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Conserved domains on  [gi|578817221|ref|XP_006717082|]
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FK506-binding protein 15 isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
125-218 1.10e-29

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 113.45  E-value: 1.10e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   125 AVEVGDSLEVAYTGWLFQnhvlGQVFDSTANKDKLLRLKLGSGKVIKGWEDGMLGMKKGGKRLLIVPPACAVGSEGVIGW 204
Cdd:pfam00254    4 KAKKGDRVTVHYTGTLED----GTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGP 79
                           90
                   ....*....|....
gi 578817221   205 TQATDSILVFEVEV 218
Cdd:pfam00254   80 VIPPNATLVFEVEL 93
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
552-814 1.80e-19

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 94.62  E-value: 1.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  552 LQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQE 631
Cdd:COG1196   237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  632 TSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLL 711
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  712 KKtrvstdQAAAEQLSLVQAELQTQWEAkcehlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQN 791
Cdd:COG1196   397 EL------AAQLEELEEAEEALLERLER-----LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
                         250       260
                  ....*....|....*....|...
gi 578817221  792 EQHIKELEKNKSQMSGVEAAASD 814
Cdd:COG1196   466 AELLEEAALLEAALAELLEELAE 488
PHA03247 super family cl33720
large tegument protein UL36; Provisional
883-1096 6.64e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 6.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  883 RPRRPSQEQsasassgQPQAPLNRERPESPMVPSEQVVEEAVPLPPQALTTSQDGhrRKGDSEAEALSEIKDGSLPPELS 962
Cdd:PHA03247 2907 RPPQPQAPP-------PPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGE--PSGAVPQPWLGALVPGRVAVPRF 2977
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  963 CIPSHRvlgPPTSIPPEPLGPVSMDSECEESLAASPMAAKPDNPSGKVCVRE-VAPDGPLQESSTRLSLTSDPEEGDPLA 1041
Cdd:PHA03247 2978 RVPQPA---PSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQtLWPPDDTEDSDADSLFDSDSERSDLEA 3054
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578817221 1042 LGPEsPGEPQPPQLKKDDVTSSTGPHKELSSTEAG--STVAGAAL--RPSHHSQRSSLS 1096
Cdd:PHA03247 3055 LDPL-PPEPHDPFAHEPDPATPEAGARESPSSQFGppPLSANAALsrRYVRSTGRSALA 3112
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
239-427 3.41e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 44.76  E-value: 3.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   239 SAAPSPIPGADNLSADPVVSPPTSIPFKSGEPALRTKSnslseqlAINTSPDAVKAKLISRMAKMgQPMLPILPPQldsn 318
Cdd:pfam03154  192 TQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHT-------LIQQTPTLHPQRLPSPHPPL-QPMTQPPPPS---- 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   319 dseiedvntlqgggQPVVTPSVQPSLHPAHPALPQMTSQAPqpsvTGLQAPSAAL-MQVSSLDSHSAVSGNAQSFQPYAG 397
Cdd:pfam03154  260 --------------QVSPQPLPQPSLHGQMPPMPHSLQTGP----SHMQHPVPPQpFPLTPQSSQSQVPPGPSPAAPGQS 321
                          170       180       190
                   ....*....|....*....|....*....|..
gi 578817221   398 MQAYAYPQASAVTSQLQPVR--PLYPAPLSQP 427
Cdd:pfam03154  322 QQRIHTPPSQSQLQSQQPPReqPLPPAPLSMP 353
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
2-100 1.86e-03

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member smart00461:

Pssm-ID: 473070  Cd Length: 106  Bit Score: 38.88  E-value: 1.86e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221      2 STPTILVATAVHAYRYTNGQYVKQGKFGAAVLG---NHTAREYRILLYISQQQPVTVARIHVNFELMVRPNNYSTFYDDQ 78
Cdd:smart00461    3 SQCIILARAVVQLYDADTKKWVPTGEGGAANLVidkNQRSYFFRIVGIKGQDKVIWNQELYKNFKYNQATPTFHQWADDK 82
                            90       100
                    ....*....|....*....|..
gi 578817221     79 RQnWSIMFESEKAAVEFNKQVC 100
Cdd:smart00461   83 CV-YGLNFASEEEAKKFRKKVL 103
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
125-218 1.10e-29

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 113.45  E-value: 1.10e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   125 AVEVGDSLEVAYTGWLFQnhvlGQVFDSTANKDKLLRLKLGSGKVIKGWEDGMLGMKKGGKRLLIVPPACAVGSEGVIGW 204
Cdd:pfam00254    4 KAKKGDRVTVHYTGTLED----GTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGP 79
                           90
                   ....*....|....
gi 578817221   205 TQATDSILVFEVEV 218
Cdd:pfam00254   80 VIPPNATLVFEVEL 93
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
116-218 1.84e-26

FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 104.49  E-value: 1.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  116 QDLIVADGPAVEVGDSLEVAYTGWLFQnhvlGQVFDSTANKDKLLRLKLGSGKVIKGWEDGMLGMKKGGKRLLIVPPACA 195
Cdd:COG0545     4 KVLKEGTGAKPKAGDTVTVHYTGTLLD----GTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
                          90       100
                  ....*....|....*....|....*.
gi 578817221  196 VGSEG---VIGwtqaTDSILVFEVEV 218
Cdd:COG0545    80 YGERGaggVIP----PNSTLVFEVEL 101
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
552-814 1.80e-19

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 94.62  E-value: 1.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  552 LQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQE 631
Cdd:COG1196   237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  632 TSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLL 711
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  712 KKtrvstdQAAAEQLSLVQAELQTQWEAkcehlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQN 791
Cdd:COG1196   397 EL------AAQLEELEEAEEALLERLER-----LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
                         250       260
                  ....*....|....*....|...
gi 578817221  792 EQHIKELEKNKSQMSGVEAAASD 814
Cdd:COG1196   466 AELLEEAALLEAALAELLEELAE 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
510-826 1.33e-18

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 92.04  E-value: 1.33e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   510 KQEILEKSNRIEEQNDKISEL-IERNQRYVEQSNLMMEKRnnSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQ 588
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELeKALAELRKELEELEEELE--QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   589 LKMTAHQKKETELQMQLTEslketdlLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEK 668
Cdd:TIGR02168  754 KELTELEAEIEELEERLEE-------AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   669 ESLEKNLsERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTrvstdQAAAEQLSLVQAELQTQWEAKCEHL--LA 746
Cdd:TIGR02168  827 ESLERRI-AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-----ESELEALLNERASLEEALALLRSELeeLS 900
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   747 SAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQ-NEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQ 825
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980

                   .
gi 578817221   826 V 826
Cdd:TIGR02168  981 I 981
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
495-834 9.41e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 69.71  E-value: 9.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  495 IMSNIQRI-----IQENERLKQEILEKSNRIEEQNDKISELIERNQRyveqsnlmMEKRNNSLQTATENTQA-------- 561
Cdd:PRK03918  370 KKEELERLkkrltGLTPEKLEKELEELEKAKEEIEEEISKITARIGE--------LKKEIKELKKAIEELKKakgkcpvc 441
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  562 -RVLHAEQEK---AKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTE-----SLKET-DLLRG--------QLTKVQ 623
Cdd:PRK03918  442 gRELTEEHRKellEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeseliKLKELaEQLKEleeklkkyNLEELE 521
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  624 AKLSELQETSEQA------QSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQErsqAEEEIDEIR 697
Cdd:PRK03918  522 KKAEEYEKLKEKLiklkgeIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEE---LEERLKELE 598
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  698 KSYQE---------ELDKLRQLLKKTRVSTDQAAAEqLSLVQAELQtQWEAKCEHLLASAKDEhlqQYQEVcaqrdayQQ 768
Cdd:PRK03918  599 PFYNEylelkdaekELEREEKELKKLEEELDKAFEE-LAETEKRLE-ELRKELEELEKKYSEE---EYEEL-------RE 666
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817221  769 KLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDpSEKVKKIMNQVfQSLRREF 834
Cdd:PRK03918  667 EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE-LEKLEKALERV-EELREKV 730
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
441-839 1.74e-10

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: 65.51  E-value: 1.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   441 MTEARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMLIPSMSVTMET--SMIMSNIQRIIQENERLK---QEILE 515
Cdd:pfam05483  309 MSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSleELLRTEQQRLEKNEDQLKiitMELQK 388
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   516 KSNRIEE----QNDKISELIERNQRYVEQSNLMMEKRNnsLQTATENTQARvlhaEQEkakVTEELAAATAQVSHLQLKM 591
Cdd:pfam05483  389 KSSELEEmtkfKNNKEVELEELKKILAEDEKLLDEKKQ--FEKIAEELKGK----EQE---LIFLLQAREKEIHDLEIQL 459
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   592 TA-------HQKKETELQMQL-TESLKETDLL---------RGQLTKVQAKLS-ELQETSEQAQSKFKSEKQNRKQLElk 653
Cdd:pfam05483  460 TAiktseehYLKEVEDLKTELeKEKLKNIELTahcdkllleNKELTQEASDMTlELKKHQEDIINCKKQEERMLKQIE-- 537
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   654 vtSLEEELTDLRVEKESLEKNLSERK-------KKSAQERSQAEEEI--------------DEIRKSYQEELDKLRQLLK 712
Cdd:pfam05483  538 --NLEEKEMNLRDELESVREEFIQKGdevkcklDKSEENARSIEYEVlkkekqmkilenkcNNLKKQIENKNKNIEELHQ 615
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   713 KTRVSTDQAAAEQLSLVQAELQTQweaKCEHLLASAK---DEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTK 789
Cdd:pfam05483  616 ENKALKKKGSAENKQLNAYEIKVN---KLELELASAKqkfEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQK 692
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 578817221   790 QNE---QH-----IKELEKNKSQMSGVeAAASDPSEKVKKIMNQVFQSLRREFELEES 839
Cdd:pfam05483  693 EIDkrcQHkiaemVALMEKHKHQYDKI-IEERDSELGLYKNKEQEQSSAKAALEIELS 749
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
123-241 1.34e-09

FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 60.55  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  123 GPAVEVGDSLEVAYTGWLfqnhVLGQVFDSTANKDKLLRLKLGSgkVIKGWEDGMLGMKKGGKRLLIVPPACAVGSEGVI 202
Cdd:PRK10902  158 GEAPKDSDTVVVNYKGTL----IDGKEFDNSYTRGEPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVP 231
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 578817221  203 GWtqATDSILVFEVEVRRVKFARDSGSDGHSVSSRDSAA 241
Cdd:PRK10902  232 GI--PANSTLVFDVELLDVKPAPKADAKPEADAKAADSA 268
PHA03247 PHA03247
large tegument protein UL36; Provisional
883-1096 6.64e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 6.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  883 RPRRPSQEQsasassgQPQAPLNRERPESPMVPSEQVVEEAVPLPPQALTTSQDGhrRKGDSEAEALSEIKDGSLPPELS 962
Cdd:PHA03247 2907 RPPQPQAPP-------PPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGE--PSGAVPQPWLGALVPGRVAVPRF 2977
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  963 CIPSHRvlgPPTSIPPEPLGPVSMDSECEESLAASPMAAKPDNPSGKVCVRE-VAPDGPLQESSTRLSLTSDPEEGDPLA 1041
Cdd:PHA03247 2978 RVPQPA---PSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQtLWPPDDTEDSDADSLFDSDSERSDLEA 3054
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578817221 1042 LGPEsPGEPQPPQLKKDDVTSSTGPHKELSSTEAG--STVAGAAL--RPSHHSQRSSLS 1096
Cdd:PHA03247 3055 LDPL-PPEPHDPFAHEPDPATPEAGARESPSSQFGppPLSANAALsrRYVRSTGRSALA 3112
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
239-427 3.41e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 44.76  E-value: 3.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   239 SAAPSPIPGADNLSADPVVSPPTSIPFKSGEPALRTKSnslseqlAINTSPDAVKAKLISRMAKMgQPMLPILPPQldsn 318
Cdd:pfam03154  192 TQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHT-------LIQQTPTLHPQRLPSPHPPL-QPMTQPPPPS---- 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   319 dseiedvntlqgggQPVVTPSVQPSLHPAHPALPQMTSQAPqpsvTGLQAPSAAL-MQVSSLDSHSAVSGNAQSFQPYAG 397
Cdd:pfam03154  260 --------------QVSPQPLPQPSLHGQMPPMPHSLQTGP----SHMQHPVPPQpFPLTPQSSQSQVPPGPSPAAPGQS 321
                          170       180       190
                   ....*....|....*....|....*....|..
gi 578817221   398 MQAYAYPQASAVTSQLQPVR--PLYPAPLSQP 427
Cdd:pfam03154  322 QQRIHTPPSQSQLQSQQPPReqPLPPAPLSMP 353
AmmeMemoSam_B TIGR04336
AmmeMemoRadiSam system protein B; Members of this protein family belong to the same domain ...
946-1004 9.34e-04

AmmeMemoRadiSam system protein B; Members of this protein family belong to the same domain family as the mammalian protein Memo (Mediator of ErbB2-driven cell MOtility). Members of the present family occur as part of a three gene system with an uncharacterized radical SAM enzyme and a homolog of the mammalian protein AMMECR1, a mammalian protein named for AMME - Alport syndrome, Mental Retardation, Midface hypoplasia, and Elliptocytosis. Memo in humans has protein-protein interaction activity with binding of phosphorylated Try, but members of this family may be active as enzymes, as suggested by homology to a class of nonheme iron dioxygenases.


Pssm-ID: 275135 [Multi-domain]  Cd Length: 269  Bit Score: 42.56  E-value: 9.34e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817221   946 AEALSEIKDGslPPELSCI--PSHRVLGPPTSIPPE-----PLGPVSMDSECEESLAASPMAAKPD 1004
Cdd:TIGR04336   55 AHAYAALKKG--RPETVVLlgPNHTGYGSGIALPPEgswetPLGDVPVDEELAEELLEHSPIIELD 118
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
587-739 1.36e-03

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


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 42.36  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  587 LQLKMTAHQKKETELQMQLTESLKE-TDLLRGQLTKVQAKLSELQEtseqAQSKFKSE-KQNRKQLELKVTSLEEELTD- 663
Cdd:cd22656    97 LELIDDLADATDDEELEEAKKTIKAlLDDLLKEAKKYQDKAAKVVD----KLTDFENQtEKDQTALETLEKALKDLLTDe 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  664 -LRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRqllKKTRVSTD-QAAAEQLSLVQA---------- 731
Cdd:cd22656   173 gGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLA---AALRLIADlTAADTDLDNLLAligpaipale 249

                  ....*...
gi 578817221  732 ELQTQWEA 739
Cdd:cd22656   250 KLQGAWQA 257
growth_prot_Scy NF041483
polarized growth protein Scy;
552-835 1.42e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.89  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  552 LQTATENTQARVLHAEQEKAKVTEELAAATAQVShlQLKMTAHQKKeTELQMQLTESLKETDLLRGQLTKVQAK-LSELQ 630
Cdd:NF041483  224 LNAASTQAQEATDHAEQLRSSTAAESDQARRQAA--ELSRAAEQRM-QEAEEALREARAEAEKVVAEAKEAAAKqLASAE 300
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  631 ETSEQAQSKFKSE-----KQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAeeEIDEIRKSYQEELD 705
Cdd:NF041483  301 SANEQRTRTAKEEiarlvGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDTAA--QLAKAARTAEEVLT 378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  706 KLRQLLKktrvSTDQAAAEQLSLVQAELqtqwEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQIT 785
Cdd:NF041483  379 KASEDAK----ATTRAAAEEAERIRREA----EAEADRLRGEAADQAEQLKGAAKDDTKEYRAKTVELQEEARRLRGEAE 450
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578817221  786 AL---------------TKQNEQHIKE--------LEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFE 835
Cdd:NF041483  451 QLraeavaegerirgeaRREAVQQIEEaartaeelLTKAKADADELRSTATAESERVRTEAIERATTLRRQAE 523
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
495-713 1.69e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 42.69  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  495 IMSNIQRIIQEnerlKQEILEKSNRIeeQN-DKISELIERNQRYVEQSNLMMEKRNNSLQTAT-ENTQARVLHAEQEKAK 572
Cdd:NF033838   63 VESHLEKILSE----IQKSLDKRKHT--QNvALNKKLSDIKTEYLYELNVLKEKSEAELTSKTkKELDAAFEQFKKDTLE 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  573 VTEELAAATAQVSHLQLKmtAHQKKETELQMQLTESLKETDLLRGQlTKVQAKLSELQETSEQAQSKFKSEKQnrKQLEL 652
Cdd:NF033838  137 PGKKVAEATKKVEEAEKK--AKDQKEEDRRNYPTNTYKTLELEIAE-SDVEVKKAELELVKEEAKEPRDEEKI--KQAKA 211
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578817221  653 KVTSLEEELTdlrvekeSLEKNLSERKK--KSAQERSQAEEEIDEIRKSYQEELDKLRQLLKK 713
Cdd:NF033838  212 KVESKKAEAT-------RLEKIKTDREKaeEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKR 267
PRK10263 PRK10263
DNA translocase FtsK; Provisional
329-423 1.83e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.76  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  329 QGGGQPVVTPSVQPSLHPAHPALPQMTSQAPQPSVTGLQA------PSAALMQVSSLDSHSAVSGN-AQSFQPYAGMQAY 401
Cdd:PRK10263  738 DGPHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQyqqpqqPVAPQPQYQQPQQPVAPQPQyQQPQQPVAPQPQY 817
                          90       100
                  ....*....|....*....|....
gi 578817221  402 AYPQASAVTSQ--LQPVRPLYPAP 423
Cdd:PRK10263  818 QQPQQPVAPQPqyQQPQQPVAPQP 841
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
2-100 1.86e-03

WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains point mutations in the majority of patients with WAS. Unknown function. Ena-like WH1 domains bind polyproline-containing peptides, and that Homer contains a WH1 domain.


Pssm-ID: 214674  Cd Length: 106  Bit Score: 38.88  E-value: 1.86e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221      2 STPTILVATAVHAYRYTNGQYVKQGKFGAAVLG---NHTAREYRILLYISQQQPVTVARIHVNFELMVRPNNYSTFYDDQ 78
Cdd:smart00461    3 SQCIILARAVVQLYDADTKKWVPTGEGGAANLVidkNQRSYFFRIVGIKGQDKVIWNQELYKNFKYNQATPTFHQWADDK 82
                            90       100
                    ....*....|....*....|..
gi 578817221     79 RQnWSIMFESEKAAVEFNKQVC 100
Cdd:smart00461   83 CV-YGLNFASEEEAKKFRKKVL 103
tig TIGR00115
trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first ...
110-183 2.17e-03

trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first chaperone to interact with nascent polypeptide. Trigger factor can bind at the same time as the signal recognition particle (SRP), but is excluded by the SRP receptor (FtsY). The central domain of trigger factor has peptidyl-prolyl cis/trans isomerase activity. This protein is found in a single copy in virtually every bacterial genome. [Protein fate, Protein folding and stabilization]


Pssm-ID: 272913 [Multi-domain]  Cd Length: 410  Bit Score: 41.77  E-value: 2.17e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817221   110 LDAVLSQ--DLIVADGPAVEVGDSLEVAYTGwlfqnHVLGQVFDSTANKDklLRLKLGSGKVIKGWEDGMLGMKKG 183
Cdd:TIGR00115  131 LERLREQnaTLVPVERGAAEKGDRVTIDFEG-----FIDGEAFEGGKAEN--FSLELGSGQFIPGFEEQLVGMKAG 199
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
125-218 1.10e-29

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 113.45  E-value: 1.10e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   125 AVEVGDSLEVAYTGWLFQnhvlGQVFDSTANKDKLLRLKLGSGKVIKGWEDGMLGMKKGGKRLLIVPPACAVGSEGVIGW 204
Cdd:pfam00254    4 KAKKGDRVTVHYTGTLED----GTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGP 79
                           90
                   ....*....|....
gi 578817221   205 TQATDSILVFEVEV 218
Cdd:pfam00254   80 VIPPNATLVFEVEL 93
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
116-218 1.84e-26

FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 104.49  E-value: 1.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  116 QDLIVADGPAVEVGDSLEVAYTGWLFQnhvlGQVFDSTANKDKLLRLKLGSGKVIKGWEDGMLGMKKGGKRLLIVPPACA 195
Cdd:COG0545     4 KVLKEGTGAKPKAGDTVTVHYTGTLLD----GTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79
                          90       100
                  ....*....|....*....|....*.
gi 578817221  196 VGSEG---VIGwtqaTDSILVFEVEV 218
Cdd:COG0545    80 YGERGaggVIP----PNSTLVFEVEL 101
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
552-814 1.80e-19

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 94.62  E-value: 1.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  552 LQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQE 631
Cdd:COG1196   237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  632 TSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLL 711
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  712 KKtrvstdQAAAEQLSLVQAELQTQWEAkcehlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQN 791
Cdd:COG1196   397 EL------AAQLEELEEAEEALLERLER-----LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
                         250       260
                  ....*....|....*....|...
gi 578817221  792 EQHIKELEKNKSQMSGVEAAASD 814
Cdd:COG1196   466 AELLEEAALLEAALAELLEELAE 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
510-826 1.33e-18

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 92.04  E-value: 1.33e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   510 KQEILEKSNRIEEQNDKISEL-IERNQRYVEQSNLMMEKRnnSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQ 588
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELeKALAELRKELEELEEELE--QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   589 LKMTAHQKKETELQMQLTEslketdlLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEK 668
Cdd:TIGR02168  754 KELTELEAEIEELEERLEE-------AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   669 ESLEKNLsERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTrvstdQAAAEQLSLVQAELQTQWEAKCEHL--LA 746
Cdd:TIGR02168  827 ESLERRI-AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-----ESELEALLNERASLEEALALLRSELeeLS 900
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   747 SAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQ-NEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQ 825
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980

                   .
gi 578817221   826 V 826
Cdd:TIGR02168  981 I 981
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
495-736 3.46e-18

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 90.77  E-value: 3.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  495 IMSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNS------LQTATENTQARVLHAEQ 568
Cdd:COG1196   258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELeerleeLEEELAELEEELEELEE 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  569 EKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRK 648
Cdd:COG1196   338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  649 QLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSyQEELDKLRQLLKKTRVSTDQAAAEQLSL 728
Cdd:COG1196   418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL-LEEAALLEAALAELLEELAEAAARLLLL 496

                  ....*...
gi 578817221  729 VQAELQTQ 736
Cdd:COG1196   497 LEAEADYE 504
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
504-814 9.62e-18

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 89.35  E-value: 9.62e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   504 QEN-ERLkQEILeksNRIEEQNDKISELIERNQRYVEQSNlmmEKRN----------NSLQTATENTQARVLHAEQEKAK 572
Cdd:TIGR02168  185 RENlDRL-EDIL---NELERQLKSLERQAEKAERYKELKA---ELRElelallvlrlEELREELEELQEELKEAEEELEE 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   573 VTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLEL 652
Cdd:TIGR02168  258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   653 KVTSLEEELTDLRVEKESLEKNLSERKKKS-----------------AQERSQAEEEIDEIRKSYQEELDKLRQL---LK 712
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEAELEELEAELeelesrleeleeqletlRSKVAQLELQIASLNNEIERLEARLERLedrRE 417
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   713 KTRVSTDQAAAEQLSLVQAELQTQWEAKCEHL--LASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQ 790
Cdd:TIGR02168  418 RLQQEIEELLKKLEEAELKELQAELEELEEELeeLQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
                          330       340       350
                   ....*....|....*....|....*....|
gi 578817221   791 NEQH------IKELEKNKSQMSGVEAAASD 814
Cdd:TIGR02168  498 QENLegfsegVKALLKNQSGLSGILGVLSE 527
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
492-819 7.73e-17

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: 86.28  E-value: 7.73e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   492 TSMI-MSNIQR--IIQE----------NERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSN-------LMMEKRN-- 549
Cdd:TIGR02169  145 TDFIsMSPVERrkIIDEiagvaefdrkKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREkaeryqaLLKEKREye 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   550 --------NSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETEL----QMQLTESLKEtdlLRG 617
Cdd:TIGR02169  225 gyellkekEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeQLRVKEKIGE---LEA 301
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   618 QLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIR 697
Cdd:TIGR02169  302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFA 381
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   698 ------KSYQEELDKLRQLLK--KTRVSTDQAAAEQLSLVQAELQTQweakcehlLASAKDEHLQQYQEVCAQRD---AY 766
Cdd:TIGR02169  382 etrdelKDYREKLEKLKREINelKRELDRLQEELQRLSEELADLNAA--------IAGIEAKINELEEEKEDKALeikKQ 453
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 578817221   767 QQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKV 819
Cdd:TIGR02169  454 EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
501-790 1.21e-16

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 85.50  E-value: 1.21e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   501 RIIQENERLKQEILEKSNRIEEQNDKISELIERNQryveqsnlMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAA 580
Cdd:TIGR02169  692 SLQSELRRIENRLDELSQELSDASRKIGEIEKEIE--------QLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKEL 763
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   581 TAQVSHLQLKMTAHQKKETELQMQLTESL------------KETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRK 648
Cdd:TIGR02169  764 EARIEELEEDLHKLEEALNDLEARLSHSRipeiqaelskleEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI 843
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   649 QLELKVTSLEEELTDLRVEKESLE----------KNLSERKKKSAQERSQAEEEIDEIRKSYQE---ELDKLRQLLKKTR 715
Cdd:TIGR02169  844 DLKEQIKSIEKEIENLNGKKEELEeeleeleaalRDLESRLGDLKKERDELEAQLRELERKIEEleaQIEKKRKRLSELK 923
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   716 VsTDQAAAEQLS----------------LVQAELQTQWEAKCEHL--LASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKC 777
Cdd:TIGR02169  924 A-KLEALEEELSeiedpkgedeeipeeeLSLEDVQAELQRVEEEIraLEPVNMLAIQEYEEVLKRLDELKEKRAKLEEER 1002
                          330
                   ....*....|...
gi 578817221   778 LALQAQITALTKQ 790
Cdd:TIGR02169 1003 KAILERIEEYEKK 1015
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
498-834 1.23e-16

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: 85.49  E-value: 1.23e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   498 NIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMmEKRNNSLQTATENTQARVLHAEQEKAKVTEEL 577
Cdd:TIGR02168  685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL-RKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   578 AAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSL 657
Cdd:TIGR02168  764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   658 EEELTDLRVEKESLEKNLSE----RKKKSAQ------ERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLS 727
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEIEEleelIEELESEleallnERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   728 LVQAELQ-TQWEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMS 806
Cdd:TIGR02168  924 LAQLELRlEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYD 1003
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 578817221   807 GVEAAASDPSEKVKKIM--------------NQVFQSLRREF 834
Cdd:TIGR02168 1004 FLTAQKEDLTEAKETLEeaieeidrearerfKDTFDQVNENF 1045
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
499-759 6.39e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 83.06  E-value: 6.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  499 IQRIIQENERLKQEILEKSNRIEEQNDKISEL---IERNQRYVEQSNLMMEKRNNSLQTAT----------ENTQARVLH 565
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELeaeLEELRLELEELELELEEAQAEEYELLaelarleqdiARLEERRRE 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  566 AEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQ 645
Cdd:COG1196   314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  646 NRKQLELKVTSLEEELTDLRVEKESLEKNLSERK---KKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAA 722
Cdd:COG1196   394 AAAELAAQLEELEEAEEALLERLERLEEELEELEealAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578817221  723 AEQLSLVQAELQTQWEAKCEHLLASAKDEHLQQYQEV 759
Cdd:COG1196   474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
555-838 8.94e-15

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 79.72  E-value: 8.94e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   555 ATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSE 634
Cdd:TIGR02168  664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   635 QAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKN---LSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLL 711
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEieeLEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   712 KKTRVSTDQAAAEQLSLVqaELQTQWEAKCEHLLASAK---------DEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQA 782
Cdd:TIGR02168  824 ERLESLERRIAATERRLE--DLEEQIEELSEDIESLAAeieeleeliEELESELEALLNERASLEEALALLRSELEELSE 901
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 578817221   783 QITALTKQNEQHIKELEKNKSQMSGVEAAAsdpsEKVKKIMNQVFQSLRREFELEE 838
Cdd:TIGR02168  902 ELRELESKRSELRRELEELREKLAQLELRL----EGLEVRIDNLQERLSEEYSLTL 953
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
573-838 1.86e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 78.44  E-value: 1.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  573 VTEELAAataQVSHLQ------LKMTAHQKKETELQMQLTesLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQN 646
Cdd:COG1196   194 ILGELER---QLEPLErqaekaERYRELKEELKELEAELL--LLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  647 RKQLELKVTSLEEELTDLRVEKESLEK---NLSERKKKSAQERSQAEEEIDEIrksyQEELDKLRQllkktRVSTDQAAA 723
Cdd:COG1196   269 LEELRLELEELELELEEAQAEEYELLAelaRLEQDIARLEERRRELEERLEEL----EEELAELEE-----ELEELEEEL 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  724 EQLSLVQAELQTQWEAKCEHL--LASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKN 801
Cdd:COG1196   340 EELEEELEEAEEELEEAEAELaeAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578817221  802 KSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFELEE 838
Cdd:COG1196   420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
499-840 2.93e-13

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: 74.72  E-value: 2.93e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   499 IQRIIQENERLKQEILEKSNRIEEQNDKISELIERnqryVEQSNLMMEKRnnslqtatentqarvlhAEQEKAKVTEELA 578
Cdd:TIGR02169  239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQL----LEELNKKIKDL-----------------GEEEQLRVKEKIG 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   579 AATAQVSHLQlkmtaHQKKETELQMQLTEslketdllrGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLE 658
Cdd:TIGR02169  298 ELEAEIASLE-----RSIAEKERELEDAE---------ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   659 EELTDLRVEKESLEKNLSERKKKSAQER---SQAEEEIDEIRKSYQEELDKLRQLlkKTRVSTDQAAAEQLSLVQAELQT 735
Cdd:TIGR02169  364 EELEDLRAELEEVDKEFAETRDELKDYReklEKLKREINELKRELDRLQEELQRL--SEELADLNAAIAGIEAKINELEE 441
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   736 QWEAKCEHLlasAKDEhlQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALtkqnEQHIKELEKNKSQMSGVEAAASDP 815
Cdd:TIGR02169  442 EKEDKALEI---KKQE--WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL----QRELAEAEAQARASEERVRGGRAV 512
                          330       340
                   ....*....|....*....|....*
gi 578817221   816 SEKVKKIMNQVFQSLRREFELEESY 840
Cdd:TIGR02169  513 EEVLKASIQGVHGTVAQLGSVGERY 537
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
558-798 5.11e-13

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 73.80  E-value: 5.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  558 NTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQM--QLTESLKETDLLRGQLTKVQAKLSELqetsEQ 635
Cdd:COG4913   607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERL----DA 682
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  636 AQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTR 715
Cdd:COG4913   683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  716 VStdQAAAEQLSLVQAELQTQwEAKCEHLLASAKDEHLQQYQEVCAQRDA-------YQQKLVQLQEKCL-ALQAQI-TA 786
Cdd:COG4913   763 VE--RELRENLEERIDALRAR-LNRAEEELERAMRAFNREWPAETADLDAdleslpeYLALLDRLEEDGLpEYEERFkEL 839
                         250
                  ....*....|..
gi 578817221  787 LTKQNEQHIKEL 798
Cdd:COG4913   840 LNENSIEFVADL 851
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
495-837 1.70e-12

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: 71.98  E-value: 1.70e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   495 IMSNIQRIIQENERLKQEILEksnrIEEQNDKISELIERNQryveqsnlmmeKRNNSLQTATENTQARVLHAEQEKAKVT 574
Cdd:TIGR04523  202 LLSNLKKKIQKNKSLESQISE----LKKQNNQLKDNIEKKQ-----------QEINEKTTEISNTQTQLNQLKDEQNKIK 266
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   575 EELAAATAQVSHLQLKMTAHQKKETELQMQLTE--SLKETDL---LRGQLTKVQAKLSELqetseqaQSKFKSEKQNRKQ 649
Cdd:TIGR04523  267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDlnNQKEQDWnkeLKSELKNQEKKLEEI-------QNQISQNNKIISQ 339
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   650 LELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIrKSYQEELDKLRQLLKKtrvstdqaaAEQLSlv 729
Cdd:TIGR04523  340 LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI-KNLESQINDLESKIQN---------QEKLN-- 407
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   730 qAELQTQWEAkcehlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITAL--------------------TK 789
Cdd:TIGR04523  408 -QQKDEQIKK-----LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLdntresletqlkvlsrsinkIK 481
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 578817221   790 QN-EQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFELE 837
Cdd:TIGR04523  482 QNlEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
500-834 3.20e-12

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 70.95  E-value: 3.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  500 QRIIQENERLK------QEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKV 573
Cdd:COG4717   139 AELAELPERLEeleerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  574 TEELAAATAQVSHLQLKMTAHQKKETELQMQ--------------LTESLKETDLLRGQLTKVQAKL-----SELQETSE 634
Cdd:COG4717   219 QEELEELEEELEQLENELEAAALEERLKEARlllliaaallallgLGGSLLSLILTIAGVLFLVLGLlallfLLLAREKA 298
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  635 QAQSKFKSEKQNRKQLELKVTSLEEELTDLRVeKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEE--LDKLRQLLK 712
Cdd:COG4717   299 SLGKEAEELQALPALEELEEEELEELLAALGL-PPDLSPEELLELLDRIEELQELLREAEELEEELQLEelEQEIAALLA 377
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  713 KTRVSTD-------------QAAAEQLSLVQAELQTQWEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLA 779
Cdd:COG4717   378 EAGVEDEeelraaleqaeeyQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAE 457
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  780 LQAQITALTKQNE-----QHIKELEKNKSQMsgVEAAASDpsEKVKKIMNQVFQSLRREF 834
Cdd:COG4717   458 LEAELEQLEEDGElaellQELEELKAELREL--AEEWAAL--KLALELLEEAREEYREER 513
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
495-834 9.41e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 69.71  E-value: 9.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  495 IMSNIQRI-----IQENERLKQEILEKSNRIEEQNDKISELIERNQRyveqsnlmMEKRNNSLQTATENTQA-------- 561
Cdd:PRK03918  370 KKEELERLkkrltGLTPEKLEKELEELEKAKEEIEEEISKITARIGE--------LKKEIKELKKAIEELKKakgkcpvc 441
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  562 -RVLHAEQEK---AKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTE-----SLKET-DLLRG--------QLTKVQ 623
Cdd:PRK03918  442 gRELTEEHRKellEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeseliKLKELaEQLKEleeklkkyNLEELE 521
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  624 AKLSELQETSEQA------QSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQErsqAEEEIDEIR 697
Cdd:PRK03918  522 KKAEEYEKLKEKLiklkgeIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEE---LEERLKELE 598
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  698 KSYQE---------ELDKLRQLLKKTRVSTDQAAAEqLSLVQAELQtQWEAKCEHLLASAKDEhlqQYQEVcaqrdayQQ 768
Cdd:PRK03918  599 PFYNEylelkdaekELEREEKELKKLEEELDKAFEE-LAETEKRLE-ELRKELEELEKKYSEE---EYEEL-------RE 666
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817221  769 KLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDpSEKVKKIMNQVfQSLRREF 834
Cdd:PRK03918  667 EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE-LEKLEKALERV-EELREKV 730
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
503-825 1.72e-11

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: 68.45  E-value: 1.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  503 IQENERLKQEILEKSNRIEEQNDKISELIERNQRYVE----QSNLMMEKRN---NSLQTATENTQARVLHAEQE--KAKV 573
Cdd:COG5185   231 IEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLeklgENAESSKRLNenaNNLIKQFENTKEKIAEYTKSidIKKA 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  574 TEE----LAAATAQVSHLQLKMtahqKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNrKQ 649
Cdd:COG5185   311 TESleeqLAAAEAEQELEESKR----ETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFK-DT 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  650 LELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLK-KTRVSTDQAAAEQLSL 728
Cdd:COG5185   386 IESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISeLNKVMREADEESQSRL 465
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  729 VQA------ELQTQWEAKCEHL------LASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKC-LALQAQITALTKQNEQHI 795
Cdd:COG5185   466 EEAydeinrSVRSKKEDLNEELtqiesrVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLkDFMRARGYAHILALENLI 545
                         330       340       350
                  ....*....|....*....|....*....|
gi 578817221  796 KELEKNKSQMSGVEAAASDPSEKVKKIMNQ 825
Cdd:COG5185   546 PASELIQASNAKTDGQAANLRTAVIDELTQ 575
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
582-841 1.48e-10

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: 65.86  E-value: 1.48e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   582 AQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEEL 661
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   662 TDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEqlslVQAELQtqwEAKC 741
Cdd:TIGR02169  754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE----IEQKLN---RLTL 826
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   742 EHLLASAKDEHLQQYQEVC-AQRDAYQQKLVQLQEKCLALQAQItaltKQNEQHIKELEKNKSqmsgveaaasDPSEKVK 820
Cdd:TIGR02169  827 EKEYLEKEIQELQEQRIDLkEQIKSIEKEIENLNGKKEELEEEL----EELEAALRDLESRLG----------DLKKERD 892
                          250       260
                   ....*....|....*....|.
gi 578817221   821 KIMNQVFQSLRREFELEESYN 841
Cdd:TIGR02169  893 ELEAQLRELERKIEELEAQIE 913
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
441-839 1.74e-10

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: 65.51  E-value: 1.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   441 MTEARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMLIPSMSVTMET--SMIMSNIQRIIQENERLK---QEILE 515
Cdd:pfam05483  309 MSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSleELLRTEQQRLEKNEDQLKiitMELQK 388
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   516 KSNRIEE----QNDKISELIERNQRYVEQSNLMMEKRNnsLQTATENTQARvlhaEQEkakVTEELAAATAQVSHLQLKM 591
Cdd:pfam05483  389 KSSELEEmtkfKNNKEVELEELKKILAEDEKLLDEKKQ--FEKIAEELKGK----EQE---LIFLLQAREKEIHDLEIQL 459
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   592 TA-------HQKKETELQMQL-TESLKETDLL---------RGQLTKVQAKLS-ELQETSEQAQSKFKSEKQNRKQLElk 653
Cdd:pfam05483  460 TAiktseehYLKEVEDLKTELeKEKLKNIELTahcdkllleNKELTQEASDMTlELKKHQEDIINCKKQEERMLKQIE-- 537
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   654 vtSLEEELTDLRVEKESLEKNLSERK-------KKSAQERSQAEEEI--------------DEIRKSYQEELDKLRQLLK 712
Cdd:pfam05483  538 --NLEEKEMNLRDELESVREEFIQKGdevkcklDKSEENARSIEYEVlkkekqmkilenkcNNLKKQIENKNKNIEELHQ 615
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   713 KTRVSTDQAAAEQLSLVQAELQTQweaKCEHLLASAK---DEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTK 789
Cdd:pfam05483  616 ENKALKKKGSAENKQLNAYEIKVN---KLELELASAKqkfEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQK 692
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 578817221   790 QNE---QH-----IKELEKNKSQMSGVeAAASDPSEKVKKIMNQVFQSLRREFELEES 839
Cdd:pfam05483  693 EIDkrcQHkiaemVALMEKHKHQYDKI-IEERDSELGLYKNKEQEQSSAKAALEIELS 749
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
615-820 3.40e-10

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: 63.24  E-value: 3.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  615 LRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLserkKKSAQERSQAEEEID 694
Cdd:COG4942    25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL----AELEKEIAELRAELE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  695 EIRKSYQEELDKL-----------------------RQLLKKTRVSTDQAAAEQLSLVQAELQTQweakcEHLLASAKDE 751
Cdd:COG4942   101 AQKEELAELLRALyrlgrqpplalllspedfldavrRLQYLKYLAPARREQAEELRADLAELAAL-----RAELEAERAE 175
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578817221  752 HLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVK 820
Cdd:COG4942   176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
593-793 4.02e-10

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: 63.24  E-value: 4.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  593 AHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLE 672
Cdd:COG4942    17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  673 KNLSERKKKSAQ---------------------------ERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTdQAAAEQ 725
Cdd:COG4942    97 AELEAQKEELAEllralyrlgrqpplalllspedfldavRRLQYLKYLAPARREQAEELRADLAELAALRAEL-EAERAE 175
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578817221  726 LSLVQAELQTQWEAkcehlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQ 793
Cdd:COG4942   176 LEALLAELEEERAA-----LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
493-826 5.36e-10

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 63.89  E-value: 5.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   493 SMIMSNIQRIIQENER---LKQEI-------LEKSNRIEEQNDKISELIERNQRYVEQ--------SNL-----MMEKRN 549
Cdd:TIGR04523  328 NQISQNNKIISQLNEQisqLKKELtnsesenSEKQRELEEKQNEIEKLKKENQSYKQEiknlesqiNDLeskiqNQEKLN 407
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   550 NSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQmQLTESLKE-TDLLRGQLTKVQAKLSE 628
Cdd:TIGR04523  408 QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD-NTRESLETqLKVLSRSINKIKQNLEQ 486
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   629 LQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEkeslEKNLSERKKKSAQERSQAEEEIDEIrksyqeELDKLR 708
Cdd:TIGR04523  487 KQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK----IEKLESEKKEKESKISDLEDELNKD------DFELKK 556
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   709 QLLKKTRVSTDQaAAEQLSLVQAEL---QTQweakcehllasaKDEHLQQyqevcaqrdaYQQKLVQLQEKCLALQAQIT 785
Cdd:TIGR04523  557 ENLEKEIDEKNK-EIEELKQTQKSLkkkQEE------------KQELIDQ----------KEKEKKDLIKEIEEKEKKIS 613
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 578817221   786 ALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQV 826
Cdd:TIGR04523  614 SLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
500-822 7.69e-10

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: 63.22  E-value: 7.69e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   500 QRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEkRNNSLQTATENTQARvlhaEQEKAKvTEELAA 579
Cdd:pfam17380  299 ERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME-RERELERIRQEERKR----ELERIR-QEEIAM 372
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   580 ATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQetseqaqsKFKSEKQNRKQLELKVTSLEE 659
Cdd:pfam17380  373 EISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEME--------QIRAEQEEARQREVRRLEEER 444
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   660 ELTDLRVEKESLEKNLS-ERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQ---LSLVQAELQT 735
Cdd:pfam17380  445 AREMERVRLEEQERQQQvERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEerkRKLLEKEMEE 524
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   736 QWEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKclalqAQITALTKQNE--QHIKELEKNKSqmsgvEAAAS 813
Cdd:pfam17380  525 RQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEER-----SRLEAMEREREmmRQIVESEKARA-----EYEAT 594

                   ....*....
gi 578817221   814 DPSEKVKKI 822
Cdd:pfam17380  595 TPITTIKPI 603
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
497-713 1.30e-09

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: 62.35  E-value: 1.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   497 SNIQRIIQENERLKQEILEKSNRIEEQNDKISELIER------------NQRYVEQSNL-MMEKRNNSLQTATENTQARV 563
Cdd:TIGR04523  412 EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkeliiknldNTRESLETQLkVLSRSINKIKQNLEQKQKEL 491
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   564 LHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTE------SLK------ETDLLRGQLTKV----QAKLS 627
Cdd:TIGR04523  492 KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEkeskisDLEdelnkdDFELKKENLEKEidekNKEIE 571
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   628 ELQET---SEQAQSKFK-------SEKQN-RKQLELK---VTSLEEELTDLRVEKESLE---KNLSERKKKSAQERSQAE 690
Cdd:TIGR04523  572 ELKQTqksLKKKQEEKQelidqkeKEKKDlIKEIEEKekkISSLEKELEKAKKENEKLSsiiKNIKSKKNKLKQEVKQIK 651
                          250       260
                   ....*....|....*....|...
gi 578817221   691 EEIDEIRKSYQEELDKLRQLLKK 713
Cdd:TIGR04523  652 ETIKEIRNKWPEIIKKIKESKTK 674
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
123-241 1.34e-09

FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 60.55  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  123 GPAVEVGDSLEVAYTGWLfqnhVLGQVFDSTANKDKLLRLKLGSgkVIKGWEDGMLGMKKGGKRLLIVPPACAVGSEGVI 202
Cdd:PRK10902  158 GEAPKDSDTVVVNYKGTL----IDGKEFDNSYTRGEPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVP 231
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 578817221  203 GWtqATDSILVFEVEVRRVKFARDSGSDGHSVSSRDSAA 241
Cdd:PRK10902  232 GI--PANSTLVFDVELLDVKPAPKADAKPEADAKAADSA 268
PTZ00121 PTZ00121
MAEBL; Provisional
507-797 1.73e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 62.47  E-value: 1.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  507 ERLKQEILEKSNRIEEQNDKiseliernqRYVEQSNLMMEKRNNSLQTATENTQArvlhaeqEKAKVTEELaaataQVSH 586
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAEEK---------KKAEEAKKAEEDKNMALRKAEEAKKA-------EEARIEEVM-----KLYE 1602
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  587 LQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQ------------AQSKFKSEKQNRKQLELKV 654
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElkkaeeenkikaAEEAKKAEEDKKKAEEAKK 1682
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  655 tslEEEltDLRVEKESLEKNlSERKKKSAQERSQAEEEI---DEIRKSYQEELDKLRQLLKKTRvsTDQAAAEQLSLVQA 731
Cdd:PTZ00121 1683 ---AEE--DEKKAAEALKKE-AEEAKKAEELKKKEAEEKkkaEELKKAEEENKIKAEEAKKEAE--EDKKKAEEAKKDEE 1754
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578817221  732 ElqtqwEAKCEHLlasaKDEHLQQYQEVCAQRDAY-QQKLVQLQEKCLALQAQITALTKQNEQHIKE 797
Cdd:PTZ00121 1755 E-----KKKIAHL----KKEEEKKAEEIRKEKEAViEEELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
505-805 2.71e-09

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 61.20  E-value: 2.71e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   505 ENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLmmekrnnslqtATENTQARVLHAEQEKAKVTEEL-AAATAQ 583
Cdd:pfam05667  223 EEEWNSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAAL-----------AGTEATSGASRSAQDLAELLSSFsGSSTTD 291
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   584 VSHLQLKMTAHQKKET---ELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEE 660
Cdd:pfam05667  292 TGLTKGSRFTHTEKLQftnEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEE 371
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   661 LTDLRVEKESLEKNLsERKKKSAQERSQAEEEIdeirksyqeelDKLRQLLkktrvstdQAAAEQLslvqAELQTQWEAK 740
Cdd:pfam05667  372 LEELKEQNEELEKQY-KVKKKTLDLLPDAEENI-----------AKLQALV--------DASAQRL----VELAGQWEKH 427
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578817221   741 CEHLLasakdEHLQQYQEVCA-QRDAYQQKLVQLQ---EKCLalqaQITALTKQNEQHIKELEKNKSQM 805
Cdd:pfam05667  428 RVPLI-----EEYRALKEAKSnKEDESQRKLEEIKelrEKIK----EVAEEAKQKEELYKQLVAEYERL 487
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
450-840 3.83e-09

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: 60.89  E-value: 3.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   450 EIRMAVSKVADKMDHLMTKVEELQKHsAGNSMLipSMSVTMETSMimSNIQRIIQE-----NERLKQ------EILEKSN 518
Cdd:pfam05483  180 ETRQVYMDLNNNIEKMILAFEELRVQ-AENARL--EMHFKLKEDH--EKIQHLEEEykkeiNDKEKQvsllliQITEKEN 254
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   519 R-------IEEQNDKISELIERNQRYVEQSNLMMEKRNNsLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLqlkm 591
Cdd:pfam05483  255 KmkdltflLEESRDKANQLEEKTKLQDENLKELIEKKDH-LTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQL---- 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   592 tahqKKETELQMQLTESLKETDLLrgQLTKVQAKLSELQETSEQAQSKFKSEKQNRK--QLELKVTSLE-EELTDLR--- 665
Cdd:pfam05483  330 ----TEEKEAQMEELNKAKAAHSF--VVTEFEATTCSLEELLRTEQQRLEKNEDQLKiiTMELQKKSSElEEMTKFKnnk 403
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   666 -VEKESLEKNLSERKK---------KSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVStDQAAAEQLSLVQAELQ- 734
Cdd:pfam05483  404 eVELEELKKILAEDEKlldekkqfeKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTS-EEHYLKEVEDLKTELEk 482
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   735 -----TQWEAKCEHLLASAKD---------EHLQQYQEVCAQRDAYQQKLVQ----LQEKCLALQAQITALTKQNEQHIK 796
Cdd:pfam05483  483 eklknIELTAHCDKLLLENKEltqeasdmtLELKKHQEDIINCKKQEERMLKqienLEEKEMNLRDELESVREEFIQKGD 562
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*...
gi 578817221   797 E----LEKNKSQMSGVEAAASdPSEKVKKIMNQVFQSLRREFELEESY 840
Cdd:pfam05483  563 EvkckLDKSEENARSIEYEVL-KKEKQMKILENKCNNLKKQIENKNKN 609
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
449-673 4.48e-09

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: 60.84  E-value: 4.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   449 TEIRMAVSKVADKMDHLMTKVEELQKhsagnsmlipsmsvtmETSMIMSNIQRIIQENERLKQEILEKSNRIEEQNDKIS 528
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQKELYALAN----------------EISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   529 ELIERNQRYVEQSNL--------------------MMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQ 588
Cdd:TIGR02168  334 ELAEELAELEEKLEElkeelesleaeleeleaeleELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   589 lkmtAHQKKETELQMQLTESLKETDL--LRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRV 666
Cdd:TIGR02168  414 ----DRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489

                   ....*..
gi 578817221   667 EKESLEK 673
Cdd:TIGR02168  490 RLDSLER 496
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
499-841 4.52e-09

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: 60.80  E-value: 4.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   499 IQRIIQENER---LKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNsLQTATENTQARVLHAEQEKAKVTE 575
Cdd:TIGR04523   67 EEKINNSNNKikiLEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNK-LEVELNKLEKQKKENKKNIDKFLT 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   576 ELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELqetsEQAQSKFKSEKQNRKQLELKVT 655
Cdd:TIGR04523  146 EIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKL----ELLLSNLKKKIQKNKSLESQIS 221
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   656 SLEEELTDLRVEKESLEKNLSERK---KKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDqaaaeQLSLVQAE 732
Cdd:TIGR04523  222 ELKKQNNQLKDNIEKKQQEINEKTteiSNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK-----QLNQLKSE 296
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   733 LQTQWEAKCEHLLASAKDEHLQ---QYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVE 809
Cdd:TIGR04523  297 ISDLNNQKEQDWNKELKSELKNqekKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLK 376
                          330       340       350
                   ....*....|....*....|....*....|..
gi 578817221   810 AAASDPSEKVKKIMNQVfQSLRREFELEESYN 841
Cdd:TIGR04523  377 KENQSYKQEIKNLESQI-NDLESKIQNQEKLN 407
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
596-813 4.61e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 60.55  E-value: 4.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  596 KKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQaqskfksekqnRKQLELKVTSLEEELTDLRVEKESLEKnl 675
Cdd:COG4717    64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE-----------LEELEAELEELREELEKLEKLLQLLPL-- 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  676 serkkksAQERSQAEEEIDEirksYQEELDKLRQllKKTRVSTDQAAAEQLSLVQAELQTQWEAKCEHLLASAKDE---H 752
Cdd:COG4717   131 -------YQELEALEAELAE----LPERLEELEE--RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdL 197
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817221  753 LQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALtkQNEQHIKELEKNKSQMSGVEAAAS 813
Cdd:COG4717   198 AEELEELQQRLAELEEELEEAQEELEELEEELEQL--ENELEAAALEERLKEARLLLLIAA 256
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
495-733 1.07e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 59.54  E-value: 1.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  495 IMSNIQRIIQENERLK--QEILEKsnrIEEQNDKISELIERNQRYVEQSNLMMEKRnnslqtaTENTQARVLHAEQEKAK 572
Cdd:COG4913   223 TFEAADALVEHFDDLEraHEALED---AREQIELLEPIRELAERYAAARERLAELE-------YLRAALRLWFAQRRLEL 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  573 VTEELAAATAQVSHLQLKMTAHQKKETELQMQLTEslketdlLRGQLTKVQ-AKLSELQETSEQAQSKFKSEKQNRKQLE 651
Cdd:COG4913   293 LEAELEELRAELARLEAELERLEARLDALREELDE-------LEAQIRGNGgDRLEQLEREIERLERELEERERRRARLE 365
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  652 LKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQL------LKKTRVSTDQ----- 720
Cdd:COG4913   366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELeaeiasLERRKSNIPArllal 445
                         250
                  ....*....|....*
gi 578817221  721 --AAAEQLSLVQAEL 733
Cdd:COG4913   446 rdALAEALGLDEAEL 460
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
507-734 1.22e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 58.38  E-value: 1.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  507 ERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTAT---ENTQARVLHAEQEKAKVTEELAAATAQ 583
Cdd:COG4372     2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLReelEQAREELEQLEEELEQARSELEQLEEE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  584 VSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTD 663
Cdd:COG4372    82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817221  664 LRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQ 734
Cdd:COG4372   162 LQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
505-834 1.47e-08

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 59.21  E-value: 1.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   505 ENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTatENTQARVLHAEQEKAKVTEELAAataQV 584
Cdd:TIGR00618  436 QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQE--TRKKAVVLARLLELQEEPCPLCG---SC 510
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   585 SHLQLKMTAHQKKETeLQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDL 664
Cdd:TIGR00618  511 IHPNPARQDIDNPGP-LTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL 589
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   665 RVEKESLEKnlsERKKKSAQERSQAEEEIDEIRKSyQEELDKLRQLLKKTRVSTDQAAAEqLSLVQAELQTQWEAKCEHL 744
Cdd:TIGR00618  590 QNITVRLQD---LTEKLSEAEDMLACEQHALLRKL-QPEQDLQDVRLHLQQCSQELALKL-TALHALQLTLTQERVREHA 664
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   745 LASAKDEhLQQYQEVCAQRDAYQQKLVQLQEKCLALqAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMN 824
Cdd:TIGR00618  665 LSIRVLP-KELLASRQLALQKMQSEKEQLTYWKEML-AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALN 742
                          330
                   ....*....|
gi 578817221   825 QVFQSLRREF 834
Cdd:TIGR00618  743 QSLKELMHQA 752
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
495-737 1.49e-08

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: 58.24  E-value: 1.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  495 IMSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLmMEKRNNSLQTATENTQARVlhaEQEKAKVT 574
Cdd:COG4942    32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-LEAELAELEKEIAELRAEL---EAQKEELA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  575 EELAAA--TAQVSHLQLKMTAHQKKETELQMQLTESLKETDllRGQLTKVQAKLSELQetseqaqskfksekQNRKQLEL 652
Cdd:COG4942   108 ELLRALyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPAR--REQAEELRADLAELA--------------ALRAELEA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  653 KVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEElDKLRQLLKKTRVSTDQAAAEQLSLVQAE 732
Cdd:COG4942   172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA-EELEALIARLEAEAAAAAERTPAAGFAA 250

                  ....*
gi 578817221  733 LQTQW 737
Cdd:COG4942   251 LKGKL 255
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
497-846 1.50e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.92  E-value: 1.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  497 SNIQRIIQENErlkQEILEKSNRIEEQNDKISELIERnQRYVEQSNLMMEKRNNSLqtatENTQARVLHAEQEKAKVTEE 576
Cdd:PRK03918  189 ENIEELIKEKE---KELEEVLREINEISSELPELREE-LEKLEKEVKELEELKEEI----EELEKELESLEGSKRKLEEK 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  577 LAAATAQVSHLQLKMTAHQKKETELQmQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLElkvtS 656
Cdd:PRK03918  261 IRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE----E 335
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  657 LEEELTDLRVEKESLEKNLSE---------------------RKKKSAQERSQAEEEIDEIRKS---YQEELDKLRQLLK 712
Cdd:PRK03918  336 KEERLEELKKKLKELEKRLEEleerhelyeeakakkeelerlKKRLTGLTPEKLEKELEELEKAkeeIEEEISKITARIG 415
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  713 --KTRVSTDQAAAEQLS-------LVQAELQtqwEAKCEHLLASAKDEH---LQQYQEVCAQRDAYQQKLVQLqEKCLAL 780
Cdd:PRK03918  416 elKKEIKELKKAIEELKkakgkcpVCGRELT---EEHRKELLEEYTAELkriEKELKEIEEKERKLRKELREL-EKVLKK 491
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817221  781 QAQITALTKQNEQhIKELEK--NKSQMSGVEAAASDpSEKVKKIMNQV---FQSLRREFELEESYNGRTIL 846
Cdd:PRK03918  492 ESELIKLKELAEQ-LKELEEklKKYNLEELEKKAEE-YEKLKEKLIKLkgeIKSLKKELEKLEELKKKLAE 560
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
546-713 1.65e-08

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: 56.47  E-value: 1.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  546 EKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMtahQKKETELQMqlteslketdlLRGQLTKVQAK 625
Cdd:COG1579    16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI---KRLELEIEE-----------VEARIKKYEEQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  626 LSELQETSE-QA-QSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEE 703
Cdd:COG1579    82 LGNVRNNKEyEAlQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
                         170
                  ....*....|
gi 578817221  704 LDKLRQLLKK 713
Cdd:COG1579   162 EAEREELAAK 171
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
442-707 1.73e-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: 58.93  E-value: 1.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   442 TEARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMLIPSmsvtmetsmIMSNIQRIIQENERLKQEILEKSNRIE 521
Cdd:TIGR02169  698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE---------LEEDLSSLEQEIENVKSELKELEARIE 768
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   522 EQNDKISEL------------------IERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQ 583
Cdd:TIGR02169  769 ELEEDLHKLeealndlearlshsripeIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   584 -------VSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTS 656
Cdd:TIGR02169  849 iksiekeIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   657 LEEELTDL----RVEKESLEKNLSERKKKSAQERSQAE---------------EEIDEIRKSYQEELDKL 707
Cdd:TIGR02169  929 LEEELSEIedpkGEDEEIPEEELSLEDVQAELQRVEEEiralepvnmlaiqeyEEVLKRLDELKEKRAKL 998
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
590-735 3.11e-08

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: 54.91  E-value: 3.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   590 KMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQaqskFKSEKQNRKQLELKVTSLEEELTDLRVEKE 669
Cdd:pfam13851   34 EIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLEN----YEKDKQSLKNLKARLKVLEKELKDLKWEHE 109
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817221   670 SLEknlsERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKtRVstdQAAAEQLSLVQAELQT 735
Cdd:pfam13851  110 VLE----QRFEKVERERDELYDKFEAAIQDVQQKTGLKNLLLEK-KL---QALGETLEKKEAQLNE 167
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
527-835 4.28e-08

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: 57.88  E-value: 4.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   527 ISELIERNQRYvEQSNLMMEK-------RNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKET 599
Cdd:pfam01576  189 ISDLEERLKKE-EKGRQELEKakrklegESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIR 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   600 ELQMQLTESLKETDLLRGQLTKV-----------QAKLSELQET--SEQAQSKFKSEKQN-----RKQLELKVTSLEEEL 661
Cdd:pfam01576  268 ELEAQISELQEDLESERAARNKAekqrrdlgeelEALKTELEDTldTTAAQQELRSKREQevtelKKALEEETRSHEAQL 347
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   662 TDLRVE------------------KESLEKNL----SERKKKSAQERS--QAEEEIDEIRKSYQEELDKLRQLLKKT-RV 716
Cdd:pfam01576  348 QEMRQKhtqaleelteqleqakrnKANLEKAKqaleSENAELQAELRTlqQAKQDSEHKRKKLEGQLQELQARLSESeRQ 427
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   717 STDqaAAEQLSLVQAELQT------QWEAKCEHLL--ASAKDEHLQQYQEVCA----QRDAYQQKLVQLQEKCLALQAQI 784
Cdd:pfam01576  428 RAE--LAEKLSKLQSELESvssllnEAEGKNIKLSkdVSSLESQLQDTQELLQeetrQKLNLSTRLRQLEDERNSLQEQL 505
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 578817221   785 -------TALTKQNEQHIKELEKNKSQMSGvEAAASDPSEKVKKIMNQVFQSLRREFE 835
Cdd:pfam01576  506 eeeeeakRNVERQLSTLQAQLSDMKKKLEE-DAGTLEALEEGKKRLQRELEALTQQLE 562
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
514-802 4.45e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 57.38  E-value: 4.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  514 LEKSNRIEEQNDKISELIER--------NQRYVEQ--------SNLMMEK------RNNSLQTATENTQaRVLHAEQEKA 571
Cdd:PRK03918  100 LDGSEVLEEGDSSVREWVERlipyhvflNAIYIRQgeidaileSDESREKvvrqilGLDDYENAYKNLG-EVIKEIKRRI 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  572 KVTEELAAATAQVshlqlkmtahQKKETELQMQLTESLKETDL-------LRGQLTKVQAKLSELQETSE---QAQSKFK 641
Cdd:PRK03918  179 ERLEKFIKRTENI----------EELIKEKEKELEEVLREINEisselpeLREELEKLEKEVKELEELKEeieELEKELE 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  642 SEKQNRKQLELKVTSLEEELTDLRVEKESLEKNlsERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRvstdqa 721
Cdd:PRK03918  249 SLEGSKRKLEEKIRELEERIEELKKEIEELEEK--VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE------ 320
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  722 aaEQLSLVQAELQtQWEAKCEHL--LASAKDEHLQQYQEVCAQRDAYQ---QKLVQLQEkclaLQAQITALTKQN-EQHI 795
Cdd:PRK03918  321 --EEINGIEERIK-ELEEKEERLeeLKKKLKELEKRLEELEERHELYEeakAKKEELER----LKKRLTGLTPEKlEKEL 393

                  ....*..
gi 578817221  796 KELEKNK 802
Cdd:PRK03918  394 EELEKAK 400
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
557-785 5.19e-08

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 57.33  E-value: 5.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  557 ENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKE--TELQMQLTESLKETDLLRGQLTKVQAKLSELQETSE 634
Cdd:COG3206   164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  635 QAQSKFKSEKQNRKQL--ELKVTSLEEELTDLRVEKESLEKNLSERkkksAQERSQAEEEIDEIRKSYQEELDKLRQLLk 712
Cdd:COG3206   244 ALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAELAELSARYTPN----HPDVIALRAQIAALRAQLQQEAQRILASL- 318
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578817221  713 KTRVSTDQAAAEQLSLVQAELQTQWEAkcehlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEkcLALQAQIT 785
Cdd:COG3206   319 EAELEALQAREASLQAQLAQLEARLAE-----LPELEAELRRLEREVEVARELYESLLQRLEE--ARLAEALT 384
PTZ00121 PTZ00121
MAEBL; Provisional
505-845 5.24e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.46  E-value: 5.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  505 ENERLKQEILEKSN--RIEEQNDKISELIERNQRYVEQSNLMMEKRN-NSLQTATENTQARVLHAEQEKAKVTE--ELAA 579
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEeeRNNEEIRKFEEARMAHFARRQAAIKAEEARKaDELKKAEEKKKADEAKKAEEKKKADEakKKAE 1312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  580 ATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQN-----------RK 648
Cdd:PTZ00121 1313 EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKadaakkkaeekKK 1392
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  649 QLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEE---------EIDEIRKSyQEELDKLRQLLKKtrvSTD 719
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEakkkaeeakKADEAKKK-AEEAKKAEEAKKK---AEE 1468
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  720 QAAAEQLSLVQAELQTQWEAKCEHLLASAKDEHLQQYQEvcAQRDAyqQKLVQLQEKCLALQAQITALTKQNEQHIKELE 799
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE--AKKKA--DEAKKAEEAKKADEAKKAEEAKKADEAKKAEE 1544
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 578817221  800 KNKSQMSGvEAAASDPSEKVKKIMNQVFQSLRREFELEESYNGRTI 845
Cdd:PTZ00121 1545 KKKADELK-KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA 1589
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
577-803 5.46e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 57.23  E-value: 5.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  577 LAAATAQVSHLQLKMTAHQKKETELQmQLtESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKsekqnrkqlELKVTS 656
Cdd:COG4913   224 FEAADALVEHFDDLERAHEALEDARE-QI-ELLEPIRELAERYAAARERLAELEYLRAALRLWFA---------QRRLEL 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  657 LEEELTDLRVEKESLEknlsERKKKSAQERSQAEEEIDEIRKSYQE----ELDKLRQLLKktrvstdqAAAEQLSLVQAE 732
Cdd:COG4913   293 LEAELEELRAELARLE----AELERLEARLDALREELDELEAQIRGnggdRLEQLEREIE--------RLERELEERERR 360
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578817221  733 LQtQWEAKCEHL---LASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQH---IKELEKNKS 803
Cdd:COG4913   361 RA-RLEALLAALglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELeaeIASLERRKS 436
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
510-802 5.53e-08

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 57.44  E-value: 5.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   510 KQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTE---ELAAATAQVSH 586
Cdd:pfam15921  456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKlrsRVDLKLQELQH 535
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   587 LQLKMTAHQKKETE---LQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQ-SKFKSEKQ-NRKQLEL--------- 652
Cdd:pfam15921  536 LKNEGDHLRNVQTEceaLKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQvEKAQLEKEiNDRRLELqefkilkdk 615
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   653 ---KVTSLEEELTDLRVEKESLEKNLSER---KKKSAQERSQAEEEIDEIR---KSYQEELDKLRQLLK---KTRVSTDQ 720
Cdd:pfam15921  616 kdaKIRELEARVSDLELEKVKLVNAGSERlraVKDIKQERDQLLNEVKTSRnelNSLSEDYEVLKRNFRnksEEMETTTN 695
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   721 AAAEQLSLVQAEL-QTQWEAKC-EHLLASAKDEHLQQYQEVCAQR---DAYQQKLVQLQEkclalqaqitALTKQN-EQH 794
Cdd:pfam15921  696 KLKMQLKSAQSELeQTRNTLKSmEGSDGHAMKVAMGMQKQITAKRgqiDALQSKIQFLEE----------AMTNANkEKH 765

                   ....*...
gi 578817221   795 IKELEKNK 802
Cdd:pfam15921  766 FLKEEKNK 773
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
568-739 5.55e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.08  E-value: 5.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  568 QEKAKVTEELAAATAQVSHL--QLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQ 645
Cdd:COG4717    81 KEAEEKEEEYAELQEELEELeeELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  646 NRKQLElkvtSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQ 725
Cdd:COG4717   161 LEEELE----ELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
                         170
                  ....*....|....
gi 578817221  726 LSLVQAELQTQWEA 739
Cdd:COG4717   237 EAAALEERLKEARL 250
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
573-825 6.71e-08

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 55.69  E-value: 6.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  573 VTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLEL 652
Cdd:COG1340     6 LSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  653 KVTSLEEELTDLRVEKESLEKNLSERKKKSAQ----ERSQ------AEEE---IDEIRKsYQEELDKLRQLLKKTR-VST 718
Cdd:COG1340    86 KLNELREELDELRKELAELNKAGGSIDKLRKEierlEWRQqtevlsPEEEkelVEKIKE-LEKELEKAKKALEKNEkLKE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  719 DQAAAEQLSLVQAELQTQWEAKCEhLLASAKDEHLQQYQ---EVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHI 795
Cdd:COG1340   165 LRAELKELRKEAEEIHKKIKELAE-EAQELHEEMIELYKeadELRKEADELHKEIVEAQEKADELHEEIIELQKELRELR 243
                         250       260       270
                  ....*....|....*....|....*....|..
gi 578817221  796 KELE--KNKSQMSGVEAAASDPSEKVKKIMNQ 825
Cdd:COG1340   244 KELKklRKKQRALKREKEKEELEEKAEEIFEK 275
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
461-846 7.64e-08

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 56.90  E-value: 7.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   461 KMDHLMTKVEELQKHSAGNSMLIPSMSVTMETSMIMSNIQRIIQENERL--KQEILEKSNRIEEQNDKISELIERNQRYV 538
Cdd:pfam02463  633 ELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELqeKAESELAKEEILRRQLEIKKKEQREKEEL 712
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   539 EQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQvshlqlkmtahqKKETELQMQLTESLKETDLlrgq 618
Cdd:pfam02463  713 KKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRL------------KKEEKEEEKSELSLKEKEL---- 776
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   619 ltkvqaklsELQETSEQAQSkfksekqNRKQLELKVTSLEEELTdlrvEKESLEKNLSERKKKSAQERSQAEEEIDEIRK 698
Cdd:pfam02463  777 ---------AEEREKTEKLK-------VEEEKEEKLKAQEEELR----ALEEELKEEAELLEEEQLLIEQEEKIKEEELE 836
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   699 SYQEEL--DKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWEAKCEHLLASAKDEHLQQYQEvcaqrdayQQKLVQLQEK 776
Cdd:pfam02463  837 ELALELkeEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEE--------KKELEEESQK 908
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578817221   777 CLALQAQITALTKQNEQHIKELEKNKSQ---MSGVEAAASDPSEKVKKIMNQVFQSLRREFELEESYNGRTIL 846
Cdd:pfam02463  909 LNLLEEKENEIEERIKEEAEILLKYEEEpeeLLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIE 981
PRK11281 PRK11281
mechanosensitive channel MscK;
588-799 8.69e-08

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 56.84  E-value: 8.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  588 QLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFkseKQNRKQLE---------------- 651
Cdd:PRK11281   44 QLDALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKL---RQAQAELEalkddndeetretlst 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  652 LKVTSLEEELTDLRVEKESLEKNLSERKK-----KSAQERSQAeeEIDEirksYQEELDKLRQLLKKTRVSTDQAAAEQL 726
Cdd:PRK11281  121 LSLRQLESRLAQTLDQLQNAQNDLAEYNSqlvslQTQPERAQA--ALYA----NSQRLQQIRNLLKGGKVGGKALRPSQR 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  727 SLVQAELQtqweakcehlLASAKDEHLQQ-----------YQevcAQRDAYQQKLVQLQEKCLALQAQITA-LTKQNEQH 794
Cdd:PRK11281  195 VLLQAEQA----------LLNAQNDLQRKslegntqlqdlLQ---KQRDYLTARIQRLEHQLQLLQEAINSkRLTLSEKT 261

                  ....*
gi 578817221  795 IKELE 799
Cdd:PRK11281  262 VQEAQ 266
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
507-819 1.01e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 56.59  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  507 ERLKQEILEKSN-----RIEEQNDKISELIERNQRYVEQSNLMMEKRNN--SLQTATENTQARVLHAEQEKAKVTEELAA 579
Cdd:PRK02224  190 DQLKAQIEEKEEkdlheRLNGLESELAELDEEIERYEEQREQARETRDEadEVLEEHEERREELETLEAEIEDLRETIAE 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  580 ATAQVSHLQLKMTAHQKKETELQMQLTESLKETDL-------LRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLEL 652
Cdd:PRK02224  270 TEREREELAEEVRDLRERLEELEEERDDLLAEAGLddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRE 349
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  653 KVTSLEEELTDLRVEKESLEKNLSERK---KKSAQERSQAEEEIDEIRKSYQ------EELDKLRQLLKKTRvstdQAAA 723
Cdd:PRK02224  350 DADDLEERAEELREEAAELESELEEAReavEDRREEIEELEEEIEELRERFGdapvdlGNAEDFLEELREER----DELR 425
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  724 EQLSLVQAELQTQWE--AKCEHLLASAKDEHLQQYQE----VCAQRDaYQQKLVQLQEKCLALQAQITALTKQNEQhIKE 797
Cdd:PRK02224  426 EREAELEATLRTARErvEEAEALLEAGKCPECGQPVEgsphVETIEE-DRERVEELEAELEDLEEEVEEVEERLER-AED 503
                         330       340
                  ....*....|....*....|..
gi 578817221  798 LEKNKSQMSGVEAAASDPSEKV 819
Cdd:PRK02224  504 LVEAEDRIERLEERREDLEELI 525
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
487-725 1.17e-07

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 54.92  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  487 SVTMETSMIMSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHA 566
Cdd:COG1340     5 ELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  567 EQEKaKVTEELAAATAQVSHLQLKMTAHQKKETELQ----MQLTESL---KETDL------LRGQLTKVQAKL---SELQ 630
Cdd:COG1340    85 EKLN-ELREELDELRKELAELNKAGGSIDKLRKEIErlewRQQTEVLspeEEKELvekikeLEKELEKAKKALeknEKLK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  631 ETSEQAQSKFKSEKQNRKQLE----------LKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKsY 700
Cdd:COG1340   164 ELRAELKELRKEAEEIHKKIKelaeeaqelhEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE-L 242
                         250       260
                  ....*....|....*....|....*
gi 578817221  701 QEELDKLRQLLKKTRVSTDQAAAEQ 725
Cdd:COG1340   243 RKELKKLRKKQRALKREKEKEELEE 267
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
566-764 1.31e-07

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 53.78  E-value: 1.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  566 AEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKfksEKQ 645
Cdd:COG1579     1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR---IKK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  646 NRKQLElKVTSlEEELTDLRVEKESLEKNLSERKKksaqERSQAEEEIDEIRKSY---QEELDKLRQLLKKTRVSTDQAA 722
Cdd:COG1579    78 YEEQLG-NVRN-NKEYEALQKEIESLKRRISDLED----EILELMERIEELEEELaelEAELAELEAELEEKKAELDEEL 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 578817221  723 AEqlslVQAELQTQwEAKCEHLLASAKDEHLQQYQEVCAQRD 764
Cdd:COG1579   152 AE----LEAELEEL-EAEREELAAKIPPELLALYERIRKRKN 188
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
595-838 1.49e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.83  E-value: 1.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   595 QKKETELQMQLTEslkeTDLLRGQ--LTKVQAKLSELQETSEQAQsKFKSEKQNRKQLELKVTsleeeLTDLRVEKESLE 672
Cdd:TIGR02168  173 RRKETERKLERTR----ENLDRLEdiLNELERQLKSLERQAEKAE-RYKELKAELRELELALL-----VLRLEELREELE 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   673 KNLSErKKKSAQERSQAEEEIDEirksYQEELDKLRqlLKKTRVSTDQAAAeqlslvQAELQTQWEAKcehllaSAKDEH 752
Cdd:TIGR02168  243 ELQEE-LKEAEEELEELTAELQE----LEEKLEELR--LEVSELEEEIEEL------QKELYALANEI------SRLEQQ 303
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   753 LQQYQEvcaqrdayqqKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRR 832
Cdd:TIGR02168  304 KQILRE----------RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR 373

                   ....*.
gi 578817221   833 EFELEE 838
Cdd:TIGR02168  374 LEELEE 379
Filament pfam00038
Intermediate filament protein;
587-811 1.96e-07

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 54.16  E-value: 1.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   587 LQLKMTAHQKKETELQMQLtESLKETDL--LRGQL-------TKVQAKLSELQETSEQAQSKFKSEKQNRkqlelkvTSL 657
Cdd:pfam00038   30 LETKISELRQKKGAEPSRL-YSLYEKEIedLRRQLdtltverARLQLELDNLRLAAEDFRQKYEDELNLR-------TSA 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   658 EEELTDLR--VEKESLEKNLSERKKKSAQErsqaeeEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQA--EL 733
Cdd:pfam00038  102 ENDLVGLRkdLDEATLARVDLEAKIESLKE------ELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSAlaEI 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   734 QTQWEAKCEHLLASAKDEHLQQYQEVCAQRD-------AYQQKLVQLQEKCLALQAQITALTKQN-----------EQHI 795
Cdd:pfam00038  176 RAQYEEIAAKNREEAEEWYQSKLEELQQAAArngdalrSAKEEITELRRTIQSLEIELQSLKKQKaslerqlaeteERYE 255
                          250
                   ....*....|....*.
gi 578817221   796 KELEKNKSQMSGVEAA 811
Cdd:pfam00038  256 LQLADYQELISELEAE 271
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
498-837 1.97e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.46  E-value: 1.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  498 NIQRIIQE----NERLKQEILEKSN---RIEEQNDKISELIErnqryvEQSNLMMEKRnnSLQTATENTQARVLHAEQEK 570
Cdd:PRK03918  166 NLGEVIKEikrrIERLEKFIKRTENieeLIKEKEKELEEVLR------EINEISSELP--ELREELEKLEKEVKELEELK 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  571 akvtEELAAATAQVshlqLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQ--AQSKFKSEKQNRK 648
Cdd:PRK03918  238 ----EEIEELEKEL----ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDEL 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  649 QlelkvtSLEEELTDLRVEKESLEKNLSERKKKSAqERSQAEEEIDEIRKSYQE------ELDKLRQLLKKTRVSTDQAA 722
Cdd:PRK03918  310 R------EIEKRLSRLEEEINGIEERIKELEEKEE-RLEELKKKLKELEKRLEEleerheLYEEAKAKKEELERLKKRLT 382
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  723 AEQLSLVQAELQTQWEAKCEHLLASAK-DEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITaltkqnEQHIKELekn 801
Cdd:PRK03918  383 GLTPEKLEKELEELEKAKEEIEEEISKiTARIGELKKEIKELKKAIEELKKAKGKCPVCGRELT------EEHRKEL--- 453
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 578817221  802 ksqMSGVEAAASDPSEKVKKIMNQVFQSLRREFELE 837
Cdd:PRK03918  454 ---LEEYTAELKRIEKELKEIEEKERKLRKELRELE 486
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
511-709 2.23e-07

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 53.00  E-value: 2.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  511 QEILEKSNRIEEQNDKISELIERnqryveqsnlmMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLK 590
Cdd:COG1579    13 QELDSELDRLEHRLKELPAELAE-----------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  591 MTAHqKKETELQmQLTeslKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLElkvTSLEEELTDLRVEKES 670
Cdd:COG1579    82 LGNV-RNNKEYE-ALQ---KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE---AELEEKKAELDEELAE 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 578817221  671 LEKNLSERKKksaqERSQAEEEIDE-IRKSYqeelDKLRQ 709
Cdd:COG1579   154 LEAELEELEA----EREELAAKIPPeLLALY----ERIRK 185
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
566-817 3.24e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 54.07  E-value: 3.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  566 AEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQET-SEQAQSKFKSEK 644
Cdd:COG3883    21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERARALYRSGG 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  645 QNrKQLELKVTSleEELTDLrVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKtrVSTDQAAAE 724
Cdd:COG3883   101 SV-SYLDVLLGS--ESFSDF-LDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE--LEAAKAELE 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  725 QLSLVQAELQTQweakcehlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQ 804
Cdd:COG3883   175 AQQAEQEALLAQ--------LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
                         250
                  ....*....|...
gi 578817221  805 MSGVEAAASDPSE 817
Cdd:COG3883   247 AGAGAAGAAGAAA 259
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
604-818 3.39e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 54.07  E-value: 3.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  604 QLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERkKKSA 683
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER-ARAL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  684 QERSQAEEEIDEI--RKSYQEELDKLRQLlkKTRVSTDQAAAEQLSLVQAELQTQweakcEHLLASAKDEHLQQYQEVCA 761
Cdd:COG3883    96 YRSGGSVSYLDVLlgSESFSDFLDRLSAL--SKIADADADLLEELKADKAELEAK-----KAELEAKLAELEALKAELEA 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578817221  762 QRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEK 818
Cdd:COG3883   169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
PTZ00121 PTZ00121
MAEBL; Provisional
504-820 5.25e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.38  E-value: 5.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  504 QENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRN--NSLQTATENTQARVLHAEQEKAKVTEELA--A 579
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKaeEAKKKAEEAKKADEAKKKAEEAKKADEAKkkA 1492
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  580 ATAQVSHLQLKMTAHQKKETElQMQLTESLKETDLLRGQLTKVQA----------KLSELQETSE--QAQSKFKSEkQNR 647
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKAD-EAKKAEEAKKADEAKKAEEAKKAdeakkaeekkKADELKKAEElkKAEEKKKAE-EAK 1570
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  648 KQLELKVTSLEEELTDLRVEKESLE---KNLSERKKKSAQERSQAEEE---IDEIRKSyQEELDKLRQLLKKTRVSTDQA 721
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEevmKLYEEEKKMKAEEAKKAEEAkikAEELKKA-EEEKKKVEQLKKKEAEEKKKA 1649
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  722 -----AAEQLSLVQAELQTQWEA---KCEHLLASAKDEhlQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNE- 792
Cdd:PTZ00121 1650 eelkkAEEENKIKAAEEAKKAEEdkkKAEEAKKAEEDE--KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEe 1727
                         330       340       350
                  ....*....|....*....|....*....|....
gi 578817221  793 ------QHIKELEKNKSQmsgVEAAASDPSEKVK 820
Cdd:PTZ00121 1728 nkikaeEAKKEAEEDKKK---AEEAKKDEEEKKK 1758
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
499-715 6.24e-07

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 53.82  E-value: 6.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   499 IQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQaRVLHAEQEKAKVTEELA 578
Cdd:pfam02463  814 AELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLK-EEELEEQKLKDELESKE 892
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   579 AATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQ-SKFKSEKQNRKQLELKVTSL 657
Cdd:pfam02463  893 EKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEeNNKEEEEERNKRLLLAKEEL 972
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 578817221   658 EEEltDLRVEKESLEKNLSERKKKSAQERsqAEEEIDEIRksyQEELDKLRQLLKKTR 715
Cdd:pfam02463  973 GKV--NLMAIEEFEEKEERYNKDELEKER--LEEEKKKLI---RAIIEETCQRLKEFL 1023
CCCAP pfam15964
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ...
504-838 6.84e-07

Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.


Pssm-ID: 435040 [Multi-domain]  Cd Length: 703  Bit Score: 53.76  E-value: 6.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   504 QENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQ 583
Cdd:pfam15964  367 RQKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMD 446
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   584 VSHL------QLKMTAHQKKETELQMQ--LTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVT 655
Cdd:pfam15964  447 VTKVcgemryQLNQTKMKKDEAEKEHReyRTKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLG 526
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   656 SLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEideirksyqeeldkLRQLLKKTRVSTDQAAAEQLSLV--QAEL 733
Cdd:pfam15964  527 ESEHQLHLTRLEKESIQQSFSNEAKAQALQAQQREQE--------------LTQKMQQMEAQHDKTVNEQYSLLtsQNTF 592
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   734 QTQWEAKCeHLLASAKDEHLQQYQEVCAQrdaYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAAS 813
Cdd:pfam15964  593 IAKLKEEC-CTLAKKLEEITQKSRSEVEQ---LSQEKEYLQDRLEKLQKRNEELEEQCVQHGRMHERMKQRLRQLDKHCQ 668
                          330       340
                   ....*....|....*....|....*
gi 578817221   814 DPSEKVKKIMNQVFQSLRREFELEE 838
Cdd:pfam15964  669 ATAQQLVQLLSKQNQLFKERQNLTE 693
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
510-800 7.07e-07

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: 53.80  E-value: 7.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  510 KQEILEKSNRIEEQNDKISELIERnQRYVEQSNLMMEKRNNSLQTATENtQARVLHAEQEKAKVTEELAAATAQVSHLQL 589
Cdd:COG3096   298 RRQLAEEQYRLVEMARELEELSAR-ESDLEQDYQAASDHLNLVQTALRQ-QEKIERYQEDLEELTERLEEQEEVVEEAAE 375
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  590 kmtahQKKETELQMQLTEslKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQL---ELKVTSLEEELTDLRV 666
Cdd:COG3096   376 -----QLAEAEARLEAAE--EEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALCglpDLTPENAEDYLAAFRA 448
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  667 EKESLEKNLSERKkksaQERSQAEEEIDEIRKSYQ------------EELDKLRQLLKKTRVSTDQAA-----------A 723
Cdd:COG3096   449 KEQQATEEVLELE----QKLSVADAARRQFEKAYElvckiageversQAWQTARELLRRYRSQQALAQrlqqlraqlaeL 524
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  724 EQLSLVQAELQTQWEAKCEHL---LASAKD-EHLQQYQEvcAQRDAYQQKLVQLQEKCLALQAQitalTKQNEQHIKELE 799
Cdd:COG3096   525 EQRLRQQQNAERLLEEFCQRIgqqLDAAEElEELLAELE--AQLEELEEQAAEAVEQRSELRQQ----LEQLRARIKELA 598

                  .
gi 578817221  800 K 800
Cdd:COG3096   599 A 599
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
557-843 7.64e-07

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 53.64  E-value: 7.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   557 ENTQARvlhaEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQL---TESLKETDLLRGQL-----------TKV 622
Cdd:pfam01576    5 EEMQAK----EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLqaeTELCAEAEEMRARLaarkqeleeilHEL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   623 QAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKN----------LSERKKKSAQERSQAEEE 692
Cdd:pfam01576   81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKikkleedillLEDQNSKLSKERKLLEER 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   693 IDEIRKSYQEELDKLRQLLKktrvstdqaaaeqlslvqaeLQTQWEAKCEHLLASAKDEHlQQYQEVCAQRDAYQQKLVQ 772
Cdd:pfam01576  161 ISEFTSNLAEEEEKAKSLSK--------------------LKNKHEAMISDLEERLKKEE-KGRQELEKAKRKLEGESTD 219
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817221   773 LQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQsLRREFELEESYNGR 843
Cdd:pfam01576  220 LQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISE-LQEDLESERAARNK 289
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
499-838 1.04e-06

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 53.05  E-value: 1.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   499 IQRIIQENERLKQEILE-----KSNRIEEQNDKisELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKV 573
Cdd:pfam02463  144 IEIIAMMKPERRLEIEEeaagsRLKRKKKEALK--KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLEL 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   574 TEELAAATAQVSHLQlkmtahqkketelqmqlteslKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKqLELK 653
Cdd:pfam02463  222 EEEYLLYLDYLKLNE---------------------ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENK-EEEK 279
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   654 VTSLEEEL-----TDLRVEKESLEK-----NLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAA 723
Cdd:pfam02463  280 EKKLQEEElkllaKEEEELKSELLKlerrkVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEE 359
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   724 EQLSLVQAELQTQWEAKCEHLLASA-------KDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIK 796
Cdd:pfam02463  360 ELEKLQEKLEQLEEELLAKKKLESErlssaakLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESI 439
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 578817221   797 ELEKNKSQMSGVEAaasDPSEKVKKIMNQVFQSLRREFELEE 838
Cdd:pfam02463  440 ELKQGKLTEEKEEL---EKQELKLLKDELELKKSEDLLKETQ 478
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
503-838 1.40e-06

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 51.84  E-value: 1.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   503 IQENERLKQEILEKSNRIEEqndkiseliernqryveqsnlMMEKRNnslqtatENTQARVLHAEQEKAKVTEELAAAta 582
Cdd:pfam13868   28 IAEKKRIKAEEKEEERRLDE---------------------MMEEER-------ERALEEEEEKEEERKEERKRYRQE-- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   583 qvshLQLKMTAHQKKEtelQMQLTESLKETDLLRGQLTKVQAKlselqetsEQAQSKFKSEKQNRKQLELKVTSleeELT 662
Cdd:pfam13868   78 ----LEEQIEEREQKR---QEEYEEKLQEREQMDEIVERIQEE--------DQAEAEEKLEKQRQLREEIDEFN---EEQ 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   663 DLRVEKESLEKNLSERK-----KKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVstDQAAAEQL--SLVQAELQT 735
Cdd:pfam13868  140 AEWKELEKEEEREEDERileylKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQD--EKAERDELraKLYQEEQER 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   736 QW-------EAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQhiKELEKNKSQMSGV 808
Cdd:pfam13868  218 KErqkereeAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAE--KRRMKRLEHRREL 295
                          330       340       350
                   ....*....|....*....|....*....|
gi 578817221   809 EAAASDPSEKVKKIMNQVFQSLRREFELEE 838
Cdd:pfam13868  296 EKQIEEREEQRAAEREEELEEGERLREEEA 325
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
540-826 1.72e-06

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 52.53  E-value: 1.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   540 QSNLMMEKRNNSLQTATENTQARvlHAEQEkakvtEELAAATAQVSHLQLKMT----AHQKKETELQMQLTESLKEtdll 615
Cdd:pfam12128  597 ASEEELRERLDKAEEALQSAREK--QAAAE-----EQLVQANGELEKASREETfartALKNARLDLRRLFDEKQSE---- 665
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   616 rgQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNL-SERKKKSAQ-------ERS 687
Cdd:pfam12128  666 --KDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVeGALDAQLALlkaaiaaRRS 743
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   688 QAEEEIDEIRKSYQEELDKLrqllkktrvSTDQAAAEQLSLVQAELQTQWE--AKCEHLLASAKDEHLQQYQEvcaQRDA 765
Cdd:pfam12128  744 GAKAELKALETWYKRDLASL---------GVDPDVIAKLKREIRTLERKIEriAVRRQEVLRYFDWYQETWLQ---RRPR 811
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817221   766 YQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQV 826
Cdd:pfam12128  812 LATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKL 872
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
507-678 1.93e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 50.31  E-value: 1.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  507 ERLKQEILEKSNRIEEQNDKISEL---IERNQRYVEQSNLMMEKRNNSLQTATENtqarvlhaeqekakvtEELAAATAQ 583
Cdd:COG1579    34 AELEDELAALEARLEAAKTELEDLekeIKRLELEIEEVEARIKKYEEQLGNVRNN----------------KEYEALQKE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  584 VSHLQLKMTAHQKKETELQMQLTEslketdlLRGQLTKVQAKLSELQETSEQAQskfksekqnrKQLELKVTSLEEELTD 663
Cdd:COG1579    98 IESLKRRISDLEDEILELMERIEE-------LEEELAELEAELAELEAELEEKK----------AELDEELAELEAELEE 160
                         170
                  ....*....|....*
gi 578817221  664 LRVEKESLEKNLSER 678
Cdd:COG1579   161 LEAEREELAAKIPPE 175
PLN02939 PLN02939
transferase, transferring glycosyl groups
447-725 2.04e-06

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 52.21  E-value: 2.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  447 HNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMLIPSMSVTMETSMIMSN---------IQRIIQENERLKQEILEKS 517
Cdd:PLN02939   97 HNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNqarlqaledLEKILTEKEALQGKINILE 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  518 NRIEEQNDKIsELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTahQKK 597
Cdd:PLN02939  177 MRLSETDARI-KLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELI--EVA 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  598 ETELQMQLTEslKETDLLRGQLTKVQAKLSELQE--------------------------TSEQAQSKFKSEKQNRkQLE 651
Cdd:PLN02939  254 ETEERVFKLE--KERSLLDASLRELESKFIVAQEdvsklsplqydcwwekvenlqdlldrATNQVEKAALVLDQNQ-DLR 330
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817221  652 LKVTSLEEELTDLRVEKESLEK-NLSERKKKSAQERSQA-EEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQ 725
Cdd:PLN02939  331 DKVDKLEASLKEANVSKFSSYKvELLQQKLKLLEERLQAsDHEIHSYIQLYQESIKEFQDTLSKLKEESKKRSLEH 406
PLN02939 PLN02939
transferase, transferring glycosyl groups
517-817 2.38e-06

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 51.83  E-value: 2.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  517 SNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENT----QARvLHAEQEKAKVTEELAAATAQVSHLQLKMT 592
Cdd:PLN02939  102 MQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNIlllnQAR-LQALEDLEKILTEKEALQGKINILEMRLS 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  593 ahqkkETELQMQLTESLK-ETDLLRGQLTKVQAKLSELQETSEQAqskfksekqnrkqlelkVTSLEEELTDLRVEKESL 671
Cdd:PLN02939  181 -----ETDARIKLAAQEKiHVEILEEQLEKLRNELLIRGATEGLC-----------------VHSLSKELDVLKEENMLL 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  672 EKNLSERKkksaqersqaeEEIDEIRKSYQE--ELDKLRQLLKKT------RVSTDQAAAEQLSLVQAELqtqWEAKCE- 742
Cdd:PLN02939  239 KDDIQFLK-----------AELIEVAETEERvfKLEKERSLLDASlrelesKFIVAQEDVSKLSPLQYDC---WWEKVEn 304
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  743 --HLLASAKD--EH----LQQYQEV--------------------CAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQH 794
Cdd:PLN02939  305 lqDLLDRATNqvEKaalvLDQNQDLrdkvdkleaslkeanvskfsSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQES 384
                         330       340       350
                  ....*....|....*....|....*....|
gi 578817221  795 IKELE------KNKSQMSGVEAAASD-PSE 817
Cdd:PLN02939  385 IKEFQdtlsklKEESKKRSLEHPADDmPSE 414
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
500-814 2.39e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 51.96  E-value: 2.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  500 QRIIQENERLKQEILEKSNRIEEQNDKISE---------------------LIERN------------------------ 534
Cdd:PRK02224  240 DEVLEEHEERREELETLEAEIEDLRETIAEterereelaeevrdlrerleeLEEERddllaeaglddadaeavearreel 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  535 -------QRYVEQSNLMMEKRNNSLQTATEN------------TQARVLHAEQEKAKvtEELAAATAQVSHLQLKMTAHQ 595
Cdd:PRK02224  320 edrdeelRDRLEECRVAAQAHNEEAESLREDaddleeraeelrEEAAELESELEEAR--EAVEDRREEIEELEEEIEELR 397
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  596 KKETELQMQL------TESLKET-DLLRGQLTKVQAKLSELQETSEQAQSKFKSEK-----QNRK---------QLELKV 654
Cdd:PRK02224  398 ERFGDAPVDLgnaedfLEELREErDELREREAELEATLRTARERVEEAEALLEAGKcpecgQPVEgsphvetieEDRERV 477
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  655 TSLEEELTDLRVEKESLEK----------------NLSERKKKSAQERSQAEEEIDEiRKSYQEELDKLRQLLKKTRVST 718
Cdd:PRK02224  478 EELEAELEDLEEEVEEVEErleraedlveaedrieRLEERREDLEELIAERRETIEE-KRERAEELRERAAELEAEAEEK 556
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  719 DQAAAEQLSLVQAELQTQweAKCEHLLASAKD--EHLQQYQEVCAQRDAYQQKLVQLQEKclalQAQITALTKQNEQHIK 796
Cdd:PRK02224  557 REAAAEAEEEAEEAREEV--AELNSKLAELKEriESLERIRTLLAAIADAEDEIERLREK----REALAELNDERRERLA 630
                         410       420
                  ....*....|....*....|....
gi 578817221  797 ELEKNKSQMSG------VEAAASD 814
Cdd:PRK02224  631 EKRERKRELEAefdearIEEARED 654
PRK11281 PRK11281
mechanosensitive channel MscK;
498-737 2.76e-06

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 51.84  E-value: 2.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  498 NIQRIIQENERLKQEILEKSNRIEEQNDKISELIERN-----QRY----VEQSNLMMEKRNNSLQTATE-----NTQARV 563
Cdd:PRK11281   74 KIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNdeetrETLstlsLRQLESRLAQTLDQLQNAQNdlaeyNSQLVS 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  564 LHAEQEKAKVteELAAATAQVSHL--QLKMTAHQKKET--ELQMQLTESLKETDLLRGQLTKVQAKLSELQETsEQAQSK 639
Cdd:PRK11281  154 LQTQPERAQA--ALYANSQRLQQIrnLLKGGKVGGKALrpSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDL-LQKQRD 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  640 FKSEKQNRkqlelkvtsLEEELTDLRvekESL-EKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVST 718
Cdd:PRK11281  231 YLTARIQR---------LEHQLQLLQ---EAInSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLLKAT 298
                         250       260
                  ....*....|....*....|
gi 578817221  719 DQAAaeqlSLVQAELQT-QW 737
Cdd:PRK11281  299 EKLN----TLTQQNLRVkNW 314
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
600-797 2.86e-06

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


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 51.23  E-value: 2.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   600 ELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLElkvtSLEEEL-------TDLRVEKESLE 672
Cdd:pfam05622   18 ELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLE----QLQEENfrletarDDYRIKCEELE 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   673 KNLSERK------KKSAQERSQAEEEIDEIRKS-------------YQEELDKLRQLLKKTRVSTDQAAaeqlSLVQAEL 733
Cdd:pfam05622   94 KEVLELQhrneelTSLAEEAQALKDEMDILRESsdkvkkleatvetYKKKLEDLGDLRRQVKLLEERNA----EYMQRTL 169
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578817221   734 QTQWEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKE 797
Cdd:pfam05622  170 QLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIE 233
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
462-797 3.55e-06

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: 51.05  E-value: 3.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   462 MDHLMTKVEELQKHSAGNSML--IPSMSVtmetsmimsnIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVE 539
Cdd:pfam07888    3 LDELVTLEEESHGEEGGTDMLlvVPRAEL----------LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   540 QSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQmQLTESLKETDLLRgql 619
Cdd:pfam07888   73 RQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELE-EDIKTLTQRVLER--- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   620 tkvQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSER----------------KKKSA 683
Cdd:pfam07888  149 ---ETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRdtqvlqlqdtittltqKLTTA 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   684 QERSQAEEEIDEIRKSYQEEL-------DKLRQLLKKTRVSTDQAAAE----------------QLSLVQAELQTQWEAK 740
Cdd:pfam07888  226 HRKEAENEALLEELRSLQERLnaserkvEGLGEELSSMAAQRDRTQAElhqarlqaaqltlqlaDASLALREGRARWAQE 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   741 CEHLLASAKDEH---------LQQYQEVCAQRDAYQQKL------------VQLQEKCLALQ---AQITALTKQNEQHIK 796
Cdd:pfam07888  306 RETLQQSAEADKdrieklsaeLQRLEERLQEERMEREKLevelgrekdcnrVQLSESRRELQelkASLRVAQKEKEQLQA 385

                   .
gi 578817221   797 E 797
Cdd:pfam07888  386 E 386
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
499-860 3.99e-06

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


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 51.29  E-value: 3.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   499 IQRIIQENERLKQEI-------LEKSNRIEEQNDKISEL-IERNQRYVEQSNLM-------MEKRNNSLQTATENTQARV 563
Cdd:pfam07111   68 ISRQLQELRRLEEEVrllretsLQQKMRLEAQAMELDALaVAEKAGQAEAEGLRaalagaeMVRKNLEEGSQRELEEIQR 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   564 LHAEQEKAKVT---EELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLsELQET-------- 632
Cdd:pfam07111  148 LHQEQLSSLTQaheEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEEL-EAQVTlveslrky 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   633 -SEQAQSKFKSE--KQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQ 709
Cdd:pfam07111  227 vGEQVPPEVHSQtwELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRS 306
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   710 LLKKTRvstDQAAAEQLSLVQAELQTQWEAK-CEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALT 788
Cdd:pfam07111  307 LLNRWR---EKVFALMVQLKAQDLEHRDSVKqLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELS 383
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   789 KQNEQHIKELEKNKS---QMSGVEAAASDPSEKVKKIMNQVFQSLRREFELEE--SYNGR---TILGTIMNTIKMVTLQL 860
Cdd:pfam07111  384 RAQEARRRQQQQTASaeeQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNrlSYAVRkvhTIKGLMARKVALAQLRQ 463
mukB PRK04863
chromosome partition protein MukB;
525-814 4.06e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 51.50  E-value: 4.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  525 DKISELIERNQRYVeqSNLMMEKRNNslqtATENTQaRVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQ 604
Cdd:PRK04863  257 DLFKHLITESTNYV--AADYMRHANE----RRVHLE-EALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQD 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  605 LtESLKEtdllrgQLTKVQaklselqeTSEQAQskfksEKQNRKQLELkvtsleEELTDLRVEKESLEKNLSERKKKSAQ 684
Cdd:PRK04863  330 Y-QAASD------HLNLVQ--------TALRQQ-----EKIERYQADL------EELEERLEEQNEVVEEADEQQEENEA 383
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  685 ERSQAEEEIDEIRKS---YQEELDKLR----------QLLKKTRVSTDQA--AAEQLSLVQAELQTQWEAKCEHLLA--- 746
Cdd:PRK04863  384 RAEAAEEEVDELKSQladYQQALDVQQtraiqyqqavQALERAKQLCGLPdlTADNAEDWLEEFQAKEQEATEELLSleq 463
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  747 ------SAKDEHLQQYQEVCA-----QRDAYQQKLVQL-----QEKCLALQAQitaltkQNEQHIKELEKNKSQMSGVEA 810
Cdd:PRK04863  464 klsvaqAAHSQFEQAYQLVRKiagevSRSEAWDVARELlrrlrEQRHLAEQLQ------QLRMRLSELEQRLRQQQRAER 537

                  ....
gi 578817221  811 AASD 814
Cdd:PRK04863  538 LLAE 541
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
575-800 4.35e-06

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: 51.11  E-value: 4.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  575 EELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKV--------QAKLSELQETSEQAQSKFKSEKQN 646
Cdd:COG3096   836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAnlladetlADRLEELREELDAAQEAQAFIQQH 915
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  647 RKQLELkvtsLEEELTDLRVEKESLEkNLSERKKKSAQERSQAEEEIDEI-----RK---SYQEEL----------DKLR 708
Cdd:COG3096   916 GKALAQ----LEPLVAVLQSDPEQFE-QLQADYLQAKEQQRRLKQQIFALsevvqRRphfSYEDAVgllgensdlnEKLR 990
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  709 QLLK-------KTRVSTDQAAAE--QLSLVQAELQTQWEAKCEhLLASAKDEhLQQY-------QEVCAQ--RDAYQQKL 770
Cdd:COG3096   991 ARLEqaeearrEAREQLRQAQAQysQYNQVLASLKSSRDAKQQ-TLQELEQE-LEELgvqadaeAEERARirRDELHEEL 1068
                         250       260       270
                  ....*....|....*....|....*....|
gi 578817221  771 VQLQEKCLALQAQITALTKQNEQHIKELEK 800
Cdd:COG3096  1069 SQNRSRRSQLEKQLTRCEAEMDSLQKRLRK 1098
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
567-840 4.36e-06

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 51.12  E-value: 4.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   567 EQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQN 646
Cdd:TIGR00618  179 TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKK 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   647 RKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQL 726
Cdd:TIGR00618  259 QQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQS 338
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   727 SL-VQAELQTQWEAKCehllasakdEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSqm 805
Cdd:TIGR00618  339 SIeEQRRLLQTLHSQE---------IHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQR-- 407
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 578817221   806 sgvEAAASDPSEKVKKIMNQVFQSLRREFELEESY 840
Cdd:TIGR00618  408 ---EQATIDTRTSAFRDLQGQLAHAKKQQELQQRY 439
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
625-744 5.16e-06

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 47.30  E-value: 5.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   625 KLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRV-------EKESLEKNLSERKKK---SAQERSQA----- 689
Cdd:pfam12718    1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHknqqleeEVEKLEEQLKEAKEKaeeSEKLKTNNenltr 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578817221   690 -----EEEIDEIRKSYQEELDKLRQllkktrvsTDQAAAEQLSLVQAELQT--QWEAKCEHL 744
Cdd:pfam12718   81 kiqllEEELEESDKRLKETTEKLRE--------TDVKAEHLERKVQALEQErdEWEKKYEEL 134
PTZ00121 PTZ00121
MAEBL; Provisional
505-943 5.39e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 5.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  505 ENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTE--ELAAATA 582
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAakKKAEEKK 1391
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  583 QVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQA-----------KLSELQETSEQ---AQSKFKSEKQNRK 648
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAdeakkkaeeakKADEAKKKAEEakkAEEAKKKAEEAKK 1471
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  649 QLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEE--------EIDEIRKSyqEELDKLRQLLK--KTRVST 718
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEakkaeeakKADEAKKA--EEAKKADEAKKaeEKKKAD 1549
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  719 DQAAAEQLSLVQAELQTQWEAKCEH--LLASAKDEHLQQYQEvcaQRDAYQQKLVQLQEKCLALQAQitaltKQNEQHIK 796
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEdkNMALRKAEEAKKAEE---ARIEEVMKLYEEEKKMKAEEAK-----KAEEAKIK 1621
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  797 --ELEKNKSQMSGVEAAASDPSEKVKKImnqvfQSLRREFEleesyngrtilgtiMNTIKMVTLQllnqqeQEKEESSSE 874
Cdd:PTZ00121 1622 aeELKKAEEEKKKVEQLKKKEAEEKKKA-----EELKKAEE--------------ENKIKAAEEA------KKAEEDKKK 1676
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817221  875 EEEEKAEERPRRPSQEQSASASSGQPQAPLNRERPESPMVPSEQV--VEEAVPLPPQALTTSQDGHRRKGD 943
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELkkAEEENKIKAEEAKKEAEEDKKKAE 1747
PHA03247 PHA03247
large tegument protein UL36; Provisional
883-1096 6.64e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 6.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  883 RPRRPSQEQsasassgQPQAPLNRERPESPMVPSEQVVEEAVPLPPQALTTSQDGhrRKGDSEAEALSEIKDGSLPPELS 962
Cdd:PHA03247 2907 RPPQPQAPP-------PPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGE--PSGAVPQPWLGALVPGRVAVPRF 2977
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  963 CIPSHRvlgPPTSIPPEPLGPVSMDSECEESLAASPMAAKPDNPSGKVCVRE-VAPDGPLQESSTRLSLTSDPEEGDPLA 1041
Cdd:PHA03247 2978 RVPQPA---PSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQtLWPPDDTEDSDADSLFDSDSERSDLEA 3054
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578817221 1042 LGPEsPGEPQPPQLKKDDVTSSTGPHKELSSTEAG--STVAGAAL--RPSHHSQRSSLS 1096
Cdd:PHA03247 3055 LDPL-PPEPHDPFAHEPDPATPEAGARESPSSQFGppPLSANAALsrRYVRSTGRSALA 3112
mukB PRK04863
chromosome partition protein MukB;
507-787 6.68e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 50.73  E-value: 6.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  507 ERLKQEILEKSNRIEEQN---DKISELIERNQRYVEQSNLMMEKRNNSL---QTATENTQARVL---HAEQ--EKAK--- 572
Cdd:PRK04863  351 ERYQADLEELEERLEEQNevvEEADEQQEENEARAEAAEEEVDELKSQLadyQQALDVQQTRAIqyqQAVQalERAKqlc 430
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  573 ----------------VTEELAAATAQVSHLQLKMTAHQ--KKETELQMQLTESL-----------KETDLLR------- 616
Cdd:PRK04863  431 glpdltadnaedwleeFQAKEQEATEELLSLEQKLSVAQaaHSQFEQAYQLVRKIagevsrseawdVARELLRrlreqrh 510
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  617 --GQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSlEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEid 694
Cdd:PRK04863  511 laEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDD-EDELEQLQEELEARLESLSESVSEARERRMALRQQ-- 587
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  695 eirksyQEELDKLRQLLKKTRVS--TDQAAAEQLSlvqaelqtqwEAKCEHLLASAK-DEHLQQYQEvcaQRDAYQQKLV 771
Cdd:PRK04863  588 ------LEQLQARIQRLAARAPAwlAAQDALARLR----------EQSGEEFEDSQDvTEYMQQLLE---RERELTVERD 648
                         330
                  ....*....|....*.
gi 578817221  772 QLQEKCLALQAQITAL 787
Cdd:PRK04863  649 ELAARKQALDEEIERL 664
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
504-835 6.69e-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: 6.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   504 QENERLKQEILEKSNRIEEQNDKISELIERnqryVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQ 583
Cdd:pfam01576  422 SESERQRAELAEKLSKLQSELESVSSLLNE----AEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDE 497
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   584 VSHL--QLKMTAHQKKETE-----LQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTS 656
Cdd:pfam01576  498 RNSLqeQLEEEEEAKRNVErqlstLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNR 577
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   657 LEEELTDLRVEKESLEKNLS--ERKKKS---------------AQERSQAE------------------------EEIDE 695
Cdd:pfam01576  578 LQQELDDLLVDLDHQRQLVSnlEKKQKKfdqmlaeekaisaryAEERDRAEaeareketralslaraleealeakEELER 657
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   696 IRKSYQEELDKL----------RQLLKKTRVSTDQAAAE---QLSLVQAELQTQWEAK--CEHLLASAKDEHLQQYQevc 760
Cdd:pfam01576  658 TNKQLRAEMEDLvsskddvgknVHELERSKRALEQQVEEmktQLEELEDELQATEDAKlrLEVNMQALKAQFERDLQ--- 734
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   761 AQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHI---KELEKN-KSQMSGVEAAASDPSEKVK--KIMNQVFQSLRREF 834
Cdd:pfam01576  735 ARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVaakKKLELDlKELEAQIDAANKGREEAVKqlKKLQAQMKDLQREL 814

                   .
gi 578817221   835 E 835
Cdd:pfam01576  815 E 815
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
126-197 6.75e-06

Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 47.02  E-value: 6.75e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578817221  126 VEVGDSLEVAYTGWLfqnhVLGQVFDSTANKDKLLrLKLGSGKVIKGWEDGMLGMKKGGKRLLIVPPACAVG 197
Cdd:COG1047     1 IEKGDVVTLHYTLKL----EDGEVFDSTFEGEPLE-FLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG 67
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
588-815 6.76e-06

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 48.84  E-value: 6.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   588 QLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQL-------------ELKV 654
Cdd:pfam12795    1 KLDELEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALqakaeaapkeilaSLSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   655 TSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAE---EEIDEIRKsyqeELDKLRQLLKKTRVSTDQAAAEQLSLVQA 731
Cdd:pfam12795   81 EELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPEraqQQLSEARQ----RLQQIRNRLNGPAPPGEPLSEAQRWALQA 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   732 ELQtqweakcehlLASAKDEHLQQYQEVC--------AQRDAYQQKLVQLQEKCLALQAQItaltkqNEQHIKELEKN-- 801
Cdd:pfam12795  157 ELA----------ALKAQIDMLEQELLSNnnrqdllkARRDLLTLRIQRLEQQLQALQELL------NEKRLQEAEQAva 220
                          250
                   ....*....|....
gi 578817221   802 KSQMSGVEAAASDP 815
Cdd:pfam12795  221 QTEQLAEEAAGDHP 234
CAGE1 pfam15066
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ...
510-690 7.95e-06

Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.


Pssm-ID: 464481  Cd Length: 528  Bit Score: 49.83  E-value: 7.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   510 KQEIL-EKSNRIEEqndKISELIErnqryvEQSNLMMEKR--NNSLQTATE---NTQARVLHAEQEKAKVTEELAAATAQ 583
Cdd:pfam15066  357 KQQVFvDIINKLKE---NVEELIE------DKYNVILEKNdiNKTLQNLQEilaNTQKHLQESRKEKETLQLELKKIKVN 427
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   584 VSHLQLK-MTAHQKKETE----LQMQLTESLKETDLLRGQLTKvqaklSELQETSEQAQSKFKSEKQNRKQLELkvtSLE 658
Cdd:pfam15066  428 YVHLQERyITEMQQKNKSvsqcLEMDKTLSKKEEEVERLQQLK-----GELEKATTSALDLLKREKETREQEFL---SLQ 499
                          170       180       190
                   ....*....|....*....|....*....|...
gi 578817221   659 EELTdlRVEKESLEknlsERKK-KSAQERSQAE 690
Cdd:pfam15066  500 EEFQ--KHEKENLE----ERQKlKSRLEKLVAQ 526
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
596-711 8.93e-06

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


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 46.09  E-value: 8.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   596 KKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQN----RKQL-ELK--VTSLEEELTDLRVEK 668
Cdd:pfam07926    1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVLhaedIKALqALReeLNELKAEIAELKAEA 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 578817221   669 ESLEKNLSERKKKSAQERSQAEEEIDEIRKSYqEELDKLRQLL 711
Cdd:pfam07926   81 ESAKAELEESEESWEEQKKELEKELSELEKRI-EDLNEQNKLL 122
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
624-821 1.40e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.68  E-value: 1.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   624 AKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEK--NLSERKKK-------------------- 681
Cdd:TIGR02169  163 AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqALLKEKREyegyellkekealerqkeai 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   682 ----SAQERSQA--EEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAA---EQLSLVQAELqtqweAKCEHLLASAKDEH 752
Cdd:TIGR02169  243 erqlASLEEELEklTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLrvkEKIGELEAEI-----ASLERSIAEKEREL 317
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578817221   753 LQ---QYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKK 821
Cdd:TIGR02169  318 EDaeeRLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
443-811 1.41e-05

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 49.57  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  443 EARQhntEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMLIPSMSVTMETSMIMSNIQRIIQENERLKQEILEKSNRIEE 522
Cdd:COG3096   289 ELRR---ELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQEKIERYQEDLEELTERLEE 365
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  523 QNDKISELIERNQRYVEQSNLmMEKRNNSL-------QTATENTQARVLHAEQ-----EKAK------------VTEELA 578
Cdd:COG3096   366 QEEVVEEAAEQLAEAEARLEA-AEEEVDSLksqladyQQALDVQQTRAIQYQQavqalEKARalcglpdltpenAEDYLA 444
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  579 AATAQVSHL---------QLKMTAHQKKETELQMQLTESL-----------KETDLLR---------GQLTKVQAKLSEL 629
Cdd:COG3096   445 AFRAKEQQAteevleleqKLSVADAARRQFEKAYELVCKIageversqawqTARELLRryrsqqalaQRLQQLRAQLAEL 524
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  630 QETSEQAQSKFKSEKQNRKQLELKVTSlEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEeldkLRQ 709
Cdd:COG3096   525 EQRLRQQQNAERLLEEFCQRIGQQLDA-AEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKE----LAA 599
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  710 LLKKTRVStdQAAAEQLslvqaelqtqweakCEHLlasakDEHLQQYQEVcaqrDAYQQKLVQLQEKCLALQAQITALTK 789
Cdd:COG3096   600 RAPAWLAA--QDALERL--------------REQS-----GEALADSQEV----TAAMQQLLEREREATVERDELAARKQ 654
                         410       420
                  ....*....|....*....|..
gi 578817221  790 QNEQHIKELeknkSQMSGVEAA 811
Cdd:COG3096   655 ALESQIERL----SQPGGAEDP 672
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
503-708 1.57e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 49.27  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  503 IQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQsnlmmEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATA 582
Cdd:PRK02224  470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-----EDRIERLEERREDLEELIAERRETIEEKRERAEELRE 544
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  583 QVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQ------AKLSELQETSEQAQSKFKSEKQNRKQLELKVTS 656
Cdd:PRK02224  545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKerieslERIRTLLAAIADAEDEIERLREKREALAELNDE 624
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578817221  657 LEEELTDLRVEKESLEKNLSERKKKSAQERSQ-AEEEIDEIrksyQEELDKLR 708
Cdd:PRK02224  625 RRERLAEKRERKRELEAEFDEARIEEAREDKErAEEYLEQV----EEKLDELR 673
DUF4618 pfam15397
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ...
620-819 1.82e-05

Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.


Pssm-ID: 464704 [Multi-domain]  Cd Length: 258  Bit Score: 47.64  E-value: 1.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   620 TKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKEsleknlSERKKKSAQeRSQAEEEIDEIRKS 699
Cdd:pfam15397   63 KQLQQAKAELQEWEEKEESKLNKLEQQLEQLNAKIQKTQEELNFLSTYKD------KEYPVKAVQ-IANLVRQLQQLKDS 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   700 YQEELDKLRQLLKKTRvstdqaaaeqlslvqAELQTQWEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLvqlqEKCLA 779
Cdd:pfam15397  136 QQDELDELEEMRRMVL---------------ESLSRKIQKKKEKILSSLAEKTLSPYQESLLQKTRDNQVM----LKEIE 196
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 578817221   780 lqaqitaltkQNEQHIKELEKN----KSQMSGVEAAASDPSEKV 819
Cdd:pfam15397  197 ----------QFREFIDELEEEipklKAEVQQLQAQRQEPREVI 230
mukB PRK04863
chromosome partition protein MukB;
507-805 2.37e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 48.80  E-value: 2.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  507 ERLKQEIleksNRIEEQNDKISELIERNQRYVEQSNLMMekrNNSLQTATEntqarvlhAEQEkakvtEELAAATAQVSH 586
Cdd:PRK04863  789 EQLRAER----EELAERYATLSFDVQKLQRLHQAFSRFI---GSHLAVAFE--------ADPE-----AELRQLNRRRVE 848
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  587 LQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKV--------QAKLSELQETSEQAQSKFKSEKQNRKQLELkvtsLE 658
Cdd:PRK04863  849 LERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLnlladetlADRVEEIREQLDEAEEAKRFVQQHGNALAQ----LE 924
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  659 EELTDLRVEKESLEK-----NLSERKKKSAQERSQAEEEIDEIRK--SYQEEL----------DKLRQLLK--------- 712
Cdd:PRK04863  925 PIVSVLQSDPEQFEQlkqdyQQAQQTQRDAKQQAFALTEVVQRRAhfSYEDAAemlaknsdlnEKLRQRLEqaeqertra 1004
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  713 KTRVSTDQAAAEQLSLVQAELQTQWEAKCEhLLASAKDEhLQQY---------QEVCAQRDAYQQKLVQLQEKCLALQAQ 783
Cdd:PRK04863 1005 REQLRQAQAQLAQYNQVLASLKSSYDAKRQ-MLQELKQE-LQDLgvpadsgaeERARARRDELHARLSANRSRRNQLEKQ 1082
                         330       340
                  ....*....|....*....|....*.
gi 578817221  784 IT----ALTKQNEQhIKELEKNKSQM 805
Cdd:PRK04863 1083 LTfceaEMDNLTKK-LRKLERDYHEM 1107
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
450-715 2.80e-05

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


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 48.51  E-value: 2.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   450 EIRMAVSKVADKMDHLMTKVEELQKHSAG--NSM--LIPSMSVTMETSMIMSNIQRIIQENERLKQEILEKSNRIEEQND 525
Cdd:TIGR01612 1115 KIKDDIKNLDQKIDHHIKALEEIKKKSENyiDEIkaQINDLEDVADKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKK 1194
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   526 KISELIErnqryVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAAtaqvshlqlkMTAHQKKETELQMQL 605
Cdd:TIGR01612 1195 LLNEIAE-----IEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKA----------MEAYIEDLDEIKEKS 1259
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   606 TESLKETdllrGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLE------LKVTSLEEELTDLRVEKESLEKNLSERK 679
Cdd:TIGR01612 1260 PEIENEM----GIEMDIKAEMETFNISHDDDKDHHIISKKHDENISdireksLKIIEDFSEESDINDIKKELQKNLLDAQ 1335
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817221   680 KKSAQ-------------------------ERSQAEEEIDEIRKSYQEELDKLRQLLKKTR 715
Cdd:TIGR01612 1336 KHNSDinlylneianiynilklnkikkiidEVKEYTKEIEENNKNIKDELDKSEKLIKKIK 1396
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
446-838 2.83e-05

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 48.50  E-value: 2.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   446 QHNTEIRMAVSKVADKMDHLMTKVEELQ-----KHSAGNSMLIPSMSVTMETSMIMSNIQRIIQENERLKQEILEKSNRI 520
Cdd:TIGR00606  688 QTEAELQEFISDLQSKLRLAPDKLKSTEselkkKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI 767
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   521 EEQ---------NDKISELIERNQRYVEQsnLMMEKRNNSLQTATENTQAR-------VLHAEQEKAKVTEELAAATAQV 584
Cdd:TIGR00606  768 EEQetllgtimpEEESAKVCLTDVTIMER--FQMELKDVERKIAQQAAKLQgsdldrtVQQVNQEKQEKQHELDTVVSKI 845
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   585 SHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQlelkVTSLEEELTDL 664
Cdd:TIGR00606  846 ELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQ----DSPLETFLEKD 921
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   665 RVEKESLEKNLSERKKKSAQERSQAEEEIDEI---RKSYQEELDKLRQLLKKTRVSTDQAAAEQLSlvqaELQTQWEAKC 741
Cdd:TIGR00606  922 QQEKEELISSKETSNKKAQDKVNDIKEKVKNIhgyMKDIENKIQDGKDDYLKQKETELNTVNAQLE----ECEKHQEKIN 997
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   742 EHLLASAKDEHLQQYQEvcaqrdayqqKLVQLQEKCLALQAQITALTKQNEQHIKELekNKSQMSGVEAAASDPSEKVKK 821
Cdd:TIGR00606  998 EDMRLMRQDIDTQKIQE----------RWLQDNLTLRKRENELKEVEEELKQHLKEM--GQMQVLQMKQEHQKLEENIDL 1065
                          410
                   ....*....|....*..
gi 578817221   822 IMNQVFQSLRREFELEE 838
Cdd:TIGR00606 1066 IKRNHVLALGRQKGYEK 1082
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
595-786 3.00e-05

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


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 48.15  E-value: 3.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   595 QKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQ---ETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESL 671
Cdd:pfam05622  303 RERLTELQQLLEDANRRKNELETQNRLANQRILELQqqvEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKK 382
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   672 EKNLSERKKKSAQERSQAEEEIDEIRKSYQEE-----------LDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQwEAK 740
Cdd:pfam05622  383 KEQIEELEPKQDSNLAQKIDELQEALRKKDEDmkameerykkyVEKAKSVIKTLDPKQNPASPPEIQALKNQLLEK-DKK 461
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817221   741 CEHLLASAKDEHLQQYQE------------VCAQRDAYQQKLVQLQ---EKCLALQAQITA 786
Cdd:pfam05622  462 IEHLERDFEKSKLQREQEeklivtawynmgMALHRKAIEERLAGLSspgQSFLARQRQATN 522
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
566-688 4.13e-05

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


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 44.55  E-value: 4.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   566 AEQEKAKVTEELAAATAQVSHLQLKM--------TAHQKKETELQMQlTESLKETDLLRGQLTKVQAKLSELQETSEQAQ 637
Cdd:pfam07926    6 LQSEIKRLKEEAADAEAQLQKLQEDLekqaeiarEAQQNYERELVLH-AEDIKALQALREELNELKAEIAELKAEAESAK 84
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 578817221   638 SKFKSEKQnrkqlelkvtSLEEEltdlrveKESLEKNLSERKKKSAQERSQ 688
Cdd:pfam07926   85 AELEESEE----------SWEEQ-------KKELEKELSELEKRIEDLNEQ 118
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
507-713 4.89e-05

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 45.82  E-value: 4.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   507 ERLKQEILEKSNRIEEQNDKISELIErnqryveqsnlmmekrnnslqtatENTQARVLHAEQEKAkvteelaaataqVSH 586
Cdd:pfam05010   11 EKARNEIEEKELEINELKAKYEELRR------------------------ENLEMRKIVAEFEKT------------IAQ 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   587 LqlkMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEeltdlRV 666
Cdd:pfam05010   55 M---IEEKQKQKELEHAEIQKVLEEKDQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLA-----RI 126
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 578817221   667 EKEslEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKK 713
Cdd:pfam05010  127 KKE--EQRYQALKAHAEEKLDQANEEIAQVRSKAKAETAALQASLRK 171
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
508-800 5.20e-05

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


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 46.73  E-value: 5.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   508 RLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAataqvshl 587
Cdd:pfam15905   55 KVKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVAS-------- 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   588 qlkmtahqkketeLQMQLTESLKETDLLRGQLT------KVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEEL 661
Cdd:pfam15905  127 -------------LEKQLLELTRVNELLKAKFSedgtqkKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNL 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   662 TDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRK--SYQEELDKLRQLLKKTRVSTDQAAAEQLSlvqaeLQTQWEA 739
Cdd:pfam15905  194 EHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITElsCVSEQVEKYKLDIAQLEELLKEKNDEIES-----LKQSLEE 268
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817221   740 KCEHLLASAKD--EHLQQYQEvcaqrdAYQQKLVQLQEKCLALQAQITALTK---QNEQHIKELEK 800
Cdd:pfam15905  269 KEQELSKQIKDlnEKCKLLES------EKEELLREYEEKEQTLNAELEELKEkltLEEQEHQKLQQ 328
PRK00106 PRK00106
ribonuclease Y;
563-732 7.14e-05

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 46.79  E-value: 7.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  563 VLHAEQEKAKVTEELAAATAQvshlQLKMTAHQKKETELQMQLTESLKETDLLRGQLTkVQAKlSELQETSEQAQSKFKS 642
Cdd:PRK00106   21 LISIKMKSAKEAAELTLLNAE----QEAVNLRGKAERDAEHIKKTAKRESKALKKELL-LEAK-EEARKYREEIEQEFKS 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  643 EKQNRKQLELKVT----SL---EEELTDLRVEKESLEKNLSErKKKSAQERsqaEEEIDEIRKSYQEELDKLRQLlkktr 715
Cdd:PRK00106   95 ERQELKQIESRLTeratSLdrkDENLSSKEKTLESKEQSLTD-KSKHIDER---EEQVEKLEEQKKAELERVAAL----- 165
                         170
                  ....*....|....*..
gi 578817221  716 vstDQAAAEQLSLVQAE 732
Cdd:PRK00106  166 ---SQAEAREIILAETE 179
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
495-691 7.16e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.36  E-value: 7.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  495 IMSNIQRIIQENERLKQEILEKSNRIEEQNDKISEL---IERNQRYVEQSNLMMEKRNNSLQT--ATENTQARVLHAeqe 569
Cdd:COG3883    35 AQAELDALQAELEELNEEYNELQAELEALQAEIDKLqaeIAEAEAEIEERREELGERARALYRsgGSVSYLDVLLGS--- 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  570 kakvtEELAAATAQVSHLQlKMTAHQKKETELQMQLTESLKET-DLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRK 648
Cdd:COG3883   112 -----ESFSDFLDRLSALS-KIADADADLLEELKADKAELEAKkAELEAKLAELEALKAELEAAKAELEAQQAEQEALLA 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 578817221  649 QLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEE 691
Cdd:COG3883   186 QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
501-812 7.50e-05

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 47.10  E-value: 7.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  501 RIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEkrnnsLQTATENtQARVLHAEQEKAKV------- 573
Cdd:PRK10246  434 QIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLAD-----VKTICEQ-EARIKDLEAQRAQLqagqpcp 507
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  574 ----TEELAAATAQVshlqLKMTAHQKKETELQMQLTESLKETDLLRGQLtkvQAKLSELQETSEQAQSKFKSEKQNRKQ 649
Cdd:PRK10246  508 lcgsTSHPAVEAYQA----LEPGVNQSRLDALEKEVKKLGEEGAALRGQL---DALTKQLQRDESEAQSLRQEEQALTQQ 580
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  650 LELKVTSL------EEELTDLRVEKESLEKNL---SERKKKSAQERSQAEEEIdeirkSYQEELDKLRQLLkktrvsTDQ 720
Cdd:PRK10246  581 WQAVCASLnitlqpQDDIQPWLDAQEEHERQLrllSQRHELQGQIAAHNQQII-----QYQQQIEQRQQQL------LTA 649
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  721 AAAEQLSLVQAELQTQWeakcehllASAKDEHLQQYQEVCAQRDAYQQKLVQLQ-------------------------- 774
Cdd:PRK10246  650 LAGYALTLPQEDEEASW--------LATRQQEAQSWQQRQNELTALQNRIQQLTplletlpqsddlphseetvaldnwrq 721
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 578817221  775 --EKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAA 812
Cdd:PRK10246  722 vhEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQAS 761
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
628-831 7.63e-05

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 47.25  E-value: 7.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  628 ELQETSEQ-AQSKFKSEKQNR--KQLELKVTSL---------EEELTDLRVEKESLEKNLSERKKKSAQERSQAEeeide 695
Cdd:COG3096   793 ERDELAEQyAKASFDVQKLQRlhQAFSQFVGGHlavafapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLD----- 867
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  696 irkSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWEAK------CEHLlaSAKDEHLQQYQEVCAQRDAYQQK 769
Cdd:COG3096   868 ---QLKEQLQLLNKLLPQANLLADETLADRLEELREELDAAQEAQafiqqhGKAL--AQLEPLVAVLQSDPEQFEQLQAD 942
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  770 LVQLQEKCLALQAQITALTK--QNEQHI------------KEL-EKNKSQMSGVEAAASDPSEKVKKI------MNQVFQ 828
Cdd:COG3096   943 YLQAKEQQRRLKQQIFALSEvvQRRPHFsyedavgllgenSDLnEKLRARLEQAEEARREAREQLRQAqaqysqYNQVLA 1022

                  ...
gi 578817221  829 SLR 831
Cdd:COG3096  1023 SLK 1025
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
635-821 1.01e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.98  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  635 QAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEK---NLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLL 711
Cdd:COG3883    13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEeynELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  712 K---KTRVSTD-----------QAAAEQLSLV-------QAELQTQWEAKCEhlLASAKDEHLQQYQEVCAQRDAYQQKL 770
Cdd:COG3883    93 RalyRSGGSVSyldvllgsesfSDFLDRLSALskiadadADLLEELKADKAE--LEAKKAELEAKLAELEALKAELEAAK 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578817221  771 VQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKK 821
Cdd:COG3883   171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
499-740 1.07e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  499 IQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRyveqsnlmMEKRNNSLQTATENTQARVLHAEQEKAKVTEELA 578
Cdd:COG4372    61 LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQ--------AQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  579 AATAQVSHLQLKMTAHQKKETELQMQLTEslketdlLRGQLTKVQAKLSELQEtsEQAQSKFKSEKQNRKQLELKVTSLE 658
Cdd:COG4372   133 QLEAQIAELQSEIAEREEELKELEEQLES-------LQEELAALEQELQALSE--AEAEQALDELLKEANRNAEKEEELA 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  659 EELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWE 738
Cdd:COG4372   204 EAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283

                  ..
gi 578817221  739 AK 740
Cdd:COG4372   284 EL 285
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
618-758 1.08e-04

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 46.10  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   618 QLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEE--LTDLRVEKESLEKNLSERKK----KSAQERSQAEE 691
Cdd:pfam15709  346 RRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEirLRKQRLEEERQRQEEEERKQrlqlQAAQERARQQQ 425
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   692 EidEIRKSYQEeldkLRQllKKTRVSTDQAAAEQLSlvQAELQTQWEAKCEHLLASAKD---EHLQQYQE 758
Cdd:pfam15709  426 E--EFRRKLQE----LQR--KKQQEEAERAEAEKQR--QKELEMQLAEEQKRLMEMAEEerlEYQRQKQE 485
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
497-709 1.23e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  497 SNIQRIiqenERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNL--------MMEKRNNSLQTATENTQAR------ 562
Cdd:COG4913   607 DNRAKL----AALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlaeysWDEIDVASAEREIAELEAElerlda 682
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  563 ----VLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESlkETDLLRGQLTKVQAKLSELQETSEQAQS 638
Cdd:COG4913   683 ssddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL--QDRLEAAEDLARLELRALLEERFAAALG 760
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817221  639 KfKSEKQNRKQLELKVTSLEEELTDLRvekESLEKNLSERKKKSAQERSQAEEEIDEIRkSYQEELDKLRQ 709
Cdd:COG4913   761 D-AVERELRENLEERIDALRARLNRAE---EELERAMRAFNREWPAETADLDADLESLP-EYLALLDRLEE 826
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
563-817 1.26e-04

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 46.29  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   563 VLHAEQEKAKVTE--ELAAATAQVSHLQLKmtahqKKETELQMQLTE-SLKETDLLRGQLTKVQAKLSELQEtsEQAQSK 639
Cdd:pfam09731  235 VEKAQSLAKLVDQykELVASERIVFQQELV-----SIFPDIIPVLKEdNLLSNDDLNSLIAHAHREIDQLSK--KLAELK 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   640 fkseKQNRKQLELKVTSLEEELTDLRVE-KESLEKNLSERKKksaQERSQAEEEIDEIRKSYQEELdklrqllkktrvst 718
Cdd:pfam09731  308 ----KREEKHIERALEKQKEELDKLAEElSARLEEVRAADEA---QLRLEFEREREEIRESYEEKL-------------- 366
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   719 dqaaaeqlslvQAELQTQWEAKCEHLlasaKDEHLQQYQEvcaqrdayqqklvqLQEKclALQAQITALTKQNEQHIKEL 798
Cdd:pfam09731  367 -----------RTELERQAEAHEEHL----KDVLVEQEIE--------------LQRE--FLQDIKEKVEEERAGRLLKL 415
                          250
                   ....*....|....*....
gi 578817221   799 EKNKSQMSGVEAAASDPSE 817
Cdd:pfam09731  416 NELLANLKGLEKATSSHSE 434
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
501-707 1.35e-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: 44.13  E-value: 1.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   501 RIIQENERLKQEILEKSNRIEEQN-DKI----SELIERNQRYVEQSNLMMEkrnnslqtatentqarvlhAEQEKAKVTE 575
Cdd:pfam13851    1 ELMKNHEKAFNEIKNYYNDITRNNlELIkslkEEIAELKKKEERNEKLMSE-------------------IQQENKRLTE 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   576 ELAAATAQVSHLQLKMTAHQK----------KETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQS--KFKSE 643
Cdd:pfam13851   62 PLQKAQEEVEELRKQLENYEKdkqslknlkaRLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQdvQQKTG 141
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578817221   644 KQNRkQLELKVTSLEEELtdlrvekESLEKNLSERKKKS---AQERSQAEEEIDEIRKSYQEELDKL 707
Cdd:pfam13851  142 LKNL-LLEKKLQALGETL-------EKKEAQLNEVLAAAnldPDALQAVTEKLEDVLESKNQLIKDL 200
Filament pfam00038
Intermediate filament protein;
514-709 1.43e-04

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 45.30  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   514 LEKSNRIEEQND----KISELIERNQRYVEQSNLMMEK-----RNNSLQTATENTQARV------LHAEQEKAKVTEELA 578
Cdd:pfam00038   17 IDKVRFLEQQNKlletKISELRQKKGAEPSRLYSLYEKeiedlRRQLDTLTVERARLQLeldnlrLAAEDFRQKYEDELN 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   579 -----------------AATAQVSHLQLKMTA-----------HQKKETELQMQLTES--LKETDLLRGQ-LTKV----- 622
Cdd:pfam00038   97 lrtsaendlvglrkdldEATLARVDLEAKIESlkeelaflkknHEEEVRELQAQVSDTqvNVEMDAARKLdLTSAlaeir 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   623 ------------------QAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQ 684
Cdd:pfam00038  177 aqyeeiaaknreeaeewyQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYEL 256
                          250       260
                   ....*....|....*....|....*
gi 578817221   685 ERSQAEEEIDEIrksyQEELDKLRQ 709
Cdd:pfam00038  257 QLADYQELISEL----EAELQETRQ 277
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
512-686 1.54e-04

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


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 45.82  E-value: 1.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   512 EILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATEN---TQARVLHAEQEKAKVTEELAAATaqvshlQ 588
Cdd:pfam05911  664 EIPSDGPLVSGSNDLKTEENKRLKEEFEQLKSEKENLEVELASCTENlesTKSQLQESEQLIAELRSELASLK------E 737
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   589 LKMTAhqkkETELQMQlTESLKETDLlrgQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTdlRVEK 668
Cdd:pfam05911  738 SNSLA----ETQLKCM-AESYEDLET---RLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLE--RNEK 807
                          170
                   ....*....|....*....
gi 578817221   669 ESLEKNL-SERKKKSAQER 686
Cdd:pfam05911  808 KESSNCDaDQEDKKLQQEK 826
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
529-707 1.58e-04

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


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 43.77  E-value: 1.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   529 ELIERNQRYVEQSNLMmEKRNNSLQTATEN-TQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTE 607
Cdd:pfam08614    4 ELIDAYNRLLDRTALL-EAENAKLQSEPESvLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVD 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   608 slketdllrgqltkVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEEL-------TDLRVEKESLekNLserkk 680
Cdd:pfam08614   83 --------------LNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELrekrklnQDLQDELVAL--QL----- 141
                          170       180
                   ....*....|....*....|....*..
gi 578817221   681 ksaqERSQAEEEIDEIRKSYQEELDKL 707
Cdd:pfam08614  142 ----QLNMAEEKLRKLEKENRELVERW 164
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
582-746 1.62e-04

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 46.19  E-value: 1.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   582 AQVSHLQLKMTAHQK-KETELQMQLTESLKETDL-LRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLE---LKVTS 656
Cdd:TIGR00606  187 ALETLRQVRQTQGQKvQEHQMELKYLKQYKEKACeIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEhnlSKIMK 266
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   657 LEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIR-------KSYQEELDKLRQLLKKTRVSTDQAAAEQLSLV 729
Cdd:TIGR00606  267 LDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYhnhqrtvREKERELVDCQRELEKLNKERRLLNQEKTELL 346
                          170
                   ....*....|....*....
gi 578817221   730 --QAELQTQWEAKCEHLLA 746
Cdd:TIGR00606  347 veQGRLQLQADRHQEHIRA 365
Macoilin pfam09726
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ...
582-789 1.77e-04

Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.


Pssm-ID: 462859 [Multi-domain]  Cd Length: 670  Bit Score: 45.61  E-value: 1.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   582 AQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKvtsLEEEl 661
Cdd:pfam09726  402 QDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKR---LKAE- 477
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   662 tdlRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQllkktrvstdqaAAEQLSLVQAELQTQWEAKC 741
Cdd:pfam09726  478 ---QEARASAEKQLAEEKKRKKEEEATAARAVALAAASRGECTESLKQ------------RKRELESEIKKLTHDIKLKE 542
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 578817221   742 EHLLA-SAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTK 789
Cdd:pfam09726  543 EQIRElEIKVQELRKYKESEKDTEVLMSALSAMQDKNQHLENSLSAETR 591
PTZ00121 PTZ00121
MAEBL; Provisional
443-936 1.79e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  443 EARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMLIPSMSVTMETSMIMSNIQRIIQENERLKQEILEK---SNR 519
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaeEKK 1391
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  520 IEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQ-LKMTAHQKKE 598
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEeAKKKAEEAKK 1471
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  599 TELQMQLTESLKETDLLRGQLTKVQAKLSELQETSE---------QAQSKFKSEK-----QNRKQLELKVTSLEEELTDL 664
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEakkkadeakKAEEAKKADEakkaeEAKKADEAKKAEEKKKADEL 1551
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  665 RVEKE---SLEKNLSERKKKSAQERSQAE---EEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWE 738
Cdd:PTZ00121 1552 KKAEElkkAEEKKKAEEAKKAEEDKNMALrkaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE 1631
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  739 AKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIK---ELEKNKSQMSGVEAAASDP 815
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKaaeALKKEAEEAKKAEELKKKE 1711
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  816 SEKVKKImnqvfQSLRREFEleesyngrtilgtiMNTIKMVTLQllnqqeqekeeSSSEEEEEKAEERPRRPSQEQSASA 895
Cdd:PTZ00121 1712 AEEKKKA-----EELKKAEE--------------ENKIKAEEAK-----------KEAEEDKKKAEEAKKDEEEKKKIAH 1761
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 578817221  896 SSGQPQAPLNRERPESPMVPSEQVVEEAVPLPPQALTTSQD 936
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD 1802
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
499-709 1.93e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.80  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  499 IQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQsnlMMEKRN--NSLQTATENTQARVLHAEQEKAKVTEE 576
Cdd:PRK02224  511 IERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE---AEEKREaaAEAEEEAEEAREEVAELNSKLAELKER 587
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  577 L-------------AAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTkvQAKLSELQETSEQAqskfkse 643
Cdd:PRK02224  588 IeslerirtllaaiADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFD--EARIEEAREDKERA------- 658
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578817221  644 KQNRKQLELKVTSLEEELTDLRVE----KESLE--KNLSERKKKSAQERSQAE---EEIDEIRKSYQEELDKLRQ 709
Cdd:PRK02224  659 EEYLEQVEEKLDELREERDDLQAEigavENELEelEELRERREALENRVEALEalyDEAEELESMYGDLRAELRQ 733
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
589-714 1.98e-04

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 44.72  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  589 LKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSekqnrkqLELKVTSLEEELTDLRVEK 668
Cdd:COG4026   121 LKSLQNIPEYNELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKK-------LREENSILEEEFDNIKSEY 193
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 578817221  669 ESLEKNLSERKKKSAQERSQAEEEIDEIrksYQEELDKLRQLLKKT 714
Cdd:COG4026   194 SDLKSRFEELLKKRLLEVFSLEELWKEL---FPEELPEEDFIYFAT 236
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
616-829 2.27e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  616 RGQLTKVQAKLSELQETSEQAQSKfksEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKksaqERSQAEEEIDE 695
Cdd:COG4372    12 RLSLFGLRPKTGILIAALSEQLRK---ALFELDKLQEELEQLREELEQAREELEQLEEELEQARS----ELEQLEEELEE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  696 IRKSYQEELDKLRQllkktrvstdqaAAEQLSLVQaelqtqweakcehllasakdehlQQYQEVCAQRDAYQQKLVQLQE 775
Cdd:COG4372    85 LNEQLQAAQAELAQ------------AQEELESLQ-----------------------EEAEELQEELEELQKERQDLEQ 129
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578817221  776 KCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQS 829
Cdd:COG4372   130 QRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
COG5022 COG5022
Myosin heavy chain [General function prediction only];
511-849 2.44e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 45.45  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  511 QEILEKSNRIEEQNDKISElIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVShlQLK 590
Cdd:COG5022   800 QPLLSLLGSRKEYRSYLAC-IIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQS--AQR 876
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  591 MTAHQKKETELQMQLTE--SLKETDLlrgQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEK 668
Cdd:COG5022   877 VELAERQLQELKIDVKSisSLKLVNL---ELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKL 953
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  669 ESLEKNLSERK--KKSAQERS----QAEEEIDEIRKSyQEELDKLRQLLKKTRV--STDQAAAEQLSLVQAELQTQWEAk 740
Cdd:COG5022   954 PELNKLHEVESklKETSEEYEdllkKSTILVREGNKA-NSELKNFKKELAELSKqyGALQESTKQLKELPVEVAELQSA- 1031
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  741 cEHLLASAKdEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITaLTKQNEQHIKELEKNKSQMSGVEAA--------A 812
Cdd:COG5022  1032 -SKIISSES-TELSILKPLQKLKGLLLLENNQLQARYKALKLRRE-NSLLDDKQLYQLESTENLLKTINVKdlevtnrnL 1108
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 578817221  813 SDPSEKVKKImnqVFQSLRREFELEESYNGRTILGTI 849
Cdd:COG5022  1109 VKPANVLQFI---VAQMIKLNLLQEISKFLSQLVNTL 1142
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
495-691 2.64e-04

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 45.33  E-value: 2.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  495 IMSNIQRIIQENERLKQEILEKSNRIEEQNDKI---SELIERNQRYVEQSNLMMEKRNNSLqtaTENTQARVLHAEQEKA 571
Cdd:COG3096   925 LVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIfalSEVVQRRPHFSYEDAVGLLGENSDL---NEKLRARLEQAEEARR 1001
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  572 KVTEELAAATAQVSH----LQLKMTAHQKKETELQmQLTESLKETDllrgqltkVQAKlselQETSEQAQSKfKSEKQNR 647
Cdd:COG3096  1002 EAREQLRQAQAQYSQynqvLASLKSSRDAKQQTLQ-ELEQELEELG--------VQAD----AEAEERARIR-RDELHEE 1067
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 578817221  648 -KQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEE 691
Cdd:COG3096  1068 lSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
567-826 2.78e-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: 45.01  E-value: 2.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   567 EQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQN 646
Cdd:TIGR04523   39 EKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQ 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   647 RKQLELKVTSLEEELTDlrvEKESLEKNLSERKKKSaQERSQAEEEIDEIRK---SYQEELDKL-RQLLKKTRVSTD--- 719
Cdd:TIGR04523  119 KNKLEVELNKLEKQKKE---NKKNIDKFLTEIKKKE-KELEKLNNKYNDLKKqkeELENELNLLeKEKLNIQKNIDKikn 194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   720 QAAAEQLSLVQAELQTQweakcEHLLASAKDEHL-QQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKEL 798
Cdd:TIGR04523  195 KLLKLELLLSNLKKKIQ-----KNKSLESQISELkKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL 269
                          250       260
                   ....*....|....*....|....*...
gi 578817221   799 EKNKSQMSGVEAAASDPSEKVKKIMNQV 826
Cdd:TIGR04523  270 SEKQKELEQNNKKIKELEKQLNQLKSEI 297
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
520-736 2.80e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.82  E-value: 2.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  520 IEEQNDKISELIERNQRYVEQSNLMMEKRNnSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQ--LKMTAHQKK 597
Cdd:COG3883    18 IQAKQKELSELQAELEAAQAELDALQAELE-ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERReeLGERARALY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  598 ETELQMQLTESLKE----TDLLRG-----QLTKVQAKL----SELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDL 664
Cdd:COG3883    97 RSGGSVSYLDVLLGsesfSDFLDRlsalsKIADADADLleelKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578817221  665 RVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQ 736
Cdd:COG3883   177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
638-825 2.80e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 44.13  E-value: 2.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  638 SKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKsYQEELDKLRQLLKKTRVS 717
Cdd:COG1340     1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQE-LREKRDELNEKVKELKEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  718 TDQaAAEQLSLVQAELQtqwEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLV-------QLQEKCLALQAQITALTKQ 790
Cdd:COG1340    80 RDE-LNEKLNELREELD---ELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVlspeeekELVEKIKELEKELEKAKKA 155
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 578817221  791 NEQHiKELEKNKSQMSGVEAAASDPSEKVKKIMNQ 825
Cdd:COG1340   156 LEKN-EKLKELRAELKELRKEAEEIHKKIKELAEE 189
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
645-822 2.84e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.20  E-value: 2.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  645 QNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDK-LRQLLKKTRVSTDQAAA 723
Cdd:PRK00409  527 ELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEiIKELRQLQKGGYASVKA 606
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  724 EQLSLVQAELQTQWEAKCEHLLASAKDEH-LQQYQEVcaqrdayqqKLVQLQEKclalqAQITALTKQNE---Q------ 793
Cdd:PRK00409  607 HELIEARKRLNKANEKKEKKKKKQKEKQEeLKVGDEV---------KYLSLGQK-----GEVLSIPDDKEaivQagimkm 672
                         170       180       190
                  ....*....|....*....|....*....|.
gi 578817221  794 --HIKELEKNKSQmsgveaaasdPSEKVKKI 822
Cdd:PRK00409  673 kvPLSDLEKIQKP----------KKKKKKKP 693
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
607-715 3.04e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.85  E-value: 3.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  607 ESLKEtdLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNR-KQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQE 685
Cdd:COG2433   376 LSIEE--ALEELIEKELPEEEPEAEREKEHEERELTEEEEEiRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEA 453
                          90       100       110
                  ....*....|....*....|....*....|..
gi 578817221  686 RSQAEEEIDEIRK--SYQEELDKLRQLLKKTR 715
Cdd:COG2433   454 RSEERREIRKDREisRLDREIERLERELEEER 485
Rabaptin pfam03528
Rabaptin;
595-802 3.04e-04

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 44.71  E-value: 3.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   595 QKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEqaqskfksEKQNRKQLELKVTslEEELTDLRVEKESLEKN 674
Cdd:pfam03528    7 QQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKE--------EDLKRQNAVLQEA--QVELDALQNQLALARAE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   675 LSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWE------AKCEHLLASA 748
Cdd:pfam03528   77 MENIKAVATVSENTKQEAIDEVKSQWQEEVASLQAIMKETVREYEVQFHRRLEQERAQWNQYREsaereiADLRRRLSEG 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 578817221   749 KDEHLQQYQEVCAQRDAYQQKLV--QLQEKCLALQAQITaltkQNEQHIKELEKNK 802
Cdd:pfam03528  157 QEEENLEDEMKKAQEDAEKLRSVvmPMEKEIAALKAKLT----EAEDKIKELEASK 208
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
501-794 3.37e-04

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 44.73  E-value: 3.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   501 RIIQ-ENERLKQEILEKSNRIEEQNdKISELIERNQRYVEqsnlmmekRNNSLQTATENTQARvLHAEQEKAKVTEELAA 579
Cdd:pfam05557   10 RLSQlQNEKKQMELEHKRARIELEK-KASALKRQLDRESD--------RNQELQKRIRLLEKR-EAEAEEALREQAELNR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   580 ATAQ----VSHLQLKMTAHQKKETELQMQLTESLKE--TDLLRGQLtKVQAKLSELQETSEQ---AQSKFKSEKQNRKQL 650
Cdd:pfam05557   80 LKKKyleaLNKKLNEKESQLADAREVISCLKNELSElrRQIQRAEL-ELQSTNSELEELQERldlLKAKASEAEQLRQNL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   651 ELKVTSL---EEELTDLRVEKESLEKNLSERKKKSAQ---------ERSQAEEEIDEIRKS------YQEELDKLRQLLK 712
Cdd:pfam05557  159 EKQQSSLaeaEQRIKELEFEIQSQEQDSEIVKNSKSElaripelekELERLREHNKHLNENienkllLKEEVEDLKRKLE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   713 KTRVSTDQAAAEQLSL--VQAELQtQWE----AKCEHL----LASAKDEHLQQYQEVCAQRD--------AYQQKLVQLQ 774
Cdd:pfam05557  239 REEKYREEAATLELEKekLEQELQ-SWVklaqDTGLNLrspeDLSRRIEQLQQREIVLKEENssltssarQLEKARRELE 317
                          330       340
                   ....*....|....*....|
gi 578817221   775 EKCLALQAQITALTKQNEQH 794
Cdd:pfam05557  318 QELAQYLKKIEDLNKKLKRH 337
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
239-427 3.41e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 44.76  E-value: 3.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   239 SAAPSPIPGADNLSADPVVSPPTSIPFKSGEPALRTKSnslseqlAINTSPDAVKAKLISRMAKMgQPMLPILPPQldsn 318
Cdd:pfam03154  192 TQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHT-------LIQQTPTLHPQRLPSPHPPL-QPMTQPPPPS---- 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   319 dseiedvntlqgggQPVVTPSVQPSLHPAHPALPQMTSQAPqpsvTGLQAPSAAL-MQVSSLDSHSAVSGNAQSFQPYAG 397
Cdd:pfam03154  260 --------------QVSPQPLPQPSLHGQMPPMPHSLQTGP----SHMQHPVPPQpFPLTPQSSQSQVPPGPSPAAPGQS 321
                          170       180       190
                   ....*....|....*....|....*....|..
gi 578817221   398 MQAYAYPQASAVTSQLQPVR--PLYPAPLSQP 427
Cdd:pfam03154  322 QQRIHTPPSQSQLQSQQPPReqPLPPAPLSMP 353
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
572-790 3.50e-04

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 43.56  E-value: 3.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   572 KVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKS--------- 642
Cdd:pfam06008   16 KINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKElaeaiknli 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   643 ----------EKQNRKQLELKVTSLEEELTDL-RVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLL 711
Cdd:pfam06008   96 dnikeinekvATLGENDFALPSSDLSRMLAEAqRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALA 175
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578817221   712 KKTRvstdqaaaEQLSLVQAELQTQWEAKCEHLLASAKDEHLQqyQEVCAQRDAYQQKLVQLQEkclaLQAQITALTKQ 790
Cdd:pfam06008  176 NALR--------DSLAEYEAKLSDLRELLREAAAKTRDANRLN--LANQANLREFQRKKEEVSE----QKNQLEETLKT 240
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
495-726 3.51e-04

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


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 44.46  E-value: 3.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   495 IMSNIQRI---IQEN----ERLKQEILEKSNR-IEEQNDKISELIER----------NQRYVEQSNLMMEKRNNSLQTAT 556
Cdd:pfam06160  235 VDKEIQQLeeqLEENlallENLELDEAEEALEeIEERIDQLYDLLEKevdakkyvekNLPEIEDYLEHAEEQNKELKEEL 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   557 ENTQARVLHAEQEKAKV---TEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKetdllrgQLTKVQAKLSELQets 633
Cdd:pfam06160  315 ERVQQSYTLNENELERVrglEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILE-------QLEEIEEEQEEFK--- 384
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   634 EQAQSKFKSEKQNRKQLELKVTSLEEelTDLRVEKE---SLEKNLSERKKKSAQERSQAEEE-------IDEIRKSYQEE 703
Cdd:pfam06160  385 ESLQSLRKDELEAREKLDEFKLELRE--IKRLVEKSnlpGLPESYLDYFFDVSDEIEDLADElnevplnMDEVNRLLDEA 462
                          250       260
                   ....*....|....*....|....
gi 578817221   704 LDKLRQLLKKTRVSTDQAA-AEQL 726
Cdd:pfam06160  463 QDDVDTLYEKTEELIDNATlAEQL 486
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
495-704 3.96e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 3.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  495 IMSNIQRIIQENERLKQEILEKS-NRIEEQNDKISELIERNQRYVEQSNlmMEKRNNSLQTATENTQARVLHAEQEKAKV 573
Cdd:PRK03918  561 LEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKD--AEKELEREEKELKKLEEELDKAFEELAET 638
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  574 TEELAAATAQVSHLQLKMTahQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEqaqsKFKSEKQNRKQLELK 653
Cdd:PRK03918  639 EKRLEELRKELEELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLE----KLKEELEEREKAKKE 712
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578817221  654 VTSLEEELTDLRVEKESLeknlserKKKSAQERSQAEEEIDEIRKSYQEEL 704
Cdd:PRK03918  713 LEKLEKALERVEELREKV-------KKYKALLKERALSKVGEIASEIFEEL 756
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
503-803 4.13e-04

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 44.65  E-value: 4.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   503 IQENE-RLKQEILEKSNRIEEQNDKISELIERNQryvEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAAT 581
Cdd:TIGR00606  370 IQSLAtRLELDGFERGPFSERQIKNFHTLVIERQ---EDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKK 446
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   582 AQVSHLQLKMtahQKKETELQmQLTESLKETDLLRGQLTKVQAKLSELQETS--EQAQSKFKSEKQNRKQLELKVTSLEE 659
Cdd:TIGR00606  447 EILEKKQEEL---KFVIKELQ-QLEGSSDRILELDQELRKAERELSKAEKNSltETLKKEVKSLQNEKADLDRKLRKLDQ 522
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   660 ELTDLRVEKESLEKNLSERKKKsaqerSQAEEEIDEIRKSYQEEL--------------DKLRQLLKKTRVSTDQAAAEQ 725
Cdd:TIGR00606  523 EMEQLNHHTTTRTQMEMLTKDK-----MDKDEQIRKIKSRHSDELtsllgyfpnkkqleDWLHSKSKEINQTRDRLAKLN 597
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   726 LSLVQAE-LQTQWEAKCEhllasAKDEHLQQYQ----EVCAQRDaYQQKLVQLQ---EKCLALQAQITALTKQNEQHIKE 797
Cdd:TIGR00606  598 KELASLEqNKNHINNELE-----SKEEQLSSYEdklfDVCGSQD-EESDLERLKeeiEKSSKQRAMLAGATAVYSQFITQ 671

                   ....*.
gi 578817221   798 LEKNKS 803
Cdd:TIGR00606  672 LTDENQ 677
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
602-835 4.21e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 44.44  E-value: 4.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  602 QMQLT-ESLKETDLLRGQLTKVQA-KLSELQETSEQA-----QSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKn 674
Cdd:PRK04778   55 KLNLTgQSEEKFEEWRQKWDEIVTnSLPDIEEQLFEAeelndKFRFRKAKHEINEIESLLDLIEEDIEQILEELQELLE- 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  675 lSErkKKSAQERSQAEEEIDEIRK-------SYQEELDKLRQLLKKTRVSTDQ-----------AAAEQLSLVQAELqTQ 736
Cdd:PRK04778  134 -SE--EKNREEVEQLKDLYRELRKsllanrfSFGPALDELEKQLENLEEEFSQfveltesgdyvEAREILDQLEEEL-AA 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  737 WEAKCEH---LLASAKDEHLQQYQEVcaqRDAYQQKLVQ---LQEkcLALQAQITALTKQ---NEQHIKELEknksqmsg 807
Cdd:PRK04778  210 LEQIMEEipeLLKELQTELPDQLQEL---KAGYRELVEEgyhLDH--LDIEKEIQDLKEQideNLALLEELD-------- 276
                         250       260       270
                  ....*....|....*....|....*....|.
gi 578817221  808 VEAAasdpSEKVKKI---MNQVFQSLRREFE 835
Cdd:PRK04778  277 LDEA----EEKNEEIqerIDQLYDILEREVK 303
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
595-716 5.18e-04

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 44.30  E-value: 5.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  595 QKKETELQMQLTESLKETDLLRGQ-LTKVQAKLSELQETSEQAQSKFKSEKQnrkqLELKVTSLEEELTDLRVEKESLEK 673
Cdd:COG0542   417 ERRLEQLEIEKEALKKEQDEASFErLAELRDELAELEEELEALKARWEAEKE----LIEEIQELKEELEQRYGKIPELEK 492
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  674 NLSERKKKSAQERSQAEEEIDE--------------IRKSYQEELDKLRQL---LKKtRV 716
Cdd:COG0542   493 ELAELEEELAELAPLLREEVTEediaevvsrwtgipVGKLLEGEREKLLNLeeeLHE-RV 551
PHA03247 PHA03247
large tegument protein UL36; Provisional
900-1136 6.12e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 6.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  900 PQAPLNRERPESPMVPSEQVVEeavPLPPQALTTSQDghrrkgdseAEALSEIKDGSLPPELscipshrvlgPPTSIPPE 979
Cdd:PHA03247 2506 PDAPPAPSRLAPAILPDEPVGE---PVHPRMLTWIRG---------LEELASDDAGDPPPPL----------PPAAPPAA 2563
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  980 PlgpvsmdsecEESLAASPMAAKPDNPSgkVCVREVAPDGPLQESSTRLSLT---SDPEEGDPLALGPESPGEPQPPQLK 1056
Cdd:PHA03247 2564 P----------DRSVPPPRPAPRPSEPA--VTSRARRPDAPPQSARPRAPVDdrgDPRGPAPPSPLPPDTHAPDPPPPSP 2631
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 1057 KDDVTSSTGPHKELSSTEAGSTVAGAALRPSHHSQRSSLS-GDEEDELFKGATLKALRPKAQPeeededeVSMKGRPPPT 1135
Cdd:PHA03247 2632 SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGrAAQASSPPQRPRRRAARPTVGS-------LTSLADPPPP 2704

                  .
gi 578817221 1136 P 1136
Cdd:PHA03247 2705 P 2705
46 PHA02562
endonuclease subunit; Provisional
434-678 6.39e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.85  E-value: 6.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  434 GDMASFLMTEARQHNTEIRMavskVADKMDHLMTKV-------EELQKHSAGNsmlipsmsVTMETSMIMSN---IQRII 503
Cdd:PHA02562  166 SEMDKLNKDKIRELNQQIQT----LDMKIDHIQQQIktynkniEEQRKKNGEN--------IARKQNKYDELveeAKTIK 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  504 QENERLKQEILEKSNRIEEQNDKISELierNQRYVEQSNLM--------MEKRNNSLQTATENtqarvLHAEQEK-AKVT 574
Cdd:PHA02562  234 AEIEELTDELLNLVMDIEDPSAALNKL---NTAAAKIKSKIeqfqkvikMYEKGGVCPTCTQQ-----ISEGPDRiTKIK 305
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  575 EELAAATAQVSHLQLKMTAHQKKE---TELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQnrkqle 651
Cdd:PHA02562  306 DKLKELQHSLEKLDTAIDELEEIMdefNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAE------ 379
                         250       260
                  ....*....|....*....|....*..
gi 578817221  652 lKVTSLEEELTDLRVEKESLEKNLSER 678
Cdd:PHA02562  380 -ELAKLQDELDKIVKTKSELVKEKYHR 405
46 PHA02562
endonuclease subunit; Provisional
497-718 6.50e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.85  E-value: 6.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  497 SNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQsnLMMEKRNNSLQTATENTQARVLHAEQEK-----A 571
Cdd:PHA02562  181 QQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDE--LVEEAKTIKAEIEELTDELLNLVMDIEDpsaalN 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  572 KVTEELAAATAQVSHLQLKMTAHQK----------------KETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQ 635
Cdd:PHA02562  259 KLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqqisegpdRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKK 338
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  636 A---QSKFKSEKQNRKQLELKVTSLE---EELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDeirksyqeELDKLRQ 709
Cdd:PHA02562  339 LlelKNKISTNKQSLITLVDKAKKVKaaiEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKY--------HRGIVTD 410

                  ....*....
gi 578817221  710 LLKKTRVST 718
Cdd:PHA02562  411 LLKDSGIKA 419
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
884-1053 6.56e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 43.91  E-value: 6.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  884 PRRPSQeqsasassgqPQAPLNRERPESPMVP--SEQVVEEAVPLPPQALTTSQDGHRRKGDSEAE-----ALSEIKDGS 956
Cdd:PTZ00449  633 PKRPPP----------PQRPSSPERPEGPKIIksPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKEtkttvVLDESFESI 702
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  957 LPPELSCIPSHRVLGPPTSIPPEPLGPVSMDSECEESLAASPMAAKPDNP--SGKVCVREVAPDGPLQESSTRL----SL 1030
Cdd:PTZ00449  703 LKETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPpeEERTFFHETPADTPLPDILAEEfkeeDI 782
                         170       180
                  ....*....|....*....|....*
gi 578817221 1031 TSDPEEGDPLALGPESPGE--PQPP 1053
Cdd:PTZ00449  783 HAETGEPDEAMKRPDSPSEheDKPP 807
NST1 pfam13945
Salt tolerance down-regulator; NST1 is a family of proteins that seem to be involved, directly ...
534-704 7.44e-04

Salt tolerance down-regulator; NST1 is a family of proteins that seem to be involved, directly or indirectly, in the salt sensitivity of some cellular functions in yeast. It does this without affecting sodium accumulation. It negatively affects salt-tolerance through an interaction with the splicing factor Msl1p. This interaction stresses the importance of efficient RNA processing under salt stress conditions.


Pssm-ID: 372833  Cd Length: 186  Bit Score: 41.80  E-value: 7.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   534 NQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQkkeTELQMQLTESLKETD 613
Cdd:pfam13945    6 NNNSQNQQQNQHDNNTVDHHSQVNSSKRKSKKKKKKKNRNGSNNNNDESSTSQSTPSPFAIT---TSSTRPVSNNPPLSS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   614 LLRGQLTKVQAKLSELQETSEQaqskfkSEKQNRKQLELKVTslEEELTDL-RVEKESLEKNLSERKKKS------AQER 686
Cdd:pfam13945   83 SAASRSAHKNNKDRSIWNTSTQ------EERENIKEFWLSLG--EEERRSLvKVEKEAVLKKMKEQQKHScsctvcGRKR 154
                          170
                   ....*....|....*...
gi 578817221   687 SQAEEEIDEIRKSYQEEL 704
Cdd:pfam13945  155 TAIEEELEVLYDAYYEEL 172
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
504-735 8.07e-04

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 44.05  E-value: 8.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  504 QENERLKQEILEKSNRIEEQNDKISELIERN----QRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAA 579
Cdd:PTZ00440  560 KLKRSMKNDIKNKIKYIEENVDHIKDIISLNdeidNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKFYKGDLQE 639
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  580 ATAQVSHLQLKMTA--HQKKETE-LQMQLTESLKETDLLR-----------GQLTKVQAKLSELQET--SEQAQSKFKSE 643
Cdd:PTZ00440  640 LLDELSHFLDDHKYlyHEAKSKEdLQTLLNTSKNEYEKLEfmksdnidniiKNLKKELQNLLSLKENiiKKQLNNIEQDI 719
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  644 KQNRKQLELKVTSLEEELTDLRVEKESLE---KNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQ 720
Cdd:PTZ00440  720 SNSLNQYTIKYNDLKSSIEEYKEEEEKLEvykHQIINRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTILNKENKISND 799
                         250
                  ....*....|....*..
gi 578817221  721 AAA--EQLSLVQAELQT 735
Cdd:PTZ00440  800 INIlkENKKNNQDLLNS 816
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
956-1136 8.61e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 8.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  956 SLPPELSCIPSHRVLGPPTSIPPEPLGPVSMDSECEESLAASPMAAKPDNPSGKVCVREVAPDGPLQESSTRLSLTSDPE 1035
Cdd:PHA03307   92 LSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQ 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221 1036 EGDPLALGPES---PGEPQPPQLKKDDVTSSTGPHKELSSTEAGSTVAGAALRPShhSQRSSLSGDEEDELfkgatlkal 1112
Cdd:PHA03307  172 AALPLSSPEETaraPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGR--SAADDAGASSSDSS--------- 240
                         170       180
                  ....*....|....*....|....
gi 578817221 1113 rpKAQPEEEDEDEVSMKGRPPPTP 1136
Cdd:PHA03307  241 --SSESSGCGWGPENECPLPRPAP 262
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
434-797 9.21e-04

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 43.64  E-value: 9.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  434 GDMASFLMTEARQH--------NTEIRMAVS-KVADKMDHLMTKVEELQKHSAGNSMLIPSMSVTMETSMimsniQRIIQ 504
Cdd:PRK10246  156 GQFAAFLNAKPKERaelleeltGTEIYGQISaMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASL-----QVLTD 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  505 ENERL--KQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLH------AEQEKA----- 571
Cdd:PRK10246  231 EEKQLltAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPARQLRphweriQEQSAAlahtr 310
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  572 ----KVTEELAAATAQVSHL-QLKMTAHQKKETELQmQLTESLKETDLLR-------------GQLTKVQAKLSELQETS 633
Cdd:PRK10246  311 qqieEVNTRLQSTMALRARIrHHAAKQSAELQAQQQ-SLNTWLAEHDRFRqwnnelagwraqfSQQTSDREQLRQWQQQL 389
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  634 EQAQSKFKS-----------------EKQNRKQ-LELKVTSLEEELTDLRVEKESLEKNLSerkkKSAQERSQAEEEIDE 695
Cdd:PRK10246  390 THAEQKLNAlpaitltltadevaaalAQHAEQRpLRQRLVALHGQIVPQQKRLAQLQVAIQ----NVTQEQTQRNAALNE 465
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  696 IRKSYQEeldKLRQLLKKTRVSTDQAAAEQLSLVQAELQTqweAKCEHLLASAKDEHLQQYQEVC-----AQRDAYQQKL 770
Cdd:PRK10246  466 MRQRYKE---KTQQLADVKTICEQEARIKDLEAQRAQLQA---GQPCPLCGSTSHPAVEAYQALEpgvnqSRLDALEKEV 539
                         410       420
                  ....*....|....*....|....*..
gi 578817221  771 VQLQEKCLALQAQITALTKQNEQHIKE 797
Cdd:PRK10246  540 KKLGEEGAALRGQLDALTKQLQRDESE 566
AmmeMemoSam_B TIGR04336
AmmeMemoRadiSam system protein B; Members of this protein family belong to the same domain ...
946-1004 9.34e-04

AmmeMemoRadiSam system protein B; Members of this protein family belong to the same domain family as the mammalian protein Memo (Mediator of ErbB2-driven cell MOtility). Members of the present family occur as part of a three gene system with an uncharacterized radical SAM enzyme and a homolog of the mammalian protein AMMECR1, a mammalian protein named for AMME - Alport syndrome, Mental Retardation, Midface hypoplasia, and Elliptocytosis. Memo in humans has protein-protein interaction activity with binding of phosphorylated Try, but members of this family may be active as enzymes, as suggested by homology to a class of nonheme iron dioxygenases.


Pssm-ID: 275135 [Multi-domain]  Cd Length: 269  Bit Score: 42.56  E-value: 9.34e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817221   946 AEALSEIKDGslPPELSCI--PSHRVLGPPTSIPPE-----PLGPVSMDSECEESLAASPMAAKPD 1004
Cdd:TIGR04336   55 AHAYAALKKG--RPETVVLlgPNHTGYGSGIALPPEgswetPLGDVPVDEELAEELLEHSPIIELD 118
EzrA COG4477
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ...
443-806 9.42e-04

Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443574 [Multi-domain]  Cd Length: 567  Bit Score: 43.29  E-value: 9.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  443 EARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMlipsmsvtmetsmimsNIQRIIQENERLKQEILEKSN---- 518
Cdd:COG4477   101 KAKKALDEIEQLLDEIEEEIEEILEELEELLESEEKNRE----------------EIEELKEKYRELRKTLLAHRHsfgp 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  519 ---RIEEQNDKISELIERNQRYVEQSNlMMEKRN--NSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTA 593
Cdd:COG4477   165 aaeELEKQLEELEPEFEEFEELTESGD-YLEAREilEQLEEELNALEELMEEIPPLLKELQTELPDQLEELKSGYREMKE 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  594 ------HQKKETELQmQLTESLKET--DLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLR 665
Cdd:COG4477   244 qgyvleHLNIEKEIE-QLEEQLKEAleLLEELDLDEAEEELEEIEEEIDELYDLLEKEVEAKKYVDKNQEELEEYLEHLK 322
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  666 VEKESLEknlserkkksaqersqaeEEIDEIRKSYQ---EELDKLRQLLKktrvstdqaaaeQLSLVQAELQTqweakce 742
Cdd:COG4477   323 EQNRELK------------------EEIDRVQQSYRlneNELEKVRNLEK------------QIEELEKRYDE------- 365
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578817221  743 hlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKqNEQHIKE-LEKNKSQMS 806
Cdd:COG4477   366 --IDERIEEEKVAYSELQEELEEIEEQLEEIEEEQEEFSEKLKSLRK-DELEAREkLDELKKKLR 427
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
441-713 9.61e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.42  E-value: 9.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   441 MTEARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNS----MLIPSMSVTMETSMIMSNIQRIIQENERLKQEI-LE 515
Cdd:TIGR00618  565 MQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSeaedMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELaLK 644
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   516 KSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARV-------------LHAEQEKAK-----VTEEL 577
Cdd:TIGR00618  645 LTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLtywkemlaqcqtlLRELETHIEeydreFNEIE 724
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   578 AAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLrgQLTKVQAKLSELQETSEQAQSKFKSEKQNRkQLELKVTSL 657
Cdd:TIGR00618  725 NASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEA--HFNNNEEVTAALQTGAELSHLAAEIQFFNR-LREEDTHLL 801
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817221   658 EEELTDLRVEKESLEKNLSERKKKSAQERSQAEE----------EIDEIRKSYQEELDKLRQLLKK 713
Cdd:TIGR00618  802 KTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSrleeksatlgEITHQLLKYEECSKQLAQLTQE 867
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
460-703 9.88e-04

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 43.67  E-value: 9.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  460 DKMDHLMTKVEELQKHSagNSMLIPSMSVTMETSMIMSNIQRIIQENERL------KQEILEKSNRIEEQNDKISELIER 533
Cdd:PTZ00440 2342 QDENYGKDKNIELNNEN--NSYIIKTKEKINNLKEEFSKLLKNIKRNNTLcnnnniKDFISNIGKSVETIKQRFSSNLPE 2419
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  534 NQRYV-------EQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLqlkmTAHQKKETELQMQLT 606
Cdd:PTZ00440 2420 KEKLHqieenlnEIKNIMNETKRISNVDAFTNKILQDIDNEKNKENNNMNAEKIDDLIENV----TSHNEKIKSELLIIN 2495
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  607 ESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQN-RKQLELKVTSLEE-------ELTDL-------------- 664
Cdd:PTZ00440 2496 DALRRVKEKKDEMNKLFNSLTENNNNNNNSAKNIVDNSTYiINELESHVSKLNEllsyidnEIKELeneklkllekakie 2575
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 578817221  665 --RVEKESLEKNLSERKKKSAQERSQAEEEI--DEIRKSYQEE 703
Cdd:PTZ00440 2576 esRKERERIESETQEDNTDEEQINRQQQERLqkEEEQKAYSQE 2618
PRK09039 PRK09039
peptidoglycan -binding protein;
509-647 1.21e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 42.65  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  509 LKQEILEKSNRIEEQNDKISELIERnqryveqsnLMMEKRNN-SLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHL 587
Cdd:PRK09039   44 LSREISGKDSALDRLNSQIAELADL---------LSLERQGNqDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAA 114
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  588 QLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKsEKQNR 647
Cdd:PRK09039  115 EGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDR-ESQAK 173
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
499-772 1.32e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.21  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   499 IQRIIQENERLKQEILEKSNRIEEQNDKISELIERN--QRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKvtEE 576
Cdd:pfam13868   78 LEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEdqAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREE--DE 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   577 LAAATAQVSHLQLKMTAHQKKETELQMQlteslKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTS 656
Cdd:pfam13868  156 RILEYLKEKAEREEEREAEREEIEEEKE-----REIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKK 230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   657 LEEELtDLRvekESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQ 736
Cdd:pfam13868  231 ARQRQ-ELQ---QAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQR 306
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 578817221   737 WEAKcehllasakdEHLQQYQEVCAQRDAYQQKLVQ 772
Cdd:pfam13868  307 AAER----------EEELEEGERLREEEAERRERIE 332
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
587-739 1.36e-03

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


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 42.36  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  587 LQLKMTAHQKKETELQMQLTESLKE-TDLLRGQLTKVQAKLSELQEtseqAQSKFKSE-KQNRKQLELKVTSLEEELTD- 663
Cdd:cd22656    97 LELIDDLADATDDEELEEAKKTIKAlLDDLLKEAKKYQDKAAKVVD----KLTDFENQtEKDQTALETLEKALKDLLTDe 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  664 -LRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRqllKKTRVSTD-QAAAEQLSLVQA---------- 731
Cdd:cd22656   173 gGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLA---AALRLIADlTAADTDLDNLLAligpaipale 249

                  ....*...
gi 578817221  732 ELQTQWEA 739
Cdd:cd22656   250 KLQGAWQA 257
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
495-726 1.37e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 42.90  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  495 IMSNIQRIIQENERLKQEI-------LEKSNR-IEEQNDKISELIERN---QRYVEQSN-------LMMEKRNNSLQTAT 556
Cdd:PRK04778  254 IEKEIQDLKEQIDENLALLeeldldeAEEKNEeIQERIDQLYDILEREvkaRKYVEKNSdtlpdflEHAKEQNKELKEEI 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  557 ENTQA--RVLHAEQEKAK-VTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKetdllrgQLTKVQAKLSELQETs 633
Cdd:PRK04778  334 DRVKQsyTLNESELESVRqLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILK-------QLEEIEKEQEKLSEM- 405
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  634 eqAQSKFKSEKQNRKQLELKVTSLEEelTDLRVEKE---SLEKNLSERKKKSAQERSQAEEEIDEIR---KSYQEELDK- 706
Cdd:PRK04778  406 --LQGLRKDELEAREKLERYRNKLHE--IKRYLEKSnlpGLPEDYLEMFFEVSDEIEALAEELEEKPinmEAVNRLLEEa 481
                         250       260
                  ....*....|....*....|....
gi 578817221  707 ---LRQLLKKTRVSTDQAA-AEQL 726
Cdd:PRK04778  482 tedVETLEEETEELVENATlTEQL 505
growth_prot_Scy NF041483
polarized growth protein Scy;
552-835 1.42e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.89  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  552 LQTATENTQARVLHAEQEKAKVTEELAAATAQVShlQLKMTAHQKKeTELQMQLTESLKETDLLRGQLTKVQAK-LSELQ 630
Cdd:NF041483  224 LNAASTQAQEATDHAEQLRSSTAAESDQARRQAA--ELSRAAEQRM-QEAEEALREARAEAEKVVAEAKEAAAKqLASAE 300
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  631 ETSEQAQSKFKSE-----KQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAeeEIDEIRKSYQEELD 705
Cdd:NF041483  301 SANEQRTRTAKEEiarlvGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDTAA--QLAKAARTAEEVLT 378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  706 KLRQLLKktrvSTDQAAAEQLSLVQAELqtqwEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQIT 785
Cdd:NF041483  379 KASEDAK----ATTRAAAEEAERIRREA----EAEADRLRGEAADQAEQLKGAAKDDTKEYRAKTVELQEEARRLRGEAE 450
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578817221  786 AL---------------TKQNEQHIKE--------LEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFE 835
Cdd:NF041483  451 QLraeavaegerirgeaRREAVQQIEEaartaeelLTKAKADADELRSTATAESERVRTEAIERATTLRRQAE 523
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
574-709 1.42e-03

Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.


Pssm-ID: 465814 [Multi-domain]  Cd Length: 117  Bit Score: 39.49  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   574 TEELAAATAQVSHLQLKMTAHQKKetelqmqlTESLK--ETDLlrgqltkvqAKLSELQETSEQAQSKFKSEKQNRKQLE 651
Cdd:pfam18595    1 SSTLAEEKEELAELERKARELQAK--------IDALQvvEKDL---------RSCIKLLEEIEAELAKLEEAKKKLKELR 63
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 578817221   652 LKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIrksyQEELDKLRQ 709
Cdd:pfam18595   64 DALEEKEIELRELERREERLQRQLENAQEKLERLREQAEEKREAA----QARLEELRE 117
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
597-837 1.52e-03

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 42.57  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   597 KETELQMQLTESLKEtdllRGQLTKVQAKLSELQETSEQAQSKFKSE-KQNRKQLELKVTSLEEELTDLRVEKESLEknl 675
Cdd:pfam07888   28 RAELLQNRLEECLQE----RAELLQAQEAANRQREKEKERYKRDREQwERQRRELESRVAELKEELRQSREKHEELE--- 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   676 sERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTrvstdQAAAEQLSLVQAELQTQWEaKCEHLLASAKDEHlqq 755
Cdd:pfam07888  101 -EKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDI-----KTLTQRVLERETELERMKE-RAKKAGAQRKEEE--- 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   756 yqevcAQRDAYQQKLVQLQEKCLALQaqitaltkqneqhiKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFE 835
Cdd:pfam07888  171 -----AERKQLQAKLQQTEEELRSLS--------------KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE 231

                   ..
gi 578817221   836 LE 837
Cdd:pfam07888  232 NE 233
YkyA pfam10368
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ...
621-800 1.68e-03

Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.


Pssm-ID: 431235 [Multi-domain]  Cd Length: 185  Bit Score: 40.65  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   621 KVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQA-EEEIDEIRKS 699
Cdd:pfam10368    1 SPEEKIYDHLEEAVELEKPFEEQQEPLVELEKKEQELYEEIIELGMDEFDEIKKLSDEALENVEEREELlEKEKESIEEA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   700 YqEELDKLRQLLKKTRvstDQAAAEQLSLVQAELQTQWEAkceHllasakDEHLQQYQE-VCAQRDAY---QQKLVQLQE 775
Cdd:pfam10368   81 K-EEFKKIKEIIEEIE---DEELKKEAEELIDAMEERYEA---Y------DELYDAYKKaLELDKELYemlKDEDLTLEE 147
                          170       180
                   ....*....|....*....|....*
gi 578817221   776 kclaLQAQITALTKQNEQHIKELEK 800
Cdd:pfam10368  148 ----LQEQIEKINESYEEVKEANEQ 168
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
495-713 1.69e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 42.69  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  495 IMSNIQRIIQEnerlKQEILEKSNRIeeQN-DKISELIERNQRYVEQSNLMMEKRNNSLQTAT-ENTQARVLHAEQEKAK 572
Cdd:NF033838   63 VESHLEKILSE----IQKSLDKRKHT--QNvALNKKLSDIKTEYLYELNVLKEKSEAELTSKTkKELDAAFEQFKKDTLE 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  573 VTEELAAATAQVSHLQLKmtAHQKKETELQMQLTESLKETDLLRGQlTKVQAKLSELQETSEQAQSKFKSEKQnrKQLEL 652
Cdd:NF033838  137 PGKKVAEATKKVEEAEKK--AKDQKEEDRRNYPTNTYKTLELEIAE-SDVEVKKAELELVKEEAKEPRDEEKI--KQAKA 211
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578817221  653 KVTSLEEELTdlrvekeSLEKNLSERKK--KSAQERSQAEEEIDEIRKSYQEELDKLRQLLKK 713
Cdd:NF033838  212 KVESKKAEAT-------RLEKIKTDREKaeEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKR 267
PRK10263 PRK10263
DNA translocase FtsK; Provisional
329-423 1.83e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.76  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  329 QGGGQPVVTPSVQPSLHPAHPALPQMTSQAPQPSVTGLQA------PSAALMQVSSLDSHSAVSGN-AQSFQPYAGMQAY 401
Cdd:PRK10263  738 DGPHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQyqqpqqPVAPQPQYQQPQQPVAPQPQyQQPQQPVAPQPQY 817
                          90       100
                  ....*....|....*....|....
gi 578817221  402 AYPQASAVTSQ--LQPVRPLYPAP 423
Cdd:PRK10263  818 QQPQQPVAPQPqyQQPQQPVAPQP 841
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
2-100 1.86e-03

WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains point mutations in the majority of patients with WAS. Unknown function. Ena-like WH1 domains bind polyproline-containing peptides, and that Homer contains a WH1 domain.


Pssm-ID: 214674  Cd Length: 106  Bit Score: 38.88  E-value: 1.86e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221      2 STPTILVATAVHAYRYTNGQYVKQGKFGAAVLG---NHTAREYRILLYISQQQPVTVARIHVNFELMVRPNNYSTFYDDQ 78
Cdd:smart00461    3 SQCIILARAVVQLYDADTKKWVPTGEGGAANLVidkNQRSYFFRIVGIKGQDKVIWNQELYKNFKYNQATPTFHQWADDK 82
                            90       100
                    ....*....|....*....|..
gi 578817221     79 RQnWSIMFESEKAAVEFNKQVC 100
Cdd:smart00461   83 CV-YGLNFASEEEAKKFRKKVL 103
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
495-800 1.93e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 42.13  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  495 IMSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIER-NQRYVEQSNLMMEKRnNSLQTATENTQARVLHAEQEKAKV 573
Cdd:PRK04778  106 EINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQlKDLYRELRKSLLANR-FSFGPALDELEKQLENLEEEFSQF 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  574 TEElaaaTAQVSHLQLKMTAHQKKETELQM-QLTESLKEtdLLRGQLTKVQAKLSELQETSEQAqskfksEKQNRKqleL 652
Cdd:PRK04778  185 VEL----TESGDYVEAREILDQLEEELAALeQIMEEIPE--LLKELQTELPDQLQELKAGYREL------VEEGYH---L 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  653 KVTSLEEELTDLRVEKESLEKNLSERKKKSAQER-SQAEEEIDEI----------RKSYQEELDKLRQLLKKTRVSTDQA 721
Cdd:PRK04778  250 DHLDIEKEIQDLKEQIDENLALLEELDLDEAEEKnEEIQERIDQLydilerevkaRKYVEKNSDTLPDFLEHAKEQNKEL 329
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  722 AAEQLSLVQA------ELQTQWEAKCEhlLASAKDEHLQQYQEVCAQRDAYQqklvQLQEKCLALQAQITALTKQNEQ-- 793
Cdd:PRK04778  330 KEEIDRVKQSytlnesELESVRQLEKQ--LESLEKQYDEITERIAEQEIAYS----ELQEELEEILKQLEEIEKEQEKls 403

                  ....*...
gi 578817221  794 -HIKELEK 800
Cdd:PRK04778  404 eMLQGLRK 411
PRK12704 PRK12704
phosphodiesterase; Provisional
560-736 2.05e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  560 QARVLHAEQEKAKVTEElAAATAQVshlqlkmtahQKKETELQMQlteslKETDLLRGQLTK-VQAKLSELQETSEQAQS 638
Cdd:PRK12704   30 EAKIKEAEEEAKRILEE-AKKEAEA----------IKKEALLEAK-----EEIHKLRNEFEKeLRERRNELQKLEKRLLQ 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  639 KFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKnlserkkksaqersqAEEEIDEIRKSYQEELDKLRQLlkktrvST 718
Cdd:PRK12704   94 KEENLDRKLELLEKREEELEKKEKELEQKQQELEK---------------KEEELEELIEEQLQELERISGL------TA 152
                         170
                  ....*....|....*...
gi 578817221  719 DQAAAEQLSLVQAELQTQ 736
Cdd:PRK12704  153 EEAKEILLEKVEEEARHE 170
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
652-786 2.07e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 42.38  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  652 LKVTSLEEELTDLRVEKESLEKnlserkkksaqERSQAEEEIDEirkSYQEELDKLRQLLKKTRvstdqaaaEQLslvqA 731
Cdd:COG0542   404 MEIDSKPEELDELERRLEQLEI-----------EKEALKKEQDE---ASFERLAELRDELAELE--------EEL----E 457
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578817221  732 ELQTQWEAKCEHL--LASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITA 786
Cdd:COG0542   458 ALKARWEAEKELIeeIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE 514
tig TIGR00115
trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first ...
110-183 2.17e-03

trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first chaperone to interact with nascent polypeptide. Trigger factor can bind at the same time as the signal recognition particle (SRP), but is excluded by the SRP receptor (FtsY). The central domain of trigger factor has peptidyl-prolyl cis/trans isomerase activity. This protein is found in a single copy in virtually every bacterial genome. [Protein fate, Protein folding and stabilization]


Pssm-ID: 272913 [Multi-domain]  Cd Length: 410  Bit Score: 41.77  E-value: 2.17e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817221   110 LDAVLSQ--DLIVADGPAVEVGDSLEVAYTGwlfqnHVLGQVFDSTANKDklLRLKLGSGKVIKGWEDGMLGMKKG 183
Cdd:TIGR00115  131 LERLREQnaTLVPVERGAAEKGDRVTIDFEG-----FIDGEAFEGGKAEN--FSLELGSGQFIPGFEEQLVGMKAG 199
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
659-790 2.30e-03

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


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 39.16  E-value: 2.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   659 EELTDLRVEKESLEKNLS--ERKKKSAQERSQAEEEI-DEIRKSYQEELdklrqLLKKTRVSTDQAAAEQLSLVQAELQt 735
Cdd:pfam07926    1 AELSSLQSEIKRLKEEAAdaEAQLQKLQEDLEKQAEIaREAQQNYEREL-----VLHAEDIKALQALREELNELKAEIA- 74
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 578817221   736 QWEAKCEhllaSAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQ 790
Cdd:pfam07926   75 ELKAEAE----SAKAELEESEESWEEQKKELEKELSELEKRIEDLNEQNKLLHDQ 125
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
500-824 2.31e-03

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


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 42.15  E-value: 2.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   500 QRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQT-------ATENTQARVLHAEQEKAK 572
Cdd:pfam06160   85 KKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLAnrfsygpAIDELEKQLAEIEEEFSQ 164
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   573 VTEElaaaTAQVSHLQLKMTAHQ-KKETELQMQLTESLKEtdLLRGQLTKVQAKLSELQETSEQAQskfksekqnRKQLE 651
Cdd:pfam06160  165 FEEL----TESGDYLEAREVLEKlEEETDALEELMEDIPP--LYEELKTELPDQLEELKEGYREME---------EEGYA 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   652 LKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQA-EEEIDEI----------RKSYQEELDKLRQLLKKTRVSTDQ 720
Cdd:pfam06160  230 LEHLNVDKEIQQLEEQLEENLALLENLELDEAEEALEEiEERIDQLydllekevdaKKYVEKNLPEIEDYLEHAEEQNKE 309
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   721 AAAEQLSLVQA-ELQTQWEAKCEHLlasakDEHLQ----QYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHI 795
Cdd:pfam06160  310 LKEELERVQQSyTLNENELERVRGL-----EKQLEelekRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFK 384
                          330       340
                   ....*....|....*....|....*....
gi 578817221   796 KELEknksQMSGVEAAASDPSEKVKKIMN 824
Cdd:pfam06160  385 ESLQ----SLRKDELEAREKLDEFKLELR 409
YkyA pfam10368
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ...
503-635 2.67e-03

Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.


Pssm-ID: 431235 [Multi-domain]  Cd Length: 185  Bit Score: 40.27  E-value: 2.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   503 IQENERLKQEILEKSNRI-EEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATE---NTQARVLHAEQEKAK-VTEEL 577
Cdd:pfam10368   27 LVELEKKEQELYEEIIELgMDEFDEIKKLSDEALENVEEREELLEKEKESIEEAKEefkKIKEIIEEIEDEELKkEAEEL 106
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578817221   578 AAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDL----LRGQLTKVQAKLSELQETSEQ 635
Cdd:pfam10368  107 IDAMEERYEAYDELYDAYKKALELDKELYEMLKDEDLtleeLQEQIEKINESYEEVKEANEQ 168
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
610-696 3.51e-03

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 40.87  E-value: 3.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   610 KETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESL-EKNLSE--RKKKSAQER 686
Cdd:TIGR04320  254 NSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTaQNNLATaqAALANAEAR 333
                           90
                   ....*....|.
gi 578817221   687 -SQAEEEIDEI 696
Cdd:TIGR04320  334 lAKAKEALANL 344
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
685-800 3.66e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 3.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  685 ERSQAEEEIDEIRKSYqEELDKLRQLLKKTRVSTD------------QAAAEQLSLVQAELQT--QWEA-KCEHLLASAK 749
Cdd:COG4913   219 EEPDTFEAADALVEHF-DDLERAHEALEDAREQIEllepirelaeryAAARERLAELEYLRAAlrLWFAqRRLELLEAEL 297
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578817221  750 DEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQ--------ITALTKQNEQHIKELEK 800
Cdd:COG4913   298 EELRAELARLEAELERLEARLDALREELDELEAQirgnggdrLEQLEREIERLERELEE 356
PHA03247 PHA03247
large tegument protein UL36; Provisional
883-1053 4.40e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 4.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  883 RPRRPSQEQSASASSGQPQAPLNRERPesPMVPSEQVVEEAVPLPPQAlttSQDGHRRKGDSEAEALSEIKDGSLPPELS 962
Cdd:PHA03247 2759 RPPTTAGPPAPAPPAAPAAGPPRRLTR--PAVASLSESRESLPSPWDP---ADPPAAVLAPAAALPPAASPAGPLPPPTS 2833
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  963 CIPSHRVLGPPTSIPPEPL-GPVSMDSECEESLAASPMAAKPDNPSGKVCVREVAPdgPLQESSTRLSLTSDPEEGDPla 1041
Cdd:PHA03247 2834 AQPTAPPPPPGPPPPSLPLgGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARP--AVSRSTESFALPPDQPERPP-- 2909
                         170
                  ....*....|..
gi 578817221 1042 lGPESPGEPQPP 1053
Cdd:PHA03247 2910 -QPQAPPPPQPQ 2920
PRK01156 PRK01156
chromosome segregation protein; Provisional
496-799 4.42e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.43  E-value: 4.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  496 MSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSlqtatENTQARVLHAEQEKAKVTE 575
Cdd:PRK01156  182 ISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNL-----KSALNELSSLEDMKNRYES 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  576 ELAAATAQVSHLQLKMTAHQKKETELqMQLT---------------------ESLKET-DLLRGQLTKVQA---KLSELQ 630
Cdd:PRK01156  257 EIKTAESDLSMELEKNNYYKELEERH-MKIIndpvyknrnyindyfkykndiENKKQIlSNIDAEINKYHAiikKLSVLQ 335
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  631 ETSEQAQSKfKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKsaQERSQAeeEIDEIRKSYQEELDKLRQL 710
Cdd:PRK01156  336 KDYNDYIKK-KSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKN--IERMSA--FISEILKIQEIDPDAIKKE 410
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  711 LKKTRVSTDQAAAEqlslvQAELQTQWEAKCEHLLASAKDEHLQQYQEVCAQ-------------RDAYQQKLVQLQEKC 777
Cdd:PRK01156  411 LNEINVKLQDISSK-----VSSLNQRIRALRENLDELSRNMEMLNGQSVCPVcgttlgeeksnhiINHYNEKKSRLEEKI 485
                         330       340
                  ....*....|....*....|..
gi 578817221  778 LALQAQITALTKQNEQHIKELE 799
Cdd:PRK01156  486 REIEIEVKDIDEKIVDLKKRKE 507
PRK11637 PRK11637
AmiB activator; Provisional
509-732 4.46e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 40.83  E-value: 4.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  509 LKQEILEKSNRIEEQNDKISELIERnqryveqsnlmMEKRNNSLQTATentqaRVLHAEQEK-AKVTEELAAATAQVSHL 587
Cdd:PRK11637   52 IQQDIAAKEKSVRQQQQQRASLLAQ-----------LKKQEEAISQAS-----RKLRETQNTlNQLNKQIDELNASIAKL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  588 -------------QLKMTAHQKKETELQMQLT--ESLKETDLLR--GQLTKV-QAKLSELQETSEQAQskfksekQNRKQ 649
Cdd:PRK11637  116 eqqqaaqerllaaQLDAAFRQGEHTGLQLILSgeESQRGERILAyfGYLNQArQETIAELKQTREELA-------AQKAE 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  650 LELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEideirksyQEELDKLRQllKKTRVSTDQAAAEQLSLV 729
Cdd:PRK11637  189 LEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKD--------QQQLSELRA--NESRLRDSIARAEREAKA 258

                  ...
gi 578817221  730 QAE 732
Cdd:PRK11637  259 RAE 261
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
623-709 4.69e-03

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


Pssm-ID: 462875 [Multi-domain]  Cd Length: 150  Bit Score: 38.75  E-value: 4.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   623 QAKLSELQETSEQAQSKFKSEKQNRKQ----LELKVTSLEEELTDLRVEKESLEK-----------NLSERKKKSAQERS 687
Cdd:pfam09744   49 NVELEELREDNEQLETQYEREKALRKRaeeeLEEIEDQWEQETKDLLSQVESLEEenrrleadhvsRLEEKEAELKKEYS 128
                           90       100
                   ....*....|....*....|..
gi 578817221   688 QAEEEIDEIRKSYQEELDKLRQ 709
Cdd:pfam09744  129 KLHERETEVLRKLKEVVDRQRD 150
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
507-753 4.71e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 41.07  E-value: 4.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  507 ERLKQEI-LEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVlhaEQEKAKVTEELAAATAQVS 585
Cdd:PRK05771   34 EDLKEELsNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDV---EEELEKIEKEIKELEEEIS 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  586 HLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQA------KLSELQETSEQAQSKFKSEKQNRK-----QLELKV 654
Cdd:PRK05771  111 ELENEIKELEQEIERLEPWGNFDLDLSLLLGFKYVSVFVgtvpedKLEELKLESDVENVEYISTDKGYVyvvvvVLKELS 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  655 TSLEEELTDLRVEKESLEknlseRKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTrvstdqaaaEQLSLVQAELQ 734
Cdd:PRK05771  191 DEVEEELKKLGFERLELE-----EEGTPSELIREIKEELEEIEKERESLLEELKELAKKY---------LEELLALYEYL 256
                         250
                  ....*....|....*....
gi 578817221  735 TQWEAKCEHLLASAKDEHL 753
Cdd:PRK05771  257 EIELERAEALSKFLKTDKT 275
mukB PRK04863
chromosome partition protein MukB;
496-713 4.91e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.10  E-value: 4.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  496 MSNIQRIIQENERLKQEILEKsnRIEEQNDKISEL------IERNQRYVEQsnlmMEKRNNSLQTATEN---TQARVLHA 566
Cdd:PRK04863  874 LSALNRLLPRLNLLADETLAD--RVEEIREQLDEAeeakrfVQQHGNALAQ----LEPIVSVLQSDPEQfeqLKQDYQQA 947
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  567 EQEKAKVTEELAAATAQVSHLqlkmtAHQKKETELQMqLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKF------ 640
Cdd:PRK04863  948 QQTQRDAKQQAFALTEVVQRR-----AHFSYEDAAEM-LAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLaqynqv 1021
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  641 ----KSEKQNRKQLelkVTSLEEELTDLRVE-KESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQ---EELDKLRQLLK 712
Cdd:PRK04863 1022 laslKSSYDAKRQM---LQELKQELQDLGVPaDSGAEERARARRDELHARLSANRSRRNQLEKQLTfceAEMDNLTKKLR 1098

                  .
gi 578817221  713 K 713
Cdd:PRK04863 1099 K 1099
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
621-844 5.11e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 40.60  E-value: 5.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   621 KVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELT--DLRVEKESLEKNLSERKKKSAQERSQAEEEIDEiRK 698
Cdd:TIGR02794   65 KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQaeQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAE-RK 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   699 SYQEELDKLRQLLKKTRVSTDQAAAEqlslvQAELQTQWEAKcehllasAKDEHLQQYQEVCAQRDAYQQKL---VQLQE 775
Cdd:TIGR02794  144 AKEEAAKQAEEEAKAKAAAEAKKKAE-----EAKKKAEAEAK-------AKAEAEAKAKAEEAKAKAEAAKAkaaAEAAA 211
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578817221   776 KCLALQAQITALTKQ------NEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFELEESYNGRT 844
Cdd:TIGR02794  212 KAEAEAAAAAAAEAErkadeaELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQNLYDDPSFRGKT 286
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
442-783 5.72e-03

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: 40.96  E-value: 5.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   442 TEARQhnTEIRMAVSKVAdKMDHLMTKVEELQKHSAGNSMLIPS--------MSVTMETSMIMSN-IQRIIQENERLKQE 512
Cdd:pfam10174  228 TKALQ--TVIEMKDTKIS-SLERNIRDLEDEVQMLKTNGLLHTEdreeeikqMEVYKSHSKFMKNkIDQLKQELSKKESE 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   513 ILEKSNRIEEQNDKISElierNQRYVE---QSNLMMEKRNNSLQTATENTQARVLHAEQ---EKAK----VTEELAAATA 582
Cdd:pfam10174  305 LLALQTKLETLTNQNSD----CKQHIEvlkESLTAKEQRAAILQTEVDALRLRLEEKESflnKKTKqlqdLTEEKSTLAG 380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   583 QVSHLQLKMTAHQKKETELQMQLtESLKEtdllrgQLTKVQAKLSELQEtseqaqskfksekqnrkqlelKVTSLEEELT 662
Cdd:pfam10174  381 EIRDLKDMLDVKERKINVLQKKI-ENLQE------QLRDKDKQLAGLKE---------------------RVKSLQTDSS 432
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   663 DLRVEKESLEKNLSErkKKSAQERSQaeEEIDEIRKSYQEELDKLRQLLKKTRvstdqaaaEQLSLVQAELQTQweakcE 742
Cdd:pfam10174  433 NTDTALTTLEEALSE--KERIIERLK--EQREREDRERLEELESLKKENKDLK--------EKVSALQPELTEK-----E 495
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 578817221   743 HLLASAKdEHLQQYQEVCAQRDAYQQKL----VQLQEKCLALQAQ 783
Cdd:pfam10174  496 SSLIDLK-EHASSLASSGLKKDSKLKSLeiavEQKKEECSKLENQ 539
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
504-703 6.03e-03

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.71  E-value: 6.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   504 QENERLKQEILEKSNRIEEqndkisELIERNQRYVEQSNLMMEKRNNS--LQTATENTQARVLHAEQEKAKVTEElaaat 581
Cdd:pfam15709  358 EEQRRLQQEQLERAEKMRE------ELELEQQRRFEEIRLRKQRLEEErqRQEEEERKQRLQLQAAQERARQQQE----- 426
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   582 aqvshlqlkmtAHQKKETELQMQlteslketdllrgqltkvqaklsELQETSEQAQskfkSEKQNRKQLELKVT------ 655
Cdd:pfam15709  427 -----------EFRRKLQELQRK-----------------------KQQEEAERAE----AEKQRQKELEMQLAeeqkrl 468
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 578817221   656 ---SLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEE 703
Cdd:pfam15709  469 memAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQ 519
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
118-183 6.82e-03

FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440310 [Multi-domain]  Cd Length: 424  Bit Score: 40.11  E-value: 6.82e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817221  118 LIVADGPAvEVGDSLEVAYTGWlfqnhVLGQVFDSTANKDklLRLKLGSGKVIKGWEDGMLGMKKG 183
Cdd:COG0544   151 LVPVERAA-EEGDRVTIDFEGT-----IDGEEFEGGKAED--YSLELGSGSFIPGFEEQLVGMKAG 208
COG5022 COG5022
Myosin heavy chain [General function prediction only];
465-708 7.23e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 40.83  E-value: 7.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  465 LMTKVEELQKHSAGNSMLIPSMSVTMETSMIM---SNIQRIIQENERLKQEILEKSN-------RIEEQNDKISELIERN 534
Cdd:COG5022   919 LIENLEFKTELIARLKKLLNNIDLEEGPSIEYvklPELNKLHEVESKLKETSEEYEDllkkstiLVREGNKANSELKNFK 998
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  535 QRYVEQS-NLM-----------MEKRNNSLQTA-----TENTQARVLHAEQE-KAKVTEELAAATAQVSHLQL-KMTAHQ 595
Cdd:COG5022   999 KELAELSkQYGalqestkqlkeLPVEVAELQSAskiisSESTELSILKPLQKlKGLLLLENNQLQARYKALKLrRENSLL 1078
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  596 KKETELQMQLTESL-KETDLLRGQLTKVQ-AKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLE-----EELTDLRVEK 668
Cdd:COG5022  1079 DDKQLYQLESTENLlKTINVKDLEVTNRNlVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEpvfqkLSVLQLELDG 1158
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 578817221  669 ESLEKNLSERKKKSA-----QERSQAEEEIDEIRKSYQEELDKLR 708
Cdd:COG5022  1159 LFWEANLEALPSPPPfaalsEKRLYQSALYDEKSKLSSSEVNDLK 1203
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
600-713 7.23e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.58  E-value: 7.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  600 ELQMQLTESLKETDLLRGQltkVQAKLSELQETSEQAQSKFKSEKQNRKQlelkvtSLEEELTDLRVEKESLEKNLSERK 679
Cdd:PRK00409  527 ELERELEQKAEEAEALLKE---AEKLKEELEEKKEKLQEEEDKLLEEAEK------EAQQAIKEAKKEADEIIKELRQLQ 597
                          90       100       110
                  ....*....|....*....|....*....|....
gi 578817221  680 KKsaQERSQAEEEIDEIRKSYQEELDKLRQLLKK 713
Cdd:PRK00409  598 KG--GYASVKAHELIEARKRLNKANEKKEKKKKK 629
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
558-835 7.39e-03

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


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 40.22  E-value: 7.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   558 NTQARVLHAEQEKAK-----VTEELAaataQVSHLQLKMtahqkkETElqmQLTESLKE--TDLLRGQLTKVQAKLSELQ 630
Cdd:pfam06160    7 KIYKEIDELEERKNElmnlpVQEELS----KVKKLNLTG------ETQ---EKFEEWRKkwDDIVTKSLPDIEELLFEAE 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   631 ETSEQaqSKFKSEKQNRKQLELKVTSLEEELTDLRvekESLeKNLSERKKKSAQERSQAEEEIDEIRKSY---------- 700
Cdd:pfam06160   74 ELNDK--YRFKKAKKALDEIEELLDDIEEDIKQIL---EEL-DELLESEEKNREEVEELKDKYRELRKTLlanrfsygpa 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   701 ----QEELDKLRQLLKKTRVSTDQ----AAAEQLSLVQ---AELQTQWEaKCEHLLASAKDEHLQQYQEVcaqRDAYQqk 769
Cdd:pfam06160  148 idelEKQLAEIEEEFSQFEELTESgdylEAREVLEKLEeetDALEELME-DIPPLYEELKTELPDQLEEL---KEGYR-- 221
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817221   770 lvQLQEK-----CLALQAQITALTKQNEQHIKELEKNksQMSGVEAAASDPSEKvkkiMNQVFQSLRREFE 835
Cdd:pfam06160  222 --EMEEEgyaleHLNVDKEIQQLEEQLEENLALLENL--ELDEAEEALEEIEER----IDQLYDLLEKEVD 284
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
566-839 7.48e-03

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 40.40  E-value: 7.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   566 AEQEKAKVTEELAAATAQVSHLQLKMtahQKKETELQmqltESLKETDLLRGQLTKVQAKLSElqETSEQAQSKFKSEKQ 645
Cdd:pfam05701   61 AEAAKAQVLEELESTKRLIEELKLNL---ERAQTEEA----QAKQDSELAKLRVEEMEQGIAD--EASVAAKAQLEVAKA 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   646 NRKQLELKVTSLEEELTDLRVEKESL--EKNLSERKkksAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAA 723
Cdd:pfam05701  132 RHAAAVAELKSVKEELESLRKEYASLvsERDIAIKR---AEEAVSASKEIEKTVEELTIELIATKESLESAHAAHLEAEE 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   724 EQLSLVQAELQ--TQWEAKCEHllasAKDEHLQQYQEVCAQRDaYQQKLVQLQEKCLALQAQITALT--KQNEQHIKELE 799
Cdd:pfam05701  209 HRIGAALAREQdkLNWEKELKQ----AEEELQRLNQQLLSAKD-LKSKLETASALLLDLKAELAAYMesKLKEEADGEGN 283
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 578817221   800 KNKSQMSGVEAAASDPSE--KVK----------KIMNQVFQSLRREFELEES 839
Cdd:pfam05701  284 EKKTSTSIQAALASAKKEleEVKaniekakdevNCLRVAAASLRSELEKEKA 335
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
507-804 7.84e-03

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


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 40.06  E-value: 7.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   507 ERLKQEILEKSNRIEEQNDKISELIERNQRyveqsnlmMEKRNNSLQTATENtqarvLHAEQEKAKVT-EELAAATAQVS 585
Cdd:pfam05622  186 ETYKRQVQELHGKLSEESKKADKLEFEYKK--------LEEKLEALQKEKER-----LIIERDTLRETnEELRCAQLQQA 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   586 HLQLKMTAHQK-----------------KETELQMQLteslkETDLLR----GQLTKVQAKLSELQETSEQAQSKFksEK 644
Cdd:pfam05622  253 ELSQADALLSPssdpgdnlaaeimpaeiREKLIRLQH-----ENKMLRlgqeGSYRERLTELQQLLEDANRRKNEL--ET 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   645 QNRKQlelkvtslEEELTDLRVEKESLEKNLSERKKK---SAQERSQAEEEIDEIRKSyQEELDKLRQLLKKTRVSTDQA 721
Cdd:pfam05622  326 QNRLA--------NQRILELQQQVEELQKALQEQGSKaedSSLLKQKLEEHLEKLHEA-QSELQKKKEQIEELEPKQDSN 396
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   722 AAEQLslvqAELQTQWEAKCEHLLASakDEHLQQYQE----VCAQRDAYQQKLVQLQekCLALQAQITALTKQNEQHIKE 797
Cdd:pfam05622  397 LAQKI----DELQEALRKKDEDMKAM--EERYKKYVEkaksVIKTLDPKQNPASPPE--IQALKNQLLEKDKKIEHLERD 468

                   ....*..
gi 578817221   798 LEKNKSQ 804
Cdd:pfam05622  469 FEKSKLQ 475
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
658-744 8.29e-03

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 38.88  E-value: 8.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   658 EEELTDLRVEKEslEKNLSERKKKSAQERSQAEEEiDEIRKsyqEELDKLRQLLKKTRvstdqAAAEQLSLVqAELQTQW 737
Cdd:pfam15927    5 EEEEERLRAEEE--EAERLEEERREEEEEERLAAE-QDRRA---EELEELKHLLEERK-----EALEKLRAE-AREEAEW 72

                   ....*....
gi 578817221   738 E--AKCEHL 744
Cdd:pfam15927   73 EryMRCDGL 81
46 PHA02562
endonuclease subunit; Provisional
600-823 8.30e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.00  E-value: 8.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  600 ELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQA----QSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNL 675
Cdd:PHA02562  178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENiarkQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  676 SERKKKSAQERSQAeEEIDEIRKSYQE-------------ELDKLRQLlkKTRVSTDQAAAEQLSLVQAELQtqwEAKCE 742
Cdd:PHA02562  258 NKLNTAAAKIKSKI-EQFQKVIKMYEKggvcptctqqiseGPDRITKI--KDKLKELQHSLEKLDTAIDELE---EIMDE 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  743 HLLASAKdehlqqYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQ---NEQHIKELEKNKSQMSgveaaaSDPSEKV 819
Cdd:PHA02562  332 FNEQSKK------LLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEfvdNAEELAKLQDELDKIV------KTKSELV 399

                  ....
gi 578817221  820 KKIM 823
Cdd:PHA02562  400 KEKY 403
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
508-707 8.47e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 8.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  508 RLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLhaEQEKAKVTEELAAATAQVSHL 587
Cdd:COG1196   586 AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTL--AGRLREVTLEGEGGSAGGSLT 663
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  588 QLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVE 667
Cdd:COG1196   664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 578817221  668 KESLEKNLSERKKKSAQERSQAEEEIDEIRKsyqeELDKL 707
Cdd:COG1196   744 EEELLEEEALEELPEPPDLEELERELERLER----EIEAL 779
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
460-854 8.76e-03

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 40.59  E-value: 8.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  460 DKMDHLMTKVEELQKhsagNSMLIPSMSVTMETSMI-MSNIQRIIQENERLKQEILEKSNRIE-----EQNDKI------ 527
Cdd:PTZ00440  863 QIVDNIIKDIENMNK----NINIIKTLNIAINRSNSnKQLVEHLLNNKIDLKNKLEQHMKIINtdniiQKNEKLnllnnl 938
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  528 ---SELIER--NQRYVEQSNLMMEKRNNSLQTATENTQARV-LHAEQEKAKVTE------ELAAATAQVSHLQLKMTAHQ 595
Cdd:PTZ00440  939 nkeKEKIEKqlSDTKINNLKMQIEKTLEYYDKSKENINGNDgTHLEKLDKEKDEwehfksEIDKLNVNYNILNKKIDDLI 1018
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  596 KKETELQMQLTESLKeTDLLRGQLTKVQAKLSELQETSEQAQSKFKSE----------KQNRKQLELKVTSLEEELTDLR 665
Cdd:PTZ00440 1019 KKQHDDIIELIDKLI-KEKGKEIEEKVDQYISLLEKMKTKLSSFHFNIdikkyknpkiKEEIKLLEEKVEALLKKIDENK 1097
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  666 VEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSyqeeLDKLRQLLKKTRVSTDQAAAEQLSLVQA-ELQTQWEAKCEHL 744
Cdd:PTZ00440 1098 NKLIEIKNKSHEHVVNADKEKNKQTEHYNKKKKS----LEKIYKQMEKTLKELENMNLEDITLNEVnEIEIEYERILIDH 1173
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221  745 LASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITAL---------TKQNEQHIKELEKNKSQMSGvEAAASDP 815
Cdd:PTZ00440 1174 IVEQINNEAKKSKTIMEEIESYKKDIDQVKKNMSKERNDHLTTfeynayydkATASYENIEELTTEAKGLKG-EANRSTN 1252
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578817221  816 SEKVKKIMNQVFQSLRRE-----------------FELEESYNGRTILGTIMNTIK 854
Cdd:PTZ00440 1253 VDELKEIKLQVFSYLQQVikennkmenalheiknmYEFLISIDSEKILKEILNSTK 1308
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
572-744 8.97e-03

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 38.40  E-value: 8.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   572 KVTEELAAATAQVSHLQLKMTAHQKketELQMQLTeslKETDLLRGQLtkvQAKLSELQETSEQAQSKFKSE-KQNRKQL 650
Cdd:pfam01442    1 LLEDSLDELSTYAEELQEQLGPVAQ---ELVDRLE---KETEALRERL---QKDLEEVRAKLEPYLEELQAKlGQNVEEL 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   651 ELKVTSLEEELTD-LRVEKESLEKNLSErkkKSAQERSQAEEEIDEIRKSYQEELDKLRQL-------LKKTRVSTDQAA 722
Cdd:pfam01442   72 RQRLEPYTEELRKrLNADAEELQEKLAP---YGEELRERLEQNVDALRARLAPYAEELRQKlaerleeLKESLAPYAEEV 148
                          170       180
                   ....*....|....*....|..
gi 578817221   723 AEQLSLVQAELQTQWEAKCEHL 744
Cdd:pfam01442  149 QAQLSQRLQELREKLEPQAEDL 170
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
621-798 9.40e-03

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 38.40  E-value: 9.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   621 KVQAKLSELQETSEQAQSKFKSEKQNrkqlelKVTSLEEELTDLRvekESLEKNLSERKKKSAQERSQAEEEIdeirksy 700
Cdd:pfam01442    1 LLEDSLDELSTYAEELQEQLGPVAQE------LVDRLEKETEALR---ERLQKDLEEVRAKLEPYLEELQAKL------- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817221   701 QEELDKLRQLLK------KTRVSTD-QAAAEQLSLVQAELQTQWEAKCEHLLAsakdeHLQQYQEvcAQRDAYQQKLVQL 773
Cdd:pfam01442   65 GQNVEELRQRLEpyteelRKRLNADaEELQEKLAPYGEELRERLEQNVDALRA-----RLAPYAE--ELRQKLAERLEEL 137
                          170       180
                   ....*....|....*....|....*
gi 578817221   774 QEKclaLQAQITALTKQNEQHIKEL 798
Cdd:pfam01442  138 KES---LAPYAEEVQAQLSQRLQEL 159
 
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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