       100       110
                   ....*....|....*....|....*....|....
gi 4557779     151 VLEEEKKRLRQENENLARRLESSSQEVARLRRGQ 184
Cdd:TIGR02169  375 EVDKEFAETRDELKDYREKLEKLKREINELKREL 408
PRK09039 PRK09039
peptidoglycan -binding protein;
91-182 3.64e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 42.65  E-value: 3.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779    91 RLSSLESLLHQLTlDQAARPQETQEGLQRELGTLR-------RERDQLETQTRELETAYSNLLRDKSVLEEEKKRLRQEN 163
Cdd:PRK09039  54 ALDRLNSQIAELA-DLLSLERQGNQDLQDSVANLRaslsaaeAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVS 132

                         90
                 ....*....|....*....
gi 4557779   164 ENLARRLESSSQEVARLRR 182
Cdd:PRK09039 133 ARALAQVELLNQQIAALRR 151
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 117-180 1.53e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 37.93  E-value: 1.53e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4557779  117 LQRELGTLRRERDQLETQTRELETAYsNLLRDK--------SVLEEEKKRLRQENENL-ARRLESSSQEVARL 180
Cdd:cd22887  16 LEAELASLEEEIKDLEEELKEKNKAN-EILNDElialqienNLLEEKLRKLQEENDELvERWMAKKQQEADKM 87
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 97-332 8.35e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.66  E-value: 8.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779   97 SLLHQLTLDQAArPQETQEGLQRELGTLRRERDQLETQTRELETAYSNLLRDKSVLEEEKKRLRQENENLARRLESSSQE 176
Cdd:COG3883 133 DLLEELKADKAE-LEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779  177 VARLRRGQCPQTRDTARAVPPGSREVSTWNldTLAFQELKSELTEVPASRILKESPSGYLRSGEGDTGCGELVWVGEPLT 256
Cdd:COG3883 212 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAA--AAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGA 289

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4557779  257 LRTAETITGKYGVWMRDPKPTYPYTQETTWRIDTVGTDVRQVFEYDLISQFMQGYPSKVHILPRPLESTGAVVYSG 332
Cdd:COG3883 290 GGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSSGGGGG 365
 
Name Accession Description Interval E-value
OLF smart00284
Olfactomedin-like domains;
246-502 1.99e-143

Olfactomedin-like domains;


Pssm-ID: 128580  Cd Length: 255  Bit Score: 411.92  E-value: 1.99e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779     246 GELVWVGEPLTLRTAETitGKYGVWMRDPKPTYPYtQETTWRIDTVGTDVRQVFEYDLISQFMQGYPSKVHILPRPLEST 325
Cdd:smart00284   1 GGLAGISKPVTLQTSWK--GKSGAWMKDPLWNTTK-KSLYWYMPLNTRVLRSVREYSSMSDFQMGKNPTDHPLPHAGQGT 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779     326 GAVVYSGSLYFQGAESRTVIRYELNTETVKAEKEIPGAGYHGQFPYSWGGYTDIDLAVDEAGLWVIYSTDEAKGAIVLSK 405
Cdd:smart00284  78 GVVVYNGSLYFNKFNSHDICRFDLTTETYQKEPLLNGAGYNNRFPYAWGGFSDIDLAVDENGLWVIYATEQNAGKIVISK 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779     406 LNPENLELEQTWETNIRKQSVANAFIICGTLYTVSSYTSADATVNFAYDTGTGISKTLTIPFKNRYKYSSMIDYNPLEKK 485
Cdd:smart00284 158 LNPATLTIENTWITTYNKRSASNAFMICGILYVTRSLGSKGEKVFYAYDTNTGKEGHLDIPFENMYEYISMLDYNPNDRK 237

                          250
                   ....*....|....*..
gi 4557779     486 LFAWDNLNMVTYDIKLS 502
Cdd:smart00284 238 LYAWNNGHLVHYDIALK 254
OLF pfam02191
Olfactomedin-like domain;
248-501 9.22e-125

Olfactomedin-like domain;


Pssm-ID: 460482  Cd Length: 246  Bit Score: 364.16  E-value: 9.22e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779    248 LVWVGEPLTLRTAEtitGKYGVWMRDPKPTYpytqETTWRIDTvGTDVRQVFEYDLISQFMQGYPSKVHILPRPLESTGA 327
Cdd:pfam02191   1 LVSVSKPVTVKLSG---GKYGAWMKDPLPPS----DKIYVTDR-GTSGNTLREYASLDDFKNGSPSKKYKLPYPWQGTGH 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779    328 VVYSGSLYFQGAESRTVIRYELNTETVKAEKEIPGAGYHGQFPYSWGGYTDIDLAVDEAGLWVIYSTDEAKGAIVLSKLN 407
Cdd:pfam02191  73 VVYNGSLYYNKYNSRNIVKYDLTTRTVAARRVLPGAGYNNRFPYSWGGHTDIDLAVDENGLWVIYATEENEGNIVVSKLD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779    408 PENLELEQTWETNIRKQSVANAFIICGTLYTVSSYTSADATVNFAYDTGTGISKTLTIPFKNRYKYSSMIDYNPLEKKLF 487
Cdd:pfam02191 153 PETLEVEQTWNTSYPKRSAGNAFMVCGVLYAVRSVNTRREEIFYAFDTYTGKEEAVSIPFPNRYGKISMLDYNPRDKKLY 232

                         250
                  ....*....|....
gi 4557779    488 AWDNLNMVTYDIKL 501
Cdd:pfam02191 233 AWDDGYQVTYPVTF 246
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
71-196 1.35e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.54  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779    71 IHNLQRDSSTQRLDLEATKARLSSLESLLHQLTLDqaarPQETQEGLQRELGTLRRERDQLETQTRELETAYSNLLRDKS 150
Cdd:COG4913  340 LEQLEREIERLERELEERERRRARLEALLAALGLP----LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR 415

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 4557779   151 VLEEEKKRLRQENENLARRLESSSQEVARLRRGQCPQTRDTARAVP 196
Cdd:COG4913  416 DLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELP 461
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
71-180 3.90e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.21  E-value: 3.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779   71 IHNLQRDSSTQRLDLEATKARLSSLESLLHQLTLDQAARPQETQ------EGLQRELGTLRRERDQLETQTRELETAYSN 144
Cdd:COG4372  61 LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELEslqeeaEELQEELEELQKERQDLEQQRKQLEAQIAE 140

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 4557779  145 LLRDKSVLEEEKKRLRQENENLARRLESSSQEVARL 180
Cdd:COG4372 141 LQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 75-182 8.82e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 8.82e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779   75 QRDSSTQRLDLEATKARLSSLESLLHQLTLDQAARpQETQEGLQRELGTLRRERDQLETQTRELETAYSNLLRDKSVLEE 154
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEEL-EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302

                        90       100
                ....*....|....*....|....*...
gi 4557779  155 EKKRLRQENENLARRLESSSQEVARLRR 182
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEE 330
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 71-182 2.15e-06

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: 49.76  E-value: 2.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779   71 IHNLQRDSSTQRLDLEATKARL-------------SSLESLLHQLTLDQAAR-----------PQETQEGLQRELGTLRR 126
Cdd:COG4942  85 LAELEKEIAELRAELEAQKEELaellralyrlgrqPPLALLLSPEDFLDAVRrlqylkylapaRREQAEELRADLAELAA 164

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4557779  127 ERDQLETQTRELETAYSNLLRDKSVLEEEKKRLRQENENLARRLESSSQEVARLRR 182
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 71-181 3.09e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 48.38  E-value: 3.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779   71 IHNLQRDSSTQRLDLEATKARLSSLESLLHQltldqaARPQETQEGLQRELGTLRRERDQLETQTREL----ETAYSNLL 146
Cdd:COG1579  54 LEDLEKEIKRLELEIEEVEARIKKYEEQLGN------VRNNKEYEALQKEIESLKRRISDLEDEILELmeriEELEEELA 127

                        90       100       110
                ....*....|....*....|....*....|....*
gi 4557779  147 RDKSVLEEEKKRLRQENENLARRLESSSQEVARLR 181
Cdd:COG1579 128 ELEAELAELEAELEEKKAELDEELAELEAELEELE 162
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 71-171 1.07e-05

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 44.94  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779     71 IHNLQRDSSTQRLDLEATKARLSSLESLLHQltldQAARPQETQEGLQRE----------LGTLRRERDQLETQTREL-- 138
Cdd:pfam07926   3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEK----QAEIAREAQQNYERElvlhaedikaLQALREELNELKAEIAELka 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 4557779    139 --ETAYSNLLRDKSVLEEEKKRLRQENENLARRLE 171
Cdd:pfam07926  79 eaESAKAELEESEESWEEQKKELEKELSELEKRIE 113
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
85-182 1.19e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779   85 LEATKARLSSLESLLHQLTlDQAARPQETQEGLQRELGTLRRERDQLETQTRELETAYSNLLRDKSVLEEEKKRLRQENE 164
Cdd:COG4372  33 LRKALFELDKLQEELEQLR-EELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111

                        90
                ....*....|....*...
gi 4557779  165 NLARRLESSSQEVARLRR 182
Cdd:COG4372 112 ELQEELEELQKERQDLEQ 129
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 57-175 1.22e-05

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 48.13  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779     57 NESSCPEQSQAMSVIHNLQRDSSTQRLDLEATKARLSSLESLLhqltldqaarpqetqEGLQRELGTLRRERDQLETQTR 136
Cdd:pfam05911 683 NKRLKEEFEQLKSEKENLEVELASCTENLESTKSQLQESEQLI---------------AELRSELASLKESNSLAETQLK 747

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 4557779    137 ELETAYSNLLRDKSVLEEEKKRLRQENENLARRLESSSQ 175
Cdd:pfam05911 748 CMAESYEDLETRLTELEAELNELRQKFEALEVELEEEKN 786
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 81-182 1.92e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 1.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779   81 QRLDLEATKARLSSLESLLHQLTLDQAARpQETQEGLQRELGTLRRERDQLETQTRELETAYSNLLRDKSVLEEEKKRLR 160
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARL-EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357

                        90       100
                ....*....|....*....|..
gi 4557779  161 QENENLARRLESSSQEVARLRR 182
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEE 379
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 71-184 2.29e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.37  E-value: 2.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779      71 IHNLQRDSSTQRLDLEATKARLSSLESLLHQLtldqaarpQETQEGLQRELGTLRRERDQLETQTRELETAYSNLLRDKS 150
Cdd:TIGR02169  303 IASLERSIAEKERELEDAEERLAKLEAEIDKL--------LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE 374

                           90       100       110
                   ....*....|....*....|....*....|....
gi 4557779     151 VLEEEKKRLRQENENLARRLESSSQEVARLRRGQ 184
Cdd:TIGR02169  375 EVDKEFAETRDELKDYREKLEKLKREINELKREL 408
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 64-181 2.51e-05

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: 47.04  E-value: 2.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779      64 QSQAMSVIHN-LQRDSSTQRLDLEATKARLSSLESllhqltldQAARPQETQEGLQRELGTLRRERDQLETQTRELETAY 142
Cdd:pfam15921  686 KSEEMETTTNkLKMQLKSAQSELEQTRNTLKSMEG--------SDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAM 757

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 4557779     143 SNLLRDKSVLEEEKKRLRQENENLARRLESSSQEVARLR 181
Cdd:pfam15921  758 TNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLR 796
YabA COG4467
Regulator of replication initiation timing YabA [Replication, recombination and repair];
129-178 4.49e-05

Regulator of replication initiation timing YabA [Replication, recombination and repair];


Pssm-ID: 443564 [Multi-domain]  Cd Length: 107  Bit Score: 42.55  E-value: 4.49e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 4557779  129 DQLETQTRELETAYSNLLRDKSVLEEEKKRLRQENENLARRLESSSQEVA 178
Cdd:COG4467  11 SELEEQLGELLKELGELKDEVAELLEENARLRIENEHLRERLEELEKKKE 60
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 72-182 4.67e-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: 46.20  E-value: 4.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779      72 HNLQRDSSTQRLDLEATKARLSSLESLLHQLTlDQAARPQETQEGLQRELGTLRRERDQLETQTRELETAYSNLLRDKSV 151
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAELE-EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390

                           90       100       110
                   ....*....|....*....|....*....|.
gi 4557779     152 LEEEKKRLRQENENLARRLESSSQEVARLRR 182
Cdd:TIGR02168  391 LELQIASLNNEIERLEARLERLEDRRERLQQ 421
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 71-181 4.71e-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: 46.20  E-value: 4.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779      71 IHNLQRDSSTQRLDLEATKARLSSLESLLHQLTlDQAARPQETQEGLQRELGTLRR--------------ERDQLETQTR 136
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLE-EQIEELSEDIESLAAEIEELEElieeleseleallnERASLEEALA 890

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 4557779     137 ELETAYSNLLRDKSVLEEEKKRLRQENENLARRLESSSQEVARLR 181
Cdd:TIGR02168  891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 48-231 5.58e-05

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: 45.88  E-value: 5.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779      48 QYTFSVASPNESSCPEQSQAMSVIHNLQRDSSTQRLDLEATKARLSSLESLLHQL--TLDQAARPQETQ-EGLQR----- 119
Cdd:pfam15921  275 EHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLrsELREAKRMYEDKiEELEKqlvla 354

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779     120 --ELGTLRRERDQLETQTRELETAYSNLL-----RDK--SVLEEEKKRLRQEN-------ENLARRLESSSQEVARLR-- 181
Cdd:pfam15921  355 nsELTEARTERDQFSQESGNLDDQLQKLLadlhkREKelSLEKEQNKRLWDRDtgnsitiDHLRRELDDRNMEVQRLEal 434

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 4557779     182 ----RGQCPQTRDTARAVPPGSRE----VSTWNLDTLAFQE-LKSELTEVPASRILKES 231
Cdd:pfam15921  435 lkamKSECQGQMERQMAAIQGKNEslekVSSLTAQLESTKEmLRKVVEELTAKKMTLES 493
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 63-194 6.27e-05

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 45.44  E-value: 6.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779     63 EQSQAMSVIHNLQRDSSTQRLDLEATKARLSSLESLLHQLTLDQAARPQETQEgLQRELGTLRRERDQLETQTRELETAY 142
Cdd:pfam19220  84 ELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRA-LEEENKALREEAQAAEKALQRAEGEL 162

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 4557779    143 SNLLRDKSVLEEEKKRLRqenenlaRRLESSSQEVARL--RRGQCPQTRDTARA 194
Cdd:pfam19220 163 ATARERLALLEQENRRLQ-------ALSEEQAAELAELtrRLAELETQLDATRA 209
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
81-182 6.57e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 6.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779    81 QRLDLEATKARLSSLESLLHQLTLDQAarpqetqeglqrELGTLRRERDQLETQTRELETAYSNLLRDKSVLEEEKKRLR 160
Cdd:COG4913  659 DEIDVASAEREIAELEAELERLDASSD------------DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE 726

                         90       100
                 ....*....|....*....|..
gi 4557779   161 QENENLARRLESSSQEVARLRR 182
Cdd:COG4913  727 EELDELQDRLEAAEDLARLELR 748
ZapB COG3074
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
 94-172 7.82e-05

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442308 [Multi-domain]  Cd Length: 79  Bit Score: 41.11  E-value: 7.82e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4557779   94 SLEsLLHQLtldqaarpQETQEGLQRELGTLRRERDQLETQTRELETAYSNLLRDKSVLEEEKKRLRQENENLARRLES 172
Cdd:COG3074   2 SLE-LLEEL--------EAKVQQAVDTIELLQMEVEELKEKNEELEQENEELQSENEELQSENEQLKTENAEWQERIRS 71
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 63-181 7.94e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.44  E-value: 7.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779      63 EQSQAMSVIHNLQRDSSTQRLDLEATKARLSSLESLLHQL-----TLDQAARPQETQEgLQRELGTLRRERDQLETQTRE 137
Cdd:TIGR02169  738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLeealnDLEARLSHSRIPE-IQAELSKLEEEVSRIEARLRE 816

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 4557779     138 LETAYSNLLRDKSVLEEEKKRLRQENENLARRLESSSQEVARLR 181
Cdd:TIGR02169  817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLN 860
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 63-182 8.00e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 8.00e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779   63 EQSQAMSVIHNLQRDSSTQRLDLEATKARLSSLESLLHQLTLDQAARpQETQEGLQRELGTLRRERDQLETQTRELETAY 142
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL-EERLEELEEELAELEEELEELEEELEELEEEL 346

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 4557779  143 SNLLRDKSVLEEEKKRLRQENENLARRLESSSQEVARLRR 182
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 63-182 8.15e-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: 45.43  E-value: 8.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779      63 EQSQAMSVIHNLQRDSSTQRLDLEATKARLSSLESLLHQLTLDQAARPQETQEGLQR------ELGTLRRERDQLETQTR 136
Cdd:TIGR02168  713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERleeaeeELAEAEAEIEELEAQIE 792

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 4557779     137 ELETAYSNLLRDKSVLEEEKKRLRQENENLARRLESSSQEVARLRR 182
Cdd:TIGR02168  793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 117-181 1.13e-04

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: 45.05  E-value: 1.13e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4557779     117 LQRELGTLRRERDQLETQTRELETAYSNLLRDKSVLEEEKKRLRQENENLARRLESSSQEVARLR 181
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
84-182 1.21e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779    84 DLEATKARLSSLESLLHQLTLDQAarpqetqeglQRELGTLRRERDQLETQTRELETAYSNLLRDKSVLEEEKKRLRQE- 162
Cdd:COG4913  263 RYAAARERLAELEYLRAALRLWFA----------QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQi 332

                         90       100
                 ....*....|....*....|
gi 4557779   163 NENLARRLESSSQEVARLRR 182
Cdd:COG4913  333 RGNGGDRLEQLEREIERLER 352
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 63-224 1.41e-04

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: 44.66  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779      63 EQSQAMSVIHNLQRDSSTQRLDLEATKARLSSL----ESLLHQLTLDQAARPQ--ETQEGLQRELGTLRRERDQLETQTR 136
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELkeelESLEAELEELEAELEEleSRLEELEEQLETLRSKVAQLELQIA 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779     137 ELETAYSNLLRDKSVLEEEKKRLRQENENLARRLESS-----SQEVARLRRGQCPQTRDTARAVPPGSREVSTWNLDTLA 211
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAelkelQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476

                          170
                   ....*....|...
gi 4557779     212 FQELKSELTEVPA 224
Cdd:TIGR02168  477 LDAAERELAQLQA 489
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 73-182 1.62e-04

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: 44.66  E-value: 1.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779      73 NLQRDSSTQRLD-----LEATKARLSSLESLLHQLTldqaARPQETQEglqrELGTLRRERDQLETQTRELETAYSNLLR 147
Cdd:TIGR02168  224 ELELALLVLRLEelreeLEELQEELKEAEEELEELT----AELQELEE----KLEELRLEVSELEEEIEELQKELYALAN 295

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 4557779     148 DKSVLEEEKKRLRQENENLARRLESSSQEVARLRR 182
Cdd:TIGR02168  296 EISRLEQQKQILRERLANLERQLEELEAQLEELES 330
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
74-182 1.81e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779    74 LQRDSSTQRLDLEATKARLSSLESLLHQLTLDQAARPQETQEGLQRELGTLRRERDQLETQTRELETAYSNllrDKSVLE 153
Cdd:COG4913  307 LEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA---SAEEFA 383

                         90       100
                 ....*....|....*....|....*....
gi 4557779   154 EEKKRLRQENENLARRLESSSQEVARLRR 182
Cdd:COG4913  384 ALRAEAAALLEALEEELEALEEALAEAEA 412
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 32-170 1.90e-04

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 42.23  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779     32 ARTAQLRKA--NDQSGRCQYTFSVASPNESSCPEQSQAMSvihnlqrdssTQRLDL-EATKA------RLSSLESLLHql 102
Cdd:pfam08614  21 AENAKLQSEpeSVLPSTSSSKLSKASPQSASIQSLEQLLA----------QLREELaELYRSrgelaqRLVDLNEELQ-- 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4557779    103 TLDQAARPQETQ-EGLQRELGTLRRERDQLETQTRELETAYSNLlRDK--------SVLEEEKKRLRQENENLARRL 170
Cdd:pfam08614  89 ELEKKLREDERRlAALEAERAQLEEKLKDREEELREKRKLNQDL-QDElvalqlqlNMAEEKLRKLEKENRELVERW 164
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 81-182 1.94e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779   81 QRLDLEATKAR----LSS-LESLLHQLTLDQAARPQETQEGLQRELGTLRRERDQLETQTRELETAYSNLLRDKSVLEEE 155
Cdd:COG1196 203 EPLERQAEKAEryreLKEeLKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282

                        90       100
                ....*....|....*....|....*..
gi 4557779  156 KKRLRQENENLARRLESSSQEVARLRR 182
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEE 309
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 63-182 2.02e-04

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: 44.28  E-value: 2.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779      63 EQSQAMSVIHNLQRDSSTQRLDLEATKARLSSLESLLHQLT--LDQAarpQETQEGLQRELGTLRRERDQLETQTRELET 140
Cdd:TIGR02168  247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQkeLYAL---ANEISRLEQQKQILRERLANLERQLEELEA 323

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 4557779     141 AYSNLLRDKSVLEEEKKRLRQENENLARRLESSSQEVARLRR 182
Cdd:TIGR02168  324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 83-184 2.28e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.01  E-value: 2.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779      83 LDLEATKARLSSLESLLHQLTLDQAA---RPQETQEGLQRE------LGT----LRRERDQLETQTRELETAYSNLLRDK 149
Cdd:pfam01576  440 SELESVSSLLNEAEGKNIKLSKDVSSlesQLQDTQELLQEEtrqklnLSTrlrqLEDERNSLQEQLEEEEEAKRNVERQL 519

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 4557779     150 SVL---------------------EEEKKRLRQENENLARRLESSSQEVARLRRGQ 184
Cdd:pfam01576  520 STLqaqlsdmkkkleedagtlealEEGKKRLQRELEALTQQLEEKAAAYDKLEKTK 575
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 83-177 2.31e-04

Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.


Pssm-ID: 463102 [Multi-domain]  Cd Length: 140  Bit Score: 41.51  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779     83 LDLEATKARLSSLESLLHQLTldqaarpQETQEgLQRELGTLRRERDQLETQTR-------ELETAYS---NLLRDKsvl 152
Cdd:pfam10473  45 LEAENSKAEVETLKAEIEEMA-------QNLRD-LELDLVTLRSEKENLTKELQkkqervsELESLNSsleNLLEEK--- 113

                          90       100
                  ....*....|....*....|....*
gi 4557779    153 EEEKKRLRQENENLARRLESSSQEV 177
Cdd:pfam10473 114 EQEKVQMKEESKTAVEMLQTQLKEL 138
PRK09039 PRK09039
peptidoglycan -binding protein;
91-182 3.64e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 42.65  E-value: 3.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779    91 RLSSLESLLHQLTlDQAARPQETQEGLQRELGTLR-------RERDQLETQTRELETAYSNLLRDKSVLEEEKKRLRQEN 163
Cdd:PRK09039  54 ALDRLNSQIAELA-DLLSLERQGNQDLQDSVANLRaslsaaeAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVS 132

                         90
                 ....*....|....*....
gi 4557779   164 ENLARRLESSSQEVARLRR 182
Cdd:PRK09039 133 ARALAQVELLNQQIAALRR 151
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 73-184 4.61e-04

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: 43.12  E-value: 4.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779      73 NLQRDSSTQRLDLEATKARLSSLESLLHQLTlDQAARPQETQEGLQRELGTLRRE--RDQLETQTRELETAYSNLLRDKS 150
Cdd:TIGR02168  383 TLRSKVAQLELQIASLNNEIERLEARLERLE-DRRERLQQEIEELLKKLEEAELKelQAELEELEEELEELQEELERLEE 461

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 4557779     151 VLEEEKKRLRQENENL---ARRLESSSQEVARLRRGQ 184
Cdd:TIGR02168  462 ALEELREELEEAEQALdaaERELAQLQARLDSLERLQ 498
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 84-200 4.93e-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: 42.44  E-value: 4.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779   84 DLEATKARLSSLESLLHQLtLDQAARPQETQEGLQRELGTLRRERDQLETQTRELETAYSNLLRDKS-------VLEEEK 156
Cdd:COG4942 130 DFLDAVRRLQYLKYLAPAR-REQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAerqkllaRLEKEL 208

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 4557779  157 KRLRQENENLARRLESSSQEVARLRRGQCPQTRDTARAVPPGSR 200
Cdd:COG4942 209 AELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 84-170 7.07e-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: 42.06  E-value: 7.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779   84 DLEATKARLSSLESLLHQLTLDQAARPQETQEgLQRELGTLRRERDQLETQTRELETAYSNLLRDKSVLEEEKKRLRQEn 163
Cdd:COG4942  28 ELEQLQQEIAELEKELAALKKEEKALLKQLAA-LERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE- 105


                ....*..
gi 4557779  164 enLARRL 170
Cdd:COG4942 106 --LAELL 110
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
65-182 8.07e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 8.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779   65 SQAMSVIHNLQRDSSTQRLDLEATKARLSSLESLLHQLTLDQAARPQETQEgLQRELGTLRRERDQLETQTRELEtaysn 144
Cdd:COG4372  34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE-LNEQLQAAQAELAQAQEELESLQ----- 107

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 4557779  145 llRDKSVLEEEKKRLRQENENLARRLESSSQEVARLRR 182
Cdd:COG4372 108 --EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQS 143
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 105-182 9.06e-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: 41.98  E-value: 9.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779     105 DQAARPQETQEGLQRELGTLRRERDQLETQTRELETAYSN-------LLRDKSVLEEEKKRLRQENENLARRLESSSQEV 177
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDasrkigeIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753


                   ....*
gi 4557779     178 ARLRR 182
Cdd:TIGR02169  754 ENVKS 758
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 63-182 9.82e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 9.82e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779   63 EQSQAMSVIHNLQRDSSTQRLDLEATKARLSSLESLLHQLTLD----------QAARPQETQEGLQRELGTLRRERDQLE 132
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEleeaqaeeyeLLAELARLEQDIARLEERRRELEERLE 319

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 4557779  133 TQTRELETAYSNLLRDKSVLEEEKKRLRQENENLARRLESSSQEVARLRR 182
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 63-182 1.09e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 1.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779   63 EQSQAMSVIHNLQRDSSTQRLDLEATKARLSSLESLLHQLTLDQAARpQETQEGLQRELGTLRRERDQLETQTRELETAY 142
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA-EEELEELAEELLEALRAAAELAAQLEELEEAE 409

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 4557779  143 SNLLRDKSVLEEEK-------KRLRQENENLARRLESSSQEVARLRR 182
Cdd:COG1196 410 EALLERLERLEEELeeleealAELEEEEEEEEEALEEAAEEEAELEE 456
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
63-182 1.10e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779   63 EQSQAMSVIHNLQRDSSTQRLDLEATKARLSSLESLLHQLTLDQAARPqetqegLQRELGTLRRERDQLETQTRELE--- 139
Cdd:COG4717  82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP------LYQELEALEAELAELPERLEELEerl 155

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 4557779  140 TAYSNLLRDKSVLEEEKKRLRQENENLAR--------RLESSSQEVARLRR 182
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEqlslateeELQDLAEELEELQQ 206
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
117-182 1.18e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.38  E-value: 1.18e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4557779  117 LQRELGTLRRERDQLETQTREL-ETAYSNLLRDKSV--LEEEKKRLRQENENLARRLESSSQEVARLRR 182
Cdd:COG2433 432 LEAELEEKDERIERLERELSEArSEERREIRKDREIsrLDREIERLERELEEERERIEELKRKLERLKE 500
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 81-180 1.23e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 1.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779   81 QRLDLEATKARLSSLESllhqltldQAARPQETQEGLQRELGTLRRERDQLETQTRELETAYSNLLRDKSVLEEEKKRLR 160
Cdd:COG4942  18 QADAAAEAEAELEQLQQ--------EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89

                        90       100
                ....*....|....*....|
gi 4557779  161 QENENLARRLESSSQEVARL 180
Cdd:COG4942  90 KEIAELRAELEAQKEELAEL 109
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
71-189 1.31e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779    71 IHNLQRDSSTQRLDLEATKARLSSLESLLHQL-TLDQAARPQETQEGLQRELGTLRRERDQLET----------QTRELE 139
Cdd:COG4913  619 LAELEEELAEAEERLEALEAELDALQERREALqRLAEYSWDEIDVASAEREIAELEAELERLDAssddlaaleeQLEELE 698

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 4557779   140 TAYSNLLRDKSVLEEEKKRLRQENENLARRLESSSQEVARLRRGQCPQTR 189
Cdd:COG4913  699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
APG6_N pfam17675
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
 81-180 1.37e-03

Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.


Pssm-ID: 465452 [Multi-domain]  Cd Length: 127  Bit Score: 38.73  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779     81 QRLD--LEATKARLSSLESLLHQLTLDQaarpQETQEGLQRELGTLRRERDQLETQTRELETAYSNLLRDKSVLEEEKKR 158
Cdd:pfam17675  12 EELDkqLEDAEKERDAYISFLKKLEKET----PEELEELEKELEKLEKEEEELLQELEELEKEREELDAELEALEEELEA 87

                          90       100
                  ....*....|....*....|....*....
gi 4557779    159 LRQENE-------NLARRLESSSQEVARL 180
Cdd:pfam17675  88 LDEEEEefwreynALQLQLLEFQDERDSL 116
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 117-180 1.53e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 37.93  E-value: 1.53e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4557779  117 LQRELGTLRRERDQLETQTRELETAYsNLLRDK--------SVLEEEKKRLRQENENL-ARRLESSSQEVARL 180
Cdd:cd22887  16 LEAELASLEEEIKDLEEELKEKNKAN-EILNDElialqienNLLEEKLRKLQEENDELvERWMAKKQQEADKM 87
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 85-194 1.70e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 1.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779   85 LEATKARLSSLESLLHQL-----TL----DQAARPQETQE---------------GLQRELGTLRRERDQLETQTRELET 140
Cdd:COG1196 181 LEATEENLERLEDILGELerqlePLerqaEKAERYRELKEelkeleaellllklrELEAELEELEAELEELEAELEELEA 260

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 4557779  141 AYSNLLRDKSVLEEEKKRLRQENENLARRLESSSQEVARLRRGQCPQTRDTARA 194
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 73-181 1.93e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779      73 NLQR--------DSSTQRLDLEATKA----RLSS-LESLLHQLTLDQAARPQETQEGLQRELGTLRRERDQLETQTRELE 139
Cdd:TIGR02168  187 NLDRledilnelERQLKSLERQAEKAerykELKAeLRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELE 266

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 4557779     140 TAYSNLLRDKSVLEEEKKRLRQENENLARRLESSSQEVARLR 181
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR 308
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 105-182 1.98e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 1.98e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4557779  105 DQAARPQETQEGLQRELGTLRRERDQLETQTRELETAYSNLLRDKSVLEEEKKRLRQENENLARRLESSSQEVARLRR 182
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 50-182 2.63e-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: 40.32  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779     50 TFSVASPNESSCPEQSQAMsvIHNL-QRDSSTQRLDLEATKARlsslesllhQLTLDQAARPQETQEGLQRE-LGTLRRE 127
Cdd:pfam15709 306 TGNMESEEERSEEDPSKAL--LEKReQEKASRDRLRAERAEMR---------RLEVERKRREQEEQRRLQQEqLERAEKM 374

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 4557779    128 RDQLE-TQTRELEtaySNLLRdKSVLEEEkkRLRQENENLARRL-ESSSQEVARLRR 182
Cdd:pfam15709 375 REELElEQQRRFE---EIRLR-KQRLEEE--RQRQEEEERKQRLqLQAAQERARQQQ 425
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
84-169 2.64e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 2.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779   84 DLEATKARLSSLESLLHQLTLDQAARPQETQEG--------LQRELGTLRRERDQLETQTRELETAYSNLLRDKSV--LE 153
Cdd:COG4717 396 EYQELKEELEELEEQLEELLGELEELLEALDEEeleeeleeLEEELEELEEELEELREELAELEAELEQLEEDGELaeLL 475

                        90
                ....*....|....*.
gi 4557779  154 EEKKRLRQENENLARR 169
Cdd:COG4717 476 QELEELKAELRELAEE 491
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
86-182 2.68e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.89  E-value: 2.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779   86 EATKARLSSLESLLHQLT--LDQAARPQETQEGLQRELGTLRRERDQLETQTRELETAYSNLLRDKSVLEEEKKRLRQEN 163
Cdd:COG1340   1 SKTDELSSSLEELEEKIEelREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80

                        90
                ....*....|....*....
gi 4557779  164 ENLARRLESSSQEVARLRR 182
Cdd:COG1340  81 DELNEKLNELREELDELRK 99
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 98-182 2.91e-03

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 38.45  E-value: 2.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779     98 LLHQLtLDQAARPQETQEGLQRELGTLRRERDQLETQTRELETAYSNLLRDKSVLEEEKKRLRQENENLARRLESSSQEV 177
Cdd:pfam11559  39 VIYEL-LQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEEL 117


                  ....*
gi 4557779    178 ARLRR 182
Cdd:pfam11559 118 QRLKN 122
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
82-182 2.97e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 2.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779   82 RLDLEATKARLS-----SLESLLHQLTLDQAARPQETQEGLQRELGTLRRErdqLETQTRELETAYSNLLRDKSVLEEEK 156
Cdd:COG4372   3 RLGEKVGKARLSlfglrPKTGILIAALSEQLRKALFELDKLQEELEQLREE---LEQAREELEQLEEELEQARSELEQLE 79

                        90       100
                ....*....|....*....|....*.
gi 4557779  157 KRLRQENENLARRLESSSQEVARLRR 182
Cdd:COG4372  80 EELEELNEQLQAAQAELAQAQEELES 105
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 82-230 3.01e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.45  E-value: 3.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779   82 RLDLEATKARLSSLESLLHQLTLDQAARPQETQEGLQRELGTLRRERDQLETQTRELETAYsnllrdksvleEEKKRLRQ 161
Cdd:COG0542 403 RMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARW-----------EAEKELIE 471

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4557779  162 ENENLARRLESSSQEVARLRRgQCPQTRDTARAVPPGSRE----------VSTWnldtlafqelkselTEVPASRILKE 230
Cdd:COG0542 472 EIQELKEELEQRYGKIPELEK-ELAELEEELAELAPLLREevteediaevVSRW--------------TGIPVGKLLEG 535
mukB PRK04863
chromosome partition protein MukB;
63-195 3.07e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.33  E-value: 3.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779     63 EQSQAMSVIHNLQRDSSTQRldleATKARLSSLESLLHqlTLDQAARPQETQEGLQRELG-----------TLRRERDQL 131
Cdd:PRK04863  490 SRSEAWDVARELLRRLREQR----HLAEQLQQLRMRLS--ELEQRLRQQQRAERLLAEFCkrlgknlddedELEQLQEEL 563

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4557779    132 ETQTRELETAYSNLLRDKSVLEEEKKRLRQENEnlarRLESSSQE-------VARLRRgQCPQTRDTARAV 195
Cdd:PRK04863  564 EARLESLSESVSEARERRMALRQQLEQLQARIQ----RLAARAPAwlaaqdaLARLRE-QSGEEFEDSQDV 629
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
63-182 3.25e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 3.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779   63 EQSQAMSVIHNLQRDSSTQRLDLEATKARLSSLESLLHQLTLDQAARPQETQ-EGLQRELGTLRRERDQLETQ------- 134
Cdd:COG3206 213 EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPViQQLRAQLAELEAELAELSARytpnhpd 292

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4557779  135 ---------------TRELETAYSNLLRDKSVLEEEKKRLRQENENLARRLESSS---QEVARLRR 182
Cdd:COG3206 293 vialraqiaalraqlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPeleAELRRLER 358
DUF4349 pfam14257
Domain of unknown function (DUF4349); This family of proteins is found in bacteria and archaea. ...
 76-145 3.42e-03

Domain of unknown function (DUF4349); This family of proteins is found in bacteria and archaea. Proteins in this family are typically between 282 and 353 amino acids in length. There is a single completely conserved residue D that may be functionally important. The N-terminus contains a lipoprotein signal peptide sequence.


Pssm-ID: 464117 [Multi-domain]  Cd Length: 213  Bit Score: 39.07  E-value: 3.42e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4557779     76 RDSSTQRLDLEAtkaRLSSLESLLHQLT--LDQAARPQETQEgLQRELGTLRRERDQLETQTRELE--TAYSNL 145
Cdd:pfam14257  81 EDVTEQYVDLEA---RLKALRASEDRLLalLERAGSVEDLLA-VERELSEVQAELESLEGQLRYLDdqVAYSTV 150
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
32-178 3.48e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 3.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779   32 ARTAQLRKANDQSgrcqytfSVASPNESSCPEQSQAMSVIHNL--QRDSSTQRL-----DLEATKARLSSLESLLHQLTL 104
Cdd:COG3206 240 ARLAALRAQLGSG-------PDALPELLQSPVIQQLRAQLAELeaELAELSARYtpnhpDVIALRAQIAALRAQLQQEAQ 312

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4557779  105 DQAARPQETQEGLQRELGTLRRERDQLETQTRELetaySNLLRDKSVLEEEKKRLRQENENLARRLESSSQEVA 178
Cdd:COG3206 313 RILASLEAELEALQAREASLQAQLAQLEARLAEL----PELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 63-195 5.01e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.55  E-value: 5.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779    63 EQSQAMSVIHNLQRDSSTQRL---DLEATKARLSSLESLLHQLtldQAARPQetQEGLQRELGTLRRERDQLETQTRELE 139
Cdd:COG3096  489 ERSQAWQTARELLRRYRSQQAlaqRLQQLRAQLAELEQRLRQQ---QNAERL--LEEFCQRIGQQLDAAEELEELLAELE 563

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4557779   140 TAYSNLLRDKSVLEEEKKRLRQENENLARRLES---------SSQEVARLRRGQCPQTRDTARAV 195
Cdd:COG3096  564 AQLEELEEQAAEAVEQRSELRQQLEQLRARIKElaarapawlAAQDALERLREQSGEALADSQEV 628
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 63-147 5.37e-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: 38.98  E-value: 5.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779   63 EQSQAMSVIHNLQRDSSTQRLDLEATKARLSSLESLLHQLtldqaarpQETQEGLQRELGTLRRERDQLETQTRELETAY 142
Cdd:COG4942  35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL--------EQELAALEAELAELEKEIAELRAELEAQKEEL 106


                ....*
gi 4557779  143 SNLLR 147
Cdd:COG4942 107 AELLR 111
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 83-182 5.74e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.23  E-value: 5.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779     83 LDLEATKARLSSLESLLHQLTLDQAARPQETQEGLQRELGT----LRRERDQLETQTRELETAYSNLLRDKSVLEEEKKR 158
Cdd:TIGR04523 274 KELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSelknQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTN 353

                          90       100
                  ....*....|....*....|....
gi 4557779    159 LRQENENLARRLESSSQEVARLRR 182
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIEKLKK 377
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 58-180 6.33e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.28  E-value: 6.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779      58 ESSCPEQSQAMSVIHNLQRDsstqrldLEATKARLSSLESLLHQLTLDQAARPQETQE------GLQRELGTLRRERDQL 131
Cdd:TIGR02169  822 NRLTLEKEYLEKEIQELQEQ-------RIDLKEQIKSIEKEIENLNGKKEELEEELEEleaalrDLESRLGDLKKERDEL 894

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 4557779     132 ETQTRELETAYSNLlrdKSVLEEEKKRLRQenenLARRLESSSQEVARL 180
Cdd:TIGR02169  895 EAQLRELERKIEEL---EAQIEKKRKRLSE----LKAKLEALEEELSEI 936
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
84-181 6.62e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 6.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779    84 DLEATKARLSSLESLLHQLTLDQA---ARPQETQEGLQ------RELGTLRRERDQLE---TQTRELETAYSNLLRDKSV 151
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRkleEKIRELEERIEelkkeiEELEEKVKELKELKekaEEYIKLSEFYEEYLDELRE 311

                         90       100       110
                 ....*....|....*....|....*....|
gi 4557779   152 LEEEKKRLRQENENLARRLESSSQEVARLR 181
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLE 341
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 97-332 8.35e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.66  E-value: 8.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779   97 SLLHQLTLDQAArPQETQEGLQRELGTLRRERDQLETQTRELETAYSNLLRDKSVLEEEKKRLRQENENLARRLESSSQE 176
Cdd:COG3883 133 DLLEELKADKAE-LEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557779  177 VARLRRGQCPQTRDTARAVPPGSREVSTWNldTLAFQELKSELTEVPASRILKESPSGYLRSGEGDTGCGELVWVGEPLT 256
Cdd:COG3883 212 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAA--AAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGA 289

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4557779  257 LRTAETITGKYGVWMRDPKPTYPYTQETTWRIDTVGTDVRQVFEYDLISQFMQGYPSKVHILPRPLESTGAVVYSG 332
Cdd:COG3883 290 GGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSSGGGGG 365
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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