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Conserved domains on  [gi|45331215|ref|NP_115805|]
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leucine zipper putative tumor suppressor 2 isoform a [Homo sapiens]

Protein Classification

DUF812 and Fez1 domain-containing protein( domain architecture ID 12072568)

DUF812 and Fez1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Fez1 pfam06818
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ...
 439-636 3.16e-81

Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.


:

Pssm-ID: 462015 [Multi-domain]  Cd Length: 198  Bit Score: 255.69  E-value: 3.16e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215   439 TKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGRARGLQEAARARELELEACSQELQRHRQ 518
Cdd:pfam06818   1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215   519 EAEQLREKAGQLDAEAAGLREPPVPPATADPFLLAESDEAKVQRAAAGVGGSLRAQVERLRVELQRERRRGEEQRDSFEG 598
Cdd:pfam06818  81 EAELLREKVGKLEEEVSGLREALSDVSPSGYESVYESDEAKEQRQEEADLGSLRREVERLRAELREERQRRERQASSFEQ 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 45331215   599 ERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQ 636
Cdd:pfam06818 161 ERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
333-538 3.32e-08

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: 56.85  E-value: 3.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215  333 LRDREAELQQLRDSLDENEATMcqayeERQRHWQREREAlredcaaqaqraqraqqllqlqvfqlqqekRQLQDDFAQLL 412
Cdd:COG4913  257 IRELAERYAAARERLAELEYLR-----AALRLWFAQRRL------------------------------ELLEAELEELR 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215  413 QEREQLERRCATLEREQRELGPRLEETKwEVCQKSG--EISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEG 490
Cdd:COG4913  302 AELARLEAELERLEARLDALREELDELE-AQIRGNGgdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 45331215  491 RARGLQEAARAR----ELELEACSQELQRHRQEAEQLREKAGQLDAEAAGLR 538
Cdd:COG4913  381 EFAALRAEAAALlealEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
 
Name Accession Description Interval E-value
Fez1 pfam06818
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ...
 439-636 3.16e-81

Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.


Pssm-ID: 462015 [Multi-domain]  Cd Length: 198  Bit Score: 255.69  E-value: 3.16e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215   439 TKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGRARGLQEAARARELELEACSQELQRHRQ 518
Cdd:pfam06818   1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215   519 EAEQLREKAGQLDAEAAGLREPPVPPATADPFLLAESDEAKVQRAAAGVGGSLRAQVERLRVELQRERRRGEEQRDSFEG 598
Cdd:pfam06818  81 EAELLREKVGKLEEEVSGLREALSDVSPSGYESVYESDEAKEQRQEEADLGSLRREVERLRAELREERQRRERQASSFEQ 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 45331215   599 ERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQ 636
Cdd:pfam06818 161 ERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 332-657 9.15e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 81.52  E-value: 9.15e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 332 KLRDREAELQQLRDSLDENEATMcQAYEERQRHWQREREALREDcaaqaqraqraqqllqlqVFQLQQEKRQLQDDFAQL 411
Cdd:COG1196 233 KLRELEAELEELEAELEELEAEL-EELEAELAELEAELEELRLE------------------LEELELELEEAQAEEYEL 293

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 412 LQEREQLERRCATLEREQRELGPRLEETKWevcqksgEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGR 491
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEE-------ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 492 ARGLQEAARARELELEACSQELQRHRQEAEQLREKAGQLDAEAAGLREppvppatadpfLLAESDEAKVQRAAAgvggsl 571
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-----------RLERLEEELEELEEA------ 429

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 572 RAQVERLRVELQRErrrgeeqrdsfEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEARELADLG 651
Cdd:COG1196 430 LAELEEEEEEEEEA-----------LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498


                ....*.
gi 45331215 652 LAEQAP 657
Cdd:COG1196 499 AEADYE 504
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 329-548 6.10e-11

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: 65.85  E-value: 6.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    329 LEGKLRDREAELQQLRDSLDENEATMCQAYEERQRHwQREREALREdcaaqaqraqraqqllqlQVFQLQQEKRQLQDDF 408
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL-KEELKALRE------------------ALDELRAELTLLNEEA 819

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    409 AQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSE-------LVALRVALREA 481
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNErasleeaLALLRSELEEL 899

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    482 RATLRVSEGRARGLQEAARARELELEACSQELQRHRQEAEQLREKA---GQLDAEAAGLREPPVPPATAD 548
Cdd:TIGR02168  900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLseeYSLTLEEAEALENKIEDDEEE 969
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
333-538 3.32e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.85  E-value: 3.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215  333 LRDREAELQQLRDSLDENEATMcqayeERQRHWQREREAlredcaaqaqraqraqqllqlqvfqlqqekRQLQDDFAQLL 412
Cdd:COG4913  257 IRELAERYAAARERLAELEYLR-----AALRLWFAQRRL------------------------------ELLEAELEELR 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215  413 QEREQLERRCATLEREQRELGPRLEETKwEVCQKSG--EISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEG 490
Cdd:COG4913  302 AELARLEAELERLEARLDALREELDELE-AQIRGNGgdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 45331215  491 RARGLQEAARAR----ELELEACSQELQRHRQEAEQLREKAGQLDAEAAGLR 538
Cdd:COG4913  381 EFAALRAEAAALlealEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 402-471 1.84e-05

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 46.05  E-value: 1.84e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45331215   402 RQLQDDFAQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSG-EISLLKQQLKESQAELVQKGSEL 471
Cdd:pfam13851  95 KVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQKTGlKNLLLEKKLQALGETLEKKEAQL 165
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
329-579 4.11e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.96  E-value: 4.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215  329 LEGKLRDREAELQQLRDSLDENEATMCQAYEERQRHWQReREALREdcaaqaqraqraqqllqlqvfqLQQEKRQLQDDF 408
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHEER-REELET----------------------LEAEIEDLRETI 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215  409 AQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVA----------L 478
Cdd:PRK02224 268 AETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAaqahneeaesL 347

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215  479 REARATLrvsEGRARGLQEAARARELELEACsqelqrhRQEAEQLREKAGQLDAEAAGLRE----PPVPPATADPFL--L 552
Cdd:PRK02224 348 REDADDL---EERAEELREEAAELESELEEA-------REAVEDRREEIEELEEEIEELRErfgdAPVDLGNAEDFLeeL 417

                        250       260
                 ....*....|....*....|....*..
gi 45331215  553 AESDEAKVQRAAagvggSLRAQVERLR 579
Cdd:PRK02224 418 REERDELREREA-----ELEATLRTAR 439
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
329-539 1.95e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.65  E-value: 1.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215  329 LEGKLRDREAELQQLRDSLDENEATMcQAYEERQRHWQREREALREDcaaqaqraqraQQLLQLQVFQLQQEKRQLQDDF 408
Cdd:PRK02224 347 LREDADDLEERAEELREEAAELESEL-EEAREAVEDRREEIEELEEE-----------IEELRERFGDAPVDLGNAEDFL 414

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215  409 AQLLQEREQLERRCATLEREQRELGPRLEETkwEVCQKSGEISLLKQQLKESQ-----AELVQKGSELVALRVALREARA 483
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVEEA--EALLEAGKCPECGQPVEGSPhvetiEEDRERVEELEAELEDLEEEVE 492

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45331215  484 TLRVSEGRARGLQEAARARELELEACS----------QELQRHRQEAEQLREKAGQLDAEAAGLRE 539
Cdd:PRK02224 493 EVEERLERAEDLVEAEDRIERLEERREdleeliaerrETIEEKRERAEELRERAAELEAEAEEKRE 558
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 337-539 5.86e-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: 43.13  E-value: 5.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    337 EAELQQLRDSLDENEATMCQAYEERQRHWQREREALREdcaaqaqraqraQQLLQLQVFQLQQEKRQLQDDFAQLLQERE 416
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE------------LSDASRKIGEIEKEIEQLEQEEEKLKERLE 740

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    417 QLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQkgSELVALRVALREARATLRVSEGRARGLQ 496
Cdd:TIGR02169  741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIE 818

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 45331215    497 EAARARELE---LEACSQELQRHRQEAE-QLREKAGQLDAEAAGLRE 539
Cdd:TIGR02169  819 QKLNRLTLEkeyLEKEIQELQEQRIDLKeQIKSIEKEIENLNGKKEE 865
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 453-529 1.24e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 39.49  E-value: 1.24e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45331215    453 LKQQLKESQAELVQKGSELVALRVALREARATLRvsegrarglQEAARARELELEACSQELQRHRQEAEQLREKAGQ 529
Cdd:smart00935  23 LEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS---------EAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQ 90
 
Name Accession Description Interval E-value
Fez1 pfam06818
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ...
 439-636 3.16e-81

Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.


Pssm-ID: 462015 [Multi-domain]  Cd Length: 198  Bit Score: 255.69  E-value: 3.16e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215   439 TKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGRARGLQEAARARELELEACSQELQRHRQ 518
Cdd:pfam06818   1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215   519 EAEQLREKAGQLDAEAAGLREPPVPPATADPFLLAESDEAKVQRAAAGVGGSLRAQVERLRVELQRERRRGEEQRDSFEG 598
Cdd:pfam06818  81 EAELLREKVGKLEEEVSGLREALSDVSPSGYESVYESDEAKEQRQEEADLGSLRREVERLRAELREERQRRERQASSFEQ 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 45331215   599 ERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQ 636
Cdd:pfam06818 161 ERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 332-657 9.15e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 81.52  E-value: 9.15e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 332 KLRDREAELQQLRDSLDENEATMcQAYEERQRHWQREREALREDcaaqaqraqraqqllqlqVFQLQQEKRQLQDDFAQL 411
Cdd:COG1196 233 KLRELEAELEELEAELEELEAEL-EELEAELAELEAELEELRLE------------------LEELELELEEAQAEEYEL 293

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 412 LQEREQLERRCATLEREQRELGPRLEETKWevcqksgEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGR 491
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEE-------ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 492 ARGLQEAARARELELEACSQELQRHRQEAEQLREKAGQLDAEAAGLREppvppatadpfLLAESDEAKVQRAAAgvggsl 571
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-----------RLERLEEELEELEEA------ 429

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 572 RAQVERLRVELQRErrrgeeqrdsfEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEARELADLG 651
Cdd:COG1196 430 LAELEEEEEEEEEA-----------LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498


                ....*.
gi 45331215 652 LAEQAP 657
Cdd:COG1196 499 AEADYE 504
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 329-548 6.10e-11

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: 65.85  E-value: 6.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    329 LEGKLRDREAELQQLRDSLDENEATMCQAYEERQRHwQREREALREdcaaqaqraqraqqllqlQVFQLQQEKRQLQDDF 408
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL-KEELKALRE------------------ALDELRAELTLLNEEA 819

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    409 AQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSE-------LVALRVALREA 481
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNErasleeaLALLRSELEEL 899

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    482 RATLRVSEGRARGLQEAARARELELEACSQELQRHRQEAEQLREKA---GQLDAEAAGLREPPVPPATAD 548
Cdd:TIGR02168  900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLseeYSLTLEEAEALENKIEDDEEE 969
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 366-655 5.36e-10

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: 62.77  E-value: 5.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    366 QREREALREDCaaqaqraqraqQLLQLQVFQLQQEKRQLQDDFAQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQ 445
Cdd:TIGR02168  676 RREIEELEEKI-----------EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    446 KSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGRARGLQEAARARELELEACSQELQRHRQEAEQLRE 525
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    526 KAGQLDAEAAGLREPPVppatadpFLLAESDEAKVQRAaagvggSLRAQVERLRVelqrerrrgeeQRDSFEGERLAWQA 605
Cdd:TIGR02168  825 RLESLERRIAATERRLE-------DLEEQIEELSEDIE------SLAAEIEELEE-----------LIEELESELEALLN 880

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 45331215    606 EKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEAR--ELADLGLAEQ 655
Cdd:TIGR02168  881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELreKLAQLELRLE 932
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 329-634 2.73e-09

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: 60.47  E-value: 2.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    329 LEGKLRDREAELQQLRDSLDENEATMCQAyEERQRHWQREREALREDcaaqaqraqraqqllqlqvfqlqqEKRQLQDDF 408
Cdd:TIGR02169  242 IERQLASLEEELEKLTEEISELEKRLEEI-EQLLEELNKKIKDLGEE------------------------EQLRVKEKI 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    409 AQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVS 488
Cdd:TIGR02169  297 GELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV 376

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    489 EGRARGLQEAARARELELEACSQELQRHRQEAEQLREKAGQLDAEAAGLREppvppATADpfllAESDEAKVQRAAAGVG 568
Cdd:TIGR02169  377 DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA-----AIAG----IEAKINELEEEKEDKA 447

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45331215    569 GSLRAQVERLrvelqrerRRGEEQRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQE 634
Cdd:TIGR02169  448 LEIKKQEWKL--------EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
400-579 1.81e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.00  E-value: 1.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215  400 EKRQLQDDFAQLLQEREQLERRCATLEREQRELGpRLEETKWE---VCQKSGEISLLKQQLkesqAELVQKGSELVALRV 476
Cdd:COG4913  618 ELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDeidVASAEREIAELEAEL----ERLDASSDDLAALEE 692

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215  477 ALREARATLRVSEGRARGLQEAARARELELEACSQELQRHRQEAEQLREKAGQLDAEAaglreppvppatADPFLLAESD 556
Cdd:COG4913  693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL------------LEERFAAALG 760

                        170       180
                 ....*....|....*....|...
gi 45331215  557 EAKVQRAAAGVGGSLRAQVERLR 579
Cdd:COG4913  761 DAVERELRENLEERIDALRARLN 783
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
333-538 3.32e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.85  E-value: 3.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215  333 LRDREAELQQLRDSLDENEATMcqayeERQRHWQREREAlredcaaqaqraqraqqllqlqvfqlqqekRQLQDDFAQLL 412
Cdd:COG4913  257 IRELAERYAAARERLAELEYLR-----AALRLWFAQRRL------------------------------ELLEAELEELR 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215  413 QEREQLERRCATLEREQRELGPRLEETKwEVCQKSG--EISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEG 490
Cdd:COG4913  302 AELARLEAELERLEARLDALREELDELE-AQIRGNGgdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 45331215  491 RARGLQEAARAR----ELELEACSQELQRHRQEAEQLREKAGQLDAEAAGLR 538
Cdd:COG4913  381 EFAALRAEAAALlealEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 329-651 4.71e-08

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: 56.60  E-value: 4.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    329 LEGKLRDREAELQQLRDSLDENEatmcQAYEERQRHWQREREALREDcAAQAQRAQRAQQLLQLQVFQLQQEKRQLQDDF 408
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELE----EELEQLRKELEELSRQISAL-RKDLARLEAEVEQLEERIAQLSKELTELEAEI 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    409 AQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVS 488
Cdd:TIGR02168  764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    489 EGRARGLQEAARARELELEACSQELQRHRQEAEQLREKAGQLDAEAAGLREppvppatadpfllAESDEAKVQRAAAGVG 568
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS-------------ELEELSEELRELESKR 910

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    569 GSLRAQVERLRvelqrerrrgeeqrDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEAR--- 645
Cdd:TIGR02168  911 SELRRELEELR--------------EKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRlkr 976


                   ....*....
gi 45331215    646 ---ELADLG 651
Cdd:TIGR02168  977 lenKIKELG 985
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
400-539 5.70e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.93  E-value: 5.70e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 400 EKRQLQDDFAQLLQEREQLERRCATLEREQRELGPRLEETK-----WEVCQKSGEISLLKQQLKESQAELVQKGSELVAL 474
Cdd:COG4717  82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEkllqlLPLYQELEALEAELAELPERLEELEERLEELREL 161

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45331215 475 RVALREARATL-RVSEGRARGLQEAARARELELEACSQELQRHRQEAEQLREKAGQLDAEAAGLRE 539
Cdd:COG4717 162 EEELEELEAELaELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 322-639 1.65e-07

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: 54.68  E-value: 1.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    322 EALLHCVLEGKLRDREAELQQLRDSLDENEaTMCQAYEERQRHWQREREALRedcaaqaqraqraqqllqLQVFQLQQEK 401
Cdd:TIGR02168  223 RELELALLVLRLEELREELEELQEELKEAE-EELEELTAELQELEEKLEELR------------------LEVSELEEEI 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    402 RQLQDDFAQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREA 481
Cdd:TIGR02168  284 EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    482 RATLRVSEGRARGLQEAARAR-------ELELEACSQELQRHRQEAEQLREKAGQLDAEAAGLREppvppatadpfllaE 554
Cdd:TIGR02168  364 EAELEELESRLEELEEQLETLrskvaqlELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK--------------K 429

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    555 SDEAKVQRAAAGVGGsLRAQVERLRVELQRERRRGEEQRDSFEGERLAWQAEKEQVIRYQ------KQLQHNYIQMYRRN 628
Cdd:TIGR02168  430 LEEAELKELQAELEE-LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarldslERLQENLEGFSEGV 508

                          330
                   ....*....|.
gi 45331215    629 RQLEQELQQLS 639
Cdd:TIGR02168  509 KALLKNQSGLS 519
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
413-638 1.77e-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: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215  413 QEREQLERRCATLEREQRELGPRLEETKWEVCQKsgEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGRa 492
Cdd:COG4913  262 ERYAAARERLAELEYLRAALRLWFAQRRLELLEA--ELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD- 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215  493 rglqeaararelELEACSQELQRHRQEAEQLREKAGQLDAEAAGLREPPvpPATADPFllaesdeAKVQRAAAGVGGSLR 572
Cdd:COG4913  339 ------------RLEQLEREIERLERELEERERRRARLEALLAALGLPL--PASAEEF-------AALRAEAAALLEALE 397

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45331215  573 AQVERLRvelqrerrrgeeqRDSFEGERLAWQAEKEQviryqkqlqhnyiqmyrrnRQLEQELQQL 638
Cdd:COG4913  398 EELEALE-------------EALAEAEAALRDLRREL-------------------RELEAEIASL 431
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 328-577 5.63e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 5.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 328 VLEGKLRDREAELQQLRDSLDENEATMcQAYEERQRHWQREREAL---REDCAAQAQRAQRAQQLLQLQVFQLQQEKRQL 404
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEEL-EELEEELEELEEELEEAeeeLEEAEAELAEAEEALLEAEAELAEAEEELEEL 384

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 405 QDDFAQLLQEREQLERRCATLEREQRELGPRLEETKWEvcqksgeisllKQQLKESQAELVQKGSELVALRVALREARAT 484
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE-----------LEELEEALAELEEEEEEEEEALEEAAEEEAE 453

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 485 LRVSEGRARGLQEAARARELELEACSQELQRHRQEAEQLREKAGQLDAEAAG-------LREPPVPPATADPFLLAESDE 557
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGflegvkaALLLAGLRGLAGAVAVLIGVE 533

                       250       260
                ....*....|....*....|
gi 45331215 558 AKVQRAAAGVGGSLRAQVER 577
Cdd:COG1196 534 AAYEAALEAALAAALQNIVV 553
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 400-646 8.21e-07

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: 52.37  E-value: 8.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    400 EKRQLQDDFAQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 479
Cdd:TIGR02168  254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    480 EARATLRVSEGRARGLQEaararelELEACSQELQRHRQEAEQLREKAGQLDAEAAGLREppvppATADPFLLAESDEAK 559
Cdd:TIGR02168  334 ELAEELAELEEKLEELKE-------ELESLEAELEELEAELEELESRLEELEEQLETLRS-----KVAQLELQIASLNNE 401

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    560 VQRaaagvggsLRAQVERLRVELQRERRRGEEQRDSF-EGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQL 638
Cdd:TIGR02168  402 IER--------LEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEELEEELEELQEELERLEEALEELREELEEA 473


                   ....*...
gi 45331215    639 SLELEARE 646
Cdd:TIGR02168  474 EQALDAAE 481
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 408-650 1.38e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 1.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    408 FAQLLQEREQLERRCATLereqrelgpRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRV 487
Cdd:TIGR02168  215 YKELKAELRELELALLVL---------RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    488 SEGRargLQEAARarelELEACSQELQRHRQEAEQLREKAGQLDAEAAGLREPPVPPATADPFLLAESDEAKVQRAaagv 567
Cdd:TIGR02168  286 LQKE---LYALAN----EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE---- 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    568 ggSLRAQVERLRVELQRERRRGEEQRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEAREL 647
Cdd:TIGR02168  355 --SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432


                   ...
gi 45331215    648 ADL 650
Cdd:TIGR02168  433 AEL 435
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 400-657 4.66e-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: 49.38  E-value: 4.66e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 400 EKRQLQDDFAQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 479
Cdd:COG4942  21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 480 EARATLRvseGRARGLQEAARARELELEACSQELQRHRQEAEQLREKAGQLDAEAAGLREppvppatadpfllaesdeak 559
Cdd:COG4942 101 AQKEELA---ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRA-------------------- 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 560 vqraaagvggsLRAQVERLRVELQRERRRGEEQRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLS 639
Cdd:COG4942 158 -----------DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226

                       250
                ....*....|....*...
gi 45331215 640 LELEARELADLGLAEQAP 657
Cdd:COG4942 227 ALIARLEAEAAAAAERTP 244
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 332-549 6.80e-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: 48.99  E-value: 6.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 332 KLRDREAELQQLRDSLDENEATMcQAYEERQRHWQREREALREDcaaqaqraqraQQLLQLQVFQLQQEKRQLQDDFAQL 411
Cdd:COG4942  21 AAAEAEAELEQLQQEIAELEKEL-AALKKEEKALLKQLAALERR-----------IAALARRIRALEQELAALEAELAEL 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 412 LQEREQLERRcatLEREQRELGPRLEETkwevcQKSGEISLLK-----------------------------QQLKESQA 462
Cdd:COG4942  89 EKEIAELRAE---LEAQKEELAELLRAL-----YRLGRQPPLAlllspedfldavrrlqylkylaparreqaEELRADLA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 463 ELVQKGSELVALRVALREARATLrvsEGRARGLQEAARARELELEACSQELQRHRQEAEQLREKAGQLDAEAAGLREPPV 542
Cdd:COG4942 161 ELAALRAELEAERAELEALLAEL---EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237


                ....*..
gi 45331215 543 PPATADP 549
Cdd:COG4942 238 AAAERTP 244
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
402-644 9.55e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 9.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215  402 RQLQDDFAQLLQEREQLERrcatlEREQRELgprLEETkwevcqksgeisllkQQLKESQAELVQKGSELVALRVALREA 481
Cdd:COG4913  228 DALVEHFDDLERAHEALED-----AREQIEL---LEPI---------------RELAERYAAARERLAELEYLRAALRLW 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215  482 RAtlrvsegrarglQEAARARELELEACSQELQRHRQEAEQLREKAGQLDAEAAGLREppvppatadpfllaesdeakvQ 561
Cdd:COG4913  285 FA------------QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEA---------------------Q 331

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215  562 RAAAGVG--GSLRAQVERLRVELQRERR--------------RGEEQRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMY 625
Cdd:COG4913  332 IRGNGGDrlEQLEREIERLERELEERERrrarleallaalglPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAE 411

                        250
                 ....*....|....*....
gi 45331215  626 RRNRQLEQELQQLSLELEA 644
Cdd:COG4913  412 AALRDLRRELRELEAEIAS 430
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
400-535 1.74e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 400 EKRQLQDDFAQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 479
Cdd:COG4372  46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ 125

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 45331215 480 EARATLRVSEGRARGLQEAARARELELEACSQELQRHRQEAEQLREKAGQLDAEAA 535
Cdd:COG4372 126 DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 402-471 1.84e-05

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 46.05  E-value: 1.84e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45331215   402 RQLQDDFAQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSG-EISLLKQQLKESQAELVQKGSEL 471
Cdd:pfam13851  95 KVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQKTGlKNLLLEKKLQALGETLEKKEAQL 165
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
329-576 1.89e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 329 LEGKLRDREAELQQLRDSLDENEATMCQAYEERQRHWQREREALREdcaaqAQRAQRAQQLLQLQVFQLQQEKRQLQDDF 408
Cdd:COG4372  43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ-----LQAAQAELAQAQEELESLQEEAEELQEEL 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 409 AQLLQEREQLERRCATLEREQRELgprleetKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVS 488
Cdd:COG4372 118 EELQKERQDLEQQRKQLEAQIAEL-------QSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 489 EGRARGLQEAARARELELEACSQELQRHRQEAEQLREKAGQLDAEAAGLREPPVPPATADPFLLAESDEAKVQRAAAGVG 568
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270


                ....*...
gi 45331215 569 GSLRAQVE 576
Cdd:COG4372 271 KDTEEEEL 278
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 400-579 1.99e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 46.46  E-value: 1.99e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 400 EKRQLQDDFAQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAEL--VQKGSELVALRVA 477
Cdd:COG1579  18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnVRNNKEYEALQKE 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 478 LREARATLRVSEGRARGLQEAARARELELEACSQELQrhrQEAEQLREKAGQLDAEAAGLREppvppatadpflLAESDE 557
Cdd:COG1579  98 IESLKRRISDLEDEILELMERIEELEEELAELEAELA---ELEAELEEKKAELDEELAELEA------------ELEELE 162

                       170       180
                ....*....|....*....|..
gi 45331215 558 AKVQRAAAGVGGSLRAQVERLR 579
Cdd:COG1579 163 AEREELAAKIPPELLALYERIR 184
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 329-486 3.26e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 45.69  E-value: 3.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 329 LEGKLRDREAELQQLRDSLDENEATMcQAYEERQRHWQREREALREDcaaqaqraqraqqLLQLQVFQLQQEKRQLQ--- 405
Cdd:COG1579  22 LEHRLKELPAELAELEDELAALEARL-EAAKTELEDLEKEIKRLELE-------------IEEVEARIKKYEEQLGNvrn 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 406 -DDFAQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARAT 484
Cdd:COG1579  88 nKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167


                ..
gi 45331215 485 LR 486
Cdd:COG1579 168 LA 169
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
329-579 4.11e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.96  E-value: 4.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215  329 LEGKLRDREAELQQLRDSLDENEATMCQAYEERQRHWQReREALREdcaaqaqraqraqqllqlqvfqLQQEKRQLQDDF 408
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHEER-REELET----------------------LEAEIEDLRETI 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215  409 AQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVA----------L 478
Cdd:PRK02224 268 AETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAaqahneeaesL 347

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215  479 REARATLrvsEGRARGLQEAARARELELEACsqelqrhRQEAEQLREKAGQLDAEAAGLRE----PPVPPATADPFL--L 552
Cdd:PRK02224 348 REDADDL---EERAEELREEAAELESELEEA-------REAVEDRREEIEELEEEIEELRErfgdAPVDLGNAEDFLeeL 417

                        250       260
                 ....*....|....*....|....*..
gi 45331215  553 AESDEAKVQRAAagvggSLRAQVERLR 579
Cdd:PRK02224 418 REERDELREREA-----ELEATLRTAR 439
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
410-539 7.32e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 7.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 410 QLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSE 489
Cdd:COG4372  14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 45331215 490 GRARGLQEAARARELELEACSQELQRHRQEAEQLREKAGQLDAEAAGLRE 539
Cdd:COG4372  94 AELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQS 143
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
329-545 1.76e-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: 1.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215  329 LEGKLRDREAELQQLRDSLDENEATMCQAYEERQRHWQREREALREdcaaqaqraqraqqllqlqvfqlqqEKRQLQDDF 408
Cdd:COG4913  300 LRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLER-------------------------EIERLEREL 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215  409 AQLLQEREQLERRCATLereqrELGPRLEEtkwevcqksgeisllkQQLKESQAELVQKGSELVALRVALREARATLRVs 488
Cdd:COG4913  355 EERERRRARLEALLAAL-----GLPLPASA----------------EEFAALRAEAAALLEALEEELEALEEALAEAEA- 412

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45331215  489 egRARGLQEAARARELELEAcsqeLQRHR----QEAEQLREkagQLdAEAAGLREPPVPPA 545
Cdd:COG4913  413 --ALRDLRRELRELEAEIAS----LERRKsnipARLLALRD---AL-AEALGLDEAELPFV 463
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
329-539 1.95e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.65  E-value: 1.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215  329 LEGKLRDREAELQQLRDSLDENEATMcQAYEERQRHWQREREALREDcaaqaqraqraQQLLQLQVFQLQQEKRQLQDDF 408
Cdd:PRK02224 347 LREDADDLEERAEELREEAAELESEL-EEAREAVEDRREEIEELEEE-----------IEELRERFGDAPVDLGNAEDFL 414

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215  409 AQLLQEREQLERRCATLEREQRELGPRLEETkwEVCQKSGEISLLKQQLKESQ-----AELVQKGSELVALRVALREARA 483
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVEEA--EALLEAGKCPECGQPVEGSPhvetiEEDRERVEELEAELEDLEEEVE 492

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45331215  484 TLRVSEGRARGLQEAARARELELEACS----------QELQRHRQEAEQLREKAGQLDAEAAGLRE 539
Cdd:PRK02224 493 EVEERLERAEDLVEAEDRIERLEERREdleeliaerrETIEEKRERAEELRERAAELEAEAEEKRE 558
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 337-539 5.86e-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: 43.13  E-value: 5.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    337 EAELQQLRDSLDENEATMCQAYEERQRHWQREREALREdcaaqaqraqraQQLLQLQVFQLQQEKRQLQDDFAQLLQERE 416
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE------------LSDASRKIGEIEKEIEQLEQEEEKLKERLE 740

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    417 QLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQkgSELVALRVALREARATLRVSEGRARGLQ 496
Cdd:TIGR02169  741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIE 818

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 45331215    497 EAARARELE---LEACSQELQRHRQEAE-QLREKAGQLDAEAAGLRE 539
Cdd:TIGR02169  819 QKLNRLTLEkeyLEKEIQELQEQRIDLKeQIKSIEKEIENLNGKKEE 865
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 329-543 1.04e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 1.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 329 LEGKLRDREAELQQLRDSLDENEATMcQAYEERQRHWQREREALREDCAAQAQRAQRAQQLLQLQVFQLqqekrqlQDDF 408
Cdd:COG4942  60 LERRIAALARRIRALEQELAALEAEL-AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLS-------PEDF 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 409 AQLLQEREQLERrcatLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVS 488
Cdd:COG4942 132 LDAVRRLQYLKY----LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 45331215 489 EGRARGLQEAARARELELEACSQELQrhRQEAEQLREKAGQLDAEAAGLREPPVP 543
Cdd:COG4942 208 LAELAAELAELQQEAEELEALIARLE--AEAAAAAERTPAAGFAALKGKLPWPVS 260
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 453-529 1.24e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 39.49  E-value: 1.24e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45331215    453 LKQQLKESQAELVQKGSELVALRVALREARATLRvsegrarglQEAARARELELEACSQELQRHRQEAEQLREKAGQ 529
Cdd:smart00935  23 LEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS---------EAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQ 90
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
408-539 1.49e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 1.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 408 FAQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRV 487
Cdd:COG4372  26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 45331215 488 SEGRARGLQEAARARELELEACSQELQRHRQEAEQLREKAGQLDAEAAGLRE 539
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
329-647 1.58e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 329 LEGKLRDREAELQQLRDSLDENEATMCQAYEERQRHWQREREALREdcaaqaqraqraqqllqlqvfqlqqEKRQLQDDF 408
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ-------------------------RLAELEEEL 215

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 409 AQLLQEREQLERRCATLEREQRELGP--RLEETKWEVCQKSGEISLLkqQLKESQAELVQKGSELVALRVAL-------- 478
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALeeRLKEARLLLLIAAALLALL--GLGGSLLSLILTIAGVLFLVLGLlallflll 293

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 479 -----------REARATLRVSEGRARGLQEAARARELELEACSQELQRHRQEAEQLREKAGQLDAEAAGLREPPVPPATA 547
Cdd:COG4717 294 arekaslgkeaEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA 373

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 548 DPFLLAESD-----EAKVQRAAAGVggSLRAQVERLRVELQRERRRGEEQRDSFEGERLawQAEKEQVIRYQKQLQHNYI 622
Cdd:COG4717 374 ALLAEAGVEdeeelRAALEQAEEYQ--ELKEELEELEEQLEELLGELEELLEALDEEEL--EEELEELEEELEELEEELE 449

                       330       340
                ....*....|....*....|....*
gi 45331215 623 QMYRRNRQLEQELQQLSLELEAREL 647
Cdd:COG4717 450 ELREELAELEAELEQLEEDGELAEL 474
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 324-537 1.78e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.42  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215   324 LLHCVLEGKLRDReAELQQLRDSLDENEATMCQAYEERQRHWQREREALREDCAAQAQRAQRAQQLLQLQVFQLQQEKR- 402
Cdd:pfam07888  31 LLQNRLEECLQER-AELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAs 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215   403 --QLQDDFAQLLQEREQLERRCATLEREQRELGPRLEEtkwevcqKSGEISLLKQQLKE--------------SQAELVQ 466
Cdd:pfam07888 110 seELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLE-------RETELERMKERAKKagaqrkeeeaerkqLQAKLQQ 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215   467 KGSELVALRVALREARATLRVSEGRARGLQE----------AARARELELEACSQELQRHRQEAEQLREKAGQLDAEAAG 536
Cdd:pfam07888 183 TEEELRSLSKEFQELRNSLAQRDTQVLQLQDtittltqkltTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSS 262


                  .
gi 45331215   537 L 537
Cdd:pfam07888 263 M 263
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 453-529 1.83e-03

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: 39.82  E-value: 1.83e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45331215 453 LKQQLKESQAELVQKGSELVALRVALREARATLRvsegrarglQEAARARELELEACSQELQRHRQEAEQLREKAGQ 529
Cdd:COG2825  48 LEKEFKKRQAELQKLEKELQALQEKLQKEAATLS---------EEERQKKERELQKKQQELQRKQQEAQQDLQKRQQ 115
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
332-486 2.35e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 2.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 332 KLRDREAELQQLrdsLDENEATMCQAYEERQRHWQREREALREdcaAQAQRAQRAQQLLQLQVFQLQQEKRQLQDDFAQL 411
Cdd:COG4717 364 QLEELEQEIAAL---LAEAGVEDEEELRAALEQAEEYQELKEE---LEELEEQLEELLGELEELLEALDEEELEEELEEL 437

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45331215 412 LQEREQLERRCATLEREQRELGPRLEETKwevcqKSGEISLLKQQ---LKESQAELVQKGSELVALRVALREARATLR 486
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLE-----EDGELAELLQEleeLKAELRELAEEWAALKLALELLEEAREEYR 510
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
400-530 3.25e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 3.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 400 EKRQLQDDFAQLLQEREQLERRCATLEREQRELGPRLEETKWEvcqksGEISLLKQQLKESQAELVQKGSELVALRVALR 479
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE-----EELEELEEELEELEEELEELREELAELEAELE 463

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45331215 480 EARATLRVSEGRARGLQEAARARELELEACS---------QELQRHRQE-AEQLREKAGQL 530
Cdd:COG4717 464 QLEEDGELAELLQELEELKAELRELAEEWAAlklalelleEAREEYREErLPPVLERASEY 524
mukB PRK04863
chromosome partition protein MukB;
403-646 3.35e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.71  E-value: 3.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215   403 QLQDDFAQLLQE----REQLERRCATLEreqrELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELV----AL 474
Cdd:PRK04863  331 QAASDHLNLVQTalrqQEKIERYQADLE----ELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAdyqqAL 406

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215   475 RV-------------ALREARATLRVSE---GRARGLQEAARARE----LELEACSQELQRHrQEAEQLREKAGQLDAEA 534
Cdd:PRK04863  407 DVqqtraiqyqqavqALERAKQLCGLPDltaDNAEDWLEEFQAKEqeatEELLSLEQKLSVA-QAAHSQFEQAYQLVRKI 485

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215   535 AGlrepPVPPATADPFLLAESDEAKVQRAAAGVGGSLRAQ-------------VERLRVELQRERRRGEEQRDSFEGERL 601
Cdd:PRK04863  486 AG----EVSRSEAWDVARELLRRLREQRHLAEQLQQLRMRlseleqrlrqqqrAERLLAEFCKRLGKNLDDEDELEQLQE 561

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 45331215   602 AWQAEKEQVIRYQKQLQHNYIQMyrrnRQLEQELQQLSLELEARE 646
Cdd:PRK04863  562 ELEARLESLSESVSEARERRMAL----RQQLEQLQARIQRLAARA 602
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 453-656 3.58e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 3.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 453 LKQQLK--ESQAELVQKgseLVALRVALREARATLRVS-----EGRARGLQEAARARELELEACSQELQRHRQEAEQLRE 525
Cdd:COG1196 198 LERQLEplERQAEKAER---YRELKEELKELEAELLLLklrelEAELEELEAELEELEAELEELEAELAELEAELEELRL 274

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215 526 KAGQLDAEAAGLREppvppatadPFLLAESDEAKVQRAAAgVGGSLRAQVERLRVELQRERRRGEEQRDSFEGERLAWQA 605
Cdd:COG1196 275 ELEELELELEEAQA---------EEYELLAELARLEQDIA-RLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 45331215 606 EKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEARELADLGLAEQA 656
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
414-527 3.65e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215  414 EREQLER---RCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELvqkgSELVALRVALREARATLRVSEG 490
Cdd:PRK03918 177 RIERLEKfikRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEG 252

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 45331215  491 RARGLQEAARARE---LELEACSQELQRHRQEAEQLREKA 527
Cdd:PRK03918 253 SKRKLEEKIRELEeriEELKKEIEELEEKVKELKELKEKA 292
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 329-533 8.77e-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: 39.33  E-value: 8.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    329 LEGKLRDREAELQQLRDSLDENEATMcqayeerqrhwqREREALREDCAAQAQRAQRAQQLLQlqvfqlqqekRQLQDdf 408
Cdd:pfam15921  595 LEKEINDRRLELQEFKILKDKKDAKI------------RELEARVSDLELEKVKLVNAGSERL----------RAVKD-- 650

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    409 aqLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISL----LKQQLKESQAELVQkgselvalrvalreARAT 484
Cdd:pfam15921  651 --IKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETttnkLKMQLKSAQSELEQ--------------TRNT 714

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45331215    485 LRVSEGR-------ARGLQEAARARELELEACSQELQ-------RHRQEAEQLREKAGQLDAE 533
Cdd:pfam15921  715 LKSMEGSdghamkvAMGMQKQITAKRGQIDALQSKIQfleeamtNANKEKHFLKEEKNKLSQE 777
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 329-539 8.86e-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: 8.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    329 LEGKLRDREAELQQLRDSLDE-----NEATMCQAYEERQRhwqREREALREDCAAQAQRAQRAQQLLQLQVFQLQQEKRQ 403
Cdd:TIGR02169  796 IQAELSKLEEEVSRIEARLREieqklNRLTLEKEYLEKEI---QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45331215    404 LQDDFAQLLQEREQLERRCATLEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALrVALREARA 483
Cdd:TIGR02169  873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED-EEIPEEEL 951

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 45331215    484 TLRVSEGRARGLQEAARARELELEACSQELQRHRQEAEQLREKAGQLDAEAAGLRE 539
Cdd:TIGR02169  952 SLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILE 1007
 
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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