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Conserved domains on  [gi|1622825706|ref|XP_028700813|]
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centrosomal protein of 85 kDa isoform X9 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
364-581 2.39e-11

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 67.00  E-value: 2.39e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  364 LKEKELLIDKQRKHISQLEQKVRE--SELQVHSALLGRpapfgdvCLLRLQELQRENTFLRAQFAQKTEALS---REKID 438
Cdd:TIGR02168  262 LQELEEKLEELRLEVSELEEEIEElqKELYALANEISR-------LEQQKQILRERLANLERQLEELEAQLEeleSKLDE 334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  439 LEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEE---RVKGRDKHINNLKKK---CQKESEQNREKQQRIETLERYLAD 512
Cdd:TIGR02168  335 LAEELAELEEKLEELKEELESLEAELEELEAELEElesRLEELEEQLETLRSKvaqLELQIASLNNEIERLEARLERLED 414
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622825706  513 LPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDK 581
Cdd:TIGR02168  415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
364-581 2.39e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 67.00  E-value: 2.39e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  364 LKEKELLIDKQRKHISQLEQKVRE--SELQVHSALLGRpapfgdvCLLRLQELQRENTFLRAQFAQKTEALS---REKID 438
Cdd:TIGR02168  262 LQELEEKLEELRLEVSELEEEIEElqKELYALANEISR-------LEQQKQILRERLANLERQLEELEAQLEeleSKLDE 334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  439 LEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEE---RVKGRDKHINNLKKK---CQKESEQNREKQQRIETLERYLAD 512
Cdd:TIGR02168  335 LAEELAELEEKLEELKEELESLEAELEELEAELEElesRLEELEEQLETLRSKvaqLELQIASLNNEIERLEARLERLED 414
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622825706  513 LPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDK 581
Cdd:TIGR02168  415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
309-587 1.15e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.96  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 309 ELSTCRQQLELIRLQMEQMQLQngaichhpaafapslpilepaqwISILNSNEHLLKEKELLIDKQRKHisqLEQKVRES 388
Cdd:COG1196   261 ELAELEAELEELRLELEELELE-----------------------LEEAQAEEYELLAELARLEQDIAR---LEERRREL 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 389 ELQvhsallgrpapfgdvcLLRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEV 468
Cdd:COG1196   315 EER----------------LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 469 KKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKstELQEKVTELESLLE 548
Cdd:COG1196   379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE--ALEEAAEEEAELEE 456
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1622825706 549 ETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEET 587
Cdd:COG1196   457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
374-570 1.50e-09

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: 59.82  E-value: 1.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 374 QRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLL--RLQELQRENTFLRAQFA-----QKTEALSREKIDLEKKLSAS 446
Cdd:pfam15905  92 QDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLekQLLELTRVNELLKAKFSedgtqKKMSSLSMELMKLRNKLEAK 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 447 EVEVQLIRESLKVALQ------KHS-EEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDH 519
Cdd:pfam15905 172 MKEVMAKQEGMEGKLQvtqknlEHSkGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEEL 251
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622825706 520 QKQsqqlKDSELKS--TELQEKVTELESLLEETQAICRDRETQLESLRQREAE 570
Cdd:pfam15905 252 LKE----KNDEIESlkQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEE 300
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
361-565 9.21e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.46  E-value: 9.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 361 EHLLKEKELLIDKQRKHISQLEQKVRESElqvhsallgrpapfgdvcllRLQELQRENTFLRAQFAQKTEALSRekidLE 440
Cdd:PRK03918  258 EEKIRELEERIEELKKEIEELEEKVKELK--------------------ELKEKAEEYIKLSEFYEEYLDELRE----IE 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 441 KKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRDKHINNLKKKcQKESEQNREKQQRIETLERYLADLPTledhQ 520
Cdd:PRK03918  314 KRLSRLEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLTGLTP----E 387
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1622825706 521 KQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLR 565
Cdd:PRK03918  388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
411-546 1.36e-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: 44.24  E-value: 1.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  411 LQELQRENTFLRAQFAQkteaLSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQ 490
Cdd:smart00787 153 LEGLKEDYKLLMKELEL----LNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLE 228
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  491 KESEQNREKQQRIETL----ERYLADLPTLEDHQKQSQQLKDSELKstELQEKVTELESL 546
Cdd:smart00787 229 ELEEELQELESKIEDLtnkkSELNTEIAEAEKKLEQCRGFTFKEIE--KLKEQLKLLQSL 286
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
438-614 6.35e-04

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: 41.66  E-value: 6.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 438 DLEKKLSASEVEVQLirESLKVALQKH---SEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADL- 513
Cdd:cd00176    18 EKEELLSSTDYGDDL--ESVEALLKKHealEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELa 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 514 ----PTLEDHQKQSQQL------------KDSELKSTELQEKVTELESLLEETQAICRD---RETQLESLRQREAEFSSA 574
Cdd:cd00176    96 eerrQRLEEALDLQQFFrdaddleqwleeKEAALASEDLGKDLESVEELLKKHKELEEEleaHEPRLKSLNELAEELLEE 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1622825706 575 GHSLQDKQSveetsgegpEVEMESWQKQYDSLQKVTEDVQ 614
Cdd:cd00176   176 GHPDADEEI---------EEKLEELNERWEELLELAEERQ 206
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
364-581 2.39e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 67.00  E-value: 2.39e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  364 LKEKELLIDKQRKHISQLEQKVRE--SELQVHSALLGRpapfgdvCLLRLQELQRENTFLRAQFAQKTEALS---REKID 438
Cdd:TIGR02168  262 LQELEEKLEELRLEVSELEEEIEElqKELYALANEISR-------LEQQKQILRERLANLERQLEELEAQLEeleSKLDE 334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  439 LEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEE---RVKGRDKHINNLKKK---CQKESEQNREKQQRIETLERYLAD 512
Cdd:TIGR02168  335 LAEELAELEEKLEELKEELESLEAELEELEAELEElesRLEELEEQLETLRSKvaqLELQIASLNNEIERLEARLERLED 414
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622825706  513 LPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDK 581
Cdd:TIGR02168  415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
309-587 1.15e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.96  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 309 ELSTCRQQLELIRLQMEQMQLQngaichhpaafapslpilepaqwISILNSNEHLLKEKELLIDKQRKHisqLEQKVRES 388
Cdd:COG1196   261 ELAELEAELEELRLELEELELE-----------------------LEEAQAEEYELLAELARLEQDIAR---LEERRREL 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 389 ELQvhsallgrpapfgdvcLLRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEV 468
Cdd:COG1196   315 EER----------------LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 469 KKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKstELQEKVTELESLLE 548
Cdd:COG1196   379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE--ALEEAAEEEAELEE 456
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1622825706 549 ETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEET 587
Cdd:COG1196   457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
408-615 1.36e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.57  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 408 LLRLQELQREntflRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRdkhINNLKK 487
Cdd:COG1196   231 LLKLRELEAE----LEELEAELEELEAELEELEAELAELEAELEELRLELE-ELELELEEAQAEEYELLAE---LARLEQ 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 488 KCQKESEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQR 567
Cdd:COG1196   303 DIARLEERRRELEERLEELEEELAEL--EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1622825706 568 EAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKVTEDVQA 615
Cdd:COG1196   381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
374-570 1.50e-09

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: 59.82  E-value: 1.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 374 QRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLL--RLQELQRENTFLRAQFA-----QKTEALSREKIDLEKKLSAS 446
Cdd:pfam15905  92 QDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLekQLLELTRVNELLKAKFSedgtqKKMSSLSMELMKLRNKLEAK 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 447 EVEVQLIRESLKVALQ------KHS-EEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDH 519
Cdd:pfam15905 172 MKEVMAKQEGMEGKLQvtqknlEHSkGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEEL 251
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622825706 520 QKQsqqlKDSELKS--TELQEKVTELESLLEETQAICRDRETQLESLRQREAE 570
Cdd:pfam15905 252 LKE----KNDEIESlkQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEE 300
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
305-615 1.18e-08

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: 58.54  E-value: 1.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  305 EQSCELSTCRQQLELIRLQMEQMQLQNGAICHHPAAFAPSLPILEP--AQWISILNSNEHLLKEKELLIDKQRKHISQLE 382
Cdd:TIGR02169  706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQeiENVKSELKELEARIEELEEDLHKLEEALNDLE 785
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  383 QKVRESelqvhsallgrpapfgdvcllRLQELQRENTFLRAQFAQKTEALSrekiDLEKKLSASEVEVQLIRESLKVALQ 462
Cdd:TIGR02169  786 ARLSHS---------------------RIPEIQAELSKLEEEVSRIEARLR----EIEQKLNRLTLEKEYLEKEIQELQE 840
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  463 KHSEevkkQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLptledhqkqSQQLKDSELKSTELQEKVTE 542
Cdd:TIGR02169  841 QRID----LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL---------KKERDELEAQLRELERKIEE 907
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622825706  543 LESLLEETQAICRDRETQLESLRQREAEFSSAghslqdKQSVEETSGEGPEVEmeswqKQYDSLQKVTEDVQA 615
Cdd:TIGR02169  908 LEAQIEKKRKRLSELKAKLEALEEELSEIEDP------KGEDEEIPEEELSLE-----DVQAELQRVEEEIRA 969
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
419-626 4.81e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.60  E-value: 4.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  419 TFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSE---EVKKQEERVKGRDKHINNLKKKCQKESEQ 495
Cdd:TIGR02168  662 TGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEEleeELEQLRKELEELSRQISALRKDLARLEAE 741
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  496 NREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAG 575
Cdd:TIGR02168  742 VEQLEERIAQLSKELTEL--EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622825706  576 HSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKVTEDVQAVTEDCGEAATE 626
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
361-565 9.21e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.46  E-value: 9.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 361 EHLLKEKELLIDKQRKHISQLEQKVRESElqvhsallgrpapfgdvcllRLQELQRENTFLRAQFAQKTEALSRekidLE 440
Cdd:PRK03918  258 EEKIRELEERIEELKKEIEELEEKVKELK--------------------ELKEKAEEYIKLSEFYEEYLDELRE----IE 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 441 KKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRDKHINNLKKKcQKESEQNREKQQRIETLERYLADLPTledhQ 520
Cdd:PRK03918  314 KRLSRLEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLTGLTP----E 387
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1622825706 521 KQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLR 565
Cdd:PRK03918  388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
352-614 1.81e-07

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: 54.26  E-value: 1.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 352 QWISILNSNEHL---LKEKELLIDKQRKHISQLEQKVRE--SELQVhsallgrpapfgdvclLRLQELQRENTFLRAQFA 426
Cdd:TIGR04523 254 QLNQLKDEQNKIkkqLSEKQKELEQNNKKIKELEKQLNQlkSEISD----------------LNNQKEQDWNKELKSELK 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 427 QKTEalsrEKIDLEKKLSASEvevQLIREsLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETL 506
Cdd:TIGR04523 318 NQEK----KLEEIQNQISQNN---KIISQ-LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL 389
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 507 ERYLADLPTLEDHQKQSQQLKDSELKS--TELQEKVTELESLLEETQaicrDRETQLESLRQREAEFSSAGHSLQDKQSV 584
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKlqQEKELLEKEIERLKETII----KNNSEIKDLTNQDSVKELIIKNLDNTRES 465
                         250       260       270
                  ....*....|....*....|....*....|
gi 1622825706 585 EETsgegpevEMESWQKQYDSLQKVTEDVQ 614
Cdd:TIGR04523 466 LET-------QLKVLSRSINKIKQNLEQKQ 488
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
410-607 1.98e-07

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: 54.30  E-value: 1.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  410 RLQELQREntflRAQfAQKTEALSREKIDLEKKLSASEVE--------VQLIRESLKVALQKHSEEVKKQEERVKGRDKH 481
Cdd:TIGR02169  199 QLERLRRE----REK-AERYQALLKEKREYEGYELLKEKEalerqkeaIERQLASLEEELEKLTEEISELEKRLEEIEQL 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  482 INNLKKKCQK--ESEQNREKQQ------RIETLERYLADLPT-LEDHQKQSQQLkDSELKST-----ELQEKVTELESLL 547
Cdd:TIGR02169  274 LEELNKKIKDlgEEEQLRVKEKigeleaEIASLERSIAEKEReLEDAEERLAKL-EAEIDKLlaeieELEREIEEERKRR 352
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  548 EETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQ 607
Cdd:TIGR02169  353 DKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQ 412
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
360-583 5.77e-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: 53.14  E-value: 5.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  360 NEHLLKEKELLIDKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLRLQELQRENTflRAQFAQKTEALSREKIDL 439
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE--VEQLEERIAQLSKELTEL 759
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  440 EKKLSASEVEVQLIRESLKVA---LQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLP-T 515
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAeaeIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATErR 839
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622825706  516 LEDHQKQSQQLKDSELKST----ELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQS 583
Cdd:TIGR02168  840 LEDLEEQIEELSEDIESLAaeieELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
304-571 9.72e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.37  E-value: 9.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  304 REQSCELSTCRQQLELIRLQMEQMQLQNGAICHHPAAFAPSLPILEP--AQWISILNSNEHLLKEKELLIDKQRKHISQL 381
Cdd:TIGR02168  694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAevEQLEERIAQLSKELTELEAEIEELEERLEEA 773
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  382 EQKVRESElqVHSALLGRpapfgdvcllRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIrESLKVAL 461
Cdd:TIGR02168  774 EEELAEAE--AEIEELEA----------QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI-AATERRL 840
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  462 QKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSElkstelqEKVT 541
Cdd:TIGR02168  841 EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL--RSELEELSEELRELE-------SKRS 911
                          250       260       270
                   ....*....|....*....|....*....|
gi 1622825706  542 ELESLLEETQAICRDRETQLESLRQREAEF 571
Cdd:TIGR02168  912 ELRRELEELREKLAQLELRLEGLEVRIDNL 941
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
361-567 1.06e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.22  E-value: 1.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  361 EHLLKEKELLID-----KQRKHISQLEQKVRESELQVHsALLGRPAPFGDV--CLLRLQELQRENTFLRAQFAQKTEALS 433
Cdd:COG4913    215 EYMLEEPDTFEAadalvEHFDDLERAHEALEDAREQIE-LLEPIRELAERYaaARERLAELEYLRAALRLWFAQRRLELL 293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  434 REKID-LEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRDkhINNLKKKCQKESEQNREKQQRIETLERYLAD 512
Cdd:COG4913    294 EAELEeLRAELARLEAELERLEARLD-ALREELDELEAQIRGNGGDR--LEQLEREIERLERELEERERRRARLEALLAA 370
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622825706  513 L--------PTLEDHQKQSQQLKDS-ELKSTELQEKVTELESLLEETQAICRDRETQLESLRQR 567
Cdd:COG4913    371 LglplpasaEEFAALRAEAAALLEAlEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
405-597 1.44e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 1.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  405 DVCLLRLQELQREntflRAQFAQKTEALSREKIDLEKKLSASEVEVQLIR----------ESLKVALQKHSEEVKKQEER 474
Cdd:TIGR02168  228 ALLVLRLEELREE----LEELQEELKEAEEELEELTAELQELEEKLEELRlevseleeeiEELQKELYALANEISRLEQQ 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  475 VKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADL-----PTLEDHQKQSQQLK-------DSELKSTELQEKVTE 542
Cdd:TIGR02168  304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELeekleELKEELESLEAELEeleaeleELESRLEELEEQLET 383
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622825706  543 LES----------LLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEME 597
Cdd:TIGR02168  384 LRSkvaqlelqiaSLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEE 448
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
410-580 1.77e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.53  E-value: 1.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 410 RLQELQRENTFLRAQFAQ---KTEALSREKIDLEKKLSASEVEVQLIRESLKVA---LQKHSEEVKKQEERVKGRDKHIN 483
Cdd:COG4942    28 ELEQLQQEIAELEKELAAlkkEEKALLKQLAALERRIAALARRIRALEQELAALeaeLAELEKEIAELRAELEAQKEELA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 484 NLKKKCQKESEQ-------------------------NREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKstELQE 538
Cdd:COG4942   108 ELLRALYRLGRQpplalllspedfldavrrlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLA--ELEE 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622825706 539 KVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQD 580
Cdd:COG4942   186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
293-602 2.02e-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: 50.98  E-value: 2.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 293 VWQPSPDTWHPREQSCELSTCRQQLEL-IRLQMEQMQLQNGAICHHPAAFAPSLPILEPAQWISILNSNEHLLKEKELL- 370
Cdd:pfam10174  57 VLKEQYRVTQEENQHLQLTIQALQDELrAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLr 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 371 ---------IDKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLR---------------LQELQRENTFLR---- 422
Cdd:pfam10174 137 ktleemelrIETQKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWERTRriaeaemqlghlevlLDQKEKENIHLReelh 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 423 -----AQFAQKTEALSR------EKI-DLEKKLSASEVEVQLIRESLKVALQKHSEEVkKQEERVKGRDKHINN----LK 486
Cdd:pfam10174 217 rrnqlQPDPAKTKALQTviemkdTKIsSLERNIRDLEDEVQMLKTNGLLHTEDREEEI-KQMEVYKSHSKFMKNkidqLK 295
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 487 KKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSqqLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQ 566
Cdd:pfam10174 296 QELSKKESELLALQTKLETLTNQNSDCKQHIEVLKES--LTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTE 373
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1622825706 567 REAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQ 602
Cdd:pfam10174 374 EKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQ 409
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
410-626 2.08e-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: 2.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 410 RLQELQREntflrAQFAQKTEALSREKIDLEKKLSASEVE-VQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKK 488
Cdd:COG1196   201 QLEPLERQ-----AEKAERYRELKEELKELEAELLLLKLReLEAELEELEAELEELEAELEELEAELAELEAELEELRLE 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 489 CQKESEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAicrDRETQLESLRQRE 568
Cdd:COG1196   276 LEELELELEEAQAEEYELLAELARL--EQDIARLEERRRELEERLEELEEELAELEEELEELEE---ELEELEEELEEAE 350
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622825706 569 AEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKVTEDVQAVTEDCGEAATE 626
Cdd:COG1196   351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
408-589 2.17e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.92  E-value: 2.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 408 LLRLQELQRENTFLRAQ---FAQKTEALSR---EKIDLEKKLSASEVEVQLIRESLKV--------ALQKHSEEVKKQEE 473
Cdd:COG4717    70 LKELKELEEELKEAEEKeeeYAELQEELEEleeELEELEAELEELREELEKLEKLLQLlplyqeleALEAELAELPERLE 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 474 RVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLAdlptledhQKQSQQLKDSELKSTELQEKVTELESLLEETQAi 553
Cdd:COG4717   150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLS--------LATEEELQDLAEELEELQQRLAELEEELEEAQE- 220
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622825706 554 crdretQLESLRQREAEFSSAGHSLQDKQSVEETSG 589
Cdd:COG4717   221 ------ELEELEEELEQLENELEAAALEERLKEARL 250
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
361-582 3.34e-06

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: 50.45  E-value: 3.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  361 EHLLKEKELLIDKQRK---HISQLEQKVRESELQVHSALLgrpapfgdvcllRLQELQRENTFLRAQFA----------Q 427
Cdd:TIGR02169  684 EGLKRELSSLQSELRRienRLDELSQELSDASRKIGEIEK------------EIEQLEQEEEKLKERLEeleedlssleQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  428 KTEALSREKIDLEKKLSASE---VEVQLIRESLKVAL--------QKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQN 496
Cdd:TIGR02169  752 EIENVKSELKELEARIEELEedlHKLEEALNDLEARLshsripeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  497 REKqqrIETLERYLADLptledhqkqSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGH 576
Cdd:TIGR02169  832 EKE---IQELQEQRIDL---------KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899

                   ....*.
gi 1622825706  577 SLQDKQ 582
Cdd:TIGR02169  900 ELERKI 905
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
498-626 3.39e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 50.42  E-value: 3.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 498 EKQQRIETLERYLADLPT----LEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSS 573
Cdd:PRK02224  472 EDRERVEELEAELEDLEEeveeVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEA 551
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 574 AGHSLQDK-QSVEETSGEGPEVEMESWQKQ------YDSLQKVtEDVQAVTEDCGEAATE 626
Cdd:PRK02224  552 EAEEKREAaAEAEEEAEEAREEVAELNSKLaelkerIESLERI-RTLLAAIADAEDEIER 610
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
373-623 3.39e-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: 50.56  E-value: 3.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  373 KQRKHISQLeQKVRESELQVHSAllgrpapfgdvcllRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQL 452
Cdd:pfam01576  324 KREQEVTEL-KKALEEETRSHEA--------------QLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAE 388
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  453 IRESLKVALQKHSEevkkQEERVKGRDKHINNLKKKCqkeSEQNREKQQRIETLERYLADLPTLedhqkqSQQLKDSELK 532
Cdd:pfam01576  389 LQAELRTLQQAKQD----SEHKRKKLEGQLQELQARL---SESERQRAELAEKLSKLQSELESV------SSLLNEAEGK 455
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  533 STELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKVTED 612
Cdd:pfam01576  456 NIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEE 535
                          250
                   ....*....|.
gi 1622825706  613 VQAVTEDCGEA 623
Cdd:pfam01576  536 DAGTLEALEEG 546
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
361-572 6.12e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.68  E-value: 6.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 361 EHLLKEKELLIDKQRKHISQLEQKVRESELQVhSALLGRpapfgdvcLLRLQELqrentflraqfAQKTEALSREKIDLE 440
Cdd:PRK03918  192 EELIKEKEKELEEVLREINEISSELPELREEL-EKLEKE--------VKELEEL-----------KEEIEELEKELESLE 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 441 KKLSASEVEVQLIRESLKvALQKHSEEVKKQEERV---KGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADL-PTL 516
Cdd:PRK03918  252 GSKRKLEEKIRELEERIE-ELKKEIEELEEKVKELkelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIeERI 330
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622825706 517 EDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAIcRDRETQLESLRQREAEFS 572
Cdd:PRK03918  331 KELEEKEERLEELKKKLKELEKRLEELEERHELYEEA-KAKKEELERLKKRLTGLT 385
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
317-591 6.32e-06

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: 49.73  E-value: 6.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  317 LELIRLQMEQMQLQNGAicHHPAAFAPslpILEPAQWISILNSNEHLLKEKELLIDKQRKHISQLEQKVRESELQ----- 391
Cdd:pfam15921  564 IEILRQQIENMTQLVGQ--HGRTAGAM---QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEkvklv 638
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  392 ---------VHSALLGRPAPFGDV--CLLRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVA 460
Cdd:pfam15921  639 nagserlraVKDIKQERDQLLNEVktSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSM 718
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  461 LQKHSEEVK---KQEERVKGRDKHINNLKKKCQKESE----QNREKQQRIETLERYLADLPTL-EDHQKQSQQLKDSELK 532
Cdd:pfam15921  719 EGSDGHAMKvamGMQKQITAKRGQIDALQSKIQFLEEamtnANKEKHFLKEEKNKLSQELSTVaTEKNKMAGELEVLRSQ 798
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622825706  533 STELQEKVTELESLLEETQ---AICRD---RETQlESLRQReaefssaghsLQDKQSVEETSGEG 591
Cdd:pfam15921  799 ERRLKEKVANMEVALDKASlqfAECQDiiqRQEQ-ESVRLK----------LQHTLDVKELQGPG 852
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
427-614 6.78e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 6.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 427 QKTEALSREKIDLEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETL 506
Cdd:PRK03918  200 KELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL 278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 507 ERYLADLPTLEDHQKQSQQLKdsELKStELQEKVTELESLLEetqaicrDRETQLESLRQREAEFSSaghslqDKQSVEE 586
Cdd:PRK03918  279 EEKVKELKELKEKAEEYIKLS--EFYE-EYLDELREIEKRLS-------RLEEEINGIEERIKELEE------KEERLEE 342
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622825706 587 TSGEGPEV-----EMESWQKQYDSLQKVTEDVQ 614
Cdd:PRK03918  343 LKKKLKELekrleELEERHELYEEAKAKKEELE 375
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
411-583 8.96e-06

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: 48.86  E-value: 8.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 411 LQELQRENTFLRAQFAQKTEALS--REKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKK 488
Cdd:TIGR04523 182 KLNIQKNIDKIKNKLLKLELLLSnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 489 CQKESEQNREKQQRIET-------LERYLADLPT-LEDHQKQSQQLKDSELKS--TELQEKVTELESLLEETQAICRDRE 558
Cdd:TIGR04523 262 QNKIKKQLSEKQKELEQnnkkikeLEKQLNQLKSeISDLNNQKEQDWNKELKSelKNQEKKLEEIQNQISQNNKIISQLN 341
                         170       180
                  ....*....|....*....|....*....
gi 1622825706 559 TQLESLRQ----REAEFSSAGHSLQDKQS 583
Cdd:TIGR04523 342 EQISQLKKeltnSESENSEKQRELEEKQN 370
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
427-586 9.46e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.88  E-value: 9.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 427 QKTEALSREKIDLEKKLSASEVEvqliRESLKvalqkhsEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETL 506
Cdd:PRK02224  251 EELETLEAEIEDLRETIAETERE----REELA-------EEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREEL 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 507 ERYLADL-PTLEDHQKQSQQL-----------KDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQR----EAE 570
Cdd:PRK02224  320 EDRDEELrDRLEECRVAAQAHneeaeslredaDDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEieelRER 399
                         170
                  ....*....|....*.
gi 1622825706 571 FSSAGHSLQDKQSVEE 586
Cdd:PRK02224  400 FGDAPVDLGNAEDFLE 415
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
410-622 1.80e-05

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: 47.58  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 410 RLQELQRE-NTFLRAQFAQKT-------------EALSREKIDLEKKlsaseveVQLIRESLKVALQKHSEEVKKQEERV 475
Cdd:pfam07888  35 RLEECLQErAELLQAQEAANRqrekekerykrdrEQWERQRRELESR-------VAELKEELRQSREKHEELEEKYKELS 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 476 KGRDKhinnLKKKCQKESEQNREKQQRIETLERYL-----------ADLPTLEDHQKQS-QQLKDSELKSTELQEKvtel 543
Cdd:pfam07888 108 ASSEE----LSEEKDALLAQRAAHEARIRELEEDIktltqrvlereTELERMKERAKKAgAQRKEEEAERKQLQAK---- 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 544 eslLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEE---TSGEGPEVEMESWQKQYDSLQKVTEDVQAVTEDC 620
Cdd:pfam07888 180 ---LQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTqklTTAHRKEAENEALLEELRSLQERLNASERKVEGL 256

                  ..
gi 1622825706 621 GE 622
Cdd:pfam07888 257 GE 258
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
426-616 1.93e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.45  E-value: 1.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 426 AQKTEALSREKIDLEKKLSASEVEVQLI---RESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQR 502
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALkkeEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 503 IETLERYLADLptLEDHQKQSQQLKDSELKStelQEKVTELESLLEETQAICRDRETQLESLRQREAEfssaghsLQDKQ 582
Cdd:COG4942    99 LEAQKEELAEL--LRALYRLGRQPPLALLLS---PEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-------LAALR 166
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622825706 583 SVEETSGEGPEVEMESWQKQYDSLQKVTEDVQAV 616
Cdd:COG4942   167 AELEAERAELEALLAELEEERAALEALKAERQKL 200
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
410-564 2.52e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 46.07  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 410 RLQELQRENTFLRAQFAQKTEALSrekiDLEKKLSASEVEVQLIRESLKVaLQKHSEEVKKQEErVKGRDKHINNLKKKC 489
Cdd:COG1579    32 ELAELEDELAALEARLEAAKTELE----DLEKEIKRLELEIEEVEARIKK-YEEQLGNVRNNKE-YEALQKEIESLKRRI 105
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622825706 490 QKESEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDselKSTELQEKVTELESLLEETQAicrDRETQLESL 564
Cdd:COG1579   106 SDLEDEILELMERIEELEEELAEL--EAELAELEAELEE---KKAELDEELAELEAELEELEA---EREELAAKI 172
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
408-626 3.26e-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: 3.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  408 LLRLQELQRENTFLR-AQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGR-------- 478
Cdd:COG3096    428 LCGLPDLTPENAEDYlAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYE-LVCKIAGEVERSQAWQTARellrryrs 506
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  479 DKHI----NNLKKKcQKESEQNREKQQRIETLeryLADLptledHQKQSQQLKDSELKSTELQEKVTELESLLEEtQAIC 554
Cdd:COG3096    507 QQALaqrlQQLRAQ-LAELEQRLRQQQNAERL---LEEF-----CQRIGQQLDAAEELEELLAELEAQLEELEEQ-AAEA 576
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  555 RDR----ETQLESLRQREAEFSS---AGHSLQDK-QSVEETSGEgpevemeswqkQYDSLQKVTEDVQAVTEDCGEAATE 626
Cdd:COG3096    577 VEQrselRQQLEQLRARIKELAArapAWLAAQDAlERLREQSGE-----------ALADSQEVTAAMQQLLEREREATVE 645
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
408-570 3.38e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 45.69  E-value: 3.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 408 LLRLQELQREntflRAQFAQKTEALSREKIDLEKKLSASEVEVqlirESLKVALQKHSEEVKKQEERVKGRDKHINNLKK 487
Cdd:COG1579     9 LLDLQELDSE----LDRLEHRLKELPAELAELEDELAALEARL----EAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 488 KcQKESEQNRE---KQQRIETLERYLADLptlEDHQKQSQQLKDselkstELQEKVTELESLLEETQA----ICRDRETQ 560
Cdd:COG1579    81 Q-LGNVRNNKEyeaLQKEIESLKRRISDL---EDEILELMERIE------ELEEELAELEAELAELEAeleeKKAELDEE 150
                         170
                  ....*....|
gi 1622825706 561 LESLRQREAE 570
Cdd:COG1579   151 LAELEAELEE 160
PTZ00121 PTZ00121
MAEBL; Provisional
410-618 4.24e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 4.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  410 RLQELQRENTFLRAQFAQKTEAlsREKIDLEKKLSasevEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINN--LKK 487
Cdd:PTZ00121  1183 KAEEVRKAEELRKAEDARKAEA--ARKAEEERKAE----EARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNeeIRK 1256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  488 KCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSE--------LKSTELQEKVTELESLLEETQAICRDRET 559
Cdd:PTZ00121  1257 FEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEekkkadeaKKKAEEAKKADEAKKKAEEAKKKADAAKK 1336
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622825706  560 QLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKVTEDVQAVTE 618
Cdd:PTZ00121  1337 KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE 1395
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
365-563 6.69e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.53  E-value: 6.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 365 KEKELL--IDKQRKHISQLEQKVRESELQVhsALLGRpapfgdvcllRLQELQRENTFLRAQFAQKTEALSREKIDLEKK 442
Cdd:COG4942    49 EEKALLkqLAALERRIAALARRIRALEQEL--AALEA----------ELAELEKEIAELRAELEAQKEELAELLRALYRL 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 443 LSASEVEVQLIRESLKVA------LQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLptL 516
Cdd:COG4942   117 GRQPPLALLLSPEDFLDAvrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL--K 194
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622825706 517 EDHQKQSQQLKDSELKS----TELQEKVTELESLLEETQAICRDRETQLES 563
Cdd:COG4942   195 AERQKLLARLEKELAELaaelAELQQEAEELEALIARLEAEAAAAAERTPA 245
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
408-612 8.16e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 8.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 408 LLRLQELQRENTFLRAQFAQKTEalsrEKIDLEKKLSASEVEVQLIRESLKVA---LQKHSEEVKKQEERVKGRDKHINN 484
Cdd:COG4372    37 LFELDKLQEELEQLREELEQARE----ELEQLEEELEQARSELEQLEEELEELneqLQAAQAELAQAQEELESLQEEAEE 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 485 LKKKCQKESEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAicRDRETQLESL 564
Cdd:COG4372   113 LQEELEELQKERQDLEQQRKQLEAQIAEL--QSEIAEREEELKELEEQLESLQEELAALEQELQALSE--AEAEQALDEL 188
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1622825706 565 RqREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKVTED 612
Cdd:COG4372   189 L-KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL 235
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
361-598 9.42e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.50  E-value: 9.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 361 EHLLKEKE-LLIDKQRKHISQLEQKVRESELQVHSALLgrpAPFGDVCLLRLQELQRentflraqfaQKTEALSREKIDL 439
Cdd:pfam17380 299 ERLRQEKEeKAREVERRRKLEEAEKARQAEMDRQAAIY---AEQERMAMERERELER----------IRQEERKRELERI 365
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 440 EKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKgrdkhinnlKKKCQKESEQNREKQQRIEtleryladlptLEDH 519
Cdd:pfam17380 366 RQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR---------KVKILEEERQRKIQQQKVE-----------MEQI 425
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 520 QKQSQQLKDSELKSTElQEKVTELESLLEETQaicrDRETQLESLRQREAEFSSAGHSL----QDKQSVEETSGEGPEVE 595
Cdd:pfam17380 426 RAEQEEARQREVRRLE-EERAREMERVRLEEQ----ERQQQVERLRQQEEERKRKKLELekekRDRKRAEEQRRKILEKE 500

                  ...
gi 1622825706 596 MES 598
Cdd:pfam17380 501 LEE 503
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
420-615 1.11e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 420 FLRAQFAqktEALSREKIDLEK----KLSASEVEVQLIRESLKVALQKHsEEVKKQEERVKGRDKHINNLKKkcqkeseQ 495
Cdd:COG4717    42 FIRAMLL---ERLEKEADELFKpqgrKPELNLKELKELEEELKEAEEKE-EEYAELQEELEELEEELEELEA-------E 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 496 NREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEEtqaiCRDRETQLESLRQREAEfSSAG 575
Cdd:COG4717   111 LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE----LEELEAELAELQEELEE-LLEQ 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1622825706 576 HSLQDKQSVEETSGegpevEMESWQKQYDSLQKVTEDVQA 615
Cdd:COG4717   186 LSLATEEELQDLAE-----ELEELQQRLAELEEELEEAQE 220
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
430-566 1.18e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 45.23  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 430 EALSREKidlEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKkkcqkesEQNREKQQRIETLERY 509
Cdd:COG2433   380 EALEELI---EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE-------AELEEKDERIERLERE 449
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622825706 510 LADLptleDHQKQSQQLKDSELKSteLQEKVTELESLLEETQAICRDRETQLESLRQ 566
Cdd:COG2433   450 LSEA----RSEERREIRKDREISR--LDREIERLERELEEERERIEELKRKLERLKE 500
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
411-546 1.36e-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: 44.24  E-value: 1.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  411 LQELQRENTFLRAQFAQkteaLSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQ 490
Cdd:smart00787 153 LEGLKEDYKLLMKELEL----LNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLE 228
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  491 KESEQNREKQQRIETL----ERYLADLPTLEDHQKQSQQLKDSELKstELQEKVTELESL 546
Cdd:smart00787 229 ELEEELQELESKIEDLtnkkSELNTEIAEAEKKLEQCRGFTFKEIE--KLKEQLKLLQSL 286
Yuri_gagarin pfam15934
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
465-590 2.00e-04

Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.


Pssm-ID: 318204 [Multi-domain]  Cd Length: 234  Bit Score: 43.41  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 465 SEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDhqkQSQQLKDSELKSTELQEKVTELE 544
Cdd:pfam15934  92 SENNRLKEEIHDLKQKNCVQARVVRKMGLELKGQEEQRVELCDKYESLLGSFEE---QCQELKRANRRVQSLQTRLSQVE 168
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1622825706 545 SLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGE 590
Cdd:pfam15934 169 KLQEELRTERKILREEVIALKEKDAKSNGRERALQDQLKCCQTEIE 214
PRK12704 PRK12704
phosphodiesterase; Provisional
434-564 2.23e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.38  E-value: 2.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 434 REKIDLEKKLSASEVEVQLIRESLKVAlqkhseEVKKQEERVKGRDKhINNLKKKCQKESEQNREK--------QQRIET 505
Cdd:PRK12704   25 RKKIAEAKIKEAEEEAKRILEEAKKEA------EAIKKEALLEAKEE-IHKLRNEFEKELRERRNElqklekrlLQKEEN 97
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622825706 506 LERYLADLptledhQKQSQQLKDSELKSTELQEKVTELESLLEETQAicrDRETQLESL 564
Cdd:PRK12704   98 LDRKLELL------EKREEELEKKEKELEQKQQELEKKEEELEELIE---EQLQELERI 147
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
406-596 3.59e-04

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: 43.94  E-value: 3.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 406 VCLLRLQELQREN-----TFLRAQFAQKTEALsREKIDLE----KKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVK 476
Cdd:pfam05483 242 VSLLLIQITEKENkmkdlTFLLEESRDKANQL-EEKTKLQdenlKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQ 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 477 GRDKHINNL--KKKCQKEsEQNREKQQRIETLERYLADLPTLEDHQKQSQQ-LKDSE----LKSTELQEKVTELESLLEE 549
Cdd:pfam05483 321 IATKTICQLteEKEAQME-ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQrLEKNEdqlkIITMELQKKSSELEEMTKF 399
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1622825706 550 TQaicrDRETQLESLRQREAEFSSAghsLQDKQSVEETSGE--GPEVEM 596
Cdd:pfam05483 400 KN----NKEVELEELKKILAEDEKL---LDEKKQFEKIAEElkGKEQEL 441
PTZ00121 PTZ00121
MAEBL; Provisional
410-618 3.93e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 3.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  410 RLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKhinnlKKKC 489
Cdd:PTZ00121  1243 KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE-----AKKA 1317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  490 QKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAicrdretqlESLRQREA 569
Cdd:PTZ00121  1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA---------DAAKKKAE 1388
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622825706  570 EFSSAGHSlqdKQSVEETSGEGPEV-EMESWQKQYDSLQKVTEDVQAVTE 618
Cdd:PTZ00121  1389 EKKKADEA---KKKAEEDKKKADELkKAAAAKKKADEAKKKAEEKKKADE 1435
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
421-623 4.25e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.49  E-value: 4.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 421 LRAQFAQKTEALSREKI-DLEKKLSASEVEVQLI----------RESLKVALQKHSEevKKQE-ERVKGRDKHINNLKKK 488
Cdd:PRK02224  192 LKAQIEEKEEKDLHERLnGLESELAELDEEIERYeeqreqaretRDEADEVLEEHEE--RREElETLEAEIEDLRETIAE 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 489 CQKE----SEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESL 564
Cdd:PRK02224  270 TEREreelAEEVRDLRERLEELEEERDDL--LAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL 347
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622825706 565 RQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKVTEDVQAVTEDCGEA 623
Cdd:PRK02224  348 REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD 406
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
357-622 5.32e-04

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: 43.17  E-value: 5.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 357 LNSNEHLLKEKELLIDKQRKHISQLE---QKVR---ESELQVHSALLGRPAPFGDVCLLrLQELQRENTFLRAQFAQKTE 430
Cdd:pfam05483 101 LKQKENKLQENRKIIEAQRKAIQELQfenEKVSlklEEEIQENKDLIKENNATRHLCNL-LKETCARSAEKTKKYEYERE 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 431 ALSREKIDL----EKKLSASE---VEVQLIRESLKVALQKHSEEVKKQEERVKgrdKHINNLKKKCQKESEQNREKQQRI 503
Cdd:pfam05483 180 ETRQVYMDLnnniEKMILAFEelrVQAENARLEMHFKLKEDHEKIQHLEEEYK---KEINDKEKQVSLLLIQITEKENKM 256
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 504 ETLERYLADLPTLEDHQKQSQQLKDSELK-STELQEKVT-ELESL-------------LEE-----TQAICR---DRETQ 560
Cdd:pfam05483 257 KDLTFLLEESRDKANQLEEKTKLQDENLKeLIEKKDHLTkELEDIkmslqrsmstqkaLEEdlqiaTKTICQlteEKEAQ 336
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622825706 561 LESLRQreaefSSAGHSL--QDKQSVEETSGEGPEVEMESWQKQYDSLQKVTEDVQAVTEDCGE 622
Cdd:pfam05483 337 MEELNK-----AKAAHSFvvTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEE 395
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
438-614 6.35e-04

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: 41.66  E-value: 6.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 438 DLEKKLSASEVEVQLirESLKVALQKH---SEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADL- 513
Cdd:cd00176    18 EKEELLSSTDYGDDL--ESVEALLKKHealEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELa 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 514 ----PTLEDHQKQSQQL------------KDSELKSTELQEKVTELESLLEETQAICRD---RETQLESLRQREAEFSSA 574
Cdd:cd00176    96 eerrQRLEEALDLQQFFrdaddleqwleeKEAALASEDLGKDLESVEELLKKHKELEEEleaHEPRLKSLNELAEELLEE 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1622825706 575 GHSLQDKQSveetsgegpEVEMESWQKQYDSLQKVTEDVQ 614
Cdd:cd00176   176 GHPDADEEI---------EEKLEELNERWEELLELAEERQ 206
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
357-549 7.72e-04

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: 42.70  E-value: 7.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 357 LNSNEHLLKEKEL--LIDKQRKHISQLEQ-----KVRESELQvhsallgrpapfgdvclLRLQELQRENTFLRAQFAQKT 429
Cdd:TIGR04523 547 LNKDDFELKKENLekEIDEKNKEIEELKQtqkslKKKQEEKQ-----------------ELIDQKEKEKKDLIKEIEEKE 609
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 430 -----------------EALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKhINNLKKKCQKE 492
Cdd:TIGR04523 610 kkisslekelekakkenEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD-IIELMKDWLKE 688
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622825706 493 SEQNREKqqRIETLERYlADLPTLEDHQKQSQQlkdsELKstELQEKVTELESLLEE 549
Cdd:TIGR04523 689 LSLHYKK--YITRMIRI-KDLPKLEEKYKEIEK----ELK--KLDEFSKELENIIKN 736
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
365-626 8.49e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 8.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 365 KEKELLIDKQRKHISQLEQKVRESELQVHSALLGRPAPfgDVCLLRLQELQRENTFLRAQFAQKTEALSREKIDLE---K 441
Cdd:PRK02224  272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADA--EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAEslrE 349
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 442 KLSASEVEVQLIRE---SLKVALQKHSEEVKKQEERVKGRDKHINNLKK----------KCQKESEQNREK----QQRIE 504
Cdd:PRK02224  350 DADDLEERAEELREeaaELESELEEAREAVEDRREEIEELEEEIEELRErfgdapvdlgNAEDFLEELREErdelREREA 429
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 505 TLErylADLPTLEDHQKQSQQL-------------KDSELKST--ELQEKVTELESLL---EETQAICRDRETQLESLRQ 566
Cdd:PRK02224  430 ELE---ATLRTARERVEEAEALleagkcpecgqpvEGSPHVETieEDRERVEELEAELedlEEEVEEVEERLERAEDLVE 506
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 567 REAEFSsaghSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKVTEDVQAVTEDCGEAATE 626
Cdd:PRK02224  507 AEDRIE----RLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAE 562
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
412-567 9.40e-04

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: 41.05  E-value: 9.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 412 QELQRENTFLRAQFAQKT---EALSREKIDLEKKLSASEVEVQLIRESLKVAlQKHSEEVKKQEERVKGRDKHINNLKKk 488
Cdd:pfam13851  29 KSLKEEIAELKKKEERNEklmSEIQQENKRLTEPLQKAQEEVEELRKQLENY-EKDKQSLKNLKARLKVLEKELKDLKW- 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 489 cqkeseQNREKQQRIETLERylaDLPTLEDHQKQSQQ--LKDSELKSTELQEKVTELESLLEEtqaicrdRETQLESLRQ 566
Cdd:pfam13851 107 ------EHEVLEQRFEKVER---ERDELYDKFEAAIQdvQQKTGLKNLLLEKKLQALGETLEK-------KEAQLNEVLA 170

                  .
gi 1622825706 567 R 567
Cdd:pfam13851 171 A 171
PTZ00121 PTZ00121
MAEBL; Provisional
413-632 1.01e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  413 ELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIREslKVALQKHSEEVKKQEERVKGRDKhinnLKKKCQK- 491
Cdd:PTZ00121  1370 EKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK--AAAAKKKADEAKKKAEEKKKADE----AKKKAEEa 1443
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  492 ----ESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKdselKSTELQEKVTELESLLEETQAICRDRETQLESLRQR 567
Cdd:PTZ00121  1444 kkadEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK----KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE 1519
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622825706  568 EAEFSSAGHSLQDKQSVEETSgEGPEVEMESWQKQYDSLQKvTEDVQAVTEdcGEAATEDGSVAL 632
Cdd:PTZ00121  1520 EAKKADEAKKAEEAKKADEAK-KAEEKKKADELKKAEELKK-AEEKKKAEE--AKKAEEDKNMAL 1580
PRK12704 PRK12704
phosphodiesterase; Provisional
428-567 1.02e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 428 KTEALSREKidlEKKLSASEvEVQLIRESLKVALQKHSEEVKKQEERVKgrdKHINNLKKKcqkeSEQNREKQQRIETLE 507
Cdd:PRK12704   48 KKEAEAIKK---EALLEAKE-EIHKLRNEFEKELRERRNELQKLEKRLL---QKEENLDRK----LELLEKREEELEKKE 116
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622825706 508 RYLadlptledhqkqSQQLKDSELKSTELQEKVTELESLLEETQAICRD--RETQLESLRQR 567
Cdd:PRK12704  117 KEL------------EQKQQELEKKEEELEELIEEQLQELERISGLTAEeaKEILLEKVEEE 166
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
355-570 1.24e-03

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: 41.87  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 355 SILNSNEHLLKEKELLIDKQRKHISQLEQKVRESE--------LQVHSALLGRPAPFGDVC---------LLRLQE--LQ 415
Cdd:COG5185   268 EKLGENAESSKRLNENANNLIKQFENTKEKIAEYTksidikkaTESLEEQLAAAEAEQELEeskretetgIQNLTAeiEQ 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 416 RENTFLRAQFAQKTEALS----REKIDLEKKLSASEVEVQLIRESL---KVALQKHSEEVKKQEERVKGR-DKHINNLKK 487
Cdd:COG5185   348 GQESLTENLEAIKEEIENivgeVELSKSSEELDSFKDTIESTKESLdeiPQNQRGYAQEILATLEDTLKAaDRQIEELQR 427
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 488 KCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQ-QLKDSELKST------ELQEKVTELES----LLEETQAICRD 556
Cdd:COG5185   428 QIEQATSSNEEVSKLLNELISELNKVMREADEESQSRlEEAYDEINRSvrskkeDLNEELTQIESrvstLKATLEKLRAK 507
                         250
                  ....*....|....
gi 1622825706 557 RETQLESLRQREAE 570
Cdd:COG5185   508 LERQLEGVRSKLDQ 521
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
354-549 1.53e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 354 ISILNSNehlLKEKELLIDKQRKhisqLEQKVRESELQVhSALLGRPAPFGDVCL----LRLQELQR-ENTFLRAQFAQK 428
Cdd:PRK03918  541 IKSLKKE---LEKLEELKKKLAE----LEKKLDELEEEL-AELLKELEELGFESVeeleERLKELEPfYNEYLELKDAEK 612
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 429 -----TEALSREKIDLEK---KLSASEVEVQLIRESLKVALQKHSEE---------------VKKQEERVKGRDKHINNL 485
Cdd:PRK03918  613 elereEKELKKLEEELDKafeELAETEKRLEELRKELEELEKKYSEEeyeelreeylelsreLAGLRAELEELEKRREEI 692
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622825706 486 KK---KCQKESEQNREKQQRIETLERYLADLptledhqkqsqqlkdselksTELQEKVTELESLLEE 549
Cdd:PRK03918  693 KKtleKLKEELEEREKAKKELEKLEKALERV--------------------EELREKVKKYKALLKE 739
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
375-609 1.70e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 375 RKHISQLEQKVRESElqvhsallgrpapfgdvclLRLQELQRENTFL-----RAQFAQKTEALSREKIDLEKKLSASEVE 449
Cdd:COG3206   181 EEQLPELRKELEEAE-------------------AALEEFRQKNGLVdlseeAKLLLQQLSELESQLAEARAELAEAEAR 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 450 VQLIRESLKVALQKHSEEVkkqeervkgRDKHINNLKkkcqkeSEQNREKQQRIETLERYLADLPTLedhqkqsqqlkds 529
Cdd:COG3206   242 LAALRAQLGSGPDALPELL---------QSPVIQQLR------AQLAELEAELAELSARYTPNHPDV------------- 293
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 530 elksTELQEKVTELESLL-EETQAICRDRETQLESLRQREAEFSSaghSLQD-KQSVEETSGEgpEVEMESWQKQYDSLQ 607
Cdd:COG3206   294 ----IALRAQIAALRAQLqQEAQRILASLEAELEALQAREASLQA---QLAQlEARLAELPEL--EAELRRLEREVEVAR 364

                  ..
gi 1622825706 608 KV 609
Cdd:COG3206   365 EL 366
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
375-586 1.99e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 375 RKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLR--LQELQRENTFLRAQFAqkTEALSREKIDLEKK-LSASEVEVQ 451
Cdd:PRK02224  250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRerLEELEEERDDLLAEAG--LDDADAEAVEARREeLEDRDEELR 327
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 452 LIRESLKVALQKHSEEVKKQEERVKGRDkhinnlkkkcqkesEQNREKQQRIETLERYLADlpTLEDHQKQSQQLKDSEL 531
Cdd:PRK02224  328 DRLEECRVAAQAHNEEAESLREDADDLE--------------ERAEELREEAAELESELEE--AREAVEDRREEIEELEE 391
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622825706 532 KSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDkqSVEE 586
Cdd:PRK02224  392 EIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARE--RVEE 444
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
410-593 2.69e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 410 RLQELQRENTFLRAQFA---QKTEALSREKIDLEKKLSASEVEVQLIRESLKVAlqkhSEEVKKQEERVKGRdkhINNLK 486
Cdd:COG3883    24 ELSELQAELEAAQAELDalqAELEELNEEYNELQAELEALQAEIDKLQAEIAEA----EAEIEERREELGER---ARALY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 487 KKCQKESE--------------QNREKQQRI-----ETLERYLADLPTLEDHQKQ-SQQLKDSELKSTELQEKVTELESL 546
Cdd:COG3883    97 RSGGSVSYldvllgsesfsdflDRLSALSKIadadaDLLEELKADKAELEAKKAElEAKLAELEALKAELEAAKAELEAQ 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1622825706 547 LEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPE 593
Cdd:COG3883   177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
408-569 2.77e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 408 LLRLQELQRENTFLRAQFAQKTEALSREKID-----LEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEE-RVKGRDKH 481
Cdd:COG4717   292 LLAREKASLGKEAEELQALPALEELEEEELEellaaLGLPPDLSPEELLELLDRIEELQELLREAEELEEElQLEELEQE 371
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 482 INNLKKKCQKESE-----------QNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEET 550
Cdd:COG4717   372 IAALLAEAGVEDEeelraaleqaeEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEEL 451
                         170
                  ....*....|....*....
gi 1622825706 551 QAICRDRETQLESLRQREA 569
Cdd:COG4717   452 REELAELEAELEQLEEDGE 470
PTZ00121 PTZ00121
MAEBL; Provisional
408-627 3.07e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 3.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  408 LLRLQELQRENTFLRAQFAQKTEALSREkidlEKKLSASEV----EVQLIRESLKVALQKHSEE-----VKKQEERVKGR 478
Cdd:PTZ00121  1515 AKKAEEAKKADEAKKAEEAKKADEAKKA----EEKKKADELkkaeELKKAEEKKKAEEAKKAEEdknmaLRKAEEAKKAE 1590
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  479 DKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSEL----KSTELQEKVTELESLLEETQAIC 554
Cdd:PTZ00121  1591 EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAeekkKAEELKKAEEENKIKAAEEAKKA 1670
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622825706  555 RDRETQLESLRQREAEFSSAGHSLQdKQSVEETSGEGPEVEMESWQKQYDSLQKVTEDVQAVTEDCGEAATED 627
Cdd:PTZ00121  1671 EEDKKKAEEAKKAEEDEKKAAEALK-KEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED 1742
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
446-627 3.11e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 446 SEVEVQLirESLK----VALQ----KHSEEVKKQEERVKgrdkHINNLKKKCQKESEQNREKQQRIETLErylADLPTLE 517
Cdd:COG1196   196 GELERQL--EPLErqaeKAERyrelKEELKELEAELLLL----KLRELEAELEELEAELEELEAELEELE---AELAELE 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 518 -DHQKQSQQLKDSELKSTELQEKVTELESLLEETqaicrdrETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEM 596
Cdd:COG1196   267 aELEELRLELEELELELEEAQAEEYELLAELARL-------EQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622825706 597 ESWQKQYDSLQKVTEDVQAVTEDCGEAATED 627
Cdd:COG1196   340 EELEEELEEAEEELEEAEAELAEAEEALLEA 370
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
410-567 3.21e-03

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 40.01  E-value: 3.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 410 RLQELQRENTFLRAQFAQkteaLSREKIDLEKKlsasevEVQLIR---ESLKVA----------LQKHSEEVKKQEERVK 476
Cdd:pfam04849 172 KLRGLEEENLKLRSEASH----LKTETDTYEEK------EQQLMSdcvEQLSEAnqqmaelseeLARKMEENLRQQEEIT 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 477 GRDKHINNLKKKCQKESEQNREKQQRIETleryladlptledhQKQSQQLKDSELKstELQEKVTELESLLEETQaicrd 556
Cdd:pfam04849 242 SLLAQIVDLQHKCKELGIENEELQQHLQA--------------SKEAQRQLTSELQ--ELQDRYAECLGMLHEAQ----- 300
                         170
                  ....*....|.
gi 1622825706 557 reTQLESLRQR 567
Cdd:pfam04849 301 --EELKELRKK 309
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
408-586 4.61e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 4.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 408 LLRLQELQREntflRAQFAQKTEALSREKIDLEKKLS----ASEVEVQLIRESLKVALQKHSEeVKKQEERVKGRDKHIN 483
Cdd:PRK03918  548 LEKLEELKKK----LAELEKKLDELEEELAELLKELEelgfESVEELEERLKELEPFYNEYLE-LKDAEKELEREEKELK 622
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 484 NLKKKCQKESEQNREKQQRIETLERYLADLPTL---EDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQ 560
Cdd:PRK03918  623 KLEEELDKAFEELAETEKRLEELRKELEELEKKyseEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
                         170       180
                  ....*....|....*....|....*.
gi 1622825706 561 LESLRQREAEFSSAGHSLQDKQSVEE 586
Cdd:PRK03918  703 LEEREKAKKELEKLEKALERVEELRE 728
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
355-567 4.74e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 4.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 355 SILNSNEHLLKEKELL---IDKQRKHISQLEQKVRESELQvhsallgrpapfgdvcllrLQELQRENTFLRAQFAQKTEA 431
Cdd:TIGR04523 381 SYKQEIKNLESQINDLeskIQNQEKLNQQKDEQIKKLQQE-------------------KELLEKEIERLKETIIKNNSE 441
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 432 LSrekiDLEKKLSAsevevqliresLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLA 511
Cdd:TIGR04523 442 IK----DLTNQDSV-----------KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622825706 512 DLptledhqkqSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQR 567
Cdd:TIGR04523 507 EL---------EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFE 553
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
410-570 6.29e-03

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 38.35  E-value: 6.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 410 RLQELQRENTFLRAQFAQKTEALsrekidleKKLSASEVEVQLIreslkvaLQKHSEEV--------------KKQEERV 475
Cdd:pfam15619  26 KLEELRKENRLLKRLQKRQEKAL--------GKYEGTESELPQL-------IARHNEEVrvlrerlrrlqekeRDLERKL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 476 KGRDKHINNLKKKCQKESEQNREKQ-QRIETLERYLADLPT-LEDHQKQSQQL-KDSELKSTELQEKVTELESLLEETQA 552
Cdd:pfam15619  91 KEKEAELLRLRDQLKRLEKLSEDKNlAEREELQKKLEQLEAkLEDKDEKIQDLeRKLELENKSFRRQLAAEKKKHKEAQE 170
                         170
                  ....*....|....*...
gi 1622825706 553 ICRDRETQLESLRQREAE 570
Cdd:pfam15619 171 EVKILQEEIERLQQKLKE 188
Rabaptin pfam03528
Rabaptin;
422-626 6.93e-03

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 39.32  E-value: 6.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 422 RAQFAQKTEALSREKIDLEKKLSASEVEvqlirESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQ------KESEQ 495
Cdd:pfam03528 132 RAQWNQYRESAEREIADLRRRLSEGQEE-----ENLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTeaedkiKELEA 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 496 NR----------EKQQRIEtLERYLADLPTledhQKQSQQlKDSELKSTELQEKVTELE------SLLEETQAICRDRET 559
Cdd:pfam03528 207 SKmkelnhyleaEKSCRTD-LEMYVAVLNT----QKSVLQ-EDAEKLRKELHEVCHLLEqerqqhNQLKHTWQKANDQFL 280
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622825706 560 QLESLRQREAE-FSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKVTEDVQAVTEDCGEAATE 626
Cdd:pfam03528 281 ESQRLLMRDMQrMESVLTSEQLRQVEEIKKKDQEEHKRARTHKEKETLKSDREHTVSIHAVFSPAGVE 348
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
365-567 8.76e-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: 39.26  E-value: 8.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  365 KEKELLIDKQRKHISQLEQKVreSELQVHSALLGrpapfgdvcllrlqelqrENTFLRAQFAQKTEALSREKIDLEKKLS 444
Cdd:TIGR00606  846 ELNRKLIQDQQEQIQHLKSKT--NELKSEKLQIG------------------TNLQRRQQFEEQLVELSTEVQSLIREIK 905
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706  445 ASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKC-----------------------QKESEQNR---- 497
Cdd:TIGR00606  906 DAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVknihgymkdienkiqdgkddylkQKETELNTvnaq 985
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622825706  498 --EKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEE-TQAICRDRETQLESLRQR 567
Cdd:TIGR00606  986 leECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQhLKEMGQMQVLQMKQEHQK 1058
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
361-572 9.08e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.23  E-value: 9.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 361 EHLLKEKEL-----LIDKQRKHISQLEQKVRESELQVhsallgrpapfgdvcllrlQELQRentfLRAQFAQKTEALSRE 435
Cdd:TIGR04523 420 EKELLEKEIerlkeTIIKNNSEIKDLTNQDSVKELII-------------------KNLDN----TRESLETQLKVLSRS 476
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825706 436 KIDLEKKLSASEVEVqlirESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLadlpt 515
Cdd:TIGR04523 477 INKIKQNLEQKQKEL----KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL----- 547
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622825706 516 ledhQKQSQQLKDSELKsTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFS 572
Cdd:TIGR04523 548 ----NKDDFELKKENLE-KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKK 599
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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