NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|13259510|ref|NP_004073|]
View 

dynactin subunit 1 isoform 1 [Homo sapiens]

Protein Classification

CAP_GLY and Dynactin domain-containing protein( domain architecture ID 13652410)

protein containing domains CAP_GLY, PLN03209, Smc, and Dynactin

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Dynactin pfam12455
Dynein associated protein; This domain family is found in eukaryotes, and is approximately 280 ...
 527-805 3.99e-93

Dynein associated protein; This domain family is found in eukaryotes, and is approximately 280 amino acids in length. The family is found in association with pfam01302. There is a single completely conserved residue E that may be functionally important. Dynactin has been associated with Dynein, a kinesin protein which is involved in organelle transport, mitotic spindle assembly and chromosome segregation. Dynactin anchors Dynein to specific subcellular structures.


:

Pssm-ID: 463591  Cd Length: 287  Bit Score: 301.07  E-value: 3.99e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    527 LQDVNRELTNQQEASVERQQQPPPET-----FDFKIKFAETKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGg 601
Cdd:pfam12455    1 LQSDLEDLRASQQITESESEDLSSRSrammdLNLKLQSSASKAQAKAIDLELRRLEAQQASEHLEIVQLFLPDSFLRRG- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    602 DHDCVLVLLLMPRLICKAELIRKQAQEKFELSENcserPGLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDV 681
Cdd:pfam12455   80 DRDSVLALLLFKRLAFKADLLASQIREKFPLSES----LILKGHVEEQLFFACELLEKLTWLSALCDRFAAALRSCSVET 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    682 YKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPLTKAIKYYQHLYSIHLAEQPEDCTMQLADHIKFTQSALDCMS 761
Cdd:pfam12455  156 FLKIGGAYPELEPVERALDGWIDLLKRDELDENECAEELQRSIAYFSHLAEVHLADSLEDLADELLMRVLLLQSALDSIA 235

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 13259510    762 VEVGRLRAFLQGGQ--------EATDIALLLRDLETSCSDIRQFCKKIRRRM 805
Cdd:pfam12455  236 AALGRLKTLLQSGLpdpdggdeEASDLFELLQTLITQARSAKVISKKILRRL 287
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 29-94 1.04e-30

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


:

Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 115.19  E-value: 1.04e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13259510     29 VGSRVEVIGkGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQI 94
Cdd:pfam01302    1 VGDRVEVPG-GRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 220-540 5.69e-22

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 103.21  E-value: 5.69e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    220 LRAQVRDLEEKLETLR--LKRAED-----KAKLKELEKHKIQLEQVQEWKSKMQEQQADLQ-RRLKEARKEAKEALEAKE 291
Cdd:TIGR02168  170 YKERRKETERKLERTRenLDRLEDilnelERQLKSLERQAEKAERYKELKAELRELELALLvLRLEELREELEELQEELK 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    292 RYMEEMADTADAIEMA-----TLDKEMAE--ERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLE 364
Cdd:TIGR02168  250 EAEEELEELTAELQELeekleELRLEVSEleEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    365 EQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALG----AEEMV 440
Cdd:TIGR02168  330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNeierLEARL 409

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    441 EMLTDRNLNLEEKVRELRETVGDLEaMNEMNDELQENARETElELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKY 520
Cdd:TIGR02168  410 ERLEDRRERLQQEIEELLKKLEEAE-LKELQAELEELEEELE-ELQEELERLEEALEELREELEEAEQALDAAERELAQL 487

                          330       340
                   ....*....|....*....|
gi 13259510    521 RQLTAHLQDVNRELTNQQEA 540
Cdd:TIGR02168  488 QARLDSLERLQENLEGFSEG 507
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 926-1046 5.58e-06

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 5.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  926 LRAAALRAEIT--DAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSA---AKDADERIEKVQTRLEE 1000
Cdd:COG1196  213 ERYRELKEELKelEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELrleLEELELELEEAQAEEYE 292

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 13259510 1001 TQALLRKKEKEF---EETMDALQADIDQLEAEKAELKQRLNSQSKRTIE 1046
Cdd:COG1196  293 LLAELARLEQDIarlEERRRELEERLEELEEELAELEEELEELEEELEE 341
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 101-220 4.02e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 4.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   101 ADTTSPETPDSSASKVLkrEGTDTTAKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGVAGASSSLgPSGSASAGELSS 180
Cdd:PHA03247 2734 ALPAAPAPPAVPAGPAT--PGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESL-PSPWDPADPPAA 2810

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 13259510   181 SEPSTPAQTPLAAPIIPTPVLTSPGAVPPLPSPSKEEEGL 220
Cdd:PHA03247 2811 VLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSL 2850
 
Name Accession Description Interval E-value
Dynactin pfam12455
Dynein associated protein; This domain family is found in eukaryotes, and is approximately 280 ...
 527-805 3.99e-93

Dynein associated protein; This domain family is found in eukaryotes, and is approximately 280 amino acids in length. The family is found in association with pfam01302. There is a single completely conserved residue E that may be functionally important. Dynactin has been associated with Dynein, a kinesin protein which is involved in organelle transport, mitotic spindle assembly and chromosome segregation. Dynactin anchors Dynein to specific subcellular structures.


Pssm-ID: 463591  Cd Length: 287  Bit Score: 301.07  E-value: 3.99e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    527 LQDVNRELTNQQEASVERQQQPPPET-----FDFKIKFAETKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGg 601
Cdd:pfam12455    1 LQSDLEDLRASQQITESESEDLSSRSrammdLNLKLQSSASKAQAKAIDLELRRLEAQQASEHLEIVQLFLPDSFLRRG- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    602 DHDCVLVLLLMPRLICKAELIRKQAQEKFELSENcserPGLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDV 681
Cdd:pfam12455   80 DRDSVLALLLFKRLAFKADLLASQIREKFPLSES----LILKGHVEEQLFFACELLEKLTWLSALCDRFAAALRSCSVET 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    682 YKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPLTKAIKYYQHLYSIHLAEQPEDCTMQLADHIKFTQSALDCMS 761
Cdd:pfam12455  156 FLKIGGAYPELEPVERALDGWIDLLKRDELDENECAEELQRSIAYFSHLAEVHLADSLEDLADELLMRVLLLQSALDSIA 235

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 13259510    762 VEVGRLRAFLQGGQ--------EATDIALLLRDLETSCSDIRQFCKKIRRRM 805
Cdd:pfam12455  236 AALGRLKTLLQSGLpdpdggdeEASDLFELLQTLITQARSAKVISKKILRRL 287
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 29-94 1.04e-30

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 115.19  E-value: 1.04e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13259510     29 VGSRVEVIGkGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQI 94
Cdd:pfam01302    1 VGDRVEVPG-GRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 29-95 8.60e-29

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 109.98  E-value: 8.60e-29
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13259510      29 VGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEA-KGKNDGTVQGRKYFTCDEGHGIFVRQSQIQ 95
Cdd:smart01052    1 VGDRVEVGGGGRRGTVRYVGPTPFAPGVWVGVELDEPlRGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 220-540 5.69e-22

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: 103.21  E-value: 5.69e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    220 LRAQVRDLEEKLETLR--LKRAED-----KAKLKELEKHKIQLEQVQEWKSKMQEQQADLQ-RRLKEARKEAKEALEAKE 291
Cdd:TIGR02168  170 YKERRKETERKLERTRenLDRLEDilnelERQLKSLERQAEKAERYKELKAELRELELALLvLRLEELREELEELQEELK 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    292 RYMEEMADTADAIEMA-----TLDKEMAE--ERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLE 364
Cdd:TIGR02168  250 EAEEELEELTAELQELeekleELRLEVSEleEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    365 EQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALG----AEEMV 440
Cdd:TIGR02168  330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNeierLEARL 409

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    441 EMLTDRNLNLEEKVRELRETVGDLEaMNEMNDELQENARETElELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKY 520
Cdd:TIGR02168  410 ERLEDRRERLQQEIEELLKKLEEAE-LKELQAELEELEEELE-ELQEELERLEEALEELREELEEAEQALDAAERELAQL 487

                          330       340
                   ....*....|....*....|
gi 13259510    521 RQLTAHLQDVNRELTNQQEA 540
Cdd:TIGR02168  488 QARLDSLERLQENLEGFSEG 507
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 221-515 1.05e-21

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 102.32  E-value: 1.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  221 RAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADT 300
Cdd:COG1196  221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  301 ADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDL 380
Cdd:COG1196  301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  381 SSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmvemltdrnlNLEEKVRELRET 460
Cdd:COG1196  381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE----------EEEEALEEAAEE 450

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 13259510  461 VGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQ 515
Cdd:COG1196  451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
221-488 1.03e-19

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 95.49  E-value: 1.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   221 RAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQewksKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADT 300
Cdd:PRK02224  474 RERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIE----RLEERREDLEELIAERRETIEEKRERAEELRERAAEL 549

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   301 ADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILK------AEIEEKGSDGAASSYQLKQLEEQNARLKDAL 374
Cdd:PRK02224  550 EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLErirtllAAIADAEDEIERLREKREALAELNDERRERL 629

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   375 vrmrdlssSEKQEHVKlqKLMEKKNQE-LEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEK 453
Cdd:PRK02224  630 --------AEKRERKR--ELEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRER 699

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 13259510   454 VRELRETVGDLEAMNEMNDELQENARETELELREQ 488
Cdd:PRK02224  700 REALENRVEALEALYDEAEELESMYGDLRAELRQR 734
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 27-425 1.01e-13

Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227569 [Multi-domain]  Cd Length: 669  Bit Score: 75.88  E-value: 1.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   27 LRVGSRVEVIGKghRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRqsqiqvfedgadttsp 106
Cdd:COG5244    4 LSVNDRVLLGDK--FGTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIFIR---------------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  107 etPDSSAskVLKRegtdtTAKTSKLRGLKPKKAPTARKTTTRRPKPTRpastgvagassslgpsgsasagELSSSEPStp 186
Cdd:COG5244   66 --PDDDS--LLNG-----NAAYEKIKGGLVCESKGMDKDGEIKQENHE----------------------DRIHFEES-- 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  187 aqtpLAAPIIPTPVLTSPGAVPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIqLEQVQEWKSKMQ 266
Cdd:COG5244  113 ----KIRRLEETIEALKSTEKEEIVELRRENEELDKINLSLRERISSEEPELNKDGSKLSYDELKEF-VEESRVQVYDMV 187

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  267 EQQADLQRRLKEARKEAKEALEAKERymeemadtadaiematldkemaeeraeslqqevealKERVDELTTDLEILKAEI 346
Cdd:COG5244  188 ELVSDISETLNRNGSIQRSSVRECER------------------------------------SNIHDVLFLVNGILDGVI 231

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  347 EEKGsdgaassyqlKQLEeqnaRLKDALVRMRDLSSSEKQEHVKLQKLMEK-KNQELEVVRQQRERLQEELSQAESTIDE 425
Cdd:COG5244  232 DELN----------GELE----RLRRQLVSLMSSHGIEVEENSRLKATLEKfQSLELKVNTLQEELYQNKLLKKFYQIYE 297
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 225-577 1.65e-10

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 65.76  E-value: 1.65e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    225 RDLEEKLETLRLKRAEDKAKLKELEKHKIQLEqvqewKSKMQEQQAdlQRRLKEarKEAKEALEAKERYMEEMADTADAI 304
Cdd:pfam02463  169 RKKKEALKKLIEETENLAELIIDLEELKLQEL-----KLKEQAKKA--LEYYQL--KEKLELEEEYLLYLDYLKLNEERI 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    305 EMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQnarlKDALVRMRDLSSSE 384
Cdd:pfam02463  240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE----LLKLERRKVDDEEK 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    385 KQEHvklQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDL 464
Cdd:pfam02463  316 LKES---EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    465 EAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVER 544
Cdd:pfam02463  393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472

                          330       340       350
                   ....*....|....*....|....*....|...
gi 13259510    545 QQQpppETFDFKIKFAETKAHAKAIEMELRQME 577
Cdd:pfam02463  473 LLK---ETQLVKLQEQLELLLSRQKLEERSQKE 502
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 216-1035 1.46e-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: 62.78  E-value: 1.46e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    216 EEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEqqadlqRRLKEARKEAKEALEAKERYME 295
Cdd:TIGR02169  171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKRE------YEGYELLKEKEALERQKEAIER 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    296 EMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELT--------TDLEILKAEIEEKGSDGAASSYQLKQLEEQN 367
Cdd:TIGR02169  245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGeeeqlrvkEKIGELEAEIASLERSIAEKERELEDAEERL 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    368 ARLK----DALVRMRDLSSSEKQEHVKLQKLMEkknqELEVVRQQRERLQEELSQAESTIDELKEQVDAAlgaEEMVEML 443
Cdd:TIGR02169  325 AKLEaeidKLLAEIEELEREIEEERKRRDKLTE----EYAELKEELEDLRAELEEVDKEFAETRDELKDY---REKLEKL 397

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    444 TDRNLNLEEKVRELRETVGDL-EAMNEMNDELqENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQtikKYRQ 522
Cdd:TIGR02169  398 KREINELKRELDRLQEELQRLsEELADLNAAI-AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ---ELYD 473

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    523 LTAHLQDVNRELTNQQE--ASVE-RQQQPPPETFDFKIKFAETKAHAKAIEMELRQM-----------EVAQANRHMSLL 588
Cdd:TIGR02169  474 LKEEYDRVEKELSKLQRelAEAEaQARASEERVRGGRAVEEVLKASIQGVHGTVAQLgsvgeryataiEVAAGNRLNNVV 553

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    589 TafmpdsflrpggDHDCV---LVLLLMPRLICKAELI--RKQAQEKFELSencseRPGLRGAAGEQLS-------FAAGL 656
Cdd:TIGR02169  554 V------------EDDAVakeAIELLKRRKAGRATFLplNKMRDERRDLS-----ILSEDGVIGFAVDlvefdpkYEPAF 616

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    657 VYSL-------SLLQATLHRYEHALSQCSVDVYKKVGSlypeMSAHERSLDFLIellhKDQLDETVNVEPLTKAIKYYQH 729
Cdd:TIGR02169  617 KYVFgdtlvveDIEAARRLMGKYRMVTLEGELFEKSGA----MTGGSRAPRGGI----LFSRSEPAELQRLRERLEGLKR 688

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    730 LYSIHLAEQPEdctmqLADHIKFTQSALDCMSVEVGRLRAflqggqeatDIALLLRDLETSCSDIRQFCKKIRrrmpgtd 809
Cdd:TIGR02169  689 ELSSLQSELRR-----IENRLDELSQELSDASRKIGEIEK---------EIEQLEQEEEKLKERLEELEEDLS------- 747

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    810 apgipaalafgpQVSDTLLDCRKHLTWVVAVLQEvaaaaaqliaplaeneglLVAALEELAfKASEQIYGTPSSSPYECL 889
Cdd:TIGR02169  748 ------------SLEQEIENVKSELKELEARIEE------------------LEEDLHKLE-EALNDLEARLSHSRIPEI 796

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    890 RQSCNILISTMNKLATAMQEGEYDAERppskpppVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEA 969
Cdd:TIGR02169  797 QAELSKLEEEVSRIEARLREIEQKLNR-------LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869

                          810       820       830       840       850       860
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13259510    970 NVRLSLLEKKLDSAAKDADERIEKVQTRLEETQALLRKKEKEFEETMDALQADIDQLEAEKAELKQ 1035
Cdd:TIGR02169  870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 926-1046 5.58e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 5.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  926 LRAAALRAEIT--DAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSA---AKDADERIEKVQTRLEE 1000
Cdd:COG1196  213 ERYRELKEELKelEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELrleLEELELELEEAQAEEYE 292

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 13259510 1001 TQALLRKKEKEF---EETMDALQADIDQLEAEKAELKQRLNSQSKRTIE 1046
Cdd:COG1196  293 LLAELARLEQDIarlEERRRELEERLEELEEELAELEEELEELEEELEE 341
PHA03247 PHA03247
large tegument protein UL36; Provisional
 101-220 4.02e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 4.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   101 ADTTSPETPDSSASKVLkrEGTDTTAKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGVAGASSSLgPSGSASAGELSS 180
Cdd:PHA03247 2734 ALPAAPAPPAVPAGPAT--PGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESL-PSPWDPADPPAA 2810

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 13259510   181 SEPSTPAQTPLAAPIIPTPVLTSPGAVPPLPSPSKEEEGL 220
Cdd:PHA03247 2811 VLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSL 2850
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 283-436 6.61e-05

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 46.59  E-value: 6.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  283 AKEALEAKERYMEEMADTADAIEMATLDKEMAE------ERAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaas 356
Cdd:cd22656   82 AQNAGGTIDSYYAEILELIDDLADATDDEELEEakktikALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEK-------- 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  357 syQLKQLEEQNARLKDALvrMRDLSSSEKQEHVKLQKLMEKKNQEL------------------EVVRQQRERLQEELSQ 418
Cdd:cd22656  154 --DQTALETLEKALKDLL--TDEGGAIARKEIKDLQKELEKLNEEYaaklkakidelkaliaddEAKLAAALRLIADLTA 229

                        170
                 ....*....|....*...
gi 13259510  419 AESTIDELKEQVDAALGA 436
Cdd:cd22656  230 ADTDLDNLLALIGPAIPA 247
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 924-1037 1.06e-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: 46.98  E-value: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    924 VELRAAALRAEITDAEglgLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLE----------KKLDSAAKDADERIEK 993
Cdd:TIGR02169  376 VDKEFAETRDELKDYR---EKLEKLKREINELKRELDRLQEELQRLSEELADLNaaiagieakiNELEEEKEDKALEIKK 452

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 13259510    994 VQTRLEETQALLRKKEKEFEetmdALQADIDQLEAEKAELKQRL 1037
Cdd:TIGR02169  453 QEWKLEQLAADLSKYEQELY----DLKEEYDRVEKELSKLQREL 492
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
945-1035 2.14e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   945 LEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADE----RIEKVQTRLEETQALLRKKEKEFEETMDALQ 1020
Cdd:PRK03918  614 LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEeeyeELREEYLELSRELAGLRAELEELEKRREEIK 693

                          90
                  ....*....|....*
gi 13259510  1021 ADIDQLEAEKAELKQ 1035
Cdd:PRK03918  694 KTLEKLKEELEEREK 708
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 104-214 2.59e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 45.29  E-value: 2.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    104 TSPETPDSSASKVLKREGTDTT--AKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGVAGASSSLGPSGSASAGELSSS 181
Cdd:pfam05109  456 TNLTAPASTGPTVSTADVTSPTpaGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNAT 535

                           90       100       110
                   ....*....|....*....|....*....|...
gi 13259510    182 EPSTPAQTPLAAPIIPTPVLTSPGAVPPLPSPS 214
Cdd:pfam05109  536 SPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPN 568
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 944-1043 5.77e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 43.47  E-value: 5.77e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510     944 KLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERI-EKVQTRLEETQALLRKKEkEFEETMDALQAD 1022
Cdd:smart00787  162 LLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAkEKLKKLLQEIMIKVKKLE-ELEEELQELESK 240

                            90       100
                    ....*....|....*....|.
gi 13259510    1023 IDQLEAEKAELKQRLNSQSKR 1043
Cdd:smart00787  241 IEDLTNKKSELNTEIAEAEKK 261
half-pint TIGR01645
poly-U binding splicing factor, half-pint family; The proteins represented by this model ...
 100-316 9.40e-04

poly-U binding splicing factor, half-pint family; The proteins represented by this model contain three RNA recognition motifs (rrm: pfam00076) and have been characterized as poly-pyrimidine tract binding proteins associated with RNA splicing factors. In the case of PUF60 (GP|6176532), in complex with p54, and in the presence of U2AF, facilitates association of U2 snRNP with pre-mRNA.


Pssm-ID: 130706 [Multi-domain]  Cd Length: 612  Bit Score: 43.52  E-value: 9.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    100 GADTTSPETPDSSASKVLKREGTDTTAKT-SKLRGLKPKKAPTARKT-TTRRPKPTRPASTGVagassslgPSGSASAGE 177
Cdd:TIGR01645  325 GPRAQSPATPSSSLPTDIGNKAVVSSAKKeAEEVPPLPQAAPAVVKPgPMEIPTPVPPPGLAI--------PSLVAPPGL 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    178 LSssePSTPAQTPLAAPIIPTPVLTSPGAVPPLPS------PSKEEEGlRAQVRDLEEKLETLRLKRAEDKAKLKELEKH 251
Cdd:TIGR01645  397 VA---PTEINPSFLASPRKKMKREKLPVTFGALDDtlawkePSKEDQT-SEDGKMLAIMGEAAAALALEPKKKKKEKEGE 472

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13259510    252 KIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKER----YMEEMADTADAIEmaTLDKEMAEE 316
Cdd:TIGR01645  473 ELQPKLVMNSEDASLASQEGMSIRGNSARHLVMQKLMRTNRsnviVLRNMVTPQDIDE--FLEGEIREE 539
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 218-394 3.58e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 41.16  E-value: 3.58e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510     218 EGLRaqvRDLEEKLETLRlkraEDKAKLKElekhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKErymeem 297
Cdd:smart00787  143 EGLK---EGLDENLEGLK----EDYKLLMK------ELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDP------ 203

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510     298 adtadaiemATLDKemAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQNARLKDALVRM 377
Cdd:smart00787  204 ---------TELDR--AKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTN-------KKSELNTEIAEAEKKLEQC 265

                           170       180
                    ....*....|....*....|.
gi 13259510     378 RDLSSSE----KQEHVKLQKL 394
Cdd:smart00787  266 RGFTFKEieklKEQLKLLQSL 286
Prefoldin_4 cd23165
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic ...
 944-1037 9.88e-03

prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic prefoldin complex. Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467481 [Multi-domain]  Cd Length: 103  Bit Score: 37.14  E-value: 9.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  944 KLEDRETVIKELKKSLKIKGEELSEANVRLSLLekkldsaakDADERIEK------VQTRLEETQALLRKKEKEFEETMD 1017
Cdd:cd23165   10 RLNARLHELKEELKAKKKELENLEDASDELELA---------DDDEPVPYkigevfVHLSLEEAQERLEKAKEELEEEIE 80

                         90       100
                 ....*....|....*....|
gi 13259510 1018 ALQADIDQLEAEKAELKQRL 1037
Cdd:cd23165   81 KLEEEIDEIEEEMKELKVQL 100
 
Name Accession Description Interval E-value
Dynactin pfam12455
Dynein associated protein; This domain family is found in eukaryotes, and is approximately 280 ...
 527-805 3.99e-93

Dynein associated protein; This domain family is found in eukaryotes, and is approximately 280 amino acids in length. The family is found in association with pfam01302. There is a single completely conserved residue E that may be functionally important. Dynactin has been associated with Dynein, a kinesin protein which is involved in organelle transport, mitotic spindle assembly and chromosome segregation. Dynactin anchors Dynein to specific subcellular structures.


Pssm-ID: 463591  Cd Length: 287  Bit Score: 301.07  E-value: 3.99e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    527 LQDVNRELTNQQEASVERQQQPPPET-----FDFKIKFAETKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGg 601
Cdd:pfam12455    1 LQSDLEDLRASQQITESESEDLSSRSrammdLNLKLQSSASKAQAKAIDLELRRLEAQQASEHLEIVQLFLPDSFLRRG- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    602 DHDCVLVLLLMPRLICKAELIRKQAQEKFELSENcserPGLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDV 681
Cdd:pfam12455   80 DRDSVLALLLFKRLAFKADLLASQIREKFPLSES----LILKGHVEEQLFFACELLEKLTWLSALCDRFAAALRSCSVET 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    682 YKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPLTKAIKYYQHLYSIHLAEQPEDCTMQLADHIKFTQSALDCMS 761
Cdd:pfam12455  156 FLKIGGAYPELEPVERALDGWIDLLKRDELDENECAEELQRSIAYFSHLAEVHLADSLEDLADELLMRVLLLQSALDSIA 235

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 13259510    762 VEVGRLRAFLQGGQ--------EATDIALLLRDLETSCSDIRQFCKKIRRRM 805
Cdd:pfam12455  236 AALGRLKTLLQSGLpdpdggdeEASDLFELLQTLITQARSAKVISKKILRRL 287
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 29-94 1.04e-30

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 115.19  E-value: 1.04e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13259510     29 VGSRVEVIGkGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQI 94
Cdd:pfam01302    1 VGDRVEVPG-GRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 29-95 8.60e-29

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 109.98  E-value: 8.60e-29
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13259510      29 VGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEA-KGKNDGTVQGRKYFTCDEGHGIFVRQSQIQ 95
Cdd:smart01052    1 VGDRVEVGGGGRRGTVRYVGPTPFAPGVWVGVELDEPlRGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 220-540 5.69e-22

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: 103.21  E-value: 5.69e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    220 LRAQVRDLEEKLETLR--LKRAED-----KAKLKELEKHKIQLEQVQEWKSKMQEQQADLQ-RRLKEARKEAKEALEAKE 291
Cdd:TIGR02168  170 YKERRKETERKLERTRenLDRLEDilnelERQLKSLERQAEKAERYKELKAELRELELALLvLRLEELREELEELQEELK 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    292 RYMEEMADTADAIEMA-----TLDKEMAE--ERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLE 364
Cdd:TIGR02168  250 EAEEELEELTAELQELeekleELRLEVSEleEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    365 EQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALG----AEEMV 440
Cdd:TIGR02168  330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNeierLEARL 409

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    441 EMLTDRNLNLEEKVRELRETVGDLEaMNEMNDELQENARETElELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKY 520
Cdd:TIGR02168  410 ERLEDRRERLQQEIEELLKKLEEAE-LKELQAELEELEEELE-ELQEELERLEEALEELREELEEAEQALDAAERELAQL 487

                          330       340
                   ....*....|....*....|
gi 13259510    521 RQLTAHLQDVNRELTNQQEA 540
Cdd:TIGR02168  488 QARLDSLERLQENLEGFSEG 507
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 221-515 1.05e-21

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 102.32  E-value: 1.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  221 RAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADT 300
Cdd:COG1196  221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  301 ADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDL 380
Cdd:COG1196  301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  381 SSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmvemltdrnlNLEEKVRELRET 460
Cdd:COG1196  381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE----------EEEEALEEAAEE 450

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 13259510  461 VGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQ 515
Cdd:COG1196  451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 221-540 2.51e-21

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: 101.29  E-value: 2.51e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    221 RAQVRDLEEKLETLRLKRAEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADT 300
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRK---ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    301 ADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEekgsdgaASSYQLKQLEEQNARLKDALVRMRDL 380
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK-------ALREALDELRAELTLLNEEAANLRER 825

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    381 SSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAAL----GAEEMVEMLTDRNLNLEEKVRE 456
Cdd:TIGR02168  826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLneraSLEEALALLRSELEELSEELRE 905

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    457 LRETVGDLE-AMNEMNDEL-QENARETELELREQ-------------LDMAGARVREAQKRVEAAQETVAD--------- 512
Cdd:TIGR02168  906 LESKRSELRrELEELREKLaQLELRLEGLEVRIDnlqerlseeysltLEEAEALENKIEDDEEEARRRLKRlenkikelg 985

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 13259510    513 ---------YQQTIKKYRQLTAHLQDVNRELTNQQEA 540
Cdd:TIGR02168  986 pvnlaaieeYEELKERYDFLTAQKEDLTEAKETLEEA 1022
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 225-547 9.98e-21

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 99.24  E-value: 9.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  225 RDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQA--------DLQRRLKEARKEAKEALEAKERYMEE 296
Cdd:COG1196  182 EATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAellllklrELEAELEELEAELEELEAELEELEAE 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  297 MADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQNARLKDALVR 376
Cdd:COG1196  262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE-------RLEELEEELAELEEELEE 334

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  377 MRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEemvEMLTDRNLNLEEKVRE 456
Cdd:COG1196  335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA---AELAAQLEELEEAEEA 411

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  457 LRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTN 536
Cdd:COG1196  412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491

                        330
                 ....*....|.
gi 13259510  537 QQEASVERQQQ 547
Cdd:COG1196  492 RLLLLLEAEAD 502
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
221-488 1.03e-19

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 95.49  E-value: 1.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   221 RAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQewksKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADT 300
Cdd:PRK02224  474 RERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIE----RLEERREDLEELIAERRETIEEKRERAEELRERAAEL 549

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   301 ADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILK------AEIEEKGSDGAASSYQLKQLEEQNARLKDAL 374
Cdd:PRK02224  550 EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLErirtllAAIADAEDEIERLREKREALAELNDERRERL 629

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   375 vrmrdlssSEKQEHVKlqKLMEKKNQE-LEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEK 453
Cdd:PRK02224  630 --------AEKRERKR--ELEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRER 699

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 13259510   454 VRELRETVGDLEAMNEMNDELQENARETELELREQ 488
Cdd:PRK02224  700 REALENRVEALEALYDEAEELESMYGDLRAELRQR 734
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 218-547 1.13e-19

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 95.77  E-value: 1.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  218 EGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEwksKMQEQQADLQRRLKEARKEAKEALEAKERYMEEM 297
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE---ELELELEEAQAEEYELLAELARLEQDIARLEERR 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  298 ADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRM 377
Cdd:COG1196  312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  378 RDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmvEMLTDRNLNLEEKVREL 457
Cdd:COG1196  392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA--ELEEEEEALLELLAELL 469

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  458 RETVGDLEAMNEMNDELQENARETELELREQLDMAG--ARVREAQKRVEAA--QETVADYQQTIKKYRQ-----LTAHLQ 528
Cdd:COG1196  470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGflEGVKAALLLAGLRglAGAVAVLIGVEAAYEAaleaaLAAALQ 549

                        330
                 ....*....|....*....
gi 13259510  529 DVNRELTNQQEASVERQQQ 547
Cdd:COG1196  550 NIVVEDDEVAAAAIEYLKA 568
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 215-511 3.54e-19

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 93.85  E-value: 3.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  215 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYM 294
Cdd:COG1196  253 AELEELEAELAELEAELEELRLELEELELELEEAQA---EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  295 EEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDAL 374
Cdd:COG1196  330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  375 VRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKV 454
Cdd:COG1196  410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 13259510  455 RELRETvgDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVA 511
Cdd:COG1196  490 AARLLL--LLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL 544
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 215-504 5.25e-19

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: 93.59  E-value: 5.25e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    215 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEAR----KEAKEALEAK 290
Cdd:TIGR02169  730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA---RIEELEEDLHKLEEALNDLEARLSHSRipeiQAELSKLEEE 806

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    291 ERYMEEMADTADAIEMA-TLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNAR 369
Cdd:TIGR02169  807 VSRIEARLREIEQKLNRlTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    370 LKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmvemltdrnln 449
Cdd:TIGR02169  887 LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED----------- 955

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 13259510    450 LEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVE 504
Cdd:TIGR02169  956 VQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIE 1010
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
215-547 1.68e-18

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 91.64  E-value: 1.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   215 KEEEGLRAQVRDLEEKLETLRLKRAE--DKAKLKELEKhkiqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKER 292
Cdd:PRK02224  272 REREELAEEVRDLRERLEELEEERDDllAEAGLDDADA-----EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAES 346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   293 YMEEMADTADaiematlDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKD 372
Cdd:PRK02224  347 LREDADDLEE-------RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE 419

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   373 ALVRMRdlsSSEKQEHVKLQKLMEK--KNQEL----------------------EVVRQQRERLQEELSQAESTIDELKE 428
Cdd:PRK02224  420 ERDELR---EREAELEATLRTARERveEAEALleagkcpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEE 496

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   429 QVDAA---LGAEEMVEMLTDRNLNLEEKVRELRETVGD----LEAMNEMNDELQENARETE---LELREQLDMAGARV-- 496
Cdd:PRK02224  497 RLERAedlVEAEDRIERLEERREDLEELIAERRETIEEkrerAEELRERAAELEAEAEEKReaaAEAEEEAEEAREEVae 576

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13259510   497 -----------REAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 547
Cdd:PRK02224  577 lnsklaelkerIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRE 638
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
218-508 2.15e-18

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 91.25  E-value: 2.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   218 EGLRAQV-----RDLEEKLETLRLKRAEDKAKLKELEKHKIQLeqvqewkskmqeqqadlqrrlKEARKEAKEALEAKER 292
Cdd:PRK02224  190 DQLKAQIeekeeKDLHERLNGLESELAELDEEIERYEEQREQA---------------------RETRDEADEVLEEHEE 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   293 YMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKD 372
Cdd:PRK02224  249 RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   373 ALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgaeemvemltdrnlnLEE 452
Cdd:PRK02224  329 RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE-----------------LEE 391

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 13259510   453 KVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQE 508
Cdd:PRK02224  392 EIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA 447
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 215-534 2.44e-18

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: 91.27  E-value: 2.44e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    215 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQvqewksKMQEQQADLQRrLKEARKEAKEALEAKErym 294
Cdd:TIGR02168  740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA------EIEELEAQIEQ-LKEELKALREALDELR--- 809

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    295 EEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDAL 374
Cdd:TIGR02168  810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    375 VRMRD-LSSSEKQEHVKLQKLMEKKnQELEVVRQQRERLQEELSQAESTIDELKEQV-----DAALGAEEMVEMLTDRNL 448
Cdd:TIGR02168  890 ALLRSeLEELSEELRELESKRSELR-RELEELREKLAQLELRLEGLEVRIDNLQERLseeysLTLEEAEALENKIEDDEE 968

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    449 NLEEKVRELRETVGDLEAMNEMN-DELQE-NARETELEL-REQLDMAGARVREAQKRVEAaqETVADYQQTIKKYRQlta 525
Cdd:TIGR02168  969 EARRRLKRLENKIKELGPVNLAAiEEYEElKERYDFLTAqKEDLTEAKETLEEAIEEIDR--EARERFKDTFDQVNE--- 1043


                   ....*....
gi 13259510    526 HLQDVNREL 534
Cdd:TIGR02168 1044 NFQRVFPKL 1052
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
216-546 1.08e-16

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 85.86  E-value: 1.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   216 EEEGLRAQVRDLEEKLETLR----LKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKE 291
Cdd:PRK02224  308 DAEAVEARREELEDRDEELRdrleECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIE 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   292 RYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEE-----------------KGSDGA 354
Cdd:PRK02224  388 ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEaealleagkcpecgqpvEGSPHV 467

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   355 AS-----------SYQLKQLEEQNARLKDALVRMRDLSSSEKQehvkLQKLMEKKNQELEVVRQQRERLQEELSQAES-- 421
Cdd:PRK02224  468 ETieedrerveelEAELEDLEEEVEEVEERLERAEDLVEAEDR----IERLEERREDLEELIAERRETIEEKRERAEElr 543

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   422 --------------------------------TIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETvgdLEAMNE 469
Cdd:PRK02224  544 eraaeleaeaeekreaaaeaeeeaeeareevaELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREK---REALAE 620

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   470 MNDELQE---NARETELELREQLDmaGARVREAQ---KRVEAAQETVADYQQTIKKYR-QLTAHLQDVNRELTNQQEASV 542
Cdd:PRK02224  621 LNDERRErlaEKRERKRELEAEFD--EARIEEARedkERAEEYLEQVEEKLDELREERdDLQAEIGAVENELEELEELRE 698


                  ....
gi 13259510   543 ERQQ 546
Cdd:PRK02224  699 RREA 702
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 254-577 2.01e-16

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: 85.12  E-value: 2.01e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    254 QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALeakerymeemadtaDAIEMATLDKEMAEERAESLQQEVEALKERVD 333
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELS--------------QELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    334 ELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALvrmRDLSSSEKQEhvKLQKLMEKKNQELEVVRQQRERLQ 413
Cdd:TIGR02169  741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL---NDLEARLSHS--RIPEIQAELSKLEEEVSRIEARLR 815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    414 eELSQAESTIDELKEQvdaalgAEEMVEMLTDRNLNLEEKVRELRETVGDLEA-MNEMNDELQE-NARETELE-----LR 486
Cdd:TIGR02169  816 -EIEQKLNRLTLEKEY------LEKEIQELQEQRIDLKEQIKSIEKEIENLNGkKEELEEELEElEAALRDLEsrlgdLK 888

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    487 EQLDMAGARVREAQKRVEAAQETVADYQQTIKkyrQLTAHLQDVNRELTnQQEASVERQQQPPPETFDFKikfaETKAHA 566
Cdd:TIGR02169  889 KERDELEAQLRELERKIEELEAQIEKKRKRLS---ELKAKLEALEEELS-EIEDPKGEDEEIPEEELSLE----DVQAEL 960

                          330
                   ....*....|.
gi 13259510    567 KAIEMELRQME 577
Cdd:TIGR02169  961 QRVEEEIRALE 971
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 214-547 3.29e-16

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: 84.35  E-value: 3.29e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    214 SKEEEGLRAQVRDLEEKLETLRLKR-AEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEakeaLEAKER 292
Cdd:TIGR02169  197 RQQLERLRREREKAERYQALLKEKReYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR----LEEIEQ 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    293 YMEEMADTADAI---EMATLDKEMAEERAE--SLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSyqlKQLEEQN 367
Cdd:TIGR02169  273 LLEELNKKIKDLgeeEQLRVKEKIGELEAEiaSLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE---REIEEER 349

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    368 ARlKDALvrMRDLSSSEKQEHVKLQKLME--KKNQELevvRQQRERLQEELSQAESTIDELKEQVDAalgaeemvemLTD 445
Cdd:TIGR02169  350 KR-RDKL--TEEYAELKEELEDLRAELEEvdKEFAET---RDELKDYREKLEKLKREINELKRELDR----------LQE 413

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    446 RNLNLEEKVRELRETVGDLEamnemndelqenARETELElrEQLDMAGARVREAQKRVEAAQETVADYQQtikKYRQLTA 525
Cdd:TIGR02169  414 ELQRLSEELADLNAAIAGIE------------AKINELE--EEKEDKALEIKKQEWKLEQLAADLSKYEQ---ELYDLKE 476

                          330       340
                   ....*....|....*....|....
gi 13259510    526 HLQDVNRELTNQQE--ASVERQQQ 547
Cdd:TIGR02169  477 EYDRVEKELSKLQRelAEAEAQAR 500
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 215-457 7.88e-15

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: 80.10  E-value: 7.88e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    215 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEkhkiqleqvqewkskmqEQQADLQRRLKEARKEAKEALEAKERYM 294
Cdd:TIGR02168  288 KELYALANEISRLEQQKQILRERLANLERQLEELE-----------------AQLEELESKLDELAEELAELEEKLEELK 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    295 EEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDAL 374
Cdd:TIGR02168  351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    375 VRMRDLSSSEKQEhvKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKV 454
Cdd:TIGR02168  431 EEAELKELQAELE--ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV 508


                   ...
gi 13259510    455 REL 457
Cdd:TIGR02168  509 KAL 511
PTZ00121 PTZ00121
MAEBL; Provisional
 215-577 3.87e-14

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 77.87  E-value: 3.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   215 KEEEGLRA-QVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQqadlQRRLKEARKEAKEALEAKERY 293
Cdd:PTZ00121 1273 KAEEARKAdELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA----KKKADAAKKKAEEAKKAAEAA 1348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   294 MEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEI-LKAEIEEKGSDgaassyQLKQLEEQNARLKD 372
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAkKKAEEDKKKAD------ELKKAAAAKKKADE 1422

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   373 ALVRMRDLsssEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEST--IDELKEQVDAALGAEEMVEMLTDRNLNL 450
Cdd:PTZ00121 1423 AKKKAEEK---KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAkkADEAKKKAEEAKKADEAKKKAEEAKKKA 1499

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   451 EE--KVRELRETVGDLEAMNEMN--DELQ--ENARETElELREQLDMAGA-RVREAQKRVEAAQETVADYQQTIKKYRQL 523
Cdd:PTZ00121 1500 DEakKAAEAKKKADEAKKAEEAKkaDEAKkaEEAKKAD-EAKKAEEKKKAdELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 13259510   524 TAHLQDVNRELtnqQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQME 577
Cdd:PTZ00121 1579 ALRKAEEAKKA---EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
PTZ00121 PTZ00121
MAEBL; Provisional
 214-519 4.43e-14

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 77.87  E-value: 4.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   214 SKEEEGLRAQVRDLEEKLETLRlKRAEDKAKLKELEKHKiQLEQVQEWKSKMQEQQADLQRRLKEARKeAKEALEAKERY 293
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAK-KAAEAKKKADEAKKAE-EAKKADEAKKAEEAKKADEAKKAEEKKK-ADELKKAEELK 1558

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   294 MEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQnaRLKDA 373
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE--KKKVE 1636

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   374 LVRMRDLSSSEKQEHVKLQKLMEK-KNQELEVVRQQRERLQEELSQAES----TIDELKEQVDAALGAEEMVEMLTDRNL 448
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKiKAAEEAKKAEEDKKKAEEAKKAEEdekkAAEALKKEAEEAKKAEELKKKEAEEKK 1716

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13259510   449 NLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKK 519
Cdd:PTZ00121 1717 KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 27-425 1.01e-13

Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227569 [Multi-domain]  Cd Length: 669  Bit Score: 75.88  E-value: 1.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   27 LRVGSRVEVIGKghRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRqsqiqvfedgadttsp 106
Cdd:COG5244    4 LSVNDRVLLGDK--FGTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIFIR---------------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  107 etPDSSAskVLKRegtdtTAKTSKLRGLKPKKAPTARKTTTRRPKPTRpastgvagassslgpsgsasagELSSSEPStp 186
Cdd:COG5244   66 --PDDDS--LLNG-----NAAYEKIKGGLVCESKGMDKDGEIKQENHE----------------------DRIHFEES-- 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  187 aqtpLAAPIIPTPVLTSPGAVPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIqLEQVQEWKSKMQ 266
Cdd:COG5244  113 ----KIRRLEETIEALKSTEKEEIVELRRENEELDKINLSLRERISSEEPELNKDGSKLSYDELKEF-VEESRVQVYDMV 187

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  267 EQQADLQRRLKEARKEAKEALEAKERymeemadtadaiematldkemaeeraeslqqevealKERVDELTTDLEILKAEI 346
Cdd:COG5244  188 ELVSDISETLNRNGSIQRSSVRECER------------------------------------SNIHDVLFLVNGILDGVI 231

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  347 EEKGsdgaassyqlKQLEeqnaRLKDALVRMRDLSSSEKQEHVKLQKLMEK-KNQELEVVRQQRERLQEELSQAESTIDE 425
Cdd:COG5244  232 DELN----------GELE----RLRRQLVSLMSSHGIEVEENSRLKATLEKfQSLELKVNTLQEELYQNKLLKKFYQIYE 297
PTZ00121 PTZ00121
MAEBL; Provisional
 215-580 2.06e-13

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 75.56  E-value: 2.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   215 KEEEGLRAQV--RDLEE--KLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQE-QQADlqrRLKEARKEAKEALEA 289
Cdd:PTZ00121 1373 KEEAKKKADAakKKAEEkkKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEkKKAD---EAKKKAEEAKKADEA 1449

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   290 KE-----RYMEEMADTADAIEMATLDKEMAEE--RAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQ 362
Cdd:PTZ00121 1450 KKkaeeaKKAEEAKKKAEEAKKADEAKKKAEEakKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK 1529

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   363 LEEqnARLKDALVRMRDLSSSE---KQEHVK----LQKLMEKKNQELEvvRQQRERLQEELSQAEST---------IDEL 426
Cdd:PTZ00121 1530 AEE--AKKADEAKKAEEKKKADelkKAEELKkaeeKKKAEEAKKAEED--KNMALRKAEEAKKAEEArieevmklyEEEK 1605

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   427 KEQVDAALGAEEmvEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLdmagARVREAQKRveAA 506
Cdd:PTZ00121 1606 KMKAEEAKKAEE--AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE----AKKAEEDKK--KA 1677

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13259510   507 QETVADYQQTIKKYRQLTAHLQDVNR--ELTNQQEASVERQQQPPPETFDFKIKFAETKAHAkaiEMELRQMEVAQ 580
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKaeELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEA---EEDKKKAEEAK 1750
PTZ00121 PTZ00121
MAEBL; Provisional
 215-580 2.74e-13

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 75.18  E-value: 2.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   215 KEEEGLRAQ-VRDLEEKLETLRLKRAEDKAKLKELEKHKiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERY 293
Cdd:PTZ00121 1171 KAEDAKKAEaARKAEEVRKAEELRKAEDARKAEAARKAE-EERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEER 1249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   294 MEEMADTADAIEMATLDKEMAEERAESLQQEVEALK----ERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNAR 369
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKaeekKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK 1329

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   370 LKDALVRMRDlsSSEKQEHVKlQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmvemLTDRNLN 449
Cdd:PTZ00121 1330 KADAAKKKAE--EAKKAAEAA-KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE----AKKKAEE 1402

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   450 LEEKVRELRETvgdlEAMNEMNDELQENAREtelelREQLDMAGARVREAQKRVEAAQEtvADYQQTIKKYRQLTAHLQD 529
Cdd:PTZ00121 1403 DKKKADELKKA----AAAKKKADEAKKKAEE-----KKKADEAKKKAEEAKKADEAKKK--AEEAKKAEEAKKKAEEAKK 1471

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 13259510   530 VNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQMEVAQ 580
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
PTZ00121 PTZ00121
MAEBL; Provisional
 215-583 4.44e-13

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 74.41  E-value: 4.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   215 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRrLKEARKEAKEALEAKE--- 291
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKkae 1428

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   292 --RYMEEMADTADAIEMATLDKEMAEE--RAESLQQEVEAlKERVDELTTDLEILKA--EIEEKGSDGAASSYQLKQLEE 365
Cdd:PTZ00121 1429 ekKKADEAKKKAEEAKKADEAKKKAEEakKAEEAKKKAEE-AKKADEAKKKAEEAKKadEAKKKAEEAKKKADEAKKAAE 1507

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   366 QNARLKDAlvrmrdLSSSEKQEHVKLQKLMEKKNQElEVVRQQRERLQEELSQAESTID-ELKEQVDAALGAEEMVEMLT 444
Cdd:PTZ00121 1508 AKKKADEA------KKAEEAKKADEAKKAEEAKKAD-EAKKAEEKKKADELKKAEELKKaEEKKKAEEAKKAEEDKNMAL 1580

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   445 DRNLNL----EEKVRELRETVGDLEAMNEMNDELQENARETELELR---------EQLDMAGA-RVREAQKRVEAAQETV 510
Cdd:PTZ00121 1581 RKAEEAkkaeEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKkaeeekkkvEQLKKKEAeEKKKAEELKKAEEENK 1660

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13259510   511 ADYQQTIKKYRQLTAHLQDVNRELTNQQEA--SVERQQQPPPETFDFKIKFAETKAHAKAI--EMELRQMEVAQANR 583
Cdd:PTZ00121 1661 IKAAEEAKKAEEDKKKAEEAKKAEEDEKKAaeALKKEAEEAKKAEELKKKEAEEKKKAEELkkAEEENKIKAEEAKK 1737
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 214-581 4.92e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.82  E-value: 4.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  214 SKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKI----QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEA 289
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEeaeaELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  290 KERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNAR 369
Cdd:COG1196  395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  370 LKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVR-QQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNL 448
Cdd:COG1196  475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKaALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE 554

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  449 NLEE---------KVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKK 519
Cdd:COG1196  555 DDEVaaaaieylkAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13259510  520 YRQLTAHLQDVNRELTNQQEASVERQQqpppETFDFKIKFAETKAHAKAIEMELRQMEVAQA 581
Cdd:COG1196  635 ALRRAVTLAGRLREVTLEGEGGSAGGS----LTGGSRRELLAALLEAEAELEELAERLAEEE 692
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
214-504 5.14e-13

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 73.94  E-value: 5.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   214 SKEEEGLRAQVRDLEEKLETLrlkrAEDKAKLKELEKHKIQLEqvqEWKSKMQEQQADLQRRLKEARKEAKEALEAKERY 293
Cdd:PRK03918  524 AEEYEKLKEKLIKLKGEIKSL----KKELEKLEELKKKLAELE---KKLDELEEELAELLKELEELGFESVEELEERLKE 596

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   294 MEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyqlkqleeqnarlkda 373
Cdd:PRK03918  597 LEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK---------------------- 654

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   374 lvrmrdlsSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTdrnlNLEEK 453
Cdd:PRK03918  655 --------KYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLE----KALER 722

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 13259510   454 VRELRETVGDLEAMNEMN--DELQENARETELELREQlDMAGARVREAQKRVE 504
Cdd:PRK03918  723 VEELREKVKKYKALLKERalSKVGEIASEIFEELTEG-KYSGVRVKAEENKVK 774
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
220-588 5.96e-13

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 73.26  E-value: 5.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  220 LRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKmQEQQADLQRRLKEARKEA---KEALEAKERYMEE 296
Cdd:COG4717   93 LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL-EAELAELPERLEELEERLeelRELEEELEELEAE 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  297 MADTADAIEMA-TLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIE------EKGSDGAASSYQLKQLEEQNAR 369
Cdd:COG4717  172 LAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEeleeelEQLENELEAAALEERLKEARLL 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  370 LKDA----LVRMRDLSSSEKQEHVK---------LQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVdAALGA 436
Cdd:COG4717  252 LLIAaallALLGLGGSLLSLILTIAgvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELL-AALGL 330

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  437 EEMVEmltdrNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELElrEQLDMAGARVREA-QKRVEAAQEtvadyqq 515
Cdd:COG4717  331 PPDLS-----PEELLELLDRIEELQELLREAEELEEELQLEELEQEIA--ALLAEAGVEDEEElRAALEQAEE------- 396

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13259510  516 tikkYRQLTAHLQDVNRELTNQQEASVERQQQPPPEtfDFKIKFAETKAHAKAIEMELRQM--EVAQANRHMSLL 588
Cdd:COG4717  397 ----YQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELreELAELEAELEQL 465
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
215-539 7.80e-13

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 73.17  E-value: 7.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   215 KEEEGLRAQVRDLEEKLETLR-----LKRAEDKA-----------KLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKE 278
Cdd:PRK03918  405 EEISKITARIGELKKEIKELKkaieeLKKAKGKCpvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE 484

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   279 ARKEAKEalEAKERYMEEMADTADAIE--MATLDKEMAEERAEslqqEVEALKERVDELTTDLEILKAEIEEKG---SDG 353
Cdd:PRK03918  485 LEKVLKK--ESELIKLKELAEQLKELEekLKKYNLEELEKKAE----EYEKLKEKLIKLKGEIKSLKKELEKLEelkKKL 558

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   354 AASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAA 433
Cdd:PRK03918  559 AELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAET 638

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   434 LGAEEMvemltdrnlnLEEKVRELREtvgdleamnEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADY 513
Cdd:PRK03918  639 EKRLEE----------LRKELEELEK---------KYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699

                         330       340
                  ....*....|....*....|....*.
gi 13259510   514 QQTIKKYRQLTAHLQDVNRELTNQQE 539
Cdd:PRK03918  700 KEELEEREKAKKELEKLEKALERVEE 725
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 201-433 1.86e-12

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: 70.56  E-value: 1.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  201 LTSPGAVPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEAR 280
Cdd:COG4942   13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER---RIAALARRIRALEQELAALEAELAELE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  281 KEAKEALEAKERYMEEMADTADAIEMATLDKEM-----------AEERAESLQQEVEALKERVDELTTDLEILKAEIEEK 349
Cdd:COG4942   90 KEIAELRAELEAQKEELAELLRALYRLGRQPPLalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  350 gsdgaasSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQ 429
Cdd:COG4942  170 -------EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242


                 ....
gi 13259510  430 VDAA 433
Cdd:COG4942  243 TPAA 246
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
215-580 2.70e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 71.63  E-value: 2.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   215 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSK-------MQEQQADLQRRLKEARKEAKEaL 287
Cdd:PRK03918  200 KELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESlegskrkLEEKIRELEERIEELKKEIEE-L 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   288 EAKERYMEEMADTADaiEMATLDKEMA---------EERAESLQQEVEALKERVDELTTDLEILKaEIEEKGSDGAASSY 358
Cdd:PRK03918  279 EEKVKELKELKEKAE--EYIKLSEFYEeyldelreiEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLE 355

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   359 QLKQLEEQNARLKDALVRMRDLSSSEKQEHV-KLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGA- 436
Cdd:PRK03918  356 ELEERHELYEEAKAKKEELERLKKRLTGLTPeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAk 435

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   437 -----------------------------EEMVEMLTDRN-------------LNLEEKVRELRETVGDLEAMNEM---- 470
Cdd:PRK03918  436 gkcpvcgrelteehrkelleeytaelkriEKELKEIEEKErklrkelrelekvLKKESELIKLKELAEQLKELEEKlkky 515

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   471 -NDELQENARETElELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPP 549
Cdd:PRK03918  516 nLEELEKKAEEYE-KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERL 594

                         410       420       430
                  ....*....|....*....|....*....|.
gi 13259510   550 PETFDFKIKFAETKAHAKAIEMELRQMEVAQ 580
Cdd:PRK03918  595 KELEPFYNEYLELKDAEKELEREEKELKKLE 625
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
223-540 3.28e-12

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 70.95  E-value: 3.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  223 QVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEakerymEEMADTAD 302
Cdd:COG4717  126 QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE------EELQDLAE 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  303 AIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAE--IEEKG------------------------------ 350
Cdd:COG4717  200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerLKEARlllliaaallallglggsllsliltiagvl 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  351 -------SDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKL-MEKKNQELEVVRQQRERLQEELSQAEST 422
Cdd:COG4717  280 flvlgllALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLpPDLSPEELLELLDRIEELQELLREAEEL 359

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  423 IDELK----EQVDAALGAEEMVEMLTD--RNLNLEEKVRELRETVGDLEAM--NEMNDELQENARETELELREQLDMAGA 494
Cdd:COG4717  360 EEELQleelEQEIAALLAEAGVEDEEElrAALEQAEEYQELKEELEELEEQleELLGELEELLEALDEEELEEELEELEE 439

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 13259510  495 RVREAQKRVEAAQETVADYQQTIKK------YRQLTAHLQDVNRELTNQQEA 540
Cdd:COG4717  440 ELEELEEELEELREELAELEAELEQleedgeLAELLQELEELKAELRELAEE 491
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
223-504 8.08e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 70.09  E-value: 8.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   223 QVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARK---EAKEALEAKERYMEEMAD 299
Cdd:PRK03918  156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSelpELREELEKLEKEVKELEE 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   300 TADAIEMAtldkemaEERAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaassyqlkqLEEQNARLKDAlvrmrd 379
Cdd:PRK03918  236 LKEEIEEL-------EKELESLEGSKRKLEEKIRELEERIEELKKEIEE--------------LEEKVKELKEL------ 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   380 lsSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRE 459
Cdd:PRK03918  289 --KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEE 366

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 13259510   460 TVGDLEAMNEMNDELQ-----------ENARETELELREQLDMAGARVREAQKRVE 504
Cdd:PRK03918  367 AKAKKEELERLKKRLTgltpeklekelEELEKAKEEIEEEISKITARIGELKKEIK 422
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
295-550 2.54e-11

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 68.12  E-value: 2.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  295 EEMADTADAI------EMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYqLKQLEEQNA 368
Cdd:COG3206  148 ELAAAVANALaeayleQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLL-LQQLSELES 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  369 RLKDALVRMRDLSSSEKQehvkLQKLMEKKNQELEVVRQQRE--RLQEELSQAESTIDELKEQvdaalgaeemvemLTDR 446
Cdd:COG3206  227 QLAEARAELAEAEARLAA----LRAQLGSGPDALPELLQSPViqQLRAQLAELEAELAELSAR-------------YTPN 289

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  447 NlnleEKVRELRETVGDLEAmnemndELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAH 526
Cdd:COG3206  290 H----PDVIALRAQIAALRA------QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359

                        250       260
                 ....*....|....*....|....*....
gi 13259510  527 LqDVNRE-----LTNQQEASVERQQQPPP 550
Cdd:COG3206  360 V-EVARElyeslLQRLEEARLAEALTVGN 387
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
242-490 6.50e-11

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 67.25  E-value: 6.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  242 KAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARkEAKEALEAKERYMEEMADTADAI-EMATLDKEMAEERAES 320
Cdd:COG4913  609 RAKLAALEA---ELAELEEELAEAEERLEALEAELDALQ-ERREALQRLAEYSWDEIDVASAErEIAELEAELERLDASS 684

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  321 lqQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHvkLQKLMEKKNQ 400
Cdd:COG4913  685 --DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEERFAAALG 760

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  401 ElEVVRQQRERLQEELSQAESTIDELKEQVDAAL-------------------GAEEMVEMLTD-RNLNLEEKVRELRET 460
Cdd:COG4913  761 D-AVERELRENLEERIDALRARLNRAEEELERAMrafnrewpaetadldadleSLPEYLALLDRlEEDGLPEYEERFKEL 839

                        250       260       270
                 ....*....|....*....|....*....|
gi 13259510  461 VgdLEAMNEMNDELQENARETELELREQLD 490
Cdd:COG4913  840 L--NENSIEFVADLLSKLRRAIREIKERID 867
PTZ00121 PTZ00121
MAEBL; Provisional
 215-504 1.02e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 66.70  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   215 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLK--EARK--EAKEALEAK 290
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaeELKKaeEEKKKVEQL 1638

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   291 ERYMEEMADTADAIEMAtldKEMAEERAESLQQEVEALKERVDELTTDLE--ILKAEIEEKGSDGAASSYQLKQLEEQNA 368
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKA---EEENKIKAAEEAKKAEEDKKKAEEAKKAEEdeKKAAEALKKEAEEAKKAEELKKKEAEEK 1715

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   369 RLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALgAEEMVEMLTDRNL 448
Cdd:PTZ00121 1716 KKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI-EEELDEEDEKRRM 1794

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 13259510   449 NLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVE 504
Cdd:PTZ00121 1795 EVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFE 1850
PTZ00121 PTZ00121
MAEBL; Provisional
 215-587 1.11e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 66.70  E-value: 1.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   215 KEEEGLRAQ-VRDLEE--KLETLRLKR-AEDKAKLKELEKHKI-QLEQVQEWKSKMQEQQADLQRRLKEARK---EAKEA 286
Cdd:PTZ00121 1238 DAEEAKKAEeERNNEEirKFEEARMAHfARRQAAIKAEEARKAdELKKAEEKKKADEAKKAEEKKKADEAKKkaeEAKKA 1317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   287 LEAKERyMEEMADTADAI----EMATLDKEMAEERAESLQQEVEALKER--VDELTTDLEILKAEIEEKGSDGAASSYQL 360
Cdd:PTZ00121 1318 DEAKKK-AEEAKKKADAAkkkaEEAKKAAEAAKAEAEAAADEAEAAEEKaeAAEKKKEEAKKKADAAKKKAEEKKKADEA 1396

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   361 KQLEEQNARlkdalvrmrdlssseKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEST--IDELKEQVDAALGAEE 438
Cdd:PTZ00121 1397 KKKAEEDKK---------------KADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAkkADEAKKKAEEAKKAEE 1461

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   439 MVEMLTDRnlnleEKVRELRETVGDLEAMNEMNDELQENARETElELREQLDmAGARVREAQKRVEAAQETVADYQQTIK 518
Cdd:PTZ00121 1462 AKKKAEEA-----KKADEAKKKAEEAKKADEAKKKAEEAKKKAD-EAKKAAE-AKKKADEAKKAEEAKKADEAKKAEEAK 1534

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   519 KYRQL-TAHLQDVNRELTNQQEASVERQQQPPPEtfdfKIKFAETKAHAKAIEMELRQMEVAQANRHMSL 587
Cdd:PTZ00121 1535 KADEAkKAEEKKKADELKKAEELKKAEEKKKAEE----AKKAEEDKNMALRKAEEAKKAEEARIEEVMKL 1600
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 225-577 1.65e-10

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 65.76  E-value: 1.65e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    225 RDLEEKLETLRLKRAEDKAKLKELEKHKIQLEqvqewKSKMQEQQAdlQRRLKEarKEAKEALEAKERYMEEMADTADAI 304
Cdd:pfam02463  169 RKKKEALKKLIEETENLAELIIDLEELKLQEL-----KLKEQAKKA--LEYYQL--KEKLELEEEYLLYLDYLKLNEERI 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    305 EMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQnarlKDALVRMRDLSSSE 384
Cdd:pfam02463  240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE----LLKLERRKVDDEEK 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    385 KQEHvklQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDL 464
Cdd:pfam02463  316 LKES---EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    465 EAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVER 544
Cdd:pfam02463  393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472

                          330       340       350
                   ....*....|....*....|....*....|...
gi 13259510    545 QQQpppETFDFKIKFAETKAHAKAIEMELRQME 577
Cdd:pfam02463  473 LLK---ETQLVKLQEQLELLLSRQKLEERSQKE 502
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
223-545 1.95e-10

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 63.39  E-value: 1.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  223 QVRDLEEKLETLRLKRAEDKAKLKELEKHKIQL-EQVQEWKSKMQEqqadLQRRLKEARKEAKEALEAKERYMEEMADta 301
Cdd:COG1340    2 KTDELSSSLEELEEKIEELREEIEELKEKRDELnEELKELAEKRDE----LNAQVKELREEAQELREKRDELNEKVKE-- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  302 daiematldkemaeeraesLQQEVEALKERVDELTTDLEILKAEIEEKGSDGaassYQLKQLEEQNARLKDALVRmRDLS 381
Cdd:COG1340   76 -------------------LKEERDELNEKLNELREELDELRKELAELNKAG----GSIDKLRKEIERLEWRQQT-EVLS 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  382 SSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQaestIDELKEQVDAalgaeemvemltdrnlnLEEKVRELRetv 461
Cdd:COG1340  132 PEEEKELVEKIKELEKELEKAKKALEKNEKLKELRAE----LKELRKEAEE-----------------IHKKIKELA--- 187

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  462 gdlEAMNEMNDELQENARETElELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYR-QLTAHLQDVNRELTNQQEA 540
Cdd:COG1340  188 ---EEAQELHEEMIELYKEAD-ELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRkELKKLRKKQRALKREKEKE 263


                 ....*
gi 13259510  541 SVERQ 545
Cdd:COG1340  264 ELEEK 268
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 220-545 2.61e-10

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: 65.04  E-value: 2.61e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    220 LRAQVRDLEEKLETLRLKRAEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMAD 299
Cdd:TIGR04523  312 LKSELKNQEKKLEEIQNQISQNNKIISQLNE---QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN 388

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    300 TADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQNARLKDALVRMRD 379
Cdd:TIGR04523  389 LESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS-------EIKDLTNQDSVKELIIKNLDN 461

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    380 LSSSEKQ-------EHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALgaeEMVEMLTDRNLNLEE 452
Cdd:TIGR04523  462 TRESLETqlkvlsrSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLK---EKIEKLESEKKEKES 538

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    453 KVRELRETVgdleamNEMNDELQENARETE-LELREQLDmagaRVREAQKRVEAAQETVadyQQTIKKYrqlTAHLQDVN 531
Cdd:TIGR04523  539 KISDLEDEL------NKDDFELKKENLEKEiDEKNKEIE----ELKQTQKSLKKKQEEK---QELIDQK---EKEKKDLI 602

                          330
                   ....*....|....*.
gi 13259510    532 RELTN--QQEASVERQ 545
Cdd:TIGR04523  603 KEIEEkeKKISSLEKE 618
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 215-483 4.17e-10

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 64.09  E-value: 4.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   215 KEEEGLRAQVRDLEEKLETLRLKRAEDKakLKELEKhKI-----QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEA 289
Cdd:PRK04778  256 KEIQDLKEQIDENLALLEELDLDEAEEK--NEEIQE-RIdqlydILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEE 332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   290 KERYMEEMADTADAIEmatldkemaeeRAESLQQEVEALKERVDELTTDLE-------ILKAEIEEkgsdgaaSSYQLKQ 362
Cdd:PRK04778  333 IDRVKQSYTLNESELE-----------SVRQLEKQLESLEKQYDEITERIAeqeiaysELQEELEE-------ILKQLEE 394

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   363 LEEQNARLKDALVRMRdlssseKQEHVKLQKLMEKKNQELEVVRQ-QRERL----QEELSQAESTIDELkeqvdaalgaE 437
Cdd:PRK04778  395 IEKEQEKLSEMLQGLR------KDELEAREKLERYRNKLHEIKRYlEKSNLpglpEDYLEMFFEVSDEI----------E 458

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 13259510   438 EMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETEL 483
Cdd:PRK04778  459 ALAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVENATLTEQ 504
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 212-520 5.07e-10

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: 63.89  E-value: 5.07e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    212 SPSKEEEGLRAQVRDLEEKLEtlrlkRAEDKAKLKElekhkIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEaLEAKe 291
Cdd:TIGR04523  381 SYKQEIKNLESQINDLESKIQ-----NQEKLNQQKD-----EQIKKLQQEKELLEKEIERLKETIIKNNSEIKD-LTNQ- 448

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    292 rymeemaDTADAIEMATLDKemaeeRAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLK 371
Cdd:TIGR04523  449 -------DSVKELIIKNLDN-----TRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLT 516

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    372 D----ALVRMRDLSSSEKQEHVKLQKL---MEKKNQELevvrqQRERLQEELSQAESTIDELKEQVDAALGA----EEMV 440
Cdd:TIGR04523  517 KkissLKEKIEKLESEKKEKESKISDLedeLNKDDFEL-----KKENLEKEIDEKNKEIEELKQTQKSLKKKqeekQELI 591

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    441 EMLTDRNLNL-------EEKVRELRETVGDLEAMNE------MNDELQENARETELEL-REQLDMAGARVREAQKRVEAA 506
Cdd:TIGR04523  592 DQKEKEKKDLikeieekEKKISSLEKELEKAKKENEklssiiKNIKSKKNKLKQEVKQiKETIKEIRNKWPEIIKKIKES 671

                          330
                   ....*....|....
gi 13259510    507 QETVADYQQTIKKY 520
Cdd:TIGR04523  672 KTKIDDIIELMKDW 685
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 216-1035 1.46e-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: 62.78  E-value: 1.46e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    216 EEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEqqadlqRRLKEARKEAKEALEAKERYME 295
Cdd:TIGR02169  171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKRE------YEGYELLKEKEALERQKEAIER 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    296 EMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELT--------TDLEILKAEIEEKGSDGAASSYQLKQLEEQN 367
Cdd:TIGR02169  245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGeeeqlrvkEKIGELEAEIASLERSIAEKERELEDAEERL 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    368 ARLK----DALVRMRDLSSSEKQEHVKLQKLMEkknqELEVVRQQRERLQEELSQAESTIDELKEQVDAAlgaEEMVEML 443
Cdd:TIGR02169  325 AKLEaeidKLLAEIEELEREIEEERKRRDKLTE----EYAELKEELEDLRAELEEVDKEFAETRDELKDY---REKLEKL 397

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    444 TDRNLNLEEKVRELRETVGDL-EAMNEMNDELqENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQtikKYRQ 522
Cdd:TIGR02169  398 KREINELKRELDRLQEELQRLsEELADLNAAI-AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ---ELYD 473

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    523 LTAHLQDVNRELTNQQE--ASVE-RQQQPPPETFDFKIKFAETKAHAKAIEMELRQM-----------EVAQANRHMSLL 588
Cdd:TIGR02169  474 LKEEYDRVEKELSKLQRelAEAEaQARASEERVRGGRAVEEVLKASIQGVHGTVAQLgsvgeryataiEVAAGNRLNNVV 553

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    589 TafmpdsflrpggDHDCV---LVLLLMPRLICKAELI--RKQAQEKFELSencseRPGLRGAAGEQLS-------FAAGL 656
Cdd:TIGR02169  554 V------------EDDAVakeAIELLKRRKAGRATFLplNKMRDERRDLS-----ILSEDGVIGFAVDlvefdpkYEPAF 616

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    657 VYSL-------SLLQATLHRYEHALSQCSVDVYKKVGSlypeMSAHERSLDFLIellhKDQLDETVNVEPLTKAIKYYQH 729
Cdd:TIGR02169  617 KYVFgdtlvveDIEAARRLMGKYRMVTLEGELFEKSGA----MTGGSRAPRGGI----LFSRSEPAELQRLRERLEGLKR 688

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    730 LYSIHLAEQPEdctmqLADHIKFTQSALDCMSVEVGRLRAflqggqeatDIALLLRDLETSCSDIRQFCKKIRrrmpgtd 809
Cdd:TIGR02169  689 ELSSLQSELRR-----IENRLDELSQELSDASRKIGEIEK---------EIEQLEQEEEKLKERLEELEEDLS------- 747

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    810 apgipaalafgpQVSDTLLDCRKHLTWVVAVLQEvaaaaaqliaplaeneglLVAALEELAfKASEQIYGTPSSSPYECL 889
Cdd:TIGR02169  748 ------------SLEQEIENVKSELKELEARIEE------------------LEEDLHKLE-EALNDLEARLSHSRIPEI 796

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    890 RQSCNILISTMNKLATAMQEGEYDAERppskpppVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEA 969
Cdd:TIGR02169  797 QAELSKLEEEVSRIEARLREIEQKLNR-------LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869

                          810       820       830       840       850       860
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13259510    970 NVRLSLLEKKLDSAAKDADERIEKVQTRLEETQALLRKKEKEFEETMDALQADIDQLEAEKAELKQ 1035
Cdd:TIGR02169  870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
255-496 2.16e-09

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 61.96  E-value: 2.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  255 LEQVQEWKSKMQEQQAD-LQRRLKEARKEAKEALEAKERYMEEMadtadAIEMATLDKEMAEERAESLQQEVEALKERVD 333
Cdd:COG3206  162 LEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQKN-----GLVDLSEEAKLLLQQLSELESQLAEARAELA 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  334 ELTTDLEILKAEIEEkGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLmekkNQELEVVRQQ-RERL 412
Cdd:COG3206  237 EAEARLAALRAQLGS-GPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIAL----RAQIAALRAQlQQEA 311

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  413 QEELSQAESTIDELKEQVDAalgAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQenARETELELREQLDMA 492
Cdd:COG3206  312 QRILASLEAELEALQAREAS---LQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLL--QRLEEARLAEALTVG 386


                 ....
gi 13259510  493 GARV 496
Cdd:COG3206  387 NVRV 390
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 223-558 2.30e-09

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 61.68  E-value: 2.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    223 QVRDLEEKLETLRLkRAEDKAKLKELEKHKiQLEQVQEWKSKMQEQQADL---QRRLKEARKEAKE--ALEAKERYMEEM 297
Cdd:pfam17380  288 QQQEKFEKMEQERL-RQEKEEKAREVERRR-KLEEAEKARQAEMDRQAAIyaeQERMAMERERELEriRQEERKRELERI 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    298 ADTADAIEMATLdKEMaeeraESLQQEVEALKERVdelttdleilKAEIEekgsdgAASSYQLKQlEEQNARLKDALVRM 377
Cdd:pfam17380  366 RQEEIAMEISRM-REL-----ERLQMERQQKNERV----------RQELE------AARKVKILE-EERQRKIQQQKVEM 422

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    378 RDL-SSSEKQEHVKLQKLMEKKNQELEVVR-------QQRERL-QEELSQAESTIDELKEQVDAALGAEEmvemltdRNL 448
Cdd:pfam17380  423 EQIrAEQEEARQREVRRLEEERAREMERVRleeqerqQQVERLrQQEEERKRKKLELEKEKRDRKRAEEQ-------RRK 495

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    449 NLEEKVRELRETVgdleamneMNDELQENARETELELREQLDMAGARVREA--QKRVEAAQETVADYQQTIKKYRQLTAH 526
Cdd:pfam17380  496 ILEKELEERKQAM--------IEEERKRKLLEKEMEERQKAIYEEERRREAeeERRKQQEMEERRRIQEQMRKATEERSR 567

                          330       340       350
                   ....*....|....*....|....*....|....
gi 13259510    527 LQ--DVNRELTNQQEASVERQQQPPPETFDFKIK 558
Cdd:pfam17380  568 LEamEREREMMRQIVESEKARAEYEATTPITTIK 601
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
216-419 2.70e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 61.32  E-value: 2.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  216 EEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLK--EARKEAKEALEAKERY 293
Cdd:COG4717  331 PPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEqaEEYQELKEELEELEEQ 410

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  294 MEEMADTADAiEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASS---------YQLKQLE 364
Cdd:COG4717  411 LEELLGELEE-LLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAEllqeleelkAELRELA 489

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13259510  365 EQNARLK---DALVRMRDLSSSEKQEHV--------------KLQKLMEKKNQELEVVRQQRERLQ-EELSQA 419
Cdd:COG4717  490 EEWAALKlalELLEEAREEYREERLPPVleraseyfsrltdgRYRLIRIDEDLSLKVDTEDGRTRPvEELSRG 562
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
299-543 2.80e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 61.85  E-value: 2.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  299 DTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILkAEIEEKGSDgaasSYQLKQLEEQNARLKDALVRMr 378
Cdd:COG4913  607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSWD----EIDVASAEREIAELEAELERL- 680

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  379 DLSSSEKQEhvkLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEML--TDRNLNLEEKVRE 456
Cdd:COG4913  681 DASSDDLAA---LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarLELRALLEERFAA 757

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  457 LRetvgdleamnemndeLQENARETELELREQLDMAGARVREAQKRVEAAQE---------------TVADYQQTIKKYR 521
Cdd:COG4913  758 AL---------------GDAVERELRENLEERIDALRARLNRAEEELERAMRafnrewpaetadldaDLESLPEYLALLD 822

                        250       260
                 ....*....|....*....|....*..
gi 13259510  522 QLTA-----HLQDVNRELTNQQEASVE 543
Cdd:COG4913  823 RLEEdglpeYEERFKELLNENSIEFVA 849
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
309-536 2.99e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 61.85  E-value: 2.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  309 LDKEMAEERAESLQQEVEALkervDELTTDLEILKAEIEekgsdgaassyQLKQLEEQNARLKDALVRMRDLSSSE---- 384
Cdd:COG4913  218 LEEPDTFEAADALVEHFDDL----ERAHEALEDAREQIE-----------LLEPIRELAERYAAARERLAELEYLRaalr 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  385 ----KQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEemVEMLTDRnlnLEEKVRELRET 460
Cdd:COG4913  283 lwfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR--LEQLERE---IERLERELEER 357

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13259510  461 VGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQEtvaDYQQTIKKYRQLTAHLQDVNRELTN 536
Cdd:COG4913  358 ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE---ALAEAEAALRDLRRELRELEAEIAS 430
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 314-544 3.61e-09

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: 60.16  E-value: 3.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  314 AEERAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaassyQLKQLEEQNARLKDALVRMRDLssseKQEHVKLQK 393
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKA----------LLKQLAALERRIAALARRIRAL----EQELAALEA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  394 LMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQ--------VDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLE 465
Cdd:COG4942   84 ELAELEKEIAELRAELEAQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13259510  466 AMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVER 544
Cdd:COG4942  164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
PLN02939 PLN02939
transferase, transferring glycosyl groups
 112-519 4.36e-09

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 61.07  E-value: 4.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   112 SASKVLKREGTDTTAKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGVAGASSSlgPSGSASAGELSSSEPSTPAQTPL 191
Cdd:PLN02939   32 AVSCRARRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMEL--PQKSTSSDDDHNRASMQRDEAIA 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   192 AAPiiptpvltspgavPPLPSPSKEEEGLRA-QVRDLEEKLE-----TLRLkraeDKAKLKELEkhkiQLEQVQEWKSKM 265
Cdd:PLN02939  110 AID-------------NEQQTNSKDGEQLSDfQLEDLVGMIQnaeknILLL----NQARLQALE----DLEKILTEKEAL 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   266 QEQQADLQRRLKEArkEAKEALEAKERYMEEMADTadaiEMATLDKEMAEERA------ESLQQEVEALKERVDELTTDL 339
Cdd:PLN02939  169 QGKINILEMRLSET--DARIKLAAQEKIHVEILEE----QLEKLRNELLIRGAteglcvHSLSKELDVLKEENMLLKDDI 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   340 EILKAEIEEKgsdgAASSYQLKQLEEQNARLKDALvrmRDLSSsekqehvklqKLMEKKNQELEVVRQQRERLQEELSQA 419
Cdd:PLN02939  243 QFLKAELIEV----AETEERVFKLEKERSLLDASL---RELES----------KFIVAQEDVSKLSPLQYDCWWEKVENL 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   420 ESTIDELKEQVDAALgaeemveMLTDRNLNLEEKVRELRETVGDLEaMNEMNDELQENARETELELREQLDMAGArvrEA 499
Cdd:PLN02939  306 QDLLDRATNQVEKAA-------LVLDQNQDLRDKVDKLEASLKEAN-VSKFSSYKVELLQQKLKLLEERLQASDH---EI 374

                         410       420
                  ....*....|....*....|
gi 13259510   500 QKRVEAAQETVADYQQTIKK 519
Cdd:PLN02939  375 HSYIQLYQESIKEFQDTLSK 394
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 226-483 4.46e-09

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 60.64  E-value: 4.46e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    226 DLEEKLETLRLKRAEDKAKLKELEkhkiqLEQVQEWKSKMQEQQADLQ---RRLKEARKEAKEALEAKERYMEEMADTAD 302
Cdd:pfam06160  234 NVDKEIQQLEEQLEENLALLENLE-----LDEAEEALEEIEERIDQLYdllEKEVDAKKYVEKNLPEIEDYLEHAEEQNK 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    303 AI--EMATLDK-----EMAEERAESLQQEVEALKERVDELTTDLE-------ILKAEIEEKGSdgaassyQLKQLEEQNA 368
Cdd:pfam06160  309 ELkeELERVQQsytlnENELERVRGLEKQLEELEKRYDEIVERLEekevaysELQEELEEILE-------QLEEIEEEQE 381

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    369 RLKDALVRMRdlssseKQEHVKLQKLMEKKNQELEVVRQ-QRERL----QEELSQAESTIDELkeqvdaalgaEEMVEML 443
Cdd:pfam06160  382 EFKESLQSLR------KDELEAREKLDEFKLELREIKRLvEKSNLpglpESYLDYFFDVSDEI----------EDLADEL 445

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 13259510    444 TDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETEL 483
Cdd:pfam06160  446 NEVPLNMDEVNRLLDEAQDDVDTLYEKTEELIDNATLAEQ 485
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 221-546 5.69e-09

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: 60.74  E-value: 5.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  221 RAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQ-VQEWKSkmqeQQADLQRRLKEARKEA---KEALEAKERymee 296
Cdd:COG3096  353 QEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEeVDSLKS----QLADYQQALDVQQTRAiqyQQAVQALEK---- 424

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  297 madtADAI-EMATLDKEMAEERAESLQQEVEALKERVDELttdleilkaeiEEKGSDGAASSYQLKQLEEQNARLKDALV 375
Cdd:COG3096  425 ----ARALcGLPDLTPENAEDYLAAFRAKEQQATEEVLEL-----------EQKLSVADAARRQFEKAYELVCKIAGEVE 489

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  376 RmrdlssseKQEHVKLQKLMEKkNQELEVVRQQRERLQEELSQAESTIDELKEqvdaalgAEEMVEML---TDRNLNLEE 452
Cdd:COG3096  490 R--------SQAWQTARELLRR-YRSQQALAQRLQQLRAQLAELEQRLRQQQN-------AERLLEEFcqrIGQQLDAAE 553

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  453 KVRELRETvgdLEAMNEMNDELQENARETELELREQLDMAGARVRE----------AQKRVEAAQETVAdyqQTIKKYRQ 522
Cdd:COG3096  554 ELEELLAE---LEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKElaarapawlaAQDALERLREQSG---EALADSQE 627

                        330       340
                 ....*....|....*....|....
gi 13259510  523 LTAHLQDVnreLTNQQEASVERQQ 546
Cdd:COG3096  628 VTAAMQQL---LEREREATVERDE 648
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 255-539 6.06e-09

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 60.36  E-value: 6.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  255 LEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADaIEMATLDKEMAEERAEsLQQEVEALKErvdE 334
Cdd:COG5185  259 VEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSID-IKKATESLEEQLAAAE-AEQELEESKR---E 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  335 LTTDLEILKAEIEEKGSDgaassyQLKQLEEQNARlKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQE 414
Cdd:COG5185  334 TETGIQNLTAEIEQGQES------LTENLEAIKEE-IENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQE 406

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  415 ELSQAESTIDELKEQVdaalgaEEMVEMLTDRNLNLEEKVRELRETVGDL-----EAMNEMNDELQENARETELELREQL 489
Cdd:COG5185  407 ILATLEDTLKAADRQI------EELQRQIEQATSSNEEVSKLLNELISELnkvmrEADEESQSRLEEAYDEINRSVRSKK 480

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 13259510  490 DmagarvrEAQKRVEAAQETVADYQQTIKKYR-QLTAHLQDVNRELTNQQE 539
Cdd:COG5185  481 E-------DLNEELTQIESRVSTLKATLEKLRaKLERQLEGVRSKLDQVAE 524
mukB PRK04863
chromosome partition protein MukB;
215-547 6.72e-09

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 60.74  E-value: 6.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   215 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEkhkIQLEQVQEWKSKMQEQqadlqRRLKEARKEAKEALEAKERYM 294
Cdd:PRK04863  293 RELYTSRRQLAAEQYRLVEMARELAELNEAESDLE---QDYQAASDHLNLVQTA-----LRQQEKIERYQADLEELEERL 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   295 EEmadTADAIEMATLDKEMAEERAESLQQEVEALK-------ERVDELTTD----------LEILK-----AEIEEKGSD 352
Cdd:PRK04863  365 EE---QNEVVEEADEQQEENEARAEAAEEEVDELKsqladyqQALDVQQTRaiqyqqavqaLERAKqlcglPDLTADNAE 441

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   353 GAASSYQlKQLEEQNARLKDALVRMRDlSSSEKQEHVKLQKLMEK----------KNQELEVVRQQRER--LQEELSQAE 420
Cdd:PRK04863  442 DWLEEFQ-AKEQEATEELLSLEQKLSV-AQAAHSQFEQAYQLVRKiagevsrseaWDVARELLRRLREQrhLAEQLQQLR 519

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   421 STIDELKEQVDAALGAEEMV---EMLTDRNLNLEEKVRELREtvgDLEAMNEMNDELQENARETELELREQLDMAGARVR 497
Cdd:PRK04863  520 MRLSELEQRLRQQQRAERLLaefCKRLGKNLDDEDELEQLQE---ELEARLESLSESVSEARERRMALRQQLEQLQARIQ 596

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   498 E----------AQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 547
Cdd:PRK04863  597 RlaarapawlaAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQA 656
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 304-466 8.42e-09

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: 57.63  E-value: 8.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  304 IEMATLDKEMA--EERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKdalvrmrdls 381
Cdd:COG1579   10 LDLQELDSELDrlEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE---------- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  382 ssEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVdaalgaEEMVEMLTDRNLNLEEKVRELRETV 461
Cdd:COG1579   80 --EQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEEL------AELEAELAELEAELEEKKAELDEEL 151


                 ....*
gi 13259510  462 GDLEA 466
Cdd:COG1579  152 AELEA 156
mukB PRK04863
chromosome partition protein MukB;
242-437 9.67e-09

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 59.97  E-value: 9.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   242 KAKLKELEKHKIQLEQVQEWKSKMQE------QQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAE 315
Cdd:PRK04863  499 RELLRRLREQRHLAEQLQQLRMRLSEleqrlrQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEAR 578

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   316 ERAESLQQEVEALKERVDELTTdleilKAEIEEKGSDGAAssyqlkQLEEQNArlkDALVRMRDLSSSEKQEHVKLQKLM 395
Cdd:PRK04863  579 ERRMALRQQLEQLQARIQRLAA-----RAPAWLAAQDALA------RLREQSG---EEFEDSQDVTEYMQQLLERERELT 644

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 13259510   396 EKKNQelevVRQQRERLQEE---LSQAESTIDE----LKEQVDAALGAE 437
Cdd:PRK04863  645 VERDE----LAARKQALDEEierLSQPGGSEDPrlnaLAERFGGVLLSE 689
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 223-577 1.18e-08

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: 59.75  E-value: 1.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    223 QVRDLEEKLETLRLKRAEDKAKLKELEkhkiqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADtad 302
Cdd:pfam15921  279 EITGLTEKASSARSQANSIQSQLEIIQ------EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEK--- 349

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    303 aiEMATLDKEMAEERAESLQ--QEVEALKERVDELTTDLEilKAEIEekgsdgaassyqLKQLEEQNARLKDalvrmRDL 380
Cdd:pfam15921  350 --QLVLANSELTEARTERDQfsQESGNLDDQLQKLLADLH--KREKE------------LSLEKEQNKRLWD-----RDT 408

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    381 SSSEKQEHvkLQKLMEKKNQELE----VVRQQRERLQEELSQAESTIDELKEQVD--AALGAE---------EMVEMLTD 445
Cdd:pfam15921  409 GNSITIDH--LRRELDDRNMEVQrleaLLKAMKSECQGQMERQMAAIQGKNESLEkvSSLTAQlestkemlrKVVEELTA 486

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    446 RNLNLEEKVRELRETVGDLE----AMNEMNDELQENARETELELRE--QLDMAGARVREAQKRVEAAQETVADYQQTIKK 519
Cdd:pfam15921  487 KKMTLESSERTVSDLTASLQekerAIEATNAEITKLRSRVDLKLQElqHLKNEGDHLRNVQTECEALKLQMAEKDKVIEI 566

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 13259510    520 YRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQME 577
Cdd:pfam15921  567 LRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELE 624
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
218-463 2.03e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.77  E-value: 2.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  218 EGLRAQVRDLEEKLETLRlkraEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQR---RLKEARKEAKEALEAKERYM 294
Cdd:COG4913  664 ASAEREIAELEAELERLD----ASSDDLAALEE---QLEELEAELEELEEELDELKGeigRLEKELEQAEEELDELQDRL 736

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  295 EEMADTADAIEMATLDKEMAEERAESLQQEV-EALKERVDELTTDLEILKAEIEEK----------------GSDGAASS 357
Cdd:COG4913  737 EAAEDLARLELRALLEERFAAALGDAVERELrENLEERIDALRARLNRAEEELERAmrafnrewpaetadldADLESLPE 816

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  358 YQ--LKQLEEQN-----ARLKDALVR-----MRDLSSSEKQEHVKLQKLMEKKNQELE--------------------VV 405
Cdd:COG4913  817 YLalLDRLEEDGlpeyeERFKELLNEnsiefVADLLSKLRRAIREIKERIDPLNDSLKripfgpgrylrlearprpdpEV 896

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 13259510  406 RQQRERLQEELSQAESTIDELKEQVDAALgaEEMVEMLTDRNlnlEEKVRELRETVGD 463
Cdd:COG4913  897 REFRQELRAVTSGASLFDEELSEARFAAL--KRLIERLRSEE---EESDRRWRARVLD 949
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 272-1039 2.72e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 2.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  272 LQRRLKEARKEAKEALEAKEryMEEMADTADAIEMAtLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEkgs 351
Cdd:COG1196  198 LERQLEPLERQAEKAERYRE--LKEELKELEAELLL-LKLRELEAELEELEAELEELEAELEELEAELAELEAELEE--- 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  352 dgaassyQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQElevvRQQRERLQEELSQAESTIDELKEQVD 431
Cdd:COG1196  272 -------LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL----EERLEELEEELAELEEELEELEEELE 340

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  432 AALGAEEMvemltdrnlnLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVA 511
Cdd:COG1196  341 ELEEELEE----------AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  512 DYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQpppetfdfkikFAETKAHAKAIEMELRQMEVAQANRHMSLLTAf 591
Cdd:COG1196  411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEE-----------AAEEEAELEEEEEALLELLAELLEEAALLEAA- 478

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  592 mpdsflrpggdhdcvlvlllmpRLICKAELIRKQAQEKFELSENCSERPGLRGA-AGEQLSFAAGLVYSLSLLQATLHRY 670
Cdd:COG1196  479 ----------------------LAELLEELAEAAARLLLLLEAEADYEGFLEGVkAALLLAGLRGLAGAVAVLIGVEAAY 536

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  671 EHALSQCSVdvykkvGSLYPEMSAHERSLDFLIELLhKDQLDETVNVEPLTKaikyyqhlysIHLAEQPEdctmqladhi 750
Cdd:COG1196  537 EAALEAALA------AALQNIVVEDDEVAAAAIEYL-KAAKAGRATFLPLDK----------IRARAALA---------- 589

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  751 kftqsaldcmsvevgRLRAFLQGGQEATDIALLLRDLEtscsdirqfckkirrrmpgtdapgIPAALAFGPQVSDTLLDC 830
Cdd:COG1196  590 ---------------AALARGAIGAAVDLVASDLREAD------------------------ARYYVLGDTLLGRTLVAA 630

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  831 RKHLTWVVAVLQEVAAAAAQLIAPLAENEGLLVAALEELafkaseqiygtpssspyeclrqscnilistmnklatamqeg 910
Cdd:COG1196  631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE----------------------------------------- 669

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  911 eydaerppskpppvelRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADER 990
Cdd:COG1196  670 ----------------LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733

                        730       740       750       760
                 ....*....|....*....|....*....|....*....|....*....
gi 13259510  991 IEKVQTRLEETQALLRKKEKEFEETMdalqADIDQLEAEKAELKQRLNS 1039
Cdd:COG1196  734 REELLEELLEEEELLEEEALEELPEP----PDLEELERELERLEREIEA 778
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
232-548 2.77e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 57.60  E-value: 2.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  232 ETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDK 311
Cdd:COG4372   31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  312 EMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgaasSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHV-- 389
Cdd:COG4372  111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER-------EEELKELEEQLESLQEELAALEQELQALSEAEAeq 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  390 KLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNE 469
Cdd:COG4372  184 ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  470 MNDELQE-NARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQP 548
Cdd:COG4372  264 ELAILVEkDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLL 343
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 220-430 3.25e-08

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 58.05  E-value: 3.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  220 LRAQVRDLEEKLETlRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEmad 299
Cdd:COG5185  287 LIKQFENTKEKIAE-YTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEE--- 362

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  300 tADAIEmATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDG-AASSYQLKQLE----------EQNA 368
Cdd:COG5185  363 -IENIV-GEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTlKAADRQIEELQrqieqatssnEEVS 440

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13259510  369 RLKDALVRMRDLSSSEKQEHVKlQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQV 430
Cdd:COG5185  441 KLLNELISELNKVMREADEESQ-SRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATL 501
PTZ00121 PTZ00121
MAEBL; Provisional
 216-507 3.31e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.61  E-value: 3.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   216 EEEGLRAQVRDLE-EKLETLRLKRAEDKAKLKELEKHKIQLEQVQEW-KSKMQEQQADLQRRLKEARK--------EAKE 285
Cdd:PTZ00121 1068 QDEGLKPSYKDFDfDAKEDNRADEATEEAFGKAEEAKKTETGKAEEArKAEEAKKKAEDARKAEEARKaedarkaeEARK 1147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   286 ALEAKERYMEEMADTADAIEMAtldkemaeERAESLQQEVEAlkERVDELTTDLEILKAEiEEKGSDGAASSYQLKQLEE 365
Cdd:PTZ00121 1148 AEDAKRVEIARKAEDARKAEEA--------RKAEDAKKAEAA--RKAEEVRKAEELRKAE-DARKAEAARKAEEERKAEE 1216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   366 qnarlkdalvrMRDLSSSEKQEHVKlqKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTD 445
Cdd:PTZ00121 1217 -----------ARKAEDAKKAEAVK--KAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADEL 1283

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13259510   446 RNLNLEEKVRELR--ETVGDLEAMNEMNDELQ--ENARETELELREQLDMAGARVREAQKRVEAAQ 507
Cdd:PTZ00121 1284 KKAEEKKKADEAKkaEEKKKADEAKKKAEEAKkaDEAKKKAEEAKKKADAAKKKAEEAKKAAEAAK 1349
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 215-512 4.38e-08

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 58.06  E-value: 4.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    215 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLE---QVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKE 291
Cdd:pfam02463  181 ETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEeeyLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEI 260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    292 RYMEEMADTADAI--EMATLDKEMAEERA------ESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAA----SSYQ 359
Cdd:pfam02463  261 EKEEEKLAQVLKEnkEEEKEKKLQEEELKllakeeEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKekeeIEEL 340

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    360 LKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQElevvRQQRERLQEELSQAESTIDELKEQVDAALGAEEM 439
Cdd:pfam02463  341 EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLE----SERLSSAAKLKEEELELKSEEEKEAQLLLELARQ 416

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13259510    440 VEMLTDRNLN-LEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVAD 512
Cdd:pfam02463  417 LEDLLKEEKKeELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLL 490
mukB PRK04863
chromosome partition protein MukB;
226-515 6.92e-08

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 57.27  E-value: 6.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   226 DLEEKLETLRLKRAEDKAKLKELEK----HKIQLEQVQEWKSKMQE--------QQADLQRRLKEARKEAKEALEAKeRY 293
Cdd:PRK04863  834 DPEAELRQLNRRRVELERALADHESqeqqQRSQLEQAKEGLSALNRllprlnllADETLADRVEEIREQLDEAEEAK-RF 912

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   294 MEEMADTADAIE--MATLDKEmaEERAESLQQEVEALKErvdelttdleilkaeieekgsdgaassyQLKQLEEQNARLK 371
Cdd:PRK04863  913 VQQHGNALAQLEpiVSVLQSD--PEQFEQLKQDYQQAQQ----------------------------TQRDAKQQAFALT 962

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   372 DALVRMRDLSSSEKQEHV-KLQKLMEKKNQELEVVRQQRERLQEELSQAE--------------STIDELKEQVDAAlgA 436
Cdd:PRK04863  963 EVVQRRAHFSYEDAAEMLaKNSDLNEKLRQRLEQAEQERTRAREQLRQAQaqlaqynqvlaslkSSYDAKRQMLQEL--K 1040

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   437 EEMVEMLTDRNLNLEEKVRELREtvgdleamnEMNDELQEN-ARETELELreQLDMAGARVREAQKRVEAAQEtvaDYQQ 515
Cdd:PRK04863 1041 QELQDLGVPADSGAEERARARRD---------ELHARLSANrSRRNQLEK--QLTFCEAEMDNLTKKLRKLER---DYHE 1106
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 226-495 7.48e-08

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: 57.27  E-value: 7.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  226 DLEEKLETLRLKRAEDKAklkELEKHKIQLEQVQEWKSKMQEQQADLQR---------------RLKEARKEAKEALEAk 290
Cdd:COG3096  833 DPEAELAALRQRRSELER---ELAQHRAQEQQLRQQLDQLKEQLQLLNKllpqanlladetladRLEELREELDAAQEA- 908

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  291 ERYMEEMADTADAIE--MATLDKEMAEEraESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgAASSYQ-----LKQL 363
Cdd:COG3096  909 QAFIQQHGKALAQLEplVAVLQSDPEQF--EQLQADYLQAKEQQRRLKQQIFALSEVVQRR----PHFSYEdavglLGEN 982

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  364 EEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgaeEMVEML 443
Cdd:COG3096  983 SDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADA-----EAEERA 1057

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  444 TDRNLNLEEKVRELRETVGDLEAM-----NEMnDELQENARETELE---LREQLDMAGAR 495
Cdd:COG3096 1058 RIRRDELHEELSQNRSRRSQLEKQltrceAEM-DSLQKRLRKAERDykqEREQVVQAKAG 1116
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 216-590 7.60e-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: 56.99  E-value: 7.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    216 EEEGLRAQVRDLEEKLETLRLKRAEDKAKL------------------KELEKHKIQLEQVQEWKSKMQEQQADLQRRLK 277
Cdd:TIGR02168  254 ELEELTAELQELEEKLEELRLEVSELEEEIeelqkelyalaneisrleQQKQILRERLANLERQLEELEAQLEELESKLD 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    278 EARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASS 357
Cdd:TIGR02168  334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    358 YQLKQLEEQNARLKDALVR--MRDLS---SSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQ--- 429
Cdd:TIGR02168  414 DRRERLQQEIEELLKKLEEaeLKELQaelEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARlds 493

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    430 ---------------------------------------------VDAALG-------------AEEMVEMLT------- 444
Cdd:TIGR02168  494 lerlqenlegfsegvkallknqsglsgilgvlselisvdegyeaaIEAALGgrlqavvvenlnaAKKAIAFLKqnelgrv 573

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510        --------------------------------------------------------------------------------
Cdd:TIGR02168  574 tflpldsikgteiqgndreilkniegflgvakdlvkfdpklrkalsyllggvlvvddldnalelakklrpgyrivtldgd 653

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    445 -------------DRNLNLEEKVRELRETVGDLEAMNEMNDELQEN---ARETELELREQLDMAGARVREAQKRVEAAQE 508
Cdd:TIGR02168  654 lvrpggvitggsaKTNSSILERRREIEELEEKIEELEEKIAELEKAlaeLRKELEELEEELEQLRKELEELSRQISALRK 733

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    509 TVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQpppetfdfkikfAETKAHAKAIEMELRQMEVAQANRHMSLL 588
Cdd:TIGR02168  734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE------------AEEELAEAEAEIEELEAQIEQLKEELKAL 801


                   ..
gi 13259510    589 TA 590
Cdd:TIGR02168  802 RE 803
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
215-427 7.72e-08

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 55.30  E-value: 7.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  215 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQL-EQVQEWKSKMQEQQADLQ-------------------- 273
Cdd:COG1340   43 EKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELnEKLNELREELDELRKELAelnkaggsidklrkeierle 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  274 --------------------RRLKEARKEAKEALEAKERYMEEMADTADA-IEMATLDKEMAE--ERAESLQQEVEALKE 330
Cdd:COG1340  123 wrqqtevlspeeekelvekiKELEKELEKAKKALEKNEKLKELRAELKELrKEAEEIHKKIKElaEEAQELHEEMIELYK 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  331 RVDELTTDLEILKAEIEEKGsdgaassyqlKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLmeKKNQELEVVRQQRE 410
Cdd:COG1340  203 EADELRKEADELHKEIVEAQ----------EKADELHEEIIELQKELRELRKELKKLRKKQRAL--KREKEKEELEEKAE 270

                        250
                 ....*....|....*...
gi 13259510  411 RLQEELSQAES-TIDELK 427
Cdd:COG1340  271 EIFEKLKKGEKlTTEELK 288
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 296-550 8.07e-08

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 55.99  E-value: 8.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  296 EMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSyqlKQLEEQNARLKDALV 375
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREELGERAR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  376 RMRD-----------LSSSEKQEHVK----LQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmv 440
Cdd:COG3883   94 ALYRsggsvsyldvlLGSESFSDFLDrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA-- 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  441 emltdrnlNLEEKVRELRETVGDLEAmnemnDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKY 520
Cdd:COG3883  172 --------ELEAQQAEQEALLAQLSA-----EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238

                        250       260       270
                 ....*....|....*....|....*....|
gi 13259510  521 RQLTAHLQDVNRELTNQQEASVERQQQPPP 550
Cdd:COG3883  239 AAAAAASAAGAGAAGAAGAAAGSAGAAGAA 268
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 223-547 8.34e-08

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: 56.95  E-value: 8.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    223 QVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEqvqewKSKMQEQQADLQRRLKEARKEAKealeakerymeemadtad 302
Cdd:TIGR04523  146 EIKKKEKELEKLNNKYNDLKKQKEELENELNLLE-----KEKLNIQKNIDKIKNKLLKLELL------------------ 202

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    303 aieMATLDKEmaEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLeeqnarlkdalvrmrdlss 382
Cdd:TIGR04523  203 ---LSNLKKK--IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQL------------------- 258

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    383 seKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgaeemvEMLTDRNLNLEEKVRELRETVG 462
Cdd:TIGR04523  259 --KDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ--------DWNKELKSELKNQEKKLEEIQN 328

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    463 DL----EAMNEMNDELQ------ENARETELELREQLdmagarvREAQKRVEAAQETVADYQQTIKKyrqLTAHLQDVNR 532
Cdd:TIGR04523  329 QIsqnnKIISQLNEQISqlkkelTNSESENSEKQREL-------EEKQNEIEKLKKENQSYKQEIKN---LESQINDLES 398

                          330
                   ....*....|....*
gi 13259510    533 ELTNQQEASVERQQQ 547
Cdd:TIGR04523  399 KIQNQEKLNQQKDEQ 413
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 219-577 1.01e-07

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 56.24  E-value: 1.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    219 GLRAQVRDLEEklETLRLKRAEDKAKLK--ELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEA--LEAK-ERY 293
Cdd:pfam05622   63 LLQKQLEQLQE--ENFRLETARDDYRIKceELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVkkLEATvETY 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    294 MEEMADTADaiematldkemaeeraesLQQEVEALKERvdelTTDLEILKAEIEEKGSDGAASSYQL----KQLEEQNAR 369
Cdd:pfam05622  141 KKKLEDLGD------------------LRRQVKLLEER----NAEYMQRTLQLEEELKKANALRGQLetykRQVQELHGK 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    370 LkdalvrmrdlsSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELK---EQVDAALGAEEMVEMLTDR 446
Cdd:pfam05622  199 L-----------SEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRETNEELRcaqLQQAELSQADALLSPSSDP 267

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    447 NLNLEEKVR--ELRETVGDLEAMNEM---NDELQENARETEL------------ELREQLDMAGARVREAQKRVE----A 505
Cdd:pfam05622  268 GDNLAAEIMpaEIREKLIRLQHENKMlrlGQEGSYRERLTELqqlledanrrknELETQNRLANQRILELQQQVEelqkA 347

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13259510    506 AQETVADYQQTIKKYRQLTAHLQ---DVNRELTNQQEASVERQqqpPPETFDFKIKFAETKAHAKAIEMELRQME 577
Cdd:pfam05622  348 LQEQGSKAEDSSLLKQKLEEHLEklhEAQSELQKKKEQIEELE---PKQDSNLAQKIDELQEALRKKDEDMKAME 419
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 220-522 1.12e-07

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: 56.72  E-value: 1.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    220 LRAQVRDLEEKLETLRLKRAEDKAKLK----ELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYME 295
Cdd:pfam01576  269 LEAQISELQEDLESERAARNKAEKQRRdlgeELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQ 348

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    296 EMADT-ADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEIL---KAEIEEKGSDGAAssyqlkQLEEQNARLK 371
Cdd:pfam01576  349 EMRQKhTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLqqaKQDSEHKRKKLEG------QLQELQARLS 422

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    372 DAlvrmrDLSSSEKQEHV-KLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEqvdaaLGAEEmvemlTDRNLNL 450
Cdd:pfam01576  423 ES-----ERQRAELAEKLsKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQE-----LLQEE-----TRQKLNL 487

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13259510    451 EEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQ 522
Cdd:pfam01576  488 STRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQ 559
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
220-380 1.18e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.46  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  220 LRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEqvQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYME---- 295
Cdd:COG4913  293 LEAELEELRAELARLEAELERLEARLDALREELDELE--AQIRGNGGDRLEQLEREIERLERELEERERRRARLEAllaa 370

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  296 -EMADTADAIEMATLdKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQNARLKDAL 374
Cdd:COG4913  371 lGLPLPASAEEFAAL-RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA-------EIASLERRKSNIPARL 442


                 ....*.
gi 13259510  375 VRMRDL 380
Cdd:COG4913  443 LALRDA 448
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 216-573 1.22e-07

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 56.52  E-value: 1.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    216 EEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEaLEAKERYME 295
Cdd:TIGR00618  436 QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCP-LCGSCIHPN 514

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    296 EMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALV 375
Cdd:TIGR00618  515 PARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITV 594

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    376 RMRDL----SSSEKQEHVKLQKLMEKKNQELEV--VRQQRERLQEELSQAESTIDEL------KEQVDAALGAEEMVEML 443
Cdd:TIGR00618  595 RLQDLteklSEAEDMLACEQHALLRKLQPEQDLqdVRLHLQQCSQELALKLTALHALqltltqERVREHALSIRVLPKEL 674

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    444 TDRNLNLEEKVRELRETV-GDLEAMNEMNDELQE---NARETELELREQLDMAGARVREAQKRVEAAQETVADYQQ---T 516
Cdd:TIGR00618  675 LASRQLALQKMQSEKEQLtYWKEMLAQCQTLLREletHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHqarT 754

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13259510    517 IKKYR---------------QLTAHLQDVNRELTNQQEASVERQQQpppetfdFKIKFAETKAHAKAIEMEL 573
Cdd:TIGR00618  755 VLKARteahfnnneevtaalQTGAELSHLAAEIQFFNRLREEDTHL-------LKTLEAEIGQEIPSDEDIL 819
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 220-503 1.29e-07

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: 56.28  E-value: 1.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    220 LRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQ-EWKSKMQEQQADLQRRLKEARKEAKEALEAKERymeema 298
Cdd:pfam15921  333 LREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESgNLDDQLQKLLADLHKREKELSLEKEQNKRLWDR------ 406

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    299 DTADAIEMATL-----DKEMAEERAESL------------QQEVEALK------ERVDELTTDLEILKAEIEEKGSDGAA 355
Cdd:pfam15921  407 DTGNSITIDHLrreldDRNMEVQRLEALlkamksecqgqmERQMAAIQgkneslEKVSSLTAQLESTKEMLRKVVEELTA 486

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    356 SSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQeelsQAESTIDELKEQVdaaLG 435
Cdd:pfam15921  487 KKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR----NVQTECEALKLQM---AE 559

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13259510    436 AEEMVEMLTDRNLNLEEKVRELRETVGdleAMNEMNDELQENARETELELRE---QLDMAGARVREAQKRV 503
Cdd:pfam15921  560 KDKVIEILRQQIENMTQLVGQHGRTAG---AMQVEKAQLEKEINDRRLELQEfkiLKDKKDAKIRELEARV 627
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 226-378 1.79e-07

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: 53.78  E-value: 1.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  226 DLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEwksKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADA-- 303
Cdd:COG1579   14 ELDSELDRLEHRLKELPAELAELEDELAALEARLE---AAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNke 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  304 -------IEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgaassyqLKQLEEQNARLKDALVR 376
Cdd:COG1579   91 yealqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK----------KAELDEELAELEAELEE 160


                 ..
gi 13259510  377 MR 378
Cdd:COG1579  161 LE 162
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 359-519 2.29e-07

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: 53.39  E-value: 2.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  359 QLKQLEEQNARLKDALVRMRDlsssekqEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEE 438
Cdd:COG1579   18 ELDRLEHRLKELPAELAELED-------ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  439 M------VEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDmagARVREAQKRVEAAQETVAD 512
Cdd:COG1579   91 YealqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD---EELAELEAELEELEAEREE 167


                 ....*..
gi 13259510  513 YQQTIKK 519
Cdd:COG1579  168 LAAKIPP 174
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 218-547 2.45e-07

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 55.14  E-value: 2.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    218 EGLRAQVRDLEEKL-----ETLRLKRA-EDKAKLKELEKH-----KIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEA 286
Cdd:pfam07111  334 KQLRGQVAELQEQVtsqsqEQAILQRAlQDKAAEVEVERMsakglQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSST 413

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    287 LEAKERYMEEMADTADAI------------EMATLDKEMAEERA-ESLQQEVEALKERVDELTTDLeilkaeieekgsdg 353
Cdd:pfam07111  414 QIWLETTMTRVEQAVARIpslsnrlsyavrKVHTIKGLMARKVAlAQLRQESCPPPPPAPPVDADL-------------- 479

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    354 aasSYQLKQLEEQNARLKDALvrmrDLSSSEKQEHV-KLQKLMEKKNQELEVVRQQrerLQEELSQAESTIDELKEQVDA 432
Cdd:pfam07111  480 ---SLELEQLREERNRLDAEL----QLSAHLIQQEVgRAREQGEAERQQLSEVAQQ---LEQELQRAQESLASVGQQLEV 549

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    433 ALGAEEMVemlTDRNLNLEEKVRELRETVGDleamnemndELQENARETELELREQLDMAGARVREAQKRVEAAQETVAD 512
Cdd:pfam07111  550 ARQGQQES---TEEAASLRQELTQQQEIYGQ---------ALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQ 617

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 13259510    513 YQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 547
Cdd:pfam07111  618 IQHRATQEKERNQELRRLQDEARKEEGQRLARRVQ 652
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
215-348 2.92e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.31  E-value: 2.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  215 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKH--KIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKER 292
Cdd:COG4913  295 AELEELRAELARLEAELERLEARLDALREELDELEAQirGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLP 374

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 13259510  293 YMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEE 348
Cdd:COG4913  375 LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 220-522 3.22e-07

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: 55.18  E-value: 3.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    220 LRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLE-QVQEWKSKMQEQQADLQRrLKEARKEAKEALEAKERYMEEMA 298
Cdd:pfam01576  487 LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQaQLSDMKKKLEEDAGTLEA-LEEGKKRLQRELEALTQQLEEKA 565

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    299 DTADAIEMA------------------------------TLDKEMAEERAESLQQEVE---ALKERVDELTTDLEILKAE 345
Cdd:pfam01576  566 AAYDKLEKTknrlqqelddllvdldhqrqlvsnlekkqkKFDQMLAEEKAISARYAEErdrAEAEAREKETRALSLARAL 645

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    346 IEEKGsdgaassyQLKQLEEQNARLK---DALVRMRDLSSSEKQEHVKLQKLMEkknQELEVVRQQRERLQEELSQAEST 422
Cdd:pfam01576  646 EEALE--------AKEELERTNKQLRaemEDLVSSKDDVGKNVHELERSKRALE---QQVEEMKTQLEELEDELQATEDA 714

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    423 IDELKEQVDAALGAEEmvEMLTDRNLNLEEKVRELRETVGDLEAmnEMNDELQENA------RETELELRE---QLDMAG 493
Cdd:pfam01576  715 KLRLEVNMQALKAQFE--RDLQARDEQGEEKRRQLVKQVRELEA--ELEDERKQRAqavaakKKLELDLKEleaQIDAAN 790

                          330       340
                   ....*....|....*....|....*....
gi 13259510    494 ARVREAQKRVEAAQETVADYQQTIKKYRQ 522
Cdd:pfam01576  791 KGREEAVKQLKKLQAQMKDLQRELEEARA 819
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 217-511 3.34e-07

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 54.73  E-value: 3.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    217 EEGLRAQVRDLEEKLETLRLKRAE-----DKAKLK-------------ELEKH-------KIQLEQVQEWKSKMQEQQAD 271
Cdd:pfam05483  466 EEHYLKEVEDLKTELEKEKLKNIEltahcDKLLLEnkeltqeasdmtlELKKHqediincKKQEERMLKQIENLEEKEMN 545

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    272 LQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEmaeERAESLQQEVEALKERVDELTTDLEILKAEIEEKGS 351
Cdd:pfam05483  546 LRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKE---KQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    352 DGAASSYQLKQLEEQNARLKDALvrmrdlsSSEKQehvKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDE---LKE 428
Cdd:pfam05483  623 KGSAENKQLNAYEIKVNKLELEL-------ASAKQ---KFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEavkLQK 692

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    429 QVDAALGAE--EMVEMLtDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETEL--------ELREQLDMagaRVRE 498
Cdd:pfam05483  693 EIDKRCQHKiaEMVALM-EKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELsnikaellSLKKQLEI---EKEE 768

                          330
                   ....*....|...
gi 13259510    499 AQKRVEAAQETVA 511
Cdd:pfam05483  769 KEKLKMEAKENTA 781
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 215-590 3.48e-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: 55.06  E-value: 3.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    215 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAK---------- 284
Cdd:TIGR02168  447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSglsgilgvls 526

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    285 EALEAKERY---MEE----------MADTADAIEMATLDKEMAEERA-------------ESLQQEVEALKERVDELTTD 338
Cdd:TIGR02168  527 ELISVDEGYeaaIEAalggrlqavvVENLNAAKKAIAFLKQNELGRVtflpldsikgteiQGNDREILKNIEGFLGVAKD 606

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    339 LEILKAEIEEKGS------------DGAASSYQLKQLEEQNARLKDALVRMRDLSS--SEKQEHVKLQKlmekkNQELEV 404
Cdd:TIGR02168  607 LVKFDPKLRKALSyllggvlvvddlDNALELAKKLRPGYRIVTLDGDLVRPGGVITggSAKTNSSILER-----RREIEE 681

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    405 VRQQRERLQEELSQAESTIDELKEQVDAalgAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELE 484
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEE---LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    485 LREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYR----QLTAHLQDVNRELTNQQEASVERQqqpppetfdFKIKFA 560
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKeelkALREALDELRAELTLLNEEAANLR---------ERLESL 829

                          410       420       430
                   ....*....|....*....|....*....|
gi 13259510    561 ETKAHAKAIEMELRQMEVAQANRHMSLLTA 590
Cdd:TIGR02168  830 ERRIAATERRLEDLEEQIEELSEDIESLAA 859
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
288-581 3.57e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 54.14  E-value: 3.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  288 EAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQN 367
Cdd:COG4372   10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  368 ARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgAEEMVEMLTDRN 447
Cdd:COG4372   90 QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE---LEEQLESLQEEL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  448 LNLEEKVRELRETVGDlEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKyrQLTAHL 527
Cdd:COG4372  167 AALEQELQALSEAEAE-QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSA--LLDALE 243

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 13259510  528 QDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQMEVAQA 581
Cdd:COG4372  244 LEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKL 297
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 216-524 3.94e-07

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: 54.13  E-value: 3.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    216 EEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEkhkIQLEQVQEWKSKMQEQQADLQRRLKEARKEAK---EALEAKER 292
Cdd:pfam07888   74 QRRELESRVAELKEELRQSREKHEELEEKYKELS---ASSEELSEEKDALLAQRAAHEARIRELEEDIKtltQRVLERET 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    293 YMEEMADTADaiEMATLDKEMAEERaESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQNARLKD 372
Cdd:pfam07888  151 ELERMKERAK--KAGAQRKEEEAER-KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDT-------QVLQLQDTITTLTQ 220

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    373 ALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEqvdAALGAEEMVEMLTDRNLNL-E 451
Cdd:pfam07888  221 KLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQ---ARLQAAQLTLQLADASLALrE 297

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13259510    452 EKVRELRETVGDLEAMNEMNDELQENARETeleLREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLT 524
Cdd:pfam07888  298 GRARWAQERETLQQSAEADKDRIEKLSAEL---QRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQ 367
PRK12704 PRK12704
phosphodiesterase; Provisional
 301-456 3.94e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 54.40  E-value: 3.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   301 ADAIEMATLDKEMAEERAESLQQEVEA-LKERVDELTTDLEilkAEIEEKGSDgaassyqLKQLEEQNARLKDALvrmrd 379
Cdd:PRK12704   34 KEAEEEAKRILEEAKKEAEAIKKEALLeAKEEIHKLRNEFE---KELRERRNE-------LQKLEKRLLQKEENL----- 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   380 lssSEKQEhvklqkLMEKKNQELEVVRQQRERLQEELSQAESTIDEL-KEQVD-----AALGAEEMVEMLTDrnlNLEEK 453
Cdd:PRK12704   99 ---DRKLE------LLEKREEELEKKEKELEQKQQELEKKEEELEELiEEQLQeleriSGLTAEEAKEILLE---KVEEE 166


                  ...
gi 13259510   454 VRE 456
Cdd:PRK12704  167 ARH 169
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
341-546 4.06e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 54.39  E-value: 4.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  341 ILKAEIEEKGSD-----GAASSYQLKQLEEQNARLKDAlvrmrdlsSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEE 415
Cdd:COG4717   46 MLLERLEKEADElfkpqGRKPELNLKELKELEEELKEA--------EEKEEEYAELQEELEELEEELEELEAELEELREE 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  416 LSQAEsTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEamnEMNDELQENARETELELREQLDMAGAR 495
Cdd:COG4717  118 LEKLE-KLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE---ELEAELAELQEELEELLEQLSLATEEE 193

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 13259510  496 VREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQ 546
Cdd:COG4717  194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 216-442 6.17e-07

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 54.06  E-value: 6.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    216 EEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWK-SKMQEQQADLQRRLKEARKEAKEALEAKERYM 294
Cdd:pfam10174  469 ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKdSKLKSLEIAVEQKKEECSKLENQLKKAHNAEE 548

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    295 EEMADTADAIEMATLDKEMAEERAES--LQQEVEALKERVDELTTD-------LEILKAEIEEKGSDGAASSYQLK---Q 362
Cdd:pfam10174  549 AVRTNPEINDRIRLLEQEVARYKEESgkAQAEVERLLGILREVENEkndkdkkIAELESLTLRQMKEQNKKVANIKhgqQ 628

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    363 LEEQNARLKDALVRMRDLSSSEKQEHVKLQKLM---EKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALgaEEM 439
Cdd:pfam10174  629 EMKKKGAQLLEEARRREDNLADNSQQLQLEELMgalEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQL--EEI 706


                   ...
gi 13259510    440 VEM 442
Cdd:pfam10174  707 LEM 709
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
312-547 6.19e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.89  E-value: 6.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   312 EMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKG---------SDGAASSYQLKQLEEQnarlKDALVRMRDLSS 382
Cdd:PRK02224  165 EEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDlherlngleSELAELDEEIERYEEQ----REQARETRDEAD 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   383 SEKQEHvklqklmEKKNQELEVVRQQRERLQEELSQAESTIDELKEQvdaalgaeemVEMLTDRNLNLEEKVRELRETVG 462
Cdd:PRK02224  241 EVLEEH-------EERREELETLEAEIEDLRETIAETEREREELAEE----------VRDLRERLEELEEERDDLLAEAG 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   463 DLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDvnrELTNQQEASV 542
Cdd:PRK02224  304 LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELES---ELEEAREAVE 380


                  ....*
gi 13259510   543 ERQQQ 547
Cdd:PRK02224  381 DRREE 385
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
209-575 6.54e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.15  E-value: 6.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  209 PLPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEkhkiqLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALE 288
Cdd:COG4913  256 PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE-----LEELRAELARLEAELERLEARLDALREELDELEA 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  289 AKERymeemADTadaiematldkemaeERAESLQQEVEALKERVDELTTDLEILKAeieekgsdgaassyQLKQLEEQNA 368
Cdd:COG4913  331 QIRG-----NGG---------------DRLEQLEREIERLERELEERERRRARLEA--------------LLAALGLPLP 376

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  369 RLKDALVRMRDlsssekqehvKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgaeemvemLTDRNL 448
Cdd:COG4913  377 ASAEEFAALRA----------EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS----------LERRKS 436

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  449 NLEEKVRELRetvgdleamnemnDELQENARETELELR---EQLDmagarVREAQKRVEAAQETV------------ADY 513
Cdd:COG4913  437 NIPARLLALR-------------DALAEALGLDEAELPfvgELIE-----VRPEEERWRGAIERVlggfaltllvppEHY 498

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13259510  514 QQTIKKYRQ--LTAHLQdVNRELTNQQEAsveRQQQPPPETFDFKIKFAETKAHAkAIEMELRQ 575
Cdd:COG4913  499 AAALRWVNRlhLRGRLV-YERVRTGLPDP---ERPRLDPDSLAGKLDFKPHPFRA-WLEAELGR 557
mukB PRK04863
chromosome partition protein MukB;
221-504 7.95e-07

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 53.81  E-value: 7.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   221 RAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQ-VQEWKSkmqeQQADLQRRLKEARKEAKEALEAKERYmeemaD 299
Cdd:PRK04863  354 QADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEeVDELKS----QLADYQQALDVQQTRAIQYQQAVQAL-----E 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   300 TADAI-EMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKA-----------------------------EIEEK 349
Cdd:PRK04863  425 RAKQLcGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsqfeqayqlvrkiagevsrseawdvarELLRR 504

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   350 GSDGAASSYQLKQLE------EQNARLKDALVRMRD---------LSSSE--KQEHVKLQKLMEKKNQELEVVRQQRERL 412
Cdd:PRK04863  505 LREQRHLAEQLQQLRmrlselEQRLRQQQRAERLLAefckrlgknLDDEDelEQLQEELEARLESLSESVSEARERRMAL 584

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   413 QEELSQAESTIDELKEQVDAALGAEEMVEmltdrnlnleekvrELRETVGDLEAMNEMNDELQENARETELELREQLDMA 492
Cdd:PRK04863  585 RQQLEQLQARIQRLAARAPAWLAAQDALA--------------RLREQSGEEFEDSQDVTEYMQQLLERERELTVERDEL 650

                         330
                  ....*....|..
gi 13259510   493 GARVREAQKRVE 504
Cdd:PRK04863  651 AARKQALDEEIE 662
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 206-438 8.20e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 52.91  E-value: 8.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  206 AVPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKE 285
Cdd:COG3883   14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA---ELEALQAEIDKLQAEIAEAEAEIEERREELGE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  286 ALeakeRYMEEMADTADAIEMATLDKEMAE--ERAESLQQEVEALKERVDELTTDLEilkaeieekgsdgaassyqlkQL 363
Cdd:COG3883   91 RA----RALYRSGGSVSYLDVLLGSESFSDflDRLSALSKIADADADLLEELKADKA---------------------EL 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13259510  364 EEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEE 438
Cdd:COG3883  146 EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 282-533 8.61e-07

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 53.90  E-value: 8.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    282 EAKEALEAKERYMEEMADTADAIEM-ATLDKEMAEERAESLQQEVE-ALKERVDELTTDLEILKAEIEEKGS----DGAA 355
Cdd:TIGR01612 1487 ELKEHIDKSKGCKDEADKNAKAIEKnKELFEQYKKDVTELLNKYSAlAIKNKFAKTKKDSEIIIKEIKDAHKkfilEAEK 1566

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    356 SSYQLKQLEEQNARLKDalvrmrDLSSSEKQEH--VKLQKLMEKKNQELEVVRQQRERLQEELSQAES--------TID- 424
Cdd:TIGR01612 1567 SEQKIKEIKKEKFRIED------DAAKNDKSNKaaIDIQLSLENFENKFLKISDIKKKINDCLKETESiekkissfSIDs 1640

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    425 ---ELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAM-NEMNDE-------LQENARETELELREQLDMAG 493
Cdd:TIGR01612 1641 qdtELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIeIDVDQHkknyeigIIEKIKEIAIANKEEIESIK 1720

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 13259510    494 ARVREAQKRVEAAQET------------------VAD-YQQTIKKYRQLTAHLQDVNRE 533
Cdd:TIGR01612 1721 ELIEPTIENLISSFNTndlegidpnekleeynteIGDiYEEFIELYNIIAGCLETVSKE 1779
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 211-521 9.91e-07

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 53.30  E-value: 9.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    211 PSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKL-----------KELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEA 279
Cdd:pfam12128  593 PEWAASEEELRERLDKAEEALQSAREKQAAAEEQLvqangelekasREETFARTALKNARLDLRRLFDEKQSEKDKKNKA 672

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    280 RKEAKEALEAKERYMEEMADTADAIEMATLDkEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAAssyQ 359
Cdd:pfam12128  673 LAERKDSANERLNSLEAQLKQLDKKHQAWLE-EQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKA---E 748

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    360 LKQLEEQNARLKDAL----VRMRDLSSSEKQEHVKLQKLmEKKNQEL--------EVVRQQRERLQEELSQAESTIDELK 427
Cdd:pfam12128  749 LKALETWYKRDLASLgvdpDVIAKLKREIRTLERKIERI-AVRRQEVlryfdwyqETWLQRRPRLATQLSNIERAISELQ 827

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    428 EQvdaaLGAEEMVEMLTDRNLNLEEKVRE-----LRETVGDLEAMNEMNDELQE--NARETELELREQLDMAGARVREAQ 500
Cdd:pfam12128  828 QQ----LARLIADTKLRRAKLEMERKASEkqqvrLSENLRGLRCEMSKLATLKEdaNSEQAQGSIGERLAQLEDLKLKRD 903

                          330       340
                   ....*....|....*....|.
gi 13259510    501 KRVEAAQETVADYQQTIKKYR 521
Cdd:pfam12128  904 YLSESVKKYVEHFKNVIADHS 924
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 262-441 1.15e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 52.52  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  262 KSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDEL------ 335
Cdd:COG3883   18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyr 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  336 ----TTDLEILkaeieeKGSDGAAS----SYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEvvrQ 407
Cdd:COG3883   98 sggsVSYLDVL------LGSESFSDfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE---A 168

                        170       180       190
                 ....*....|....*....|....*....|....
gi 13259510  408 QRERLQEELSQAESTIDELKEQVDAALGAEEMVE 441
Cdd:COG3883  169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 220-504 1.28e-06

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 52.80  E-value: 1.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    220 LRAQVRDLEEKLET--LRLKRAEDKAKL--KELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARK---------EAKEA 286
Cdd:pfam05483  354 FEATTCSLEELLRTeqQRLEKNEDQLKIitMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKlldekkqfeKIAEE 433

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    287 LEAKERYM--------EEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSY 358
Cdd:pfam05483  434 LKGKEQELifllqareKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTL 513

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    359 QLKQLEEqnarlkdalvrmrDLSSSEKQEHVKLQK---LMEKKNQ---ELEVVR----QQRERLQEELSQAESTIDELKE 428
Cdd:pfam05483  514 ELKKHQE-------------DIINCKKQEERMLKQienLEEKEMNlrdELESVReefiQKGDEVKCKLDKSEENARSIEY 580

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    429 QVdaaLGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEM------NDELQENARET-----ELELREQLDMAGARVR 497
Cdd:pfam05483  581 EV---LKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAlkkkgsAENKQLNAYEIkvnklELELASAKQKFEEIID 657


                   ....*..
gi 13259510    498 EAQKRVE 504
Cdd:pfam05483  658 NYQKEIE 664
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
217-344 2.11e-06

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 50.21  E-value: 2.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  217 EEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLE-QVQEWkskmqEQQADLQrrLKEARKE-AKEALEAKERYM 294
Cdd:COG1842   25 EKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEaEAEKW-----EEKARLA--LEKGREDlAREALERKAELE 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 13259510  295 EEMADTADAIematldkEMAEERAESLQQEVEALKERVDELTTDLEILKA 344
Cdd:COG1842   98 AQAEALEAQL-------AQLEEQVEKLKEALRQLESKLEELKAKKDTLKA 140
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 214-487 2.44e-06

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 52.28  E-value: 2.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    214 SKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKM----QEQQADLQRRLKEARKEAKEALEA 289
Cdd:pfam02463  292 AKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKElkelEIKREAEEEEEEELEKLQEKLEQL 371

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    290 KERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEI--EEKGSDGAASSYQLKQLEEQN 367
Cdd:pfam02463  372 EEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEleILEEEEESIELKQGKLTEEKE 451

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    368 ARLKDALVRMRDLSSSEKQEHvklqklmEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRN 447
Cdd:pfam02463  452 ELEKQELKLLKDELELKKSED-------LLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRI 524

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 13259510    448 LNLEEKVRELRETVGDLEAMNEMNDELQENARETELELRE 487
Cdd:pfam02463  525 ISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQ 564
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 247-539 2.50e-06

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 52.05  E-value: 2.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    247 ELEKHKIQLEQVQEWKSKMQEQQadlqrrlKEARKEAKEALEAKERYMEEMADtadaiematldkemaeeRAESLQQEVE 326
Cdd:pfam05557    3 ELIESKARLSQLQNEKKQMELEH-------KRARIELEKKASALKRQLDRESD-----------------RNQELQKRIR 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    327 ALKERVDELTtdlEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDAlvrmRDLSSSEKQEHVKLQKLMEKKNQEL---- 402
Cdd:pfam05557   59 LLEKREAEAE---EALREQAELNRLKKKYLEALNKKLNEKESQLADA----REVISCLKNELSELRRQIQRAELELqstn 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    403 ---EVVRQQRERLQEELSQAESTIDELKEQVDAalgaeemvemLTDRNLNLEEKVRELRETVGDLEAMNEMNDELqenAR 479
Cdd:pfam05557  132 selEELQERLDLLKAKASEAEQLRQNLEKQQSS----------LAEAEQRIKELEFEIQSQEQDSEIVKNSKSEL---AR 198

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13259510    480 ETELE-LREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQE 539
Cdd:pfam05557  199 IPELEkELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQ 259
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 226-490 2.58e-06

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 51.78  E-value: 2.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    226 DLEEKLETLRLKRAedKAKLKELEkhkiqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYME---------- 295
Cdd:pfam06160   71 EAEELNDKYRFKKA--KKALDEIE------ELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRElrktllanrf 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    296 EMADTADAIE--MATLDKE---------------------MAEERAESLQQEVEALKERVDELTTD----LEILKAEIEE 348
Cdd:pfam06160  143 SYGPAIDELEkqLAEIEEEfsqfeeltesgdylearevleKLEEETDALEELMEDIPPLYEELKTElpdqLEELKEGYRE 222

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    349 KGSDGAASSY-----QLKQLEEQNARLKDALVRMRDLSSSEKQEHVK-----LQKLMEKKNQELEVVRQQRERLQEELSQ 418
Cdd:pfam06160  223 MEEEGYALEHlnvdkEIQQLEEQLEENLALLENLELDEAEEALEEIEeridqLYDLLEKEVDAKKYVEKNLPEIEDYLEH 302

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    419 AESTIDELKEQVD--------------AALGAEEMVEMLTDRNLNLEEKVRE-----------LRETVGDLEAMNEMNDE 473
Cdd:pfam06160  303 AEEQNKELKEELErvqqsytlneneleRVRGLEKQLEELEKRYDEIVERLEEkevayselqeeLEEILEQLEEIEEEQEE 382

                          330       340
                   ....*....|....*....|
gi 13259510    474 LQE---NARETELELREQLD 490
Cdd:pfam06160  383 FKEslqSLRKDELEAREKLD 402
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 223-330 2.64e-06

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 51.75  E-value: 2.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   223 QVRDLEEKLETLRlKRAEDKAKlkELEKHKIQLEQV-QEWKSKMQEQQADLQRRLKEARKEAKEAL-EAKE--------- 291
Cdd:PRK00409  517 KLNELIASLEELE-RELEQKAE--EAEALLKEAEKLkEELEEKKEKLQEEEDKLLEEAEKEAQQAIkEAKKeadeiikel 593

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 13259510   292 RYMEEMADTA----DAIEMATLDKEMAEERAESLQQEVEALKE 330
Cdd:PRK00409  594 RQLQKGGYASvkahELIEARKRLNKANEKKEKKKKKQKEKQEE 636
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 210-547 3.00e-06

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 51.75  E-value: 3.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    210 LPSPSKEEE-GLRAQVRDLEEKLETLrlkraedKAKLKELEKHKIQLEQVQEWKSKMQEQQADLqrrlkEARKEAKEALE 288
Cdd:pfam10174  172 LPKKSGEEDwERTRRIAEAEMQLGHL-------EVLLDQKEKENIHLREELHRRNQLQPDPAKT-----KALQTVIEMKD 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    289 AKERYMEEM-ADTADAIEMATLDKEM-AEERAESLQQeVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQ 366
Cdd:pfam10174  240 TKISSLERNiRDLEDEVQMLKTNGLLhTEDREEEIKQ-MEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQ 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    367 NAR-------LKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgAEEM 439
Cdd:pfam10174  319 NSDckqhievLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDV---KERK 395

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    440 VEMLTDRNLNLEEKVR-------ELRETVGDLE--------AMNEMNDELQENARETElELREQldmagaRVREAQKRve 504
Cdd:pfam10174  396 INVLQKKIENLQEQLRdkdkqlaGLKERVKSLQtdssntdtALTTLEEALSEKERIIE-RLKEQ------REREDRER-- 466

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 13259510    505 aaQETVADYQQTIKKYRQLTAHLQdvnRELTNQQEASVERQQQ 547
Cdd:pfam10174  467 --LEELESLKKENKDLKEKVSALQ---PELTEKESSLIDLKEH 504
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 317-461 3.36e-06

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 51.62  E-value: 3.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  317 RAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLME 396
Cdd:COG0542  405 EIDSKPEELDELERRLEQLEIEKEALKKEQDE------ASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKE 478

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13259510  397 KKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAE-----------EMVEMLTDRNLNLEEkvrELRETV 461
Cdd:COG0542  479 ELEQRYGKIPELEKELAELEEELAELAPLLREEVTEEDIAEvvsrwtgipvgKLLEGEREKLLNLEE---ELHERV 551
PRK12704 PRK12704
phosphodiesterase; Provisional
 227-365 3.67e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 51.32  E-value: 3.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   227 LEEKLETLRLKRAEDKAK--LKELEK--HKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEaLEAKERYMEEmadtad 302
Cdd:PRK12704   24 VRKKIAEAKIKEAEEEAKriLEEAKKeaEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQK-LEKRLLQKEE------ 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13259510   303 aiemaTLDKEMaeERAESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgaaSSYQLKQLEE 365
Cdd:PRK12704   97 -----NLDRKL--ELLEKREEELEKKEKELEQKQQELEKKEEELEEL------IEEQLQELER 146
PRK11281 PRK11281
mechanosensitive channel MscK;
205-492 3.70e-06

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 51.45  E-value: 3.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   205 GAVPPLPSpskeEEGLRAQVrdleEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMqeqqADLQRRLKEARKEAK 284
Cdd:PRK11281   30 ASNGDLPT----EADVQAQL----DALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEET----EQLKQQLAQAPAKLR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   285 EALEAKERYMEEmADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLe 364
Cdd:PRK11281   98 QAQAELEALKDD-NDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQI- 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   365 eqNARLKDALVRMRDLSSSEKQ----EHVKLQKLMEKKNQELEVVRQ-------QRE-------RLQEE----------- 415
Cdd:PRK11281  176 --RNLLKGGKVGGKALRPSQRVllqaEQALLNAQNDLQRKSLEGNTQlqdllqkQRDyltariqRLEHQlqllqeainsk 253

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13259510   416 -LSQAESTIDELKEQVDAA-LGAEEMVEMLTDRNLNLEEKVrelretvgdLEAMNEMNDELQENareteLELREQLDMA 492
Cdd:PRK11281  254 rLTLSEKTVQEAQSQDEAArIQANPLVAQELEINLQLSQRL---------LKATEKLNTLTQQN-----LRVKNWLDRL 318
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 314-552 3.95e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.60  E-value: 3.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  314 AEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGsdgaassyqlKQLEEQNARLKDAlvrmrdlssseKQEHVKLQK 393
Cdd:COG3883   14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELN----------EEYNELQAELEAL-----------QAEIDKLQA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  394 LMEKKNQELEvvrQQRERLQEELSQA------ESTIDELK--EQVDAALGAEEMVEMLTDRNLNLeekVRELRETVGDLE 465
Cdd:COG3883   73 EIAEAEAEIE---ERREELGERARALyrsggsVSYLDVLLgsESFSDFLDRLSALSKIADADADL---LEELKADKAELE 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  466 AMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQ 545
Cdd:COG3883  147 AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226


                 ....*..
gi 13259510  546 QQPPPET 552
Cdd:COG3883  227 AAAAAAA 233
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 263-490 4.59e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 4.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  263 SKMQEQQADLQRRLKEARKEAKEALEAKERYMEEmadTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEIL 342
Cdd:COG1196  580 DKIRARAALAAALARGAIGAAVDLVASDLREADA---RYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  343 KAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEST 422
Cdd:COG1196  657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13259510  423 IDELKEQVDAALGAEEMVEMLTDRNLN-LEEKVRELREtvgDLEAMNEMN----DELQEnARETELELREQLD 490
Cdd:COG1196  737 LLEELLEEEELLEEEALEELPEPPDLEeLERELERLER---EIEALGPVNllaiEEYEE-LEERYDFLSEQRE 805
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 216-419 5.43e-06

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 49.26  E-value: 5.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    216 EEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQ----VQEWKSKMQEQQADLQRRLKEARKEAKEALEake 291
Cdd:pfam00261   37 EVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERgrkvLENRALKDEEKMEILEAQLKEAKEIAEEADR--- 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    292 RYMEemadTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEiEEKGSDgAASSYQLkQLEEQNARLK 371
Cdd:pfam00261  114 KYEE----VARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEAS-EEKASE-REDKYEE-QIRFLTEKLK 186

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 13259510    372 DALVRMRDlsssEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQA 419
Cdd:pfam00261  187 EAETRAEF----AERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQT 230
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 220-583 5.45e-06

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: 50.94  E-value: 5.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    220 LRAQVRDLEEKLETL--RLKRAEDKAKLKELEKHKIQlEQVQEWKSKMQEQQADLQRRLKEarkeaKEALEAKERYMEEm 297
Cdd:pfam01576   66 LAARKQELEEILHELesRLEEEEERSQQLQNEKKKMQ-QHIQDLEEQLDEEEAARQKLQLE-----KVTTEAKIKKLEE- 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    298 adtadaiematlDKEMAEERAESLQQEVEALKERVDELTTDLeilkAEIEEKgsdgAASSYQLKQLEEqnARLKDALVRM 377
Cdd:pfam01576  139 ------------DILLLEDQNSKLSKERKLLEERISEFTSNL----AEEEEK----AKSLSKLKNKHE--AMISDLEERL 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    378 RdlssSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmvEMLTDRNlNLEEKVREL 457
Cdd:pfam01576  197 K----KEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE--EETAQKN-NALKKIREL 269

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    458 RETVGDLEAMNEMNDELQENARETELELREQLdmagarvrEAQK-RVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTN 536
Cdd:pfam01576  270 EAQISELQEDLESERAARNKAEKQRRDLGEEL--------EALKtELEDTLDTTAAQQELRSKREQEVTELKKALEEETR 341

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 13259510    537 QQEASVERQQQpppetfdfkikfaetkAHAKAIEMELRQMEVAQANR 583
Cdd:pfam01576  342 SHEAQLQEMRQ----------------KHTQALEELTEQLEQAKRNK 372
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 926-1046 5.58e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 5.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  926 LRAAALRAEIT--DAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSA---AKDADERIEKVQTRLEE 1000
Cdd:COG1196  213 ERYRELKEELKelEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELrleLEELELELEEAQAEEYE 292

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 13259510 1001 TQALLRKKEKEF---EETMDALQADIDQLEAEKAELKQRLNSQSKRTIE 1046
Cdd:COG1196  293 LLAELARLEQDIarlEERRRELEERLEELEEELAELEEELEELEEELEE 341
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 925-1046 6.18e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 6.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  925 ELRAAALRAEITDAEGlglKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDAdERIEKVQTRLEETQAL 1004
Cdd:COG1196  252 EAELEELEAELAELEA---ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR-RELEERLEELEEELAE 327

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 13259510 1005 LRKKEKEFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIE 1046
Cdd:COG1196  328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 924-1036 6.28e-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: 48.77  E-value: 6.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  924 VELRAAALRAEITDAE----GLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSA---------------- 983
Cdd:COG1579   22 LEHRLKELPAELAELEdelaALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyealqkeiesl 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13259510  984 ----------AKDADERIEKVQTRLEETQALLRKKEKEFEETMDALQADIDQLEAEKAELKQR 1036
Cdd:COG1579  102 krrisdledeILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 221-534 6.57e-06

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 50.24  E-value: 6.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    221 RAQVRDLEEKLETLR-LKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEaKERYMEEMAD 299
Cdd:pfam06160    9 YKEIDELEERKNELMnLPVQEELSKVKKLNLTGETQEKFEEWRKKWDDIVTKSLPDIEELLFEAEELND-KYRFKKAKKA 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    300 TADAiematldkemaEERAESLQQEVEALKERVDELTTDLEILKAEIEE---------------KGSDGAAssyqLKQLE 364
Cdd:pfam06160   88 LDEI-----------EELLDDIEEDIKQILEELDELLESEEKNREEVEElkdkyrelrktllanRFSYGPA----IDELE 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    365 EQNARLKDALVRMRDLSSSekQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEST----IDELKEqvdaalGAEEMV 440
Cdd:pfam06160  153 KQLAEIEEEFSQFEELTES--GDYLEAREVLEKLEEETDALEELMEDIPPLYEELKTElpdqLEELKE------GYREME 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    441 EM---LTDRNL-----NLEEKVRELRETV--GDLEAMNEMNDELQENAreteLELREQLdmagarvreaQKRVEAAQEtv 510
Cdd:pfam06160  225 EEgyaLEHLNVdkeiqQLEEQLEENLALLenLELDEAEEALEEIEERI----DQLYDLL----------EKEVDAKKY-- 288

                          330       340
                   ....*....|....*....|....
gi 13259510    511 adYQQTIKKYRQLTAHLQDVNREL 534
Cdd:pfam06160  289 --VEKNLPEIEDYLEHAEEQNKEL 310
PTZ00121 PTZ00121
MAEBL; Provisional
 215-581 8.85e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.52  E-value: 8.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   215 KEEEGLRAQ-VRDLEEKLETLRLKRAEDkAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKeAKEALEAKERY 293
Cdd:PTZ00121 1123 KAEDARKAEeARKAEDARKAEEARKAED-AKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRK-AEELRKAEDAR 1200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   294 MEEMADTADaiematldkemAEERAESLQQEVEAlkERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEqnARLKDA 373
Cdd:PTZ00121 1201 KAEAARKAE-----------EERKAEEARKAEDA--KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEE--ARMAHF 1265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   374 LVRMRDLSSSEKQEHVKLQKLMEKKNqelevvrqqrerlQEELSQAEST--IDELKEQVDAALGAEEmvemLTDRNLNLE 451
Cdd:PTZ00121 1266 ARRQAAIKAEEARKADELKKAEEKKK-------------ADEAKKAEEKkkADEAKKKAEEAKKADE----AKKKAEEAK 1328

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   452 EKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQ---ETVADYQQTIKKYRQLTAHLQ 528
Cdd:PTZ00121 1329 KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKkkaEEKKKADEAKKKAEEDKKKAD 1408

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 13259510   529 DVNRELTNQQEASVERQQQPPPETFDFKIKFAETKahAKAIEMELRQMEVAQA 581
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA--KKADEAKKKAEEAKKA 1459
PRK01156 PRK01156
chromosome segregation protein; Provisional
 218-531 1.07e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 49.90  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   218 EGLRAQVRDLEE---KLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQ---EQQADLQRRLKEARKEAKEALEAKE 291
Cdd:PRK01156  315 SNIDAEINKYHAiikKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNsylKSIESLKKKIEEYSKNIERMSAFIS 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   292 RYMEEMADTADAI--EMATLDKEMAE--ERAESLQQEVEALKERVDELTTDLEILKA----------------------- 344
Cdd:PRK01156  395 EILKIQEIDPDAIkkELNEINVKLQDisSKVSSLNQRIRALRENLDELSRNMEMLNGqsvcpvcgttlgeeksnhiinhy 474

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   345 ------------EIEEKGSDGAASSYQLKQLEEQNA------------RLKDALVRMRDLSSSE---KQEHVKLQKLMEK 397
Cdd:PRK01156  475 nekksrleekirEIEIEVKDIDEKIVDLKKRKEYLEseeinksineynKIESARADLEDIKIKInelKDKHDKYEEIKNR 554

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   398 -KNQELEVVRQQRERLQEELSQA--------ESTIDELKEQV-DAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEam 467
Cdd:PRK01156  555 yKSLKLEDLDSKRTSWLNALAVIslidietnRSRSNEIKKQLnDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLN-- 632

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13259510   468 NEMNdELQENARETElELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVN 531
Cdd:PRK01156  633 NKYN-EIQENKILIE-KLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAK 694
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 212-335 1.07e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  212 SPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKE 291
Cdd:COG1196  657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 13259510  292 RYMEEMADTADAIEMATLDKEMAEERAEsLQQEVEALKERVDEL 335
Cdd:COG1196  737 LLEELLEEEELLEEEALEELPEPPDLEE-LERELERLEREIEAL 779
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 215-428 1.20e-05

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 49.97  E-value: 1.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    215 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQE-WKSKMQEQQADLQRRLKEARKEAKEALEAKErY 293
Cdd:TIGR00618  683 QKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSsLGSDLAAREDALNQSLKELMHQARTVLKART-E 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    294 MEEMADTADAIEMATLDKEmaeeraESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGaassyqlkqleEQNARLKDA 373
Cdd:TIGR00618  762 AHFNNNEEVTAALQTGAEL------SHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSD-----------EDILNLQCE 824

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 13259510    374 LVrmrdlssseKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKE 428
Cdd:TIGR00618  825 TL---------VQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK 870
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 210-570 1.32e-05

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 49.66  E-value: 1.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    210 LPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKE---- 285
Cdd:TIGR00606  579 LHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQraml 658

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    286 --ALEAKERYMEEMAD--------------TADAIEMATLDKE----MAEERAESLQQEVEALKERVDELTTDLEILKAE 345
Cdd:TIGR00606  659 agATAVYSQFITQLTDenqsccpvcqrvfqTEAELQEFISDLQsklrLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSI 738

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    346 IEEKgsdgaasSYQLKQLEEQNARLKDALVRMR-DLSSSEKQEHVKLQKLMEKKNQELEVVRQQreRLQEELSQAESTID 424
Cdd:TIGR00606  739 IDLK-------EKEIPELRNKLQKVNRDIQRLKnDIEEQETLLGTIMPEEESAKVCLTDVTIME--RFQMELKDVERKIA 809

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    425 ELKEQVDAALGAEEMVEMltdrNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELRE------QLDMAGARVRE 498
Cdd:TIGR00606  810 QQAAKLQGSDLDRTVQQV----NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNElkseklQIGTNLQRRQQ 885

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13259510    499 AQKRVEAAQETVADYQQTIKKYR-------QLTAHLQDVNRELTNQQEASVERQQQpppETFDFKIKFAETKAHAKAIE 570
Cdd:TIGR00606  886 FEEQLVELSTEVQSLIREIKDAKeqdspleTFLEKDQQEKEELISSKETSNKKAQD---KVNDIKEKVKNIHGYMKDIE 961
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 268-507 1.32e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.06  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  268 QQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTtdlEILKAEIE 347
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR---EELGERAR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  348 EKGSDGAASSYQLKQLEEQNarLKDALVRMRDLSSSEKQEhvklQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELK 427
Cdd:COG3883   94 ALYRSGGSVSYLDVLLGSES--FSDFLDRLSALSKIADAD----ADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  428 EQVDAALGAEEMVEMLTDRnlnLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQ 507
Cdd:COG3883  168 AAKAELEAQQAEQEALLAQ---LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 238-437 1.52e-05

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: 49.57  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  238 RAEDKAK--LKELEKHKIQLEQVQEWKSKMQE------QQADLQRRLKEARKEAKEALEAKERyMEEMADTADAiEMATL 309
Cdd:COG3096  492 QAWQTARelLRRYRSQQALAQRLQQLRAQLAEleqrlrQQQNAERLLEEFCQRIGQQLDAAEE-LEELLAELEA-QLEEL 569

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  310 DKEMAE--ERAESLQQEVEALKERVDELTTdleilKAEIEEKGSDgaassyQLKQLEEQ-NARLKDalvrmrdlsSSEKQ 386
Cdd:COG3096  570 EEQAAEavEQRSELRQQLEQLRARIKELAA-----RAPAWLAAQD------ALERLREQsGEALAD---------SQEVT 629

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13259510  387 EHvkLQKLMEKK---NQELEVVRQQRERLQ---EELSQAESTID----ELKEQVDAALGAE 437
Cdd:COG3096  630 AA--MQQLLEREreaTVERDELAARKQALEsqiERLSQPGGAEDprllALAERLGGVLLSE 688
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
 305-541 1.83e-05

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.


Pssm-ID: 462861 [Multi-domain]  Cd Length: 302  Bit Score: 48.03  E-value: 1.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    305 EMATLDKEMA--EERAESLQQEVEALKERVDELTT---DLEILKAEIEEkgsdgaassyQLKQLEEQNARLKDALVRMRD 379
Cdd:pfam09728   33 EMKRLQKDLKklKKKQDQLQKEKDQLQSELSKAILaksKLEKLCRELQK----------QNKKLKEESKKLAKEEEEKRK 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    380 LSSSEKQEHVK-LQKLMEKKNQELEVVRQQRERLQEELsqaESTID--ELKE-QVDAALGAEEMVEMLTDRNLNLEEKVR 455
Cdd:pfam09728  103 ELSEKFQSTLKdIQDKMEEKSEKNNKLREENEELREKL---KSLIEqyELRElHFEKLLKTKELEVQLAEAKLQQATEEE 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    456 ELRETVGDLEAMNEMNDELQEnARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELT 535
Cdd:pfam09728  180 EKKAQEKEVAKARELKAQVQT-LSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTTFKKEMEKMSKKIKKLEKENLTWK 258


                   ....*.
gi 13259510    536 NQQEAS 541
Cdd:pfam09728  259 RKWEKS 264
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 223-539 1.83e-05

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 49.20  E-value: 1.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    223 QVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERymeemadTAD 302
Cdd:TIGR00618  373 QQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAEL-------CAA 445

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    303 AIEMATLDKEMAEERAESLQQeveALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSS 382
Cdd:TIGR00618  446 AITCTAQCEKLEKIHLQESAQ---SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDN 522

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    383 SE---------KQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEST-------IDELKEQVDAALGAEEMVEMLTDR 446
Cdd:TIGR00618  523 PGpltrrmqrgEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSfsiltqcDNRSKEDIPNLQNITVRLQDLTEK 602

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    447 NLNLEEKVR--------ELRETVGDLEAMNEMNDELQENARE------TELEL-REQLDMAGARVREAQKRVEAAQETVA 511
Cdd:TIGR00618  603 LSEAEDMLAceqhallrKLQPEQDLQDVRLHLQQCSQELALKltalhaLQLTLtQERVREHALSIRVLPKELLASRQLAL 682

                          330       340
                   ....*....|....*....|....*...
gi 13259510    512 DYQQTikKYRQLTAHLQDVNRELTNQQE 539
Cdd:TIGR00618  683 QKMQS--EKEQLTYWKEMLAQCQTLLRE 708
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 217-393 1.87e-05

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 48.27  E-value: 1.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    217 EEGLRAQVRDLEEKLETLRLKR-AEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARK---EAKEALEAKER 292
Cdd:pfam15905  147 EDGTQKKMSSLSMELMKLRNKLeAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKekiEEKSETEKLLE 226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    293 YMEEMADTADAIEMATLD----KEMAEERA---ESLQQEVEA----LKERVDELTTDLEILKAEIEEKgsdgaassyqLK 361
Cdd:pfam15905  227 YITELSCVSEQVEKYKLDiaqlEELLKEKNdeiESLKQSLEEkeqeLSKQIKDLNEKCKLLESEKEEL----------LR 296

                          170       180       190
                   ....*....|....*....|....*....|..
gi 13259510    362 QLEEQNARLKDALVRMRDLSSSEKQEHVKLQK 393
Cdd:pfam15905  297 EYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 226-592 1.91e-05

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 49.06  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   226 DLEEKLETLRLKRAedKAKLKELEkhkiqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYmEEM-------- 297
Cdd:PRK04778   90 EAEELNDKFRFRKA--KHEINEIE------SLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLY-RELrksllanr 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   298 ---ADTADAIE--MATLDKEMAEerAESLQQE---------VEALKERVDELTTDLEILKAEIEEKGSDGAAssyQLKQL 363
Cdd:PRK04778  161 fsfGPALDELEkqLENLEEEFSQ--FVELTESgdyveareiLDQLEEELAALEQIMEEIPELLKELQTELPD---QLQEL 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   364 EEQNARLKDA---------LVRMRDLssseKQEHVKLQKLMEkkNQELEVVRQQRERLQEELSQ--------------AE 420
Cdd:PRK04778  236 KAGYRELVEEgyhldhldiEKEIQDL----KEQIDENLALLE--ELDLDEAEEKNEEIQERIDQlydilerevkarkyVE 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   421 STIDELKEQVDAAlgaEEMVEML---TDR-------NLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLD 490
Cdd:PRK04778  310 KNSDTLPDFLEHA---KEQNKELkeeIDRvkqsytlNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELE 386

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   491 MAGARVREAQKRVEAAQETVADY-------QQTIKKYRQLtahLQDVNREltnqqeasVERQQQPP-PEtfDFKIKFAET 562
Cdd:PRK04778  387 EILKQLEEIEKEQEKLSEMLQGLrkdeleaREKLERYRNK---LHEIKRY--------LEKSNLPGlPE--DYLEMFFEV 453

                         410       420       430
                  ....*....|....*....|....*....|..
gi 13259510   563 KAHAKAIEMEL--RQMEVAQANRHMSLLTAFM 592
Cdd:PRK04778  454 SDEIEALAEELeeKPINMEAVNRLLEEATEDV 485
PRK01156 PRK01156
chromosome segregation protein; Provisional
 220-574 2.25e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 48.74  E-value: 2.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   220 LRAQVRD---LEEKLETLRLKRAEDKAKLKELEK-HKIQLEQVQEWKSKMQEQQADLQrRLKEARKEAKEALEAKERYME 295
Cdd:PRK01156  178 LRAEISNidyLEEKLKSSNLELENIKKQIADDEKsHSITLKEIERLSIEYNNAMDDYN-NLKSALNELSSLEDMKNRYES 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   296 EMADTADAIEMATLD----KEMAEERAESLQQEVEALKERVDE---LTTDLEILKAEIEekGSDGAASSYQ--LKQLEEQ 366
Cdd:PRK01156  257 EIKTAESDLSMELEKnnyyKELEERHMKIINDPVYKNRNYINDyfkYKNDIENKKQILS--NIDAEINKYHaiIKKLSVL 334

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   367 NARLKDALV---RMRDLS---SSEKQEHVKLQKLM---EKKNQELEVVRQQRERLQEELSQAESTidelkeqvdAALGAE 437
Cdd:PRK01156  335 QKDYNDYIKkksRYDDLNnqiLELEGYEMDYNSYLksiESLKKKIEEYSKNIERMSAFISEILKI---------QEIDPD 405

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   438 EMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENAR-----------ETELELREQLDMAGARVREAQKRVEAA 506
Cdd:PRK01156  406 AIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcGTTLGEEKSNHIINHYNEKKSRLEEKI 485

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13259510   507 QETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETK-AHAKAIEMELR 574
Cdd:PRK01156  486 REIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKdKHDKYEEIKNR 554
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 214-429 2.64e-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: 48.91  E-value: 2.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    214 SKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKhkiQLEqvqewksKMQEQQADLQRRLKEARKEAKEaLEAKERY 293
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE---ELE-------ELEAALRDLESRLGDLKKERDE-LEAQLRE 900

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    294 MEemadtaDAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyqLKQLEEQNARLKDA 373
Cdd:TIGR02169  901 LE------RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS--------LEDVQAELQRVEEE 966

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 13259510    374 LVRMRDLSSSEKQEHvklqKLMEKKNQELEvvrQQRERLQEELSQAESTIDELKEQ 429
Cdd:TIGR02169  967 IRALEPVNMLAIQEY----EEVLKRLDELK---EKRAKLEEERKAILERIEEYEKK 1015
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
235-518 2.76e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.97  E-value: 2.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  235 RLKRAEDKAKL---KELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDK 311
Cdd:COG4372    3 RLGEKVGKARLslfGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  312 EMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKL 391
Cdd:COG4372   83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK-------ERQDLEQQRKQLEAQIAELQSEIAEREEELKEL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  392 QKLMEKKNQELEVVRQQRERLQEELSQAestidELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMN 471
Cdd:COG4372  156 EEQLESLQEELAALEQELQALSEAEAEQ-----ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAK 230

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 13259510  472 DELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIK 518
Cdd:COG4372  231 LGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEE 277
PRK12705 PRK12705
hypothetical protein; Provisional
 261-424 3.00e-05

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 48.17  E-value: 3.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   261 WKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAiematLDKEMAEERAESLQQEVEALKERVDELTTDLE 340
Cdd:PRK12705   24 LLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERN-----QQRQEARREREELQREEERLVQKEEQLDARAE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   341 ILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQehvklQKLMEKKNQELEVVRQQRERLQEELSQAE 420
Cdd:PRK12705   99 KLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQAR-----KLLLKLLDAELEEEKAQRVKKIEEEADLE 173


                  ....
gi 13259510   421 STID 424
Cdd:PRK12705  174 AERK 177
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 226-554 3.13e-05

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 48.43  E-value: 3.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    226 DLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEW---KSKMQEQQADLQRRLKEARKEAKEaLEAKERYMEEmadTAD 302
Cdd:TIGR00618  209 CTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYltqKREAQEEQLKKQQLLKQLRARIEE-LRAQEAVLEE---TQE 284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    303 AIEMATLDKEMAEEraeslQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQnarlkdalvrmRDLSS 382
Cdd:TIGR00618  285 RINRARKAAPLAAH-----IKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ-----------RRLLQ 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    383 SEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAES-TIDELKEQVDAALGAEEMVEMLTDRNLNLEEkvRELRETV 461
Cdd:TIGR00618  349 TLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQkTTLTQKLQSLCKELDILQREQATIDTRTSAF--RDLQGQL 426

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    462 GDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEAS 541
Cdd:TIGR00618  427 AHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPL 506

                          330
                   ....*....|...
gi 13259510    542 VERQQQPPPETFD 554
Cdd:TIGR00618  507 CGSCIHPNPARQD 519
PRK11281 PRK11281
mechanosensitive channel MscK;
270-545 3.23e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 48.37  E-value: 3.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   270 ADLQRRLKEArKEAKEALEAKERYMEEMADTadaieMATLDK-EMAEERAESLQQEVEALKERVDELTTDLEILKAEIEE 348
Cdd:PRK11281   39 ADVQAQLDAL-NKQKLLEAEDKLVQQDLEQT-----LALLDKiDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   349 KgSDGAASSYQLKQLEEQNARLKDALvrmrdlsssekQEhvkLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKE 428
Cdd:PRK11281  113 E-TRETLSTLSLRQLESRLAQTLDQL-----------QN---AQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRN 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   429 QVDAALGAEEmvemltdrNLNLEEKVRELRETVGdLEAMNEMN-DELQENARETELeLREQLDMAGARVREAQKRVEAAQ 507
Cdd:PRK11281  178 LLKGGKVGGK--------ALRPSQRVLLQAEQAL-LNAQNDLQrKSLEGNTQLQDL-LQKQRDYLTARIQRLEHQLQLLQ 247

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 13259510   508 ETV-----ADYQQTIKKYRQltahLQDVNRELTN---QQEASVERQ 545
Cdd:PRK11281  248 EAInskrlTLSEKTVQEAQS----QDEAARIQANplvAQELEINLQ 289
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 215-512 3.62e-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: 48.19  E-value: 3.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    215 KEEEGLRAQVRDLEEKLETLRLK-RAEDKAKLKELEKHKIQLEQVQEWKSKMqEQQADLQRRLKEARKEAKEALEAKERY 293
Cdd:pfam15921  419 RELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQGKNESLEKVSSLTAQL-ESTKEMLRKVVEELTAKKMTLESSERT 497

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    294 MEEMADTADAIEMAT-------------LDKEMAE--------ERAESLQQEVEALKERVDELTTDLEILKAEIE----- 347
Cdd:pfam15921  498 VSDLTASLQEKERAIeatnaeitklrsrVDLKLQElqhlknegDHLRNVQTECEALKLQMAEKDKVIEILRQQIEnmtql 577

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    348 --EKGSDGAASSYQLKQLEEQ--NARL-----------KDALVRMRDLSSSEKQ-EHVKLQKLMEKKNQELEVVRQQRER 411
Cdd:pfam15921  578 vgQHGRTAGAMQVEKAQLEKEinDRRLelqefkilkdkKDAKIRELEARVSDLElEKVKLVNAGSERLRAVKDIKQERDQ 657

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    412 LQEELSQAESTIDELKEQVDAAL-----GAEEMvEMLTDR-NLNLEEKVRELRETVGDLEAMNEMNDelqeNARETELEL 485
Cdd:pfam15921  658 LLNEVKTSRNELNSLSEDYEVLKrnfrnKSEEM-ETTTNKlKMQLKSAQSELEQTRNTLKSMEGSDG----HAMKVAMGM 732

                          330       340
                   ....*....|....*....|....*..
gi 13259510    486 REQLDMAGARVREAQKRVEAAQETVAD 512
Cdd:pfam15921  733 QKQITAKRGQIDALQSKIQFLEEAMTN 759
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
276-431 3.91e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 47.93  E-value: 3.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  276 LKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEeraesLQQEVEALKERVDElttdleiLKAEIEEKgsdgaa 355
Cdd:COG2433  378 IEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRR-----LEEQVERLEAEVEE-------LEAELEEK------ 439

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13259510  356 ssyqlkqlEEQNARLKDALVRMRdlsSSEKQEHvklqklmeKKNQELEVVRQQRERLQEELSQAESTIDELKEQVD 431
Cdd:COG2433  440 --------DERIERLERELSEAR---SEERREI--------RKDREISRLDREIERLERELEEERERIEELKRKLE 496
PHA03247 PHA03247
large tegument protein UL36; Provisional
 101-220 4.02e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 4.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   101 ADTTSPETPDSSASKVLkrEGTDTTAKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGVAGASSSLgPSGSASAGELSS 180
Cdd:PHA03247 2734 ALPAAPAPPAVPAGPAT--PGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESL-PSPWDPADPPAA 2810

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 13259510   181 SEPSTPAQTPLAAPIIPTPVLTSPGAVPPLPSPSKEEEGL 220
Cdd:PHA03247 2811 VLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSL 2850
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 215-488 4.66e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 47.79  E-value: 4.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    215 KEEEGLRAQVRDLEEKLETLR---------LKRAEDKAKLKeLEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEake 285
Cdd:pfam05483  527 KQEERMLKQIENLEEKEMNLRdelesvreeFIQKGDEVKCK-LDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ--- 602

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    286 aLEAKERYMEEMADTADAIEmatldkemAEERAESLQQEVEALKerVDELTTDLEILKAEIEEKgSDGAASSYQLKQLEE 365
Cdd:pfam05483  603 -IENKNKNIEELHQENKALK--------KKGSAENKQLNAYEIK--VNKLELELASAKQKFEEI-IDNYQKEIEDKKISE 670

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    366 QNarlkdaLVRMRDLSSSEKQEHVKLQKLMEKKNQE--------LEVVRQQRERLQEElSQAESTIDELKEQVDAALGAE 437
Cdd:pfam05483  671 EK------LLEEVEKAKAIADEAVKLQKEIDKRCQHkiaemvalMEKHKHQYDKIIEE-RDSELGLYKNKEQEQSSAKAA 743

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 13259510    438 EMVEMLTDRNlnleekvrELRETVGDLEAMNEMNDELQENARETELELREQ 488
Cdd:pfam05483  744 LEIELSNIKA--------ELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
46 PHA02562
endonuclease subunit; Provisional
 220-464 4.88e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 47.70  E-value: 4.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   220 LRAQVRDLEEKLETLRLKRAEDKAKLKELEKHkiqleqVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMAD 299
Cdd:PHA02562  172 NKDKIRELNQQIQTLDMKIDHIQQQIKTYNKN------IEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLN 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   300 tadaiematLDKEMaEERAESLQ---QEVEALKERVDELTTDLEILKaeieekgsDGAASSYQLKQLEEQNARLKDALVR 376
Cdd:PHA02562  246 ---------LVMDI-EDPSAALNklnTAAAKIKSKIEQFQKVIKMYE--------KGGVCPTCTQQISEGPDRITKIKDK 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   377 MRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRErLQEELSQAESTIDELKEQVDAALGA-EEMVEMLTDRNLNLEEKVR 455
Cdd:PHA02562  308 LKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLE-LKNKISTNKQSLITLVDKAKKVKAAiEELQAEFVDNAEELAKLQD 386


                  ....*....
gi 13259510   456 ELRETVGDL 464
Cdd:PHA02562  387 ELDKIVKTK 395
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
214-420 4.99e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.70  E-value: 4.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  214 SKEEEGLRAQVRDLEEKLETLRlkraedkaklkelEKHKIqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERY 293
Cdd:COG3206  181 EEQLPELRKELEEAEAALEEFR-------------QKNGL--VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  294 MEEMADTADAIEMATLDKEMAEERAE--SLQQEVEALKER-------VDELTTDLEILKAEIEEKGSDGAASSY-QLKQL 363
Cdd:COG3206  246 RAQLGSGPDALPELLQSPVIQQLRAQlaELEAELAELSARytpnhpdVIALRAQIAALRAQLQQEAQRILASLEaELEAL 325

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 13259510  364 EEQNARLKDALVRMRDLSSSEKQEHVKLQKLmekkNQELEVVRQQRERLQEELSQAE 420
Cdd:COG3206  326 QAREASLQAQLAQLEARLAELPELEAELRRL----EREVEVARELYESLLQRLEEAR 378
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 220-537 5.28e-05

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 47.43  E-value: 5.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    220 LRAQVRDLEEKLETLRLK---RAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQA---DLQRRLKEAR------------- 280
Cdd:pfam05557  144 LKAKASEAEQLRQNLEKQqssLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELAripELEKELERLRehnkhlnenienk 223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    281 ---KEAKEALEAKERYMEEMADTADAIEM--------------------ATLDKEMA-EERAESLQQEVEALKERVDELT 336
Cdd:pfam05557  224 lllKEEVEDLKRKLEREEKYREEAATLELekekleqelqswvklaqdtgLNLRSPEDlSRRIEQLQQREIVLKEENSSLT 303

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    337 TDLEILKAEIEEKGSDGAAssyQLKQLEEQNARLK--DALVRM-----------RDL----------------SSSEKQE 387
Cdd:pfam05557  304 SSARQLEKARRELEQELAQ---YLKKIEDLNKKLKrhKALVRRlqrrvllltkeRDGyrailesydkeltmsnYSPQLLE 380

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    388 HVK-LQKLMEKKNQELEVVRQQRERLQEEL-------SQAESTIDELKEQVDAA--LGAEEMVEMLTDRNLNLEEKVREL 457
Cdd:pfam05557  381 RIEeAEDMTQKMQAHNEEMEAQLSVAEEELggykqqaQTLERELQALRQQESLAdpSYSKEEVDSLRRKLETLELERQRL 460

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    458 RETVGDLEA---------MNEMND----ELQEN----ARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTI--- 517
Cdd:pfam05557  461 REQKNELEMelerrclqgDYDPKKtkvlHLSMNpaaeAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTstm 540

                          410       420
                   ....*....|....*....|..
gi 13259510    518 --KKYRQLTAHLQDvnRELTNQ 537
Cdd:pfam05557  541 nfKEVLDLRKELES--AELKNQ 560
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 214-547 5.84e-05

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 47.53  E-value: 5.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    214 SKEEEGLRAQVRDLEEKLETLRLKRAEDKAKlkELEKHKIQLEQVQEWKSK--------MQEQQADLQRRLKEARKEAKE 285
Cdd:pfam12128  360 EERLKALTGKHQDVTAKYNRRRSKIKEQNNR--DIAGIKDKLAKIREARDRqlavaeddLQALESELREQLEAGKLEFNE 437

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    286 ALEAKERYMEEMA---DTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKaeieekgsdgaassyqlKQ 362
Cdd:pfam12128  438 EEYRLKSRLGELKlrlNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQAR-----------------KR 500

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    363 LEEQNARLKDALVRMRDLSSSEKQEHvklQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEM 442
Cdd:pfam12128  501 RDQASEALRQASRRLEERQSALDELE---LQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGE 577

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    443 LTDRNLNLEEKVRELRETVGDLEAMNEMNDELQE---NARETELELREQLDMAGARVREAQKRVEAAQETvadYQQTIKK 519
Cdd:pfam12128  578 LNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEalqSAREKQAAAEEQLVQANGELEKASREETFARTA---LKNARLD 654

                          330       340       350
                   ....*....|....*....|....*....|..
gi 13259510    520 YRQLTAHLQD----VNRELTNQQEASVERQQQ 547
Cdd:pfam12128  655 LRRLFDEKQSekdkKNKALAERKDSANERLNS 686
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 216-494 5.86e-05

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: 47.64  E-value: 5.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  216 EEEGLRAQVRDLEEKLETlRLKRAEDkaklkELEKHKIQLEQVQEwkskmQEQQAdLQRR--LKEARKEAKEALEAKERY 293
Cdd:COG3096  974 DAVGLLGENSDLNEKLRA-RLEQAEE-----ARREAREQLRQAQA-----QYSQY-NQVLasLKSSRDAKQQTLQELEQE 1041

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  294 MEEMADTADAIematldkemAEERAES----LQQEVEALKERVDELTTDLEILKAEIEEkgsdgaaSSYQLKQLEEQNAR 369
Cdd:COG3096 1042 LEELGVQADAE---------AEERARIrrdeLHEELSQNRSRRSQLEKQLTRCEAEMDS-------LQKRLRKAERDYKQ 1105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  370 LKDALVrmrdlssSEKQEHVKLQKLMEKKNQELEVVRQqrerlqeELSQAEStiDELKEQVDAALGAEEMV----EMLTD 445
Cdd:COG3096 1106 EREQVV-------QAKAGWCAVLRLARDNDVERRLHRR-------ELAYLSA--DELRSMSDKALGALRLAvadnEHLRD 1169

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13259510  446 rNLNLEE-------KV-------RELRE--------TVGDLEAMNEMNDELqenARET-ELELREQlDMAGA 494
Cdd:COG3096 1170 -ALRLSEdprrperKVqfyiavyQHLRErirqdiirTDDPVEAIEQMEIEL---ARLTeELTSREQ-KLAIS 1236
CCDC73 pfam15818
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ...
 227-551 6.16e-05

Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.


Pssm-ID: 464893 [Multi-domain]  Cd Length: 1048  Bit Score: 47.63  E-value: 6.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    227 LEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTAD-AIE 305
Cdd:pfam15818    9 LLEALEELRMRREAETQYEEQIGKIIVETQELKWQKETLQNQKETLAKQHKEAMAVFKKQLQMKMCALEEEKGKYQlATE 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    306 MATLDKEMAEERAESLQQEVEALKERVDELTTDLEI--LKAEIEEKGSDGAASSY-----QLKQLEEQNARL----KDAL 374
Cdd:pfam15818   89 IKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKLQLhlLAKEDHHKQLNEIEKYYatitgQFGLVKENHGKLeqnvQEAI 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    375 VRMRDLSS-SEKQE--------------------HVKLQKLMEKKNQELEVVRQQRERLQEELS---------QAEST-I 423
Cdd:pfam15818  169 QLNKRLSAlNKKQEseicslkkelkkvtsdliksKVTCQYKMGEENINLTIKEQKFQELQERLNmelelnkkiNEEIThI 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    424 DELKEQVDAALG-AEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAgarVREAQKR 502
Cdd:pfam15818  249 QEEKQDIIISFQhMQQLLQQQTQANTEMEAELKALKENNQTLERDNELQREKVKENEEKFLNLQNEHEKA---LGTWKKH 325

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 13259510    503 VEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPE 551
Cdd:pfam15818  326 VEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQKKFEEDKKFQNVPE 374
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 220-468 6.40e-05

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: 47.48  E-value: 6.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    220 LRAQVRDLEEKLETLRLKRAEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEAleAKERYMEEMAD 299
Cdd:pfam01576  803 LQAQMKDLQRELEEARASRDEILAQSKESEK---KLKNLEAELLQLQEDLAASERARRQAQQERDEL--ADEIASGASGK 877

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    300 TADAIEMATLDKEMA--EERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRM 377
Cdd:pfam01576  878 SALQDEKRRLEARIAqlEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEM 957

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    378 RDLSSSEKQEHV-----KLQKLMEKKNQEL-------EVVRQQRERLQEELSQAES---TIDELKEQVDAALGA------ 436
Cdd:pfam01576  958 EGTVKSKFKSSIaaleaKIAQLEEQLEQESrerqaanKLVRRTEKKLKEVLLQVEDerrHADQYKDQAEKGNSRmkqlkr 1037

                          250       260       270
                   ....*....|....*....|....*....|....
gi 13259510    437 --EEMVEMLTDRNLNLEEKVRELRETVGDLEAMN 468
Cdd:pfam01576 1038 qlEEAEEEASRANAARRKLQRELDDATESNESMN 1071
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 283-436 6.61e-05

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 46.59  E-value: 6.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  283 AKEALEAKERYMEEMADTADAIEMATLDKEMAE------ERAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaas 356
Cdd:cd22656   82 AQNAGGTIDSYYAEILELIDDLADATDDEELEEakktikALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEK-------- 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  357 syQLKQLEEQNARLKDALvrMRDLSSSEKQEHVKLQKLMEKKNQEL------------------EVVRQQRERLQEELSQ 418
Cdd:cd22656  154 --DQTALETLEKALKDLL--TDEGGAIARKEIKDLQKELEKLNEEYaaklkakidelkaliaddEAKLAAALRLIADLTA 229

                        170
                 ....*....|....*...
gi 13259510  419 AESTIDELKEQVDAALGA 436
Cdd:cd22656  230 ADTDLDNLLALIGPAIPA 247
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 216-429 6.66e-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: 47.42  E-value: 6.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    216 EEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKH--KIQLEQVqewksKMQEQQADLQRRLKEARKEAKEALEAKERY 293
Cdd:pfam15921  591 EKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARvsDLELEKV-----KLVNAGSERLRAVKDIKQERDQLLNEVKTS 665

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    294 MEEMADTADAIEMAtldKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEE-KGSDG-------------AASSYQ 359
Cdd:pfam15921  666 RNELNSLSEDYEVL---KRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSmEGSDGhamkvamgmqkqiTAKRGQ 742

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13259510    360 LKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLME----KKNQ---ELEVVRQQRERLQEELSQAESTIDELKEQ 429
Cdd:pfam15921  743 IDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELStvatEKNKmagELEVLRSQERRLKEKVANMEVALDKASLQ 819
mukB PRK04863
chromosome partition protein MukB;
215-547 7.41e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 47.26  E-value: 7.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   215 KEEEGLRAQVRDLEEKLETLRLKRAEDK--AKLKELEKHKIQLEQVQEWKSKMQ---EQQADLQRRLkEARKE---AKEA 286
Cdd:PRK04863  223 PENSGVRKAFQDMEAALRENRMTLEAIRvtQSDRDLFKHLITESTNYVAADYMRhanERRVHLEEAL-ELRRElytSRRQ 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   287 LEAKERYMEEMADTADAIematldkemaEERAESLQQEVEALKERVDELTTDLeILKAEIEEKGSDGAASSYqlkQLEEQ 366
Cdd:PRK04863  302 LAAEQYRLVEMARELAEL----------NEAESDLEQDYQAASDHLNLVQTAL-RQQEKIERYQADLEELEE---RLEEQ 367

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   367 NARLKDA--LVRMRDLSSSEKQEHVK-LQKLMEKKNQELEVvrQQRERLQEElsQAESTIDELKEQVD----AALGAEEM 439
Cdd:PRK04863  368 NEVVEEAdeQQEENEARAEAAEEEVDeLKSQLADYQQALDV--QQTRAIQYQ--QAVQALERAKQLCGlpdlTADNAEDW 443

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   440 VEMLTDRNLNLEEKVRELRETVGDLEAMNEMND----------------ELQENARETELELREQLDMAG------ARVR 497
Cdd:PRK04863  444 LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEqayqlvrkiagevsrsEAWDVARELLRRLREQRHLAEqlqqlrMRLS 523

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13259510   498 EAQKRVE---AAQETVADYQQTIKK-----------YRQLTAHLQDVNRELTNQQE-ASVERQQQ 547
Cdd:PRK04863  524 ELEQRLRqqqRAERLLAEFCKRLGKnlddedeleqlQEELEARLESLSESVSEARErRMALRQQL 588
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 228-536 7.81e-05

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: 47.25  E-value: 7.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  228 EEKLETLRLKRAE----------DKAKLKELEKHKIQL--EQVQEW--------KSKMQEQQADLQRRLKEARKEAKEAL 287
Cdd:COG3096  784 EKRLEELRAERDElaeqyakasfDVQKLQRLHQAFSQFvgGHLAVAfapdpeaeLAALRQRRSELERELAQHRAQEQQLR 863

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  288 EAKERYMEEMADTADAI-EMATLDKEMAEERAESLQQEVEALKERVDELT------TDLEILKAEIEEKGSDGAASSYQL 360
Cdd:COG3096  864 QQLDQLKEQLQLLNKLLpQANLLADETLADRLEELREELDAAQEAQAFIQqhgkalAQLEPLVAVLQSDPEQFEQLQADY 943

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  361 KQLEEQNARLKDALVRMRDLssSEKQEHVKLQKL--MEKKNQELEvvrqqrERLQEELSQAESTIDELKEQVDAALG-AE 437
Cdd:COG3096  944 LQAKEQQRRLKQQIFALSEV--VQRRPHFSYEDAvgLLGENSDLN------EKLRARLEQAEEARREAREQLRQAQAqYS 1015

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  438 EMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMND-ELQENARETELELREQLDMAGARVREAQK---RVEAAQETVAdy 513
Cdd:COG3096 1016 QYNQVLASLKSSRDAKQQTLQELEQELEELGVQADaEAEERARIRRDELHEELSQNRSRRSQLEKqltRCEAEMDSLQ-- 1093

                        330       340
                 ....*....|....*....|...
gi 13259510  514 qqtiKKYRQLTAHLQDVNRELTN 536
Cdd:COG3096 1094 ----KRLRKAERDYKQEREQVVQ 1112
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 215-578 8.59e-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: 8.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    215 KEEEGLRAQVRDLEEKLETLRLKRaedkaklkelekhkiqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYM 294
Cdd:pfam15921  103 KQKFYLRQSVIDLQTKLQEMQMER-----------------DAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDML 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    295 EEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEieekgSDGAASSYQLKQLEEQNARLKDAL 374
Cdd:pfam15921  166 EDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFR-----SLGSAISKILRELDTEISYLKGRI 240

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    375 VRMRDlsssekqehvKLQKLMEKKNQELEVVRQQ-RERLQEELSQAESTIDELKEQVDAALGA--------EEMVEMLTD 445
Cdd:pfam15921  241 FPVED----------QLEALKSESQNKIELLLQQhQDRIEQLISEHEVEITGLTEKASSARSQansiqsqlEIIQEQARN 310

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    446 RNLNLEEKVRELRETVGDLEAmnemndELQENARETE---LELREQLDMAGARVREAqkRVEAAQETvadyQQTIKKYRQ 522
Cdd:pfam15921  311 QNSMYMRQLSDLESTVSQLRS------ELREAKRMYEdkiEELEKQLVLANSELTEA--RTERDQFS----QESGNLDDQ 378

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 13259510    523 LTAHLQDVNREltnQQEASVERQQQppPETFDFKIKFAETKAHAKAiEMELRQMEV 578
Cdd:pfam15921  379 LQKLLADLHKR---EKELSLEKEQN--KRLWDRDTGNSITIDHLRR-ELDDRNMEV 428
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 216-547 9.59e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 46.64  E-value: 9.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    216 EEEGLRAQVRDLEEKLETLRLKRAEDK--AKLKELEKHKiqleQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERY 293
Cdd:pfam05483  177 EREETRQVYMDLNNNIEKMILAFEELRvqAENARLEMHF----KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEK 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    294 MEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAE----------IEEKGSDGAASSYQLK-- 361
Cdd:pfam05483  253 ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSlqrsmstqkaLEEDLQIATKTICQLTee 332

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    362 ---QLEEQN-ARLKDALVrmrdlSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELK---------- 427
Cdd:pfam05483  333 keaQMEELNkAKAAHSFV-----VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTkfknnkevel 407

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    428 EQVDAALGAEemvEMLTDRNLNLEEKVRELR----ETVGDLEAM-NEMND-ELQENARETELE--LREQLDMAGARVREA 499
Cdd:pfam05483  408 EELKKILAED---EKLLDEKKQFEKIAEELKgkeqELIFLLQAReKEIHDlEIQLTAIKTSEEhyLKEVEDLKTELEKEK 484

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 13259510    500 QKRVeaaqETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 547
Cdd:pfam05483  485 LKNI----ELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQ 528
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 254-349 1.03e-04

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 44.01  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  254 QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTA--DAIEMATLDKEMAEERAESLQQE-VEALKE 330
Cdd:COG0711   39 GLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEAkaEAEAEAERIIAQAEAEIEQERAKaLAELRA 118

                         90       100
                 ....*....|....*....|.
gi 13259510  331 RVDELTTDL--EILKAEIEEK 349
Cdd:COG0711  119 EVADLAVAIaeKILGKELDAA 139
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 924-1065 1.04e-04

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: 45.30  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  924 VELRAAALRAEITDAEglgLKLEDRETVIKELKKSLK-IKGE--------ELSEANVRLSLLEKK---LDSAAKDADERI 991
Cdd:COG1579   50 AKTELEDLEKEIKRLE---LEIEEVEARIKKYEEQLGnVRNNkeyealqkEIESLKRRISDLEDEileLMERIEELEEEL 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13259510  992 EKVQTRLEETQALLRKKEKEFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIEGLR-GPPPSGIATLVSGIAG 1065
Cdd:COG1579  127 AELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPELLALYERIRkRKNGLAVVPVEGGACG 201
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 924-1037 1.06e-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: 46.98  E-value: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    924 VELRAAALRAEITDAEglgLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLE----------KKLDSAAKDADERIEK 993
Cdd:TIGR02169  376 VDKEFAETRDELKDYR---EKLEKLKREINELKRELDRLQEELQRLSEELADLNaaiagieakiNELEEEKEDKALEIKK 452

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 13259510    994 VQTRLEETQALLRKKEKEFEetmdALQADIDQLEAEKAELKQRL 1037
Cdd:TIGR02169  453 QEWKLEQLAADLSKYEQELY----DLKEEYDRVEKELSKLQREL 492
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 228-368 1.06e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 46.34  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   228 EEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEAleAKERYMEEMADTADAIEMA 307
Cdd:PRK09510   86 QQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAA--AKAKAEAEAKRAAAAAKKA 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13259510   308 TLDKEMAEERAESLQQEVEALKERVDELTTdleilKAEIEEKGSDGAASSYQLKQLEEQNA 368
Cdd:PRK09510  164 AAEAKKKAEAEAAKKAAAEAKKKAEAEAAA-----KAAAEAKKKAEAEAKKKAAAEAKKKA 219
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 215-539 1.07e-04

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


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 46.18  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    215 KEEEGLRAQVRDLEEKLETLRlkRAEDKAKLKELEKHKIQLEQVQE-WKSKMQEQQADLQRRLKEARKEAKEALEAKERY 293
Cdd:pfam15558   18 KEEQRMRELQQQAALAWEELR--RRDQKRQETLERERRLLLQQSQEqWQAEKEQRKARLGREERRRADRREKQVIEKESR 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    294 MEEMADTADAIEMATLDKEMAEERAESLQQEvEALKERVDELTTDLEILKAEIEEKGSDgAASSYQLKQLEEQNarlkda 373
Cdd:pfam15558   96 WREQAEDQENQRQEKLERARQEAEQRKQCQE-QRLKEKEEELQALREQNSLQLQERLEE-ACHKRQLKEREEQK------ 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    374 lvRMRDLSSSEKQEHVKLQKLMEKKNQElevvrqqrERLQEELSQaestidELKEQVdaalgAEEMVEMLtdrnlnLEEK 453
Cdd:pfam15558  168 --KVQENNLSELLNHQARKVLVDCQAKA--------EELLRRLSL------EQSLQR-----SQENYEQL------VEER 220

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    454 VRELREtvgdlEAMNEmNDELQENARETELELREQLDMAGARVREAQKRVE----AAQETVADYQQTIKKYRQLTAHLQD 529
Cdd:pfam15558  221 HRELRE-----KAQKE-EEQFQRAKWRAEEKEEERQEHKEALAELADRKIQqarqVAHKTVQDKAQRARELNLEREKNHH 294

                          330
                   ....*....|
gi 13259510    530 VNRELTNQQE 539
Cdd:pfam15558  295 ILKLKVEKEE 304
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
303-532 1.17e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  303 AIEMATLDKEMAE------ERAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaassyqLKQLEEQNARLKDALVR 376
Cdd:COG4717   45 AMLLERLEKEADElfkpqgRKPELNLKELKELEEELKEAEEKEEEYAELQEE-----------LEELEEELEELEAELEE 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  377 MRdlsssekQEHVKLQKLmekknQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRnlnLEEKVRE 456
Cdd:COG4717  114 LR-------EELEKLEKL-----LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE---LAELQEE 178

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13259510  457 LRETVgdleamnemnDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNR 532
Cdd:COG4717  179 LEELL----------EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 244-485 1.18e-04

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 46.39  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   244 KLKELEKHKIQLEQvqewKSKMQEQQADLQRRLKEA--RKEAKEALEA-KERYMEEMADTADaiemaTLDKEMAEErAES 320
Cdd:PLN03229  539 MLNEFSRAKALSEK----KSKAEKLKAEINKKFKEVmdRPEIKEKMEAlKAEVASSGASSGD-----ELDDDLKEK-VEK 608

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   321 LQQEVEA-LKERVDELTTDLEILKAEIEEKGSDGAASSYQLK--QLEEQNARLKDALVRMRDLSSSekqehVKLQKLmek 397
Cdd:PLN03229  609 MKKEIELeLAGVLKSMGLEVIGVTKKNKDTAEQTPPPNLQEKieSLNEEINKKIERVIRSSDLKSK-----IELLKL--- 680

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   398 knqelEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEmltdRNLNLEEKVRELRETVGDLEAMNEMNDELQEN 477
Cdd:PLN03229  681 -----EVAKASKTPDVTEKEKIEALEQQIKQKIAEALNSSELKE----KFEELEAELAAARETAAESNGSLKNDDDKEED 751


                  ....*...
gi 13259510   478 ARETELEL 485
Cdd:PLN03229  752 SKEDGSRV 759
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 214-332 1.20e-04

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 46.61  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  214 SKEE-EGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAker 292
Cdd:COG0542  438 SFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE--- 514

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 13259510  293 ymeemADTADAIEMAT---LDKeMAEERAESLQQEVEALKERV 332
Cdd:COG0542  515 -----EDIAEVVSRWTgipVGK-LLEGEREKLLNLEEELHERV 551
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 392-583 1.26e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.91  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  392 QKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAAlgaEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEmn 471
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL---ERRIAALARRIRALEQELAALEAELAELEKEIA-- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  472 dELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQpppe 551
Cdd:COG4942   94 -ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE---- 168

                        170       180       190
                 ....*....|....*....|....*....|..
gi 13259510  552 tfdFKIKFAETKAHAKAIEMELRQMEVAQANR 583
Cdd:COG4942  169 ---LEAERAELEALLAELEEERAALEALKAER 197
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 406-566 1.31e-04

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: 46.48  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  406 RQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRnLNL-------EEKVRELREtvgDLEAMNEMNDElQENA 478
Cdd:COG3096  295 FGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDH-LNLvqtalrqQEKIERYQE---DLEELTERLEE-QEEV 369

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  479 REtelELREQLDMAGARVREAQKRVEAAQETVADYQQTIK-------KYRQLTAHLQDVNR-----ELT-----NQQEAS 541
Cdd:COG3096  370 VE---EAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDvqqtraiQYQQAVQALEKARAlcglpDLTpenaeDYLAAF 446

                        170       180
                 ....*....|....*....|....*
gi 13259510  542 VERQQQPPPETFDFKIKFAETKAHA 566
Cdd:COG3096  447 RAKEQQATEEVLELEQKLSVADAAR 471
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 249-546 1.35e-04

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 46.37  E-value: 1.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    249 EKHKIQLEQVQEWkskMQEQQAdLQRRLKEARKEAKEALEAKERYMEEMadtadaiEMATLDKE-MAEERAESLQQEveA 327
Cdd:pfam12128  214 PKSRLNRQQVEHW---IRDIQA-IAGIMKIRPEFTKLQQEFNTLESAEL-------RLSHLHFGyKSDETLIASRQE--E 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    328 LKERVDELTTDLEILKAEIEEKgsdgaassyqlkqLEEQNARLKDAlvrmrDLSSSEKQEHVKLqkLMEKKNQELEVVRQ 407
Cdd:pfam12128  281 RQETSAELNQLLRTLDDQWKEK-------------RDELNGELSAA-----DAAVAKDRSELEA--LEDQHGAFLDADIE 340

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    408 QRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNL--EEKVRELRETVGDLEAMNEMNDELQENARET---- 481
Cdd:pfam12128  341 TAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKikEQNNRDIAGIKDKLAKIREARDRQLAVAEDDlqal 420

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13259510    482 ELELREQLDMAGARVREAQKRVEAAQET----VADYQQTIKKYRQLTAHLQDVN--RELTNQQEASVERQQ 546
Cdd:pfam12128  421 ESELREQLEAGKLEFNEEEYRLKSRLGElklrLNQATATPELLLQLENFDERIEraREEQEAANAEVERLQ 491
Filament pfam00038
Intermediate filament protein;
220-489 1.36e-04

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 45.68  E-value: 1.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    220 LRAQVRDLEEKLETLRLKRAEDKAKL-----KELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYM 294
Cdd:pfam00038   23 LEQQNKLLETKISELRQKKGAEPSRLyslyeKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAE 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    295 EEMADTADAIEMATLDKEMAEERAESLQQEVEALK----ERVDELTTDLeilkaeieekgsdgaasSYQLKQLEEQNARL 370
Cdd:pfam00038  103 NDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKknheEEVRELQAQV-----------------SDTQVNVEMDAARK 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    371 KDALVRMRDLSSS-EKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDaALGAEemVEMLTDRNLN 449
Cdd:pfam00038  166 LDLTSALAEIRAQyEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQ-SLEIE--LQSLKKQKAS 242

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 13259510    450 LEEKVRELRET-VGDLEAMNEMNDELQENARETELELREQL 489
Cdd:pfam00038  243 LERQLAETEERyELQLADYQELISELEAELQETRQEMARQL 283
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 243-371 1.65e-04

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: 42.63  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    243 AKLKELEKHKIQLEQVQEwkskmqEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLdkemAEERAESLQ 322
Cdd:pfam07926    1 AELSSLQSEIKRLKEEAA------DAEAQLQKLQEDLEKQAEIAREAQQNYERELVLHAEDIKALQA----LREELNELK 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 13259510    323 QEVEALKERVDELTTDLEILKAEIEEkgsdgaassyQLKQLEEQNARLK 371
Cdd:pfam07926   71 AEIAELKAEAESAKAELEESEESWEE----------QKKELEKELSELE 109
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
256-494 1.75e-04

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 45.84  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  256 EQVQEWKSKMQEQQAdLQRRLKEARKEAKEALEAKERY---MEEMaDTAD--AIEMATLDKEM-----AEERAESLQQEV 325
Cdd:COG0497  155 ELLEEYREAYRAWRA-LKKELEELRADEAERARELDLLrfqLEEL-EAAAlqPGEEEELEEERrrlsnAEKLREALQEAL 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  326 EALKERVDELTTDLEILKAEIEEkgsdgaASSYQlKQLEEQNARLKDALVRMRDLSSS------------EKQEHV---- 389
Cdd:COG0497  233 EALSGGEGGALDLLGQALRALER------LAEYD-PSLAELAERLESALIELEEAASElrryldslefdpERLEEVeerl 305

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  390 -KLQKLMEKKNQELEVVRQQRERLQEELSQ---AESTIDELKEQVDAALGAeemvemltdrnlnLEEKVREL----RETV 461
Cdd:COG0497  306 aLLRRLARKYGVTVEELLAYAEELRAELAElenSDERLEELEAELAEAEAE-------------LLEAAEKLsaarKKAA 372

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 13259510  462 GDLEAmnEMNDELQ----ENAR-ETELELREQLDMAGA 494
Cdd:COG0497  373 KKLEK--AVTAELAdlgmPNARfEVEVTPLEEPGPNGA 408
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
390-547 1.92e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 1.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  390 KLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEmltdrnlNLEEKVRELRETVGDLEAMNE 469
Cdd:COG4717   54 EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELE-------ELEAELEELREELEKLEKLLQ 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13259510  470 MNDELQENAretelELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 547
Cdd:COG4717  127 LLPLYQELE-----ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
PrfA COG0216
Protein chain release factor RF1 [Translation, ribosomal structure and biogenesis]; Protein ...
 227-342 1.99e-04

Protein chain release factor RF1 [Translation, ribosomal structure and biogenesis]; Protein chain release factor RF1 is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 439986 [Multi-domain]  Cd Length: 356  Bit Score: 44.99  E-value: 1.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  227 LEEKLETLrlkraedKAKLKELEKhkiQLEQ------VQEWKSKMQEQqADLQ------RRLKEARKEAKEAleakerym 294
Cdd:COG0216    2 MLDKLEAL-------EERYEELEA---LLSDpevisdQKRFRKLSKEY-AELEpiveayREYKKLLEDIEEA-------- 62

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 13259510  295 EEMADTADAIEMatldKEMAEEraeslqqEVEALKERVDELTTDLEIL 342
Cdd:COG0216   63 KELLEEESDPEM----REMAKE-------ELEELEARLEELEEELKIL 99
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 236-540 2.09e-04

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 45.40  E-value: 2.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    236 LKRAEDkaklkELEKHKIQLEQVQEWKSKMQEQQADLQRRLKE--ARKEAKEALEAKERYMEEMADTADAIEMATLDKEM 313
Cdd:pfam05701  228 LKQAEE-----ELQRLNQQLLSAKDLKSKLETASALLLDLKAElaAYMESKLKEEADGEGNEKKTSTSIQAALASAKKEL 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    314 AEERA--ESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKD--ALVRMRDLSSSEKQehV 389
Cdd:pfam05701  303 EEVKAniEKAKDEVNCLRVAAASLRSELEKEKAELASLRQREGMASIAVSSLEAELNRTKSeiALVQAKEKEAREKM--V 380

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    390 KLQKLMEKKNQELE----VVRQQRERL---QEELSQA-------ESTIDELKEQVDAALGAEEMVemLTDRNLNLEEKVR 455
Cdd:pfam05701  381 ELPKQLQQAAQEAEeaksLAQAAREELrkaKEEAEQAkaaastvESRLEAVLKEIEAAKASEKLA--LAAIKALQESESS 458

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    456 ELRETVGDLEAM----NEMNDELQENARETElelreqlDMAGARVREAQKRVEAAQETvadyqqtikKYRQLtAHLQDVN 531
Cdd:pfam05701  459 AESTNQEDSPRGvtlsLEEYYELSKRAHEAE-------ELANKRVAEAVSQIEEAKES---------ELRSL-EKLEEVN 521


                   ....*....
gi 13259510    532 RELTNQQEA 540
Cdd:pfam05701  522 REMEERKEA 530
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 220-438 2.09e-04

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 45.98  E-value: 2.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    220 LRAQVRDLEEKLETL--RLKRAEDKaklkELEKHKIQLEQVQEWKSKMQEQQADLqrrlkEARKEAKEALEAKERYMEEM 297
Cdd:pfam12128  313 ADAAVAKDRSELEALedQHGAFLDA----DIETAAADQEQLPSWQSELENLEERL-----KALTGKHQDVTAKYNRRRSK 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    298 ADTADAIEMATLDKEMA---EERAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaaSSYQLK-QLEEQNARLKDA 373
Cdd:pfam12128  384 IKEQNNRDIAGIKDKLAkirEARDRQLAVAEDDLQALESELREQLEAGKLEFNE-------EEYRLKsRLGELKLRLNQA 456

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13259510    374 LVrmrdlSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAestiDELKEQVDAALGAEE 438
Cdd:pfam12128  457 TA-----TPELLLQLENFDERIERAREEQEAANAEVERLQSELRQA----RKRRDQASEALRQAS 512
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
945-1035 2.14e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   945 LEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADE----RIEKVQTRLEETQALLRKKEKEFEETMDALQ 1020
Cdd:PRK03918  614 LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEeeyeELREEYLELSRELAGLRAELEELEKRREEIK 693

                          90
                  ....*....|....*
gi 13259510  1021 ADIDQLEAEKAELKQ 1035
Cdd:PRK03918  694 KTLEKLKEELEEREK 708
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 319-429 2.22e-04

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: 42.24  E-value: 2.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    319 ESLQQEVEALKERVDELTTDLEILKAEIEE--KGSDGAASSYQlKQLEEQNARLKdALVRMRDLSSSEKQEHVKLQKLME 396
Cdd:pfam07926    4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEKqaEIAREAQQNYE-RELVLHAEDIK-ALQALREELNELKAEIAELKAEAE 81

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 13259510    397 KKNQELEVVR----QQRERLQEELSQAESTIDELKEQ 429
Cdd:pfam07926   82 SAKAELEESEesweEQKKELEKELSELEKRIEDLNEQ 118
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 104-214 2.59e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 45.29  E-value: 2.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    104 TSPETPDSSASKVLKREGTDTT--AKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGVAGASSSLGPSGSASAGELSSS 181
Cdd:pfam05109  456 TNLTAPASTGPTVSTADVTSPTpaGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNAT 535

                           90       100       110
                   ....*....|....*....|....*....|...
gi 13259510    182 EPSTPAQTPLAAPIIPTPVLTSPGAVPPLPSPS 214
Cdd:pfam05109  536 SPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPN 568
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 227-502 2.64e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.91  E-value: 2.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    227 LEEKLETLRLKRAEDKAKLKELEKH-----KIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMadta 301
Cdd:pfam13868   28 IAEKKRIKAEEKEEERRLDEMMEEEreralEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQM---- 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    302 daieMATLDKEMAEERAESLQQ--EVEALKERVDELTTDLEILKAE--IEEKGSDGAASSYQLKQLEEQNARLKdalvRM 377
Cdd:pfam13868  104 ----DEIVERIQEEDQAEAEEKleKQRQLREEIDEFNEEQAEWKELekEEEREEDERILEYLKEKAEREEEREA----ER 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    378 RDLSSSEKQEHVKLQKLMEKKNQElevvRQQRERLQEELSQAESTIDE-LKEQVDAALGAEEMVEMLTDRNLNLEEKVRE 456
Cdd:pfam13868  176 EEIEEEKEREIARLRAQQEKAQDE----KAERDELRAKLYQEEQERKErQKEREEAEKKARQRQELQQAREEQIELKERR 251

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 13259510    457 LRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKR 502
Cdd:pfam13868  252 LAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEK 297
46 PHA02562
endonuclease subunit; Provisional
 341-536 2.94e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 45.01  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   341 ILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHvklQKLMEKKNQELEVVRQQRERLQEELSQAE 420
Cdd:PHA02562  171 LNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARK---QNKYDELVEEAKTIKAEIEELTDELLNLV 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   421 STIDE--------------LKEQVDAALG--------------------AEEMVEMLTDRNLNLEEKVRELRETVGDLEA 466
Cdd:PHA02562  248 MDIEDpsaalnklntaaakIKSKIEQFQKvikmyekggvcptctqqiseGPDRITKIKDKLKELQHSLEKLDTAIDELEE 327

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13259510   467 -MNEMND---ELQENARETELElREQLDMAGARVREAQKRVEAAQETVADYQQTIKKyrqLTAHLQDVNRELTN 536
Cdd:PHA02562  328 iMDEFNEqskKLLELKNKISTN-KQSLITLVDKAKKVKAAIEELQAEFVDNAEELAK---LQDELDKIVKTKSE 397
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 402-577 3.32e-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: 3.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    402 LEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNL-----EEKVRELRETVGDLEAMNEMNDELQE 476
Cdd:TIGR02168  181 LERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALlvlrlEELREELEELQEELKEAEEELEELTA 260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    477 NARETELELrEQLDmagARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPP------- 549
Cdd:TIGR02168  261 ELQELEEKL-EELR---LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELEskldela 336

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 13259510    550 -------PETFDFKIKFAETKAHAKAIEMELRQME 577
Cdd:TIGR02168  337 eelaeleEKLEELKEELESLEAELEELEAELEELE 371
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 906-1039 3.83e-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: 45.06  E-value: 3.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    906 AMQEGEYDAERPPSKPPPVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKgeeLSEANVRLSLLEKKLDSaak 985
Cdd:TIGR02169  654 AMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE---LSDASRKIGEIEKEIEQ--- 727

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 13259510    986 dADERIEKVQTRLEETQALLRKKEKEFEE---TMDALQADIDQLEAEKAELKQRLNS 1039
Cdd:TIGR02169  728 -LEQEEEKLKERLEELEEDLSSLEQEIENvksELKELEARIEELEEDLHKLEEALND 783
CASP_C pfam08172
CASP C terminal; This domain is the C-terminal region of the CASP family of proteins. It is a ...
 314-455 3.86e-04

CASP C terminal; This domain is the C-terminal region of the CASP family of proteins. It is a Golgi membrane protein which is thought to have a role in vesicle transport.


Pssm-ID: 462392 [Multi-domain]  Cd Length: 247  Bit Score: 43.81  E-value: 3.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    314 AEERAESLQQEVEALKERVDELTTDLEILKAEIEE--KGSDGA-ASSYQLKQLEEQNARLKDALVrmrdLSSSEKQEHVK 390
Cdd:pfam08172    2 LQEELSSLNAELEEQQELNAKLENDLLKVQDEASNafSFNDASsAGSGVSRYPPSGGRRSPTSSI----ISGFEPSESSS 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13259510    391 LQKlmekkNQELEVVRQQRER-------LQEELSQAESTIDELKEQVDAalgaeemveMLTDrNLNLEEKVR 455
Cdd:pfam08172   78 SSD-----SSILPIVTSQRDRfrqrnaeLEEELRKQFETISSLRQEIAS---------LQKD-NLKLYEKTR 134
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 925-1043 4.21e-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: 4.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    925 ELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSaakdADERIEKVQTRLEETQAL 1004
Cdd:TIGR02168  221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE----LEEEIEELQKELYALANE 296

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 13259510   1005 LRKKEKEFEET---MDALQADIDQLEAEKAELKQRLNSQSKR 1043
Cdd:TIGR02168  297 ISRLEQQKQILrerLANLERQLEELEAQLEELESKLDELAEE 338
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 234-511 4.39e-04

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 44.63  E-value: 4.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    234 LRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEM 313
Cdd:pfam05701  126 LEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELIATKESLESAHAAHLE 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    314 AEER----AESLQQEVEALKERVDELTTDLEILKAEI----EEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEK 385
Cdd:pfam05701  206 AEEHrigaALAREQDKLNWEKELKQAEEELQRLNQQLlsakDLKSKLETASALLLDLKAELAAYMESKLKEEADGEGNEK 285

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    386 QEHVKLQKLMEKKNQELEVVRQQRER--------------LQEELSQAESTIDELKEQVDAALGAEemvemltdrnLNLE 451
Cdd:pfam05701  286 KTSTSIQAALASAKKELEEVKANIEKakdevnclrvaaasLRSELEKEKAELASLRQREGMASIAV----------SSLE 355

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    452 EkvrELRETVGDLEAMNEMNDElqenARETELELREQLDMAGARVREAQKRVEAAQETVA 511
Cdd:pfam05701  356 A---ELNRTKSEIALVQAKEKE----AREKMVELPKQLQQAAQEAEEAKSLAQAAREELR 408
PRK12704 PRK12704
phosphodiesterase; Provisional
 237-366 4.54e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.38  E-value: 4.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   237 KRAEDKAKLKELE------KHKIQLEQ-VQEWKSKMQEQQADLQRRlKEARKEAKEALEAKERYMEEMADTADAiEMATL 309
Cdd:PRK12704   49 KEAEAIKKEALLEakeeihKLRNEFEKeLRERRNELQKLEKRLLQK-EENLDRKLELLEKREEELEKKEKELEQ-KQQEL 126

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 13259510   310 DKEmaEERAESLQQEVEALKERVDELTTD--LEILKAEIEEKGSDGAASsyQLKQLEEQ 366
Cdd:PRK12704  127 EKK--EEELEELIEEQLQELERISGLTAEeaKEILLEKVEEEARHEAAV--LIKEIEEE 181
PRK12704 PRK12704
phosphodiesterase; Provisional
 214-319 5.25e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.00  E-value: 5.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   214 SKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEalEAKERY 293
Cdd:PRK12704   85 QKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQ---KQQELEKKEEELEELIEEQLQELERISGLTAE--EAKEIL 159

                          90       100
                  ....*....|....*....|....*.
gi 13259510   294 MEEMADTADAiEMATLDKEMaEERAE 319
Cdd:PRK12704  160 LEKVEEEARH-EAAVLIKEI-EEEAK 183
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 257-576 5.57e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 44.65  E-value: 5.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    257 QVQEWKSKMQEQQADLQRRLKEARKEAKEaleaKERYMEEMADTAD--AIEMATLDKEMAE--ERAESLQQEVEALKERV 332
Cdd:TIGR00606  692 ELQEFISDLQSKLRLAPDKLKSTESELKK----KEKRRDEMLGLAPgrQSIIDLKEKEIPElrNKLQKVNRDIQRLKNDI 767

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    333 DELTTDLEILKAEiEEKGSDGAASSYQLKQLEEQnarLKDALVRMRDL-----SSSEKQEHVKLQKLMEKKNQELEVVRQ 407
Cdd:TIGR00606  768 EEQETLLGTIMPE-EESAKVCLTDVTIMERFQME---LKDVERKIAQQaaklqGSDLDRTVQQVNQEKQEKQHELDTVVS 843

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    408 QRERLQEELSQAESTIDELKEQVDaALGAEEM-VEMLTDRNLNLEEKVRELRETVgdleamNEMNDELQEnARETELELR 486
Cdd:TIGR00606  844 KIELNRKLIQDQQEQIQHLKSKTN-ELKSEKLqIGTNLQRRQQFEEQLVELSTEV------QSLIREIKD-AKEQDSPLE 915

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    487 EQLDMAGARVREAQKRVEAAQETVADYQQTIK-KYRQLTAHLQDVNRELtnqQEASVERQQQPPPETFDFKIKFAETKAH 565
Cdd:TIGR00606  916 TFLEKDQQEKEELISSKETSNKKAQDKVNDIKeKVKNIHGYMKDIENKI---QDGKDDYLKQKETELNTVNAQLEECEKH 992

                          330
                   ....*....|.
gi 13259510    566 AKAIEMELRQM 576
Cdd:TIGR00606  993 QEKINEDMRLM 1003
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 225-547 5.60e-04

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 44.27  E-value: 5.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   225 RDLEEKLETLRLKRAEDKAKL--KELEKHKIQL-EQVQEWKSKMQEQQ------ADLQRRLKEARKEAKEALEAKERYME 295
Cdd:PRK10929   82 AELRQQLNNERDEPRSVPPNMstDALEQEILQVsSQLLEKSRQAQQEQdrareiSDSLSQLPQQQTEARRQLNEIERRLQ 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   296 EMADTADAIEMATLdkemaeeraESLQQEVEALKERVDELttDLEILKAEIEEKGSDGAASSYQlKQLEEQNARLKDALV 375
Cdd:PRK10929  162 TLGTPNTPLAQAQL---------TALQAESAALKALVDEL--ELAQLSANNRQELARLRSELAK-KRSQQLDAYLQALRN 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   376 RMRDLSSSEKQEHVKLQKLMEKKNQEL-----EVVRQQRErLQEELSQAESTIDELKEQVDAAlgaeemvemlTDRNLNL 450
Cdd:PRK10929  230 QLNSQRQREAERALESTELLAEQSGDLpksivAQFKINRE-LSQALNQQAQRMDLIASQQRQA----------ASQTLQV 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   451 EEKVRELRETVGDLEAMNEMNDELQEN-ARETELELREQLD--MAGARVreaqKRVEaaqetvadYQQTIKKYRQLTAHL 527
Cdd:PRK10929  299 RQALNTLREQSQWLGVSNALGEALRAQvARLPEMPKPQQLDteMAQLRV----QRLR--------YEDLLNKQPQLRQIR 366

                         330       340
                  ....*....|....*....|
gi 13259510   528 QDVNRELTNQQEASVERQQQ 547
Cdd:PRK10929  367 QADGQPLTAEQNRILDAQLR 386
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
214-332 5.60e-04

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 42.89  E-value: 5.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  214 SKEEEGLRAQVRDLEEKLETLRLKRAEDKAKlkelekhkiqlEQVQEWKSKMQEQQADLQrrlkeaRKEAKEALEAKERY 293
Cdd:COG1842  111 EEQVEKLKEALRQLESKLEELKAKKDTLKAR-----------AKAAKAQEKVNEALSGID------SDDATSALERMEEK 173

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 13259510  294 MEEMADTADAI-EMA---TLDKEMAE-ERAESLQQEVEALKERV 332
Cdd:COG1842  174 IEEMEARAEAAaELAagdSLDDELAElEADSEVEDELAALKAKM 217
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
245-483 5.62e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 5.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  245 LKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAieMATLDKEMAEERAESLQQE 324
Cdd:COG4717  294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL--LREAEELEEELQLEELEQE 371

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  325 VEALKERVDelTTDLEILKAEIEekgsdgaassyQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKlmEKKNQELEV 404
Cdd:COG4717  372 IAALLAEAG--VEDEEELRAALE-----------QAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEE 436

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13259510  405 VRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNlNLEEKVRELRETVGDLEAMNEMNDELQENARETEL 483
Cdd:COG4717  437 LEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELE-ELKAELRELAEEWAALKLALELLEEAREEYREERL 514
PTZ00121 PTZ00121
MAEBL; Provisional
 207-432 5.69e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 5.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   207 VPPLPSPSKEEEGLRAQVRDLEEKLetlRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQ---QADLQRRLKEARKEA 283
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEEN---KIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAlkkEAEEAKKAEELKKKE 1711

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   284 KEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEvEALKERVDELTTDLEILKAEIEEkgsdgaassyQLKQL 363
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAEEIRK----------EKEAV 1780

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13259510   364 EEQNARLKDALVRMrDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDA 432
Cdd:PTZ00121 1781 IEEELDEEDEKRRM-EVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADA 1848
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 944-1043 5.77e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 43.47  E-value: 5.77e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510     944 KLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERI-EKVQTRLEETQALLRKKEkEFEETMDALQAD 1022
Cdd:smart00787  162 LLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAkEKLKKLLQEIMIKVKKLE-ELEEELQELESK 240

                            90       100
                    ....*....|....*....|.
gi 13259510    1023 IDQLEAEKAELKQRLNSQSKR 1043
Cdd:smart00787  241 IEDLTNKKSELNTEIAEAEKK 261
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 908-1038 5.80e-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: 5.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    908 QEGEYDAERPPSKPPPVELRAAALRAEITDA----EGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSA 983
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEELAELEEKLEELkeelESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 13259510    984 AKD---ADERIEKVQTRLEETQALLRKKEKEFEET-MDALQADIDQLEAEKAELKQRLN 1038
Cdd:TIGR02168  399 NNEierLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEELQEELE 457
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 197-422 6.34e-04

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: 43.79  E-value: 6.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    197 PTPVLTSPGAVPPLPSPSKEE--EGLRAQVRDLEEKLETLRLKRAEDKA-----KLKELEKHKIQLEQVQEWKSKMQEQQ 269
Cdd:pfam15709  299 PTQTFVVTGNMESEEERSEEDpsKALLEKREQEKASRDRLRAERAEMRRleverKRREQEEQRRLQQEQLERAEKMREEL 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    270 ADLQRRLKEARKEAKEALEAKERYMEEMAdtadaiEMATLDKEMAEERAESLQQEVEalkervdelTTDLEILKAEIEEK 349
Cdd:pfam15709  379 ELEQQRRFEEIRLRKQRLEEERQRQEEEE------RKQRLQLQAAQERARQQQEEFR---------RKLQELQRKKQQEE 443

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13259510    350 GSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEhvKLQKLMEKKNQELEvVRQQRERLQEELSQAEST 422
Cdd:pfam15709  444 AERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQR--QKQEAEEKARLEAE-ERRQKEEEAARLALEEAM 513
PCRF pfam03462
PCRF domain; This domain is found in peptide chain release factors.
 242-335 6.99e-04

PCRF domain; This domain is found in peptide chain release factors.


Pssm-ID: 460929 [Multi-domain]  Cd Length: 192  Bit Score: 41.99  E-value: 6.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    242 KAKLKELEKhkiQLEQVQEWKSkmqeqQADLQRRLKEaRKEAKEALEAKERYMEEMADTADAIEMATLD--KEMAEERAE 319
Cdd:pfam03462    2 EERYEELEA---LLSDPDVWDD-----QKRAQKLSKE-YSELEPIVEAYREYKQALEDLEEAKELLEDPelAELAEEELE 72

                           90
                   ....*....|....*.
gi 13259510    320 SLQQEVEALKERVDEL 335
Cdd:pfam03462   73 ELEKRLEELEEELKLL 88
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 215-547 7.70e-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: 7.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    215 KEEEGLRAQVRDLEEKLETLR--LKRAEDkAKLK---ELEKHKIQL--------EQVQEWKSKMQEQQADLQRRLKEARK 281
Cdd:pfam01576  685 RSKRALEQQVEEMKTQLEELEdeLQATED-AKLRlevNMQALKAQFerdlqardEQGEEKRRQLVKQVRELEAELEDERK 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    282 EAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTT---DLEILKAEIEEKGSDGAASSY 358
Cdd:pfam01576  764 QRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARAsrdEILAQSKESEKKLKNLEAELL 843

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    359 QLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEV-VRQQRERLQEELSQAESTIDELK------EQVD 431
Cdd:pfam01576  844 QLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEArIAQLEEELEEEQSNTELLNDRLRkstlqvEQLT 923

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    432 AALGAEE-MVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETEL-ELREQLD-------MAGARVREAQKR 502
Cdd:pfam01576  924 TELAAERsTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALEAKIaQLEEQLEqesrerqAANKLVRRTEKK 1003

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 13259510    503 VEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 547
Cdd:pfam01576 1004 LKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASR 1048
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 227-477 7.78e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 43.66  E-value: 7.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    227 LEEKLETLRLKRAEDKAKLKELekhKIQLEQVQEWKSKMQEQQADLQRRLKEarkeaKEA-LEAKERYMEEMAD--TADA 303
Cdd:pfam10174  308 LQTKLETLTNQNSDCKQHIEVL---KESLTAKEQRAAILQTEVDALRLRLEE-----KESfLNKKTKQLQDLTEekSTLA 379

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    304 IEMATLdKEM---AEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNA---RLKDALVRM 377
Cdd:pfam10174  380 GEIRDL-KDMldvKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSekeRIIERLKEQ 458

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    378 RDLSSSEKQEHVklqklmEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDA-ALGAEEMVEMLTDRNLNLEEKVRE 456
Cdd:pfam10174  459 REREDRERLEEL------ESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSlASSGLKKDSKLKSLEIAVEQKKEE 532

                          250       260
                   ....*....|....*....|.
gi 13259510    457 LRETVGDLEAMNEMNDELQEN 477
Cdd:pfam10174  533 CSKLENQLKKAHNAEEAVRTN 553
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 964-1049 8.23e-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: 43.21  E-value: 8.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  964 EELSEANVRLSLLEKKLDSAAKDADERIEKVQtRLEETQALLRKKEKEFEETMDALQADIDQLEAEKAELKQRLNSQSKR 1043
Cdd:COG4942   27 AELEQLQQEIAELEKELAALKKEEKALLKQLA-ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105


                 ....*.
gi 13259510 1044 TIEGLR 1049
Cdd:COG4942  106 LAELLR 111
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 149-434 8.88e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 43.70  E-value: 8.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   149 RPK------PTRPASTGVAGASSSLGPSGSASAGELSSSEPSTPAQTPLAAPIIPTPVLTSP--GAVPPLPS------PS 214
Cdd:PRK07994  360 HPAaplpepEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQllAARQQLQRaqgatkAK 439

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   215 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKhkiqlEQVQEWKskmqEQQADLQRRLKEAR-KEAKEALEAkery 293
Cdd:PRK07994  440 KSEPAAASRARPVNSALERLASVRPAPSALEKAPAK-----KEAYRWK----ATNPVEVKKEPVATpKALKKALEH---- 506

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   294 meemadtADAIEMATLDKEMAEERAESLqQEVEALKerVDELTTDLeILKAEIEEKGSD----GAASSYQLKQLEEQNAR 369
Cdd:PRK07994  507 -------EKTPELAAKLAAEAIERDPWA-ALVSQLG--LPGLVEQL-ALNAWKEEHDNGevclHLRPSQRHLNSPRAQQR 575

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13259510   370 LKDALvrmrdlsSSEKQEHVKLqKLMEKKNQELEVVRQQRERLQEE-LSQAES------TIDELKEQVDAAL 434
Cdd:PRK07994  576 LAEAL-------SELLGRTVEL-TIEEDDNPAVETPLEWRQRIYEEkLAQAEEsiiadpNIQTLRQFFDAEL 639
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
197-350 9.38e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 43.31  E-value: 9.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  197 PTPVLTSPGAVPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEkhkiqleqvqewkskmqeqqadlqRRL 276
Cdd:COG2433  395 PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLE------------------------REL 450

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13259510  277 KEARKEAKEALEaKERYMEEMadtadaiematldkemaEERAESLQQEVEALKERVDELTTDLEILKA--EIEEKG 350
Cdd:COG2433  451 SEARSEERREIR-KDREISRL-----------------DREIERLERELEEERERIEELKRKLERLKElwKLEHSG 508
half-pint TIGR01645
poly-U binding splicing factor, half-pint family; The proteins represented by this model ...
 100-316 9.40e-04

poly-U binding splicing factor, half-pint family; The proteins represented by this model contain three RNA recognition motifs (rrm: pfam00076) and have been characterized as poly-pyrimidine tract binding proteins associated with RNA splicing factors. In the case of PUF60 (GP|6176532), in complex with p54, and in the presence of U2AF, facilitates association of U2 snRNP with pre-mRNA.


Pssm-ID: 130706 [Multi-domain]  Cd Length: 612  Bit Score: 43.52  E-value: 9.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    100 GADTTSPETPDSSASKVLKREGTDTTAKT-SKLRGLKPKKAPTARKT-TTRRPKPTRPASTGVagassslgPSGSASAGE 177
Cdd:TIGR01645  325 GPRAQSPATPSSSLPTDIGNKAVVSSAKKeAEEVPPLPQAAPAVVKPgPMEIPTPVPPPGLAI--------PSLVAPPGL 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    178 LSssePSTPAQTPLAAPIIPTPVLTSPGAVPPLPS------PSKEEEGlRAQVRDLEEKLETLRLKRAEDKAKLKELEKH 251
Cdd:TIGR01645  397 VA---PTEINPSFLASPRKKMKREKLPVTFGALDDtlawkePSKEDQT-SEDGKMLAIMGEAAAALALEPKKKKKEKEGE 472

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13259510    252 KIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKER----YMEEMADTADAIEmaTLDKEMAEE 316
Cdd:TIGR01645  473 ELQPKLVMNSEDASLASQEGMSIRGNSARHLVMQKLMRTNRsnviVLRNMVTPQDIDE--FLEGEIREE 539
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 217-491 9.58e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 43.38  E-value: 9.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   217 EEGLrAQVRDLEEKLETLRLKRAEdkAKLKELEKHKIQLEQVQEWKSKMQEQQADLQ-RRLKEARKEAKEALEAKErymE 295
Cdd:PRK05771   27 ELGV-VHIEDLKEELSNERLRKLR--SLLTKLSEALDKLRSYLPKLNPLREEKKKVSvKSLEELIKDVEEELEKIE---K 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   296 EMadtadaiematldKEMAEERAEsLQQEVEALKERVDELT--TDLEI-LKAEIEEKGSDGAASSYQLKQLEEQNARLKD 372
Cdd:PRK05771  101 EI-------------KELEEEISE-LENEIKELEQEIERLEpwGNFDLdLSLLLGFKYVSVFVGTVPEDKLEELKLESDV 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   373 ALVrmrDLSSSEKQEH----VKLQKLMEKKNQELEVVRQQRERLQEELSQAEsTIDELKEQvdaalgaeemvemltdrnl 448
Cdd:PRK05771  167 ENV---EYISTDKGYVyvvvVVLKELSDEVEEELKKLGFERLELEEEGTPSE-LIREIKEE------------------- 223

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 13259510   449 nLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDM 491
Cdd:PRK05771  224 -LEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAEA 265
IFT57 pfam10498
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ...
 214-378 1.04e-03

Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles found at the periphery of cells of diverse organizms. Intra-flagellar transport (IFT) is required for the assembly and maintenance of eukaryotic cilia and flagella, and consists of the bidirectional movement of large protein particles between the base and the distal tip of the organelle. IFT particles contain multiple copies of two distinct protein complexes, A and B, which contain at least 6 and 11 protein subunits. IFT57 is part of complex B but is not, however, required for the core subunits to stay associated. This protein is known as Huntington-interacting protein-1 in humans.


Pssm-ID: 463118 [Multi-domain]  Cd Length: 360  Bit Score: 43.02  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    214 SKEEEGLRAQVRDLEEKLETLR----LKRAEdKAKLKELEKHkiqLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALE- 288
Cdd:pfam10498  183 SKPREIIESNVDAAEWKLELERvlpqLKVTI-KADAKDWRAH---LEQMKQHKKSIEESLPDTKSQLDKLHTDISKTLEk 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    289 --AKERY----MEEMADtadaiEMATLDKEMAEERaESLQQEVEALKERVDEL---TTDLEILKAEIEEKG---SDGAas 356
Cdd:pfam10498  259 ieSREKYinsqLEPLIQ-----EYREAQDELSEVQ-EKYKQLSEGVTERTRELaeiTEELEKVKQEMEERGssmTDGS-- 330

                          170       180
                   ....*....|....*....|..
gi 13259510    357 syqlkqleeQNARLKDALVRMR 378
Cdd:pfam10498  331 ---------PLVKIKQALTKLK 343
prfA PRK00591
peptide chain release factor 1; Validated
 227-342 1.05e-03

peptide chain release factor 1; Validated


Pssm-ID: 234801 [Multi-domain]  Cd Length: 359  Bit Score: 42.76  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   227 LEEKLETLrlkraedKAKLKELEKhkiQLEQ------VQEWKSKMQEQqADLQ------RRLKEARKEAKEAleakerym 294
Cdd:PRK00591    4 MLDKLEAL-------EERYEELEA---LLSDpevisdQKRFRKLSKEY-AELEpiveayREYKQAQEDLEEA-------- 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 13259510   295 EEMADTADAIEMatldKEMAEEraeslqqEVEALKERVDELTTDLEIL 342
Cdd:PRK00591   65 KEMLEEESDPEM----REMAKE-------ELKELEERLEELEEELKIL 101
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
221-365 1.10e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 42.94  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  221 RAQVRDLEEKLETLRLKRAEDKAklkELEKHKIQLEQVQEWKSKMQEQQADLQ---------RRLKEARKEAKEALEAKE 291
Cdd:COG2268  222 EAEEAELEQEREIETARIAEAEA---ELAKKKAEERREAETARAEAEAAYEIAeanaerevqRQLEIAEREREIELQEKE 298

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13259510  292 RYMEEMADTADAIEMATLDKEMAEERAEslqQEVEALKERvdeLTTDLEILKAEIEEKGSDGAASSYQ--LKQLEE 365
Cdd:COG2268  299 AEREEAELEADVRKPAEAEKQAAEAEAE---AEAEAIRAK---GLAEAEGKRALAEAWNKLGDAAILLmlIEKLPE 368
Prefoldin_4 cd23165
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic ...
 271-345 1.13e-03

prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic prefoldin complex. Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467481 [Multi-domain]  Cd Length: 103  Bit Score: 39.84  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  271 DLQRRLKEARK-----EAKEALEAKERYMEEMADTADAIEMATLD-------------------KEMAEERAESLQQEVE 326
Cdd:cd23165    1 DQQKINKFSRLnarlhELKEELKAKKKELENLEDASDELELADDDepvpykigevfvhlsleeaQERLEKAKEELEEEIE 80

                         90
                 ....*....|....*....
gi 13259510  327 ALKERVDELTTDLEILKAE 345
Cdd:cd23165   81 KLEEEIDEIEEEMKELKVQ 99
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 215-329 1.22e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.56  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  215 KEEEGLRAQVRDLEEKLetLRLKRAEDKAKLKELEKHkiQLEQVQEWKSKMQEqqadlqrRLKEARKEAKEALEAKERym 294
Cdd:cd16269  200 IEAERAKAEAAEQERKL--LEEQQRELEQKLEDQERS--YEEHLRQLKEKMEE-------ERENLLKEQERALESKLK-- 266

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 13259510  295 eemadtadaiEMATLDKEMAEERAESLQQEVEALK 329
Cdd:cd16269  267 ----------EQEALLEEGFKEQAELLQEEIRSLK 291
Caldesmon pfam02029
Caldesmon;
215-508 1.24e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 42.93  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    215 KEEEGLRAQVRDLEEKLETlrlKRAEDKAKLKELEKHKIQLEQ-VQEWKSKMQEQQadlQRRLKEARKEAKEaleakerY 293
Cdd:pfam02029   23 KEEEEPSGQVTESVEPNEH---NSYEEDSELKPSGQGGLDEEEaFLDRTAKREERR---QKRLQEALERQKE-------F 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    294 MEEMADTADAIemATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEE-KGSDGAASSYQlkQLEEQNARLKD 372
Cdd:pfam02029   90 DPTIADEKESV--AERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQEnKWSTEVRQAEE--EGEEEEDKSEE 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    373 ALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMV---EMLTDRNLN 449
Cdd:pfam02029  166 AEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSqerEEEAEVFLE 245

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 13259510    450 LEEKVRELRETVGDLEamNEMNDELQENARETELELREQLdmagaRVREAQKRVEAAQE 508
Cdd:pfam02029  246 AEQKLEELRRRRQEKE--SEEFEKLRQKQQEAELELEELK-----KKREERRKLLEEEE 297
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 231-530 1.39e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 43.11  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    231 LETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKealeAKERYMEEMADTADAIEmATLD 310
Cdd:TIGR00606  188 LETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVK----SYENELDPLKNRLKEIE-HNLS 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    311 KEMaeeraeSLQQEVEALKERVDELTTDLEILKAEIEE--KGSDgaassYQLKQLEEQNARLkdalvrmrdlSSSEKQEH 388
Cdd:TIGR00606  263 KIM------KLDNEIKALKSRKKQMEKDNSELELKMEKvfQGTD-----EQLNDLYHNHQRT----------VREKEREL 321

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    389 VKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDA--ALGAEEMVEMLTD---RNLNLEEKVRELRETV-- 461
Cdd:TIGR00606  322 VDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRArdSLIQSLATRLELDgfeRGPFSERQIKNFHTLVie 401

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13259510    462 ---GDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDV 530
Cdd:TIGR00606  402 rqeDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRI 473
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 224-461 1.49e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 42.49  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    224 VRDLEEKLETLRLKRAEDKAKLK----ELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEArKEAKEALEAKerymeeMAD 299
Cdd:pfam15905   75 QKELEKEIRALVQERGEQDKRLQaleeELEKVEAKLNAAVREKTSLSASVASLEKQLLEL-TRVNELLKAK------FSE 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    300 TADAIEMATLDKEMAEERA--ESLQQEVEALKE----RVDELTTDLEILKAEI---EEKGSD----GAASSYQLKQLEEQ 366
Cdd:pfam15905  148 DGTQKKMSSLSMELMKLRNklEAKMKEVMAKQEgmegKLQVTQKNLEHSKGKVaqlEEKLVStekeKIEEKSETEKLLEY 227

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    367 NARLKDAlvrmRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQrerLQEELSQAESTIDELKEQVDAALGA-EEMVEMLTD 445
Cdd:pfam15905  228 ITELSCV----SEQVEKYKLDIAQLEELLKEKNDEIESLKQS---LEEKEQELSKQIKDLNEKCKLLESEkEELLREYEE 300

                          250
                   ....*....|....*.
gi 13259510    446 RNLNLEEKVRELRETV 461
Cdd:pfam15905  301 KEQTLNAELEELKEKL 316
PRK01156 PRK01156
chromosome segregation protein; Provisional
 214-529 1.52e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 42.97  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   214 SKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERY 293
Cdd:PRK01156  203 KKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERH 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   294 MEEMADTADA-----IEMATLDKEMAEERA--ESLQQEVEALKERVDELtTDLEILKAEIEEKGSDGAASSYQLKQLEEQ 366
Cdd:PRK01156  283 MKIINDPVYKnrnyiNDYFKYKNDIENKKQilSNIDAEINKYHAIIKKL-SVLQKDYNDYIKKKSRYDDLNNQILELEGY 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   367 NARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQEL-------EVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEM 439
Cdd:PRK01156  362 EMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILkiqeidpDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDE 441

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   440 V----EMLTDRNL------NL-EEKVRELRETVG-DLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQ 507
Cdd:PRK01156  442 LsrnmEMLNGQSVcpvcgtTLgEEKSNHIINHYNeKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEY 521

                         330       340
                  ....*....|....*....|..
gi 13259510   508 ETVADYQQTIKKYRQLTAHLQD 529
Cdd:PRK01156  522 NKIESARADLEDIKIKINELKD 543
TolC COG1538
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
274-546 1.53e-03

Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441147 [Multi-domain]  Cd Length: 367  Bit Score: 42.33  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  274 RRLKEARKEAKEALEAKERYMEE--MADTADA-IEMATLDKEM--AEERAESLQQEVEALKERVDE-LTTDLEILKAEIE 347
Cdd:COG1538   50 RARIEAAKAQAEAAEADLRAARLdlAAEVAQAyFDLLAAQEQLalAEENLALAEELLELARARYEAgLASRLDVLQAEAQ 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  348 EkgsdgAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELK 427
Cdd:COG1538  130 L-----AQARAQLAQAEAQLAQARNALALLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSEALERRPDLRAAEAQLEAAE 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  428 EQVDAA-------------LGAEEMVEMLTDRN------LNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQ 488
Cdd:COG1538  205 AEIGVAraaflpslslsasYGYSSSDDLFSGGSdtwsvgLSLSLPLFDGGRNRARVRAAKAQLEQAEAQYEQTVLQALQE 284

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13259510  489 LDMAGARVREAQKRVEAAQETVAD----YQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQ 546
Cdd:COG1538  285 VEDALAALRAAREQLEALEEALEAaeeaLELARARYRAGLASLLDVLDAQRELLQAQLNLIQ 346
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 925-1115 1.65e-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: 42.74  E-value: 1.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    925 ELRAAALRAEITDAEGLGLKLEDRE--TVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKD---ADERIEKVQTRLE 999
Cdd:TIGR02168  254 ELEELTAELQELEEKLEELRLEVSEleEEIEELQKELYALANEISRLEQQKQILRERLANLERQleeLEAQLEELESKLD 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   1000 ETQALLRKKEKEFEET---MDALQADIDQLEAEKAELKQRLNSQSKRtieglrgpppsgIATLVSGIAGEEQQRGAIPGq 1076
Cdd:TIGR02168  334 ELAEELAELEEKLEELkeeLESLEAELEELEAELEELESRLEELEEQ------------LETLRSKVAQLELQIASLNN- 400

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 13259510   1077 apgsvpgpglvkdsplllqQISAMRLHISQLQHENSILK 1115
Cdd:TIGR02168  401 -------------------EIERLEARLERLEDRRERLQ 420
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 220-303 1.66e-03

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: 40.69  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    220 LRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQL--------EQVQEWKSKMQEQQADLQ----------RRLKEARK 281
Cdd:pfam08614   76 LAQRLVDLNEELQELEKKLREDERRLAALEAERAQLeeklkdreEELREKRKLNQDLQDELValqlqlnmaeEKLRKLEK 155

                           90       100
                   ....*....|....*....|..
gi 13259510    282 EAKEALEakeRYMEEMADTADA 303
Cdd:pfam08614  156 ENRELVE---RWMKRKGQEAEA 174
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 225-590 1.70e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 42.73  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    225 RDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEArkeAKEALEAKERYMEEMADTADAi 304
Cdd:TIGR00606  440 RTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNS---LTETLKKEVKSLQNEKADLDR- 515

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    305 EMATLDKEMAE-ERAESLQQEVEALKErvDELTTDLEILKaeIEEKGSDGAASSY----QLKQLEEQNARLKDALVRMRD 379
Cdd:TIGR00606  516 KLRKLDQEMEQlNHHTTTRTQMEMLTK--DKMDKDEQIRK--IKSRHSDELTSLLgyfpNKKQLEDWLHSKSKEINQTRD 591

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    380 LSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQA------ESTIDELKEQVD------AALGA-----EEMVEM 442
Cdd:TIGR00606  592 RLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsqdeESDLERLKEEIEksskqrAMLAGatavySQFITQ 671

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    443 LTDRNLNLEEKVRELRETVGDLeamNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQ 522
Cdd:TIGR00606  672 LTDENQSCCPVCQRVFQTEAEL---QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPE 748

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13259510    523 LTAHLQDVNRELtnQQEASVERQQQPPPETFDFKIKFAETKAHAKAIeMELRQMEVAQANRHMSLLTA 590
Cdd:TIGR00606  749 LRNKLQKVNRDI--QRLKNDIEEQETLLGTIMPEEESAKVCLTDVTI-MERFQMELKDVERKIAQQAA 813
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 391-581 1.78e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.51  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   391 LQKLMEKKNQELEVVRQQRERLQEELSQaesTIDELKEQVDAALgaeemvemltdrnLNLEEKVRELREtvgdleamnem 470
Cdd:PRK00409  528 LERELEQKAEEAEALLKEAEKLKEELEE---KKEKLQEEEDKLL-------------EEAEKEAQQAIK----------- 580

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   471 ndELQENARETELELREQLDMAGARVR-----EAQKRVEAAQETVADYQQTIK------------KYRQL--TAHLQDV- 530
Cdd:PRK00409  581 --EAKKEADEIIKELRQLQKGGYASVKaheliEARKRLNKANEKKEKKKKKQKekqeelkvgdevKYLSLgqKGEVLSIp 658

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   531 -NRELTNQ--------QEASVERQQQPPPETFDfKIKFAETKAHAKAIEMELRQMEVAQA 581
Cdd:PRK00409  659 dDKEAIVQagimkmkvPLSDLEKIQKPKKKKKK-KPKTVKPKPRTVSLELDLRGMRYEEA 717
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
924-1046 1.86e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   924 VELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKkldsaAKDADERIEKVQTRLE-ETQ 1002
Cdd:PRK03918  312 IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEE-----AKAKKEELERLKKRLTgLTP 386

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 13259510  1003 ALLRKKEKEFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIE 1046
Cdd:PRK03918  387 EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 214-414 1.96e-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: 42.74  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    214 SKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVqewKSKMQEQQADLQRRLKEARkeaKEALEAKERY 293
Cdd:TIGR02168  872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE---LEELREKLAQLELRLEGLE---VRIDNLQERL 945

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    294 MEEMADTADAIEMATLDKEMAEERAEslqQEVEALKERVDELTtdlEILKAEIEEkgsdgaassyqlkqLEEQNARLKDA 373
Cdd:TIGR02168  946 SEEYSLTLEEAEALENKIEDDEEEAR---RRLKRLENKIKELG---PVNLAAIEE--------------YEELKERYDFL 1005

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 13259510    374 LVRMRDLSSSEKQehvkLQKLMEKKNQELevvrqqRERLQE 414
Cdd:TIGR02168 1006 TAQKEDLTEAKET----LEEAIEEIDREA------RERFKD 1036
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 241-404 2.13e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.51  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   241 DKAKlKELEKHKIQLEQVQEwksKMQEQQADLQRRLKEARKEAKEAleakERYMEEMADTADAIEmATLDKEMAEERaES 320
Cdd:PRK00409  505 EEAK-KLIGEDKEKLNELIA---SLEELERELEQKAEEAEALLKEA----EKLKEELEEKKEKLQ-EEEDKLLEEAE-KE 574

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   321 LQQEVEALKERVDELTTDLEILKaeieekgsDGAASSYQLKQLEEQNARLKDALvrmrdlssSEKQEHVKLQKlmeKKNQ 400
Cdd:PRK00409  575 AQQAIKEAKKEADEIIKELRQLQ--------KGGYASVKAHELIEARKRLNKAN--------EKKEKKKKKQK---EKQE 635


                  ....
gi 13259510   401 ELEV 404
Cdd:PRK00409  636 ELKV 639
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
911-1049 2.14e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.15  E-value: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  911 EYDAERPPSKPPPVELRAAALRAEITDAEGlglKLEDRETVIKELKkslkikgEELSEanvrlslLEKKLdsaaKDADER 990
Cdd:COG2433  384 ELIEKELPEEEPEAEREKEHEERELTEEEE---EIRRLEEQVERLE-------AEVEE-------LEAEL----EEKDER 442

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 13259510  991 IEKVQTRLEETQALLRKKEKEFEEtMDALQADIDQLEAEKAELKQRlNSQSKRTIEGLR 1049
Cdd:COG2433  443 IERLERELSEARSEERREIRKDRE-ISRLDREIERLERELEEERER-IEELKRKLERLK 499
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 222-416 2.15e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 40.89  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  222 AQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQL-EQVQEWKSKMQEQQADLQRR---LKEARKEAKEALEAKERYMEEM 297
Cdd:cd00176   33 ESVEALLKKHEALEAELAAHEERVEALNELGEQLiEEGHPDAEEIQERLEELNQRweeLRELAEERRQRLEEALDLQQFF 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  298 ADTADaiematLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgaasSYQLKQLEEQNARLKDalvRM 377
Cdd:cd00176  113 RDADD------LEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH-------EPRLKSLNELAEELLE---EG 176

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 13259510  378 RDLSSSEKQEhvKLQKLMEKKNQELEVVRQQRERLQEEL 416
Cdd:cd00176  177 HPDADEEIEE--KLEELNERWEELLELAEERQKKLEEAL 213
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 313-498 2.28e-03

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 40.32  E-value: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    313 MAEERAESLQQEVEALKERVDElttDLEILKAEIEEKgsdgaassyqlkqLEEQNARLKDALVRMRDLSSSEkqehvkLQ 392
Cdd:pfam01442   23 VAQELVDRLEKETEALRERLQK---DLEEVRAKLEPY-------------LEELQAKLGQNVEELRQRLEPY------TE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    393 KLMEKKNQELEVVRQQRERLQEEL-SQAESTIDELKEQVDAAlgAEEMVEmltdrnlNLEEKVRELRETVGdleamnEMN 471
Cdd:pfam01442   81 ELRKRLNADAEELQEKLAPYGEELrERLEQNVDALRARLAPY--AEELRQ-------KLAERLEELKESLA------PYA 145

                          170       180
                   ....*....|....*....|....*..
gi 13259510    472 DELQENARETELELREQLDMAGARVRE 498
Cdd:pfam01442  146 EEVQAQLSQRLQELREKLEPQAEDLRE 172
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 220-530 2.39e-03

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: 42.47  E-value: 2.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    220 LRAQVRDLEEK---LETLRLKR----AEDKAKLKELEKHKIQLEQvqeWKSKMQEQQADLQRRLKEARKEAKEALEAKER 292
Cdd:pfam01576  164 FTSNLAEEEEKaksLSKLKNKHeamiSDLEERLKKEEKGRQELEK---AKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    293 YMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVD--------------ELTTDLEILKAEIEEKGSDGAASSY 358
Cdd:pfam01576  241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLEseraarnkaekqrrDLGEELEALKTELEDTLDTTAAQQE 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    359 QLKQLEEQNARLKDALvrmrdlsSSEKQEH-VKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVdAALGAE 437
Cdd:pfam01576  321 LRSKREQEVTELKKAL-------EEETRSHeAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESEN-AELQAE 392

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    438 emVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVAdyqqti 517
Cdd:pfam01576  393 --LRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVS------ 464

                          330
                   ....*....|...
gi 13259510    518 kkyrQLTAHLQDV 530
Cdd:pfam01576  465 ----SLESQLQDT 473
Caldesmon pfam02029
Caldesmon;
216-512 2.43e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 42.16  E-value: 2.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    216 EEEGLRAQVRDLEEKLEtLRLKRAEDKAKLKELEKHKIQL------EQVQEWKSKMQEQQADLQRRLKEARKEAKEALEA 289
Cdd:pfam02029   60 EEEAFLDRTAKREERRQ-KRLQEALERQKEFDPTIADEKEsvaerkENNEEEENSSWEKEEKRDSRLGRYKEEETEIREK 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    290 KER---YMEEMADTADAIEMATLDKEMAEERAESL----QQEVEALKERVDELTTDLEILKAE---IEEKGSDGAASSYQ 359
Cdd:pfam02029  139 EYQenkWSTEVRQAEEEGEEEEDKSEEAEEVPTENfakeEVKDEKIKKEKKVKYESKVFLDQKrghPEVKSQNGEEEVTK 218

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    360 LKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLmEKKNQELEvvRQQRERLQEELSQAESTIDELKeqvdaalgaeem 439
Cdd:pfam02029  219 LKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEEL-RRRRQEKE--SEEFEKLRQKQQEAELELEELK------------ 283

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13259510    440 vemltdrnlnleeKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVAD 512
Cdd:pfam02029  284 -------------KKREERRKLLEEEEQRRKQEEAERKLREEEEKRRMKEEIERRRAEAAEKRQKLPEDSSSE 343
mukB PRK04863
chromosome partition protein MukB;
210-547 2.48e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 42.25  E-value: 2.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   210 LPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQ-VQEWKSKMQEQQAdLQRRLKEARKEAKEALE 288
Cdd:PRK04863  546 LGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQArIQRLAARAPAWLA-AQDALARLREQSGEEFE 624

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   289 AKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVE--------------ALKER-----VDELTTDLEILKAEIEEK 349
Cdd:PRK04863  625 DSQDVTEYMQQLLERERELTVERDELAARKQALDEEIErlsqpggsedprlnALAERfggvlLSEIYDDVSLEDAPYFSA 704

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   350 GSDGAAS-------SYQLKQLEEQNARLKDALV------RMRD-LSSSEKQEHVKLQKLMEK-----------------K 398
Cdd:PRK04863  705 LYGPARHaivvpdlSDAAEQLAGLEDCPEDLYLiegdpdSFDDsVFSVEELEKAVVVKIADRqwrysrfpevplfgraaR 784

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   399 NQELEVVRQQRERLQEELSQAESTIDELK---EQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQ 475
Cdd:PRK04863  785 EKRIEQLRAEREELAERYATLSFDVQKLQrlhQAFSRFIGSHLAVAFEADPEAELRQLNRRRVELERALADHESQEQQQR 864

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   476 ---ENARETELELREQLDMA--------GARVREAQKRVEAAQET---VADYQQTIKKYRQLTAHLQ---DVNRELTNQQ 538
Cdd:PRK04863  865 sqlEQAKEGLSALNRLLPRLnlladetlADRVEEIREQLDEAEEAkrfVQQHGNALAQLEPIVSVLQsdpEQFEQLKQDY 944


                  ....*....
gi 13259510   539 EASVERQQQ 547
Cdd:PRK04863  945 QQAQQTQRD 953
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 205-366 2.53e-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: 42.25  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  205 GAVPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQ----VQEWKSKMQEQQADLQRRLKEAR 280
Cdd:COG3096  512 QRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAqleeLEEQAAEAVEQRSELRQQLEQLR 591

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  281 KEAKEaLEAKERYMEEMADTADAIEM---ATLD--KEMAEERAESLQQEVEALKERvDELTTDLEILKAEIEEKGSDGAA 355
Cdd:COG3096  592 ARIKE-LAARAPAWLAAQDALERLREqsgEALAdsQEVTAAMQQLLEREREATVER-DELAARKQALESQIERLSQPGGA 669

                        170
                 ....*....|.
gi 13259510  356 SSYQLKQLEEQ 366
Cdd:COG3096  670 EDPRLLALAER 680
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
397-547 2.56e-03

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 41.57  E-value: 2.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  397 KKNQELevVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTdrnlNLEEKVRELRETVGDLEAMNEMNDELQE 476
Cdd:COG1566   68 KKGQVL--ARLDPTDLQAALAQAEAQLAAAEAQLARLEAELGAEAEIA----AAEAQLAAAQAQLDLAQRELERYQALYK 141

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13259510  477 NaretELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVnreltNQQEASVERQQQ 547
Cdd:COG1566  142 K----GAVSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQV-----AQAEAALAQAEL 203
EzrA COG4477
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ...
 218-348 2.65e-03

Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443574 [Multi-domain]  Cd Length: 567  Bit Score: 42.14  E-value: 2.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  218 EGLRAQVRDLEEKLETLRLKRAEDKAKLKELekhKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEM 297
Cdd:COG4477  350 RNLEKQIEELEKRYDEIDERIEEEKVAYSEL---QEELEEIEEQLEEIEEEQEEFSEKLKSLRKDELEAREKLDELKKKL 426

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13259510  298 ADTADAIEMATL---------DKEMAEERAESLQQE-------VEALKERVDELTTDLEILKAEIEE 348
Cdd:COG4477  427 REIKRRLEKSNLpglpeeyleMFEEASDEIEELSEElnevplnMDEVNRLLEEAEEDIETLEEKTEE 493
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 215-487 2.65e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.03  E-value: 2.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    215 KEEEGLRAQVRDLE----EKLETLRLKRAEDKAKLK-ELE---KHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEA 286
Cdd:pfam17380  360 RELERIRQEEIAMEisrmRELERLQMERQQKNERVRqELEaarKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRR 439

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    287 LEakerymeemadtadaiematldkemaEERAeslqQEVEALKERVDELTTDLEILKAEIEEKgsdgaassyQLKQLEEQ 366
Cdd:pfam17380  440 LE--------------------------EERA----REMERVRLEEQERQQQVERLRQQEEER---------KRKKLELE 480

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    367 NARlkdalvrmRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDR 446
Cdd:pfam17380  481 KEK--------RDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR 552

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 13259510    447 nlNLEEKVRELRETVGDLEAMnEMNDELQENARETELELRE 487
Cdd:pfam17380  553 --RIQEQMRKATEERSRLEAM-EREREMMRQIVESEKARAE 590
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 288-515 2.70e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.12  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   288 EAKERYMEEMADTADAIE-MATLDKEMAEER--AESLQQEVEALKERVDELTTDLEilkaEIEEKGSDGAASSYQ--LKQ 362
Cdd:PRK00409  506 EAKKLIGEDKEKLNELIAsLEELERELEQKAeeAEALLKEAEKLKEELEEKKEKLQ----EEEDKLLEEAEKEAQqaIKE 581

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   363 LEEQNARLKDALVRMRDlsssEKQEHVKLQKLMEKKNQelevVRQQRERLQEELSQAESTIDELKEqvdaalGAE----- 437
Cdd:PRK00409  582 AKKEADEIIKELRQLQK----GGYASVKAHELIEARKR----LNKANEKKEKKKKKQKEKQEELKV------GDEvkyls 647

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   438 -----EMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELRE---QLDMAGARVREAQKRVEAA--Q 507
Cdd:PRK00409  648 lgqkgEVLSIPDDKEAIVQAGIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPRTvslELDLRGMRYEEALERLDKYldD 727


                  ....*...
gi 13259510   508 ETVADYQQ 515
Cdd:PRK00409  728 ALLAGYGE 735
PRK01156 PRK01156
chromosome segregation protein; Provisional
 217-520 2.73e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 42.20  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   217 EEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEW-KSKMQEQQADLQRRLKEARKEAKEaLEAKERYME 295
Cdd:PRK01156  464 EEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYlESEEINKSINEYNKIESARADLED-IKIKINELK 542

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   296 EMADTADAI--EMATLDKEMAEERAESLQQ--------EVEALKERVDELTT---DLEILKAEIEEKGSDgaASSY---Q 359
Cdd:PRK01156  543 DKHDKYEEIknRYKSLKLEDLDSKRTSWLNalavisliDIETNRSRSNEIKKqlnDLESRLQEIEIGFPD--DKSYidkS 620

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   360 LKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRErLQEELSQAESTIDELKEQVDAAL----G 435
Cdd:PRK01156  621 IREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKE-ITSRINDIEDNLKKSRKALDDAKanraR 699

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   436 AEEMVEMLTDRNLNLEEKVRELREtvgDLEAMNEMndelqENARETELELREQLDMAGArvrEAQKRVEAAQETVADYQQ 515
Cdd:PRK01156  700 LESTIEILRTRINELSDRINDINE---TLESMKKI-----KKAIGDLKRLREAFDKSGV---PAMIRKSASQAMTSLTRK 768


                  ....*
gi 13259510   516 TIKKY 520
Cdd:PRK01156  769 YLFEF 773
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 191-331 2.83e-03

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: 40.30  E-value: 2.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    191 LAAPIIPTPVLTSPGAVPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEkhkiqlEQVQEWKSKMQEQQ- 269
Cdd:pfam08614   26 LQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLN------EELQELEKKLREDEr 99

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13259510    270 --ADLQRR---LKEARKEAKEALEAKERYMEEMADtadaiEMATLDKE--MAEERAESLQQEVEALKER 331
Cdd:pfam08614  100 rlAALEAEraqLEEKLKDREEELREKRKLNQDLQD-----ELVALQLQlnMAEEKLRKLEKENRELVER 163
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 925-1042 3.07e-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: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  925 ELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTRLEETQAL 1004
Cdd:COG1196  280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 13259510 1005 LRKKEKEFEETMDALQADIDQLEAEKAELKQRLNSQSK 1042
Cdd:COG1196  360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
COG5644 COG5644
U3 small nucleolar RNA-associated protein 14 [Function unknown];
267-512 3.07e-03

U3 small nucleolar RNA-associated protein 14 [Function unknown];


Pssm-ID: 227931 [Multi-domain]  Cd Length: 869  Bit Score: 42.00  E-value: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  267 EQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAI-EMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAE 345
Cdd:COG5644  331 EPRTESERKMHQALLDAGLENESALKKQEELALNKLSVeEVAERTRQLRFMRELMFREERKAKRVAKIKSKTYRKIRKNR 410

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  346 IEEKGSDGAASSyqlkQLEEQNARLKDALVRMrdlssseKQEHVKLQKLMEKknqelevvrqqrerLQEELSQAESTIDE 425
Cdd:COG5644  411 KEKEMALIPKSE----DLENEKSEEARALERM-------TQRHKNTSSWTRK--------------MLERASHGEGTREA 465

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  426 LKEQVDAalgAEEMVEMLTDRNLNLEEKVRElrETVGDLEamNEMNDELQENARETELELREQLDMAGARVREAQKRvEA 505
Cdd:COG5644  466 VNEQIRK---GDELMQRIHGKEIMDGEDVSE--FSDSDYD--TNEQVSTAFEKIRNEEELKGVLGMKFMRDASNRQM-AA 537


                 ....*..
gi 13259510  506 AQETVAD 512
Cdd:COG5644  538 SKISVAD 544
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 257-480 3.56e-03

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 41.55  E-value: 3.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    257 QVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDEL- 335
Cdd:pfam05701   32 QTVERRKLVELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAKQDSELAKLRVEEMe 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    336 -----------TTDLEILKAEIEEKGSDGAASSYQLKQLEEQnarlKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEV 404
Cdd:pfam05701  112 qgiadeasvaaKAQLEVAKARHAAAVAELKSVKEELESLRKE----YASLVSERDIAIKRAEEAVSASKEIEKTVEELTI 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    405 vrqQRERLQEELSQAESTIDELKEQ-VDAALGAEEmvEMLT-DRNLN-LEEKVRELRETV---GDLEAMNEMNDELQENA 478
Cdd:pfam05701  188 ---ELIATKESLESAHAAHLEAEEHrIGAALAREQ--DKLNwEKELKqAEEELQRLNQQLlsaKDLKSKLETASALLLDL 262


                   ..
gi 13259510    479 RE 480
Cdd:pfam05701  263 KA 264
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 218-394 3.58e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 41.16  E-value: 3.58e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510     218 EGLRaqvRDLEEKLETLRlkraEDKAKLKElekhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKErymeem 297
Cdd:smart00787  143 EGLK---EGLDENLEGLK----EDYKLLMK------ELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDP------ 203

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510     298 adtadaiemATLDKemAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQNARLKDALVRM 377
Cdd:smart00787  204 ---------TELDR--AKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTN-------KKSELNTEIAEAEKKLEQC 265

                           170       180
                    ....*....|....*....|.
gi 13259510     378 RDLSSSE----KQEHVKLQKL 394
Cdd:smart00787  266 RGFTFKEieklKEQLKLLQSL 286
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 216-370 3.69e-03

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


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 40.90  E-value: 3.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    216 EEEGLRAQVRDLEEKLETLR--LKRAEDKAkLKELEKHKIQL----EQVQEWKSKMQEQQADLQRRLKEARKEAKEALEA 289
Cdd:pfam09787   55 ERDLLREEIQKLRGQIQQLRteLQELEAQQ-QEEAESSREQLqeleEQLATERSARREAEAELERLQEELRYLEEELRRS 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    290 KERYMEEMADTADAIEMATlDKEMAEERAESLQQEVEAlkeRVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNAR 369
Cdd:pfam09787  134 KATLQSRIKDREAEIEKLR-NQLTSKSQSSSSQSELEN---RLHQLTETLIQKQTMLEALSTEKNSLVLQLERMEQQIKE 209


                   .
gi 13259510    370 L 370
Cdd:pfam09787  210 L 210
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
931-1037 3.79e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 3.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   931 LRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDAdERIEKVQTRLEEtqalLRKKEK 1010
Cdd:PRK03918  174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV-KELEELKEEIEE----LEKELE 248

                          90       100
                  ....*....|....*....|....*..
gi 13259510  1011 EFEETMDALQADIDQLEAEKAELKQRL 1037
Cdd:PRK03918  249 SLEGSKRKLEEKIRELEERIEELKKEI 275
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 215-501 3.81e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 41.55  E-value: 3.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    215 KEEEGLRAQVRDLEEKLETLRLKRAEdkaklkELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYM 294
Cdd:pfam05667  310 NEAPAATSSPPTKVETEEELQQQREE------ELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELE 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    295 EEMADTADAIEMAtldkEMAEERAESLQQEVEALKERVDELTT-----------DLEILKAEIEEKGSDgaaSSYQLKQL 363
Cdd:pfam05667  384 KQYKVKKKTLDLL----PDAEENIAKLQALVDASAQRLVELAGqwekhrvplieEYRALKEAKSNKEDE---SQRKLEEI 456

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    364 EEQNARLKD--ALVRMRDlsssekQEHVKLQKLMEKKNQE----------LEVV---RQQRERLQEELSQaestIDELKE 428
Cdd:pfam05667  457 KELREKIKEvaEEAKQKE------ELYKQLVAEYERLPKDvsrsaytrriLEIVkniKKQKEEITKILSD----TKSLQK 526

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13259510    429 QVDAALGAEEMVEMLTDRNLNLEEKVRE-LRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQK 501
Cdd:pfam05667  527 EINSLTGKLDRTFTVTDELVFKDAKKDEsVRKAYKYLAALHENCEQLIQTVEETGTIMREIRDLEEQIETESGK 600
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 927-1039 4.13e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 4.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  927 RAAALRAEITDAEGlglKLEDRETVIKELKKSLKIKGEELSEANV------------RLSLLeKKLDSAAKDADERIEKV 994
Cdd:COG3883   66 EIDKLQAEIAEAEA---EIEERREELGERARALYRSGGSVSYLDVllgsesfsdfldRLSAL-SKIADADADLLEELKAD 141

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 13259510  995 QTRLEETQALLRKKEKEFEETMDALQADIDQLEAEKAELKQRLNS 1039
Cdd:COG3883  142 KAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQ 186
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 215-373 4.35e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 40.82  E-value: 4.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  215 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKhkiQLEQVQEWKSKMQEQQ--ADLQRRLKEARKE----AKEALE 288
Cdd:cd22656  128 KEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEK---ALKDLLTDEGGAIARKeiKDLQKELEKLNEEyaakLKAKID 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  289 AKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERV-------DELTTDLEILKAEIEEKGSDGAA---SSY 358
Cdd:cd22656  205 ELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALeklqgawQAIATDLDSLKDLLEDDISKIPAailAKL 284

                        170
                 ....*....|....*
gi 13259510  359 QLKQLEEQNARLKDA 373
Cdd:cd22656  285 ELEKAIEKWNELAEK 299
Not3 pfam04065
Not1 N-terminal domain, CCR4-Not complex component;
229-371 4.41e-03

Not1 N-terminal domain, CCR4-Not complex component;


Pssm-ID: 461155 [Multi-domain]  Cd Length: 228  Bit Score: 40.22  E-value: 4.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    229 EKLEtlrlkrAEDKAKLKELEKHKiqlEQVQEW--------KSKMQEQqadlqRRLKEARKEAKEALEakeRYMEEMADT 300
Cdd:pfam04065   40 EKLE------ADLKKEIKKLQRLR---DQIKTWlssndikdKKKLLEN-----RKLIEEAMERFKAVE---KESKTKAFS 102

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13259510    301 ADAIEMATLDKEMAEERAEslQQEVEALKERVDELTTDLEILKAEIE-----EKGSDGAASSYQLKQLEEQNARLK 371
Cdd:pfam04065  103 KEGLSLAAASKLDPKEKEK--AEARDWLSDSIDELNRQIEALEAEIEslqaqKKKKKKDSEKARLEELEKLIERHK 176
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 248-430 4.70e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 41.18  E-value: 4.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    248 LEKHKIQLEQVQE----WKSKMQEQQADLQRrLKEARKEAKEALEAK-ERYmeemadtadaiematldkEMAEERAESLQ 322
Cdd:pfam10168  549 LKKHDLAREEIQKrvklLKLQKEQQLQELQS-LEEERKSLSERAEKLaEKY------------------EEIKDKQEKLM 609

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    323 QEVEALKERVDELTTDL-EILKAEIEEkgsdgaASSYQlKQLEEQNARLKDALVRMrdlssSEKQEHVKLQKLMEKKNqE 401
Cdd:pfam10168  610 RRCKKVLQRLNSQLPVLsDAEREMKKE------LETIN-EQLKHLANAIKQAKKKM-----NYQRYQIAKSQSIRKKS-S 676

                          170       180
                   ....*....|....*....|....*....
gi 13259510    402 LEVVRQQRERLQEELSQAESTIDELKEQV 430
Cdd:pfam10168  677 LSLSEKQRKTIKEILKQLGSEIDELIKQV 705
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 229-459 5.22e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 41.07  E-value: 5.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   229 EKLETLRLKRAEDK--AKLKELE-------KHKIQLEQVQEWKSKMQEQQADLqRRLKEARKEAKEALEAKERYmeEMAD 299
Cdd:PRK05771    7 KKVLIVTLKSYKDEvlEALHELGvvhiedlKEELSNERLRKLRSLLTKLSEAL-DKLRSYLPKLNPLREEKKKV--SVKS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   300 TADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILK----------AEIEEKGSDGAASSYQLKQLEEQNAR 369
Cdd:PRK05771   84 LEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwgnfdldlsLLLGFKYVSVFVGTVPEDKLEELKLE 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   370 LKDALVrmrDLSSSEKQEH----VKLQKLMEKKNQELEVVRQQRERL------QEELSQAESTIDELKEQVDAALG-AEE 438
Cdd:PRK05771  164 SDVENV---EYISTDKGYVyvvvVVLKELSDEVEEELKKLGFERLELeeegtpSELIREIKEELEEIEKERESLLEeLKE 240

                         250       260
                  ....*....|....*....|.
gi 13259510   439 MVEMLTDRNLNLEEKVRELRE 459
Cdd:PRK05771  241 LAKKYLEELLALYEYLEIELE 261
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 319-424 5.58e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 41.09  E-value: 5.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   319 ESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLkdalvrmrdlssseKQEHVKLQKlmekk 398
Cdd:PRK11448  145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQEL--------------EAQLEQLQE----- 205

                          90       100
                  ....*....|....*....|....*.
gi 13259510   399 nQELEVVRQQRERLQEELSQAESTID 424
Cdd:PRK11448  206 -KAAETSQERKQKRKEITDQAAKRLE 230
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 210-420 5.60e-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: 41.26  E-value: 5.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    210 LPSPSKEEEGLRAQVRDLEEKLETLRLK-RAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAkEALE 288
Cdd:pfam15921  669 LNSLSEDYEVLKRNFRNKSEEMETTTNKlKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQI-DALQ 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    289 AKERYMEEmadtadAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAeieekgsdgaassyqlkqleeQNA 368
Cdd:pfam15921  748 SKIQFLEE------AMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRS---------------------QER 800

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 13259510    369 RLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQElevvrQQRERLQEELSQAE 420
Cdd:pfam15921  801 RLKEKVANMEVALDKASLQFAECQDIIQRQEQE-----SVRLKLQHTLDVKE 847
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 207-306 5.72e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 41.09  E-value: 5.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   207 VPPlPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEwksKMQEQQADLQRRLKEARKEAKEA 286
Cdd:PRK11448  135 VPP-EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAA---ELEEKQQELEAQLEQLQEKAAET 210

                          90       100
                  ....*....|....*....|.
gi 13259510   287 -LEAKERYMEEMADTADAIEM 306
Cdd:PRK11448  211 sQERKQKRKEITDQAAKRLEL 231
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 254-345 6.05e-03

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


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 38.19  E-value: 6.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  254 QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADtaDAIEMATLDKEMAEERA-ESLQQEVEALKERV 332
Cdd:cd06503   38 SLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKE--EILAEAKEEAERILEQAkAEIEQEKEKALAEL 115

                         90
                 ....*....|...
gi 13259510  333 DELTTDLEILKAE 345
Cdd:cd06503  116 RKEVADLAVEAAE 128
PHA03247 PHA03247
large tegument protein UL36; Provisional
 108-223 6.22e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 6.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   108 TPDSSASKVLKREGTDTTAK--TSKLRGLKPKKAPTARKT---TTRRPKPTRPASTGVAGASSSLGPSGSASAGELSSSE 182
Cdd:PHA03247  360 TPPSSLEDLSAGRHHPKRASlpTRKRRSARHAATPFARGPggdDQTRPAAPVPASVPTPAPTPVPASAPPPPATPLPSAE 439

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 13259510   183 PSTPAQTPLAAPIIPTPVLTSPGAVPPLPSPSKEEEGLRAQ 223
Cdd:PHA03247  440 PGSDDGPAPPPERQPPAPATEPAPDDPDDATRKALDALRER 480
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 214-528 6.62e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.80  E-value: 6.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    214 SKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQ-EWKSKMQEQQADLQRRLKEARKEAKEALEAKER 292
Cdd:TIGR00606  240 VKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNsELELKMEKVFQGTDEQLNDLYHNHQRTVREKER 319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    293 ymeEMADTADAI-----EMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIE---EKGSDGAASSYQLKQ-- 362
Cdd:TIGR00606  320 ---ELVDCQRELeklnkERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRlelDGFERGPFSERQIKNfh 396

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    363 ---LEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEqvdaalgaeem 439
Cdd:TIGR00606  397 tlvIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQ----------- 465

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    440 VEMLTDRNLNLEEkvrELRETVGDLEAMNEMNDELQENARETELElREQLDMAGARVREAQKRVEAAQETVADYQQTIKK 519
Cdd:TIGR00606  466 LEGSSDRILELDQ---ELRKAERELSKAEKNSLTETLKKEVKSLQ-NEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLT 541


                   ....*....
gi 13259510    520 YRQLTAHLQ 528
Cdd:TIGR00606  542 KDKMDKDEQ 550
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
925-1039 6.97e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 6.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  925 ELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDAD--------------ER 990
Cdd:COG4913  263 RYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDeleaqirgnggdrlEQ 342

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 13259510  991 IEKVQTRLEETQALLRKKEKEFEETMDALQ----ADIDQLEAEKAELKQRLNS 1039
Cdd:COG4913  343 LEREIERLERELEERERRRARLEALLAALGlplpASAEEFAALRAEAAALLEA 395
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 107-222 7.01e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.92  E-value: 7.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510   107 ETPDSSASKVlKREGTDTTAKTSKLRGLKPKKAPTARKTTTRRPKPTR-----PASTGVAGASSSLGPSGSAS-AGELSS 180
Cdd:PHA03307  254 ECPLPRPAPI-TLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPsspgsGPAPSSPRASSSSSSSRESSsSSTSSS 332

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 13259510   181 SEPSTPAQTPLAAPIIPTPVLTSPGAVPPLPSPSKEEEGLRA 222
Cdd:PHA03307  333 SESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRA 374
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 952-1042 7.30e-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: 40.13  E-value: 7.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  952 IKELKKSLKIKGEELSEANVRLSLLEKKLDSAA---KDADERIEKVQTRLEETQALLRKKEKEFEETMDALQADIDQLEA 1028
Cdd:COG4942   22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLkqlAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101

                         90
                 ....*....|....
gi 13259510 1029 EKAELKQRLNSQSK 1042
Cdd:COG4942  102 QKEELAELLRALYR 115
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 184-571 7.39e-03

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 40.51  E-value: 7.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    184 STPAQTPLAAPIIPTPVLTSPGAVPPLPSPSKEEEglrAQVRDLEEKLETLRLKRAEDKAKLKElEKHKIQLEQVQEWKS 263
Cdd:pfam09731   71 VVSAVTGESKEPKEEKKQVKIPRQSGVSSEVAEEE---KEATKDAAEAKAQLPKSEQEKEKALE-EVLKEAISKAESATA 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    264 KMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMAtLDKEMAEERAESLQQEVEALKERVDEL------TT 337
Cdd:pfam09731  147 VAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEA-LAEKLKEVINLAKQSEEEAAPPLLDAApetppkLP 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    338 DLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDA-LVRMRD-----LSSSEKQEHVKLQKLMEKKNQELEVVRQQRER 411
Cdd:pfam09731  226 EHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQeLVSIFPdiipvLKEDNLLSNDDLNSLIAHAHREIDQLSKKLAE 305

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    412 LQ-EELSQAESTIDELKEQVDAAlgAEEMVEmltdrnlNLEEKVRELREtvgDLEAMNEmnDELQENARETELELREQLD 490
Cdd:pfam09731  306 LKkREEKHIERALEKQKEELDKL--AEELSA-------RLEEVRAADEA---QLRLEFE--REREEIRESYEEKLRTELE 371

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    491 MAGARVREAQKRVEAAQETVADYQqtikkyrqltaHLQDVNRELTNQQEAsverqqqpppetfdFKIKFAETKAHAKAIE 570
Cdd:pfam09731  372 RQAEAHEEHLKDVLVEQEIELQRE-----------FLQDIKEKVEEERAG--------------RLLKLNELLANLKGLE 426


                   .
gi 13259510    571 M 571
Cdd:pfam09731  427 K 427
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 256-546 7.66e-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: 40.87  E-value: 7.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    256 EQVQEWKSKMQEQQADLQRRLkearKEAKEALEAKERYMEEmadtaDAIEMATLDKEMAEERAESL------QQEVEALK 329
Cdd:pfam15921   74 EHIERVLEEYSHQVKDLQRRL----NESNELHEKQKFYLRQ-----SVIDLQTKLQEMQMERDAMAdirrreSQSQEDLR 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    330 ERVDELTTDLEILKAEIEEKGSDGAASSYQLKQL----EEQNARLKDALVRMRDLSSSEKQEHVKLQKlMEKKNQELEVV 405
Cdd:pfam15921  145 NQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMmlshEGVLQEIRSILVDFEEASGKKIYEHDSMST-MHFRSLGSAIS 223

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    406 RQQRErLQEELSQAESTIDELKEQVDaALGAEEM--VEMLTDRNLN---------------LEEKVRELRETVGDLEAMN 468
Cdd:pfam15921  224 KILRE-LDTEISYLKGRIFPVEDQLE-ALKSESQnkIELLLQQHQDrieqliseheveitgLTEKASSARSQANSIQSQL 301

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13259510    469 EMndeLQENARETELELREQLDMAGARVREAQKRVEAAQETVADyqqtikKYRQLTAHLQDVNRELTnqqEASVERQQ 546
Cdd:pfam15921  302 EI---IQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYED------KIEELEKQLVLANSELT---EARTERDQ 367
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 215-459 7.83e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.90  E-value: 7.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    215 KEEEGLRAQVRDLEEKLETLRLKRA---EDKAKLKELEKHKIQL--------EQVQEWKSKMQEQQADLQRRLKEARKEA 283
Cdd:pfam13868   85 REQKRQEEYEEKLQEREQMDEIVERiqeEDQAEAEEKLEKQRQLreeidefnEEQAEWKELEKEEEREEDERILEYLKEK 164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    284 KEALEAKERYMEEMADtadaiematlDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQL 363
Cdd:pfam13868  165 AEREEEREAEREEIEE----------EKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQR 234

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    364 EEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEvvRQQRERLQEELSQAESTIDELKEQVDAalgAEEMVEMl 443
Cdd:pfam13868  235 QELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDE--EIEQEEAEKRRMKRLEHRRELEKQIEE---REEQRAA- 308

                          250
                   ....*....|....*.
gi 13259510    444 tDRNLNLEEKVRELRE 459
Cdd:pfam13868  309 -EREEELEEGERLREE 323
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 925-1046 7.86e-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: 7.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  925 ELRAAALRAEITDAEGlglKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTRLEETQAL 1004
Cdd:COG1196  315 EERLEELEEELAELEE---ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 13259510 1005 LRKKEkefeetmdALQADIDQLEAEKAELKQRLNSQSKRTIE 1046
Cdd:COG1196  392 LRAAA--------ELAAQLEELEEAEEALLERLERLEEELEE 425
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 248-476 7.96e-03

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: 39.12  E-value: 7.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    248 LEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEmadtadaiematldkemaeeraesLQQEVEA 327
Cdd:pfam13851    3 MKNHEKAFNEIKNYYNDITRNNLELIKSLKEEIAELKKKEERNEKLMSE------------------------IQQENKR 58

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    328 LKERVDELTTDLEILKAEIEEKGSDGAAssyqlkqLEEQNARLKDALVRMRDLssseKQEHVKLQKLMEKKNQELEVVRQ 407
Cdd:pfam13851   59 LTEPLQKAQEEVEELRKQLENYEKDKQS-------LKNLKARLKVLEKELKDL----KWEHEVLEQRFEKVERERDELYD 127

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13259510    408 QRERLQEELSQAEstidELKEQVdaalgAEEMVEMLTDrnlNLEEKVRELRETVG----DLEAMNEMNDELQE 476
Cdd:pfam13851  128 KFEAAIQDVQQKT----GLKNLL-----LEKKLQALGE---TLEKKEAQLNEVLAaanlDPDALQAVTEKLED 188
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
921-1049 9.22e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 9.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  921 PPPVELRAAALRAEITDAEGLGLKLEDRETVIKELKKsLKIKGEELSEANVRLSLLEKKLDSAAKDADER-IEKVQTRLE 999
Cdd:COG4913  220 EPDTFEAADALVEHFDDLERAHEALEDAREQIELLEP-IRELAERYAAARERLAELEYLRAALRLWFAQRrLELLEAELE 298

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 13259510 1000 ETQALLRKKEKEfeetMDALQADIDQLEAEKAELKQRLNSQSKRTIEGLR 1049
Cdd:COG4913  299 ELRAELARLEAE----LERLEARLDALREELDELEAQIRGNGGDRLEQLE 344
Rabaptin pfam03528
Rabaptin;
251-429 9.72e-03

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 40.09  E-value: 9.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    251 HKIQLEQVQ--EWKSKMQEQQADLQRRLKEARKEakEALEAKERYMEEMADTADAI------EMATLDKEMAEerAESLQ 322
Cdd:pfam03528  126 RRLEQERAQwnQYRESAEREIADLRRRLSEGQEE--ENLEDEMKKAQEDAEKLRSVvmpmekEIAALKAKLTE--AEDKI 201

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    323 QEVEALKerVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKN-QE 401
Cdd:pfam03528  202 KELEASK--MKELNHYLEAEKSCRTDLEMYVAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANdQF 279

                          170       180       190
                   ....*....|....*....|....*....|..
gi 13259510    402 LEVVR---QQRERLQEELSQAE-STIDELKEQ 429
Cdd:pfam03528  280 LESQRllmRDMQRMESVLTSEQlRQVEEIKKK 311
DUF4349 pfam14257
Domain of unknown function (DUF4349); This family of proteins is found in bacteria and archaea. ...
 267-341 9.82e-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: 9.82e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13259510    267 EQQADLqrrlkEARKEAKEALEakERYMEEMADTADAIEMATLDKEMAEERA--ESLQQEVEALKERVDELTTDLEI 341
Cdd:pfam14257   85 EQYVDL-----EARLKALRASE--DRLLALLERAGSVEDLLAVERELSEVQAelESLEGQLRYLDDQVAYSTVTLTL 154
Prefoldin_4 cd23165
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic ...
 944-1037 9.88e-03

prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic prefoldin complex. Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467481 [Multi-domain]  Cd Length: 103  Bit Score: 37.14  E-value: 9.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510  944 KLEDRETVIKELKKSLKIKGEELSEANVRLSLLekkldsaakDADERIEK------VQTRLEETQALLRKKEKEFEETMD 1017
Cdd:cd23165   10 RLNARLHELKEELKAKKKELENLEDASDELELA---------DDDEPVPYkigevfVHLSLEEAQERLEKAKEELEEEIE 80

                         90       100
                 ....*....|....*....|
gi 13259510 1018 ALQADIDQLEAEKAELKQRL 1037
Cdd:cd23165   81 KLEEEIDEIEEEMKELKVQL 100
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 317-546 9.91e-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: 39.88  E-value: 9.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    317 RAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQL----KQLEEQNARLKDALVRMRDLSSSEKQEHVKLQ 392
Cdd:pfam07888   28 RAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWerqrRELESRVAELKEELRQSREKHEELEEKYKELS 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    393 KLMEKKNQELEVVRQQRErlqeelsQAESTIDELkeqvdaalgaEEMVEMLTDRNLNLEEKVRELRETV----GDLEAMN 468
Cdd:pfam07888  108 ASSEELSEEKDALLAQRA-------AHEARIREL----------EEDIKTLTQRVLERETELERMKERAkkagAQRKEEE 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13259510    469 EMNDELQENARETELELRE-QLDMAGARVREAQKRVEAA--QETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQ 545
Cdd:pfam07888  171 AERKQLQAKLQQTEEELRSlSKEFQELRNSLAQRDTQVLqlQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASE 250


                   .
gi 13259510    546 Q 546
Cdd:pfam07888  251 R 251
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH