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Conserved domains on  [gi|578817219|ref|XP_006717081|]
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FK506-binding protein 15 isoform X1 [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;
193-286 1.16e-29

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 113.45  E-value: 1.16e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   193 AVEVGDSLEVAYTGWLFQnhvlGQVFDSTANKDKLLRLKLGSGKVIKGWEDGMLGMKKGGKRLLIVPPACAVGSEGVIGW 272
Cdd:pfam00254    4 KAKKGDRVTVHYTGTLED----GTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGP 79

                           90
                   ....*....|....
gi 578817219   273 TQATDSILVFEVEV 286
Cdd:pfam00254   80 VIPPNATLVFEVEL 93
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 578-884 2.32e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 91.27  E-value: 2.32e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   578 KQEILEKSNRIEEQNDKISEL-IERNQRYVEQSNLMMEKRnnSLQTATENTQAKVTE---ELAAATAQVSHLQLKMTAHQ 653
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELeKALAELRKELEELEEELE--QLRKELEELSRQISAlrkDLARLEAEVEQLEERIAQLS 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   654 KKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNL 733
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   734 sERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTrvstdQAAAEQLSLVQAELQTQWEAKCEHL--LASAKDEHL 811
Cdd:TIGR02168  834 -AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-----ESELEALLNERASLEEALALLRSELeeLSEELRELE 907

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578817219   812 QQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQ-NEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQV 884
Cdd:TIGR02168  908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 941-1154 9.07e-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: 50.32  E-value: 9.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  941 RPRRPSQEQsasassgQPQAPLNRERPESPMVPSEQVVEEAVPLPPQALTTSQDGhrRKGDSEAEALSEIKDGSLPPELS 1020
Cdd:PHA03247 2907 RPPQPQAPP-------PPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGE--PSGAVPQPWLGALVPGRVAVPRF 2977

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219 1021 CIPSHRvlgPPTSIPPEPLGPVSMDSECEESLAASPMAAKPDNPSGKVCVRE-VAPDGPLQESSTRLSLTSDPEEGDPLA 1099
Cdd:PHA03247 2978 RVPQPA---PSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQtLWPPDDTEDSDADSLFDSDSERSDLEA 3054

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578817219 1100 LGPEsPGEPQPPQLKKDDVTSSTGPHKELSSTEAG--STVAGAAL--RPSHHSQRSSLS 1154
Cdd:PHA03247 3055 LDPL-PPEPHDPFAHEPDPATPEAGARESPSSQFGppPLSANAALsrRYVRSTGRSALA 3112
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 307-495 3.13e-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: 45.14  E-value: 3.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   307 SAAPSPIPGADNLSADPVVSPPTSIPFKSGEPALRTKSnslseqlAINTSPDAVKAKLISRMAKMgQPMLPILPPQldsn 386
Cdd:pfam03154  192 TQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHT-------LIQQTPTLHPQRLPSPHPPL-QPMTQPPPPS---- 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   387 dseiedvntlqgggQPVVTPSVQPSLHPAHPALPQMTSQAPqpsvTGLQAPSAAL-MQVSSLDSHSAVSGNAQSFQPYAG 465
Cdd:pfam03154  260 --------------QVSPQPLPQPSLHGQMPPMPHSLQTGP----SHMQHPVPPQpFPLTPQSSQSQVPPGPSPAAPGQS 321

                          170       180       190
                   ....*....|....*....|....*....|..
gi 578817219   466 MQAYAYPQASAVTSQLQPVR--PLYPAPLSQP 495
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 ...
 70-168 1.96e-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: 1.96e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219     70 STPTILVATAVHAYRYTNGQYVKQGKFGAAVLG---NHTAREYRILLYISQQQPVTVARIHVNFELMVRPNNYSTFYDDQ 146
Cdd:smart00461    3 SQCIILARAVVQLYDADTKKWVPTGEGGAANLVidkNQRSYFFRIVGIKGQDKVIWNQELYKNFKYNQATPTFHQWADDK 82

                            90       100
                    ....*....|....*....|..
gi 578817219    147 RQnWSIMFESEKAAVEFNKQVC 168
Cdd:smart00461   83 CV-YGLNFASEEEAKKFRKKVL 103
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
193-286 1.16e-29

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 113.45  E-value: 1.16e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   193 AVEVGDSLEVAYTGWLFQnhvlGQVFDSTANKDKLLRLKLGSGKVIKGWEDGMLGMKKGGKRLLIVPPACAVGSEGVIGW 272
Cdd:pfam00254    4 KAKKGDRVTVHYTGTLED----GTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGP 79

                           90
                   ....*....|....
gi 578817219   273 TQATDSILVFEVEV 286
Cdd:pfam00254   80 VIPPNATLVFEVEL 93
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 184-286 1.93e-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: 1.93e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  184 QDLIVADGPAVEVGDSLEVAYTGWLFQnhvlGQVFDSTANKDKLLRLKLGSGKVIKGWEDGMLGMKKGGKRLLIVPPACA 263
Cdd:COG0545     4 KVLKEGTGAKPKAGDTVTVHYTGTLLD----GTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79

                          90       100
                  ....*....|....*....|....*.
gi 578817219  264 VGSEG---VIGwtqaTDSILVFEVEV 286
Cdd:COG0545    80 YGERGaggVIP----PNSTLVFEVEL 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 578-884 2.32e-18

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 91.27  E-value: 2.32e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   578 KQEILEKSNRIEEQNDKISEL-IERNQRYVEQSNLMMEKRnnSLQTATENTQAKVTE---ELAAATAQVSHLQLKMTAHQ 653
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELeKALAELRKELEELEEELE--QLRKELEELSRQISAlrkDLARLEAEVEQLEERIAQLS 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   654 KKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNL 733
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   734 sERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTrvstdQAAAEQLSLVQAELQTQWEAKCEHL--LASAKDEHL 811
Cdd:TIGR02168  834 -AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-----ESELEALLNERASLEEALALLRSELeeLSEELRELE 907

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578817219   812 QQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQ-NEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQV 884
Cdd:TIGR02168  908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 563-817 5.79e-18

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 90.00  E-value: 5.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  563 IMSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQ--AKVTEELAAATA 640
Cdd:COG1196   258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEelAELEEELEELEE 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  641 QVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELT 720
Cdd:COG1196   338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  721 DLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSyQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWEakcE 800
Cdd:COG1196   418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL-EEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR---L 493

                         250
                  ....*....|....*..
gi 578817219  801 HLLASAKDEHLQQYQEV 817
Cdd:COG1196   494 LLLLEAEADYEGFLEGV 510
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 509-897 2.82e-12

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: 71.29  E-value: 2.82e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   509 MTEARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMLIPSMSVTMET--SMIMSNIQRIIQENERLK---QEILE 583
Cdd:pfam05483  309 MSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSleELLRTEQQRLEKNEDQLKiitMELQK 388

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   584 KSNRIEE----QNDKISELIERNQRYVEQSNLMMEKRN-NSLQTATENTQAKVTEELAAATAQVSHLQLKMTA------- 651
Cdd:pfam05483  389 KSSELEEmtkfKNNKEVELEELKKILAEDEKLLDEKKQfEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAiktseeh 468

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   652 HQKKETELQMQL-TESLKETDLL---------RGQLTKVQAKLS-ELQETSEQAQSKFKSEKQNRKQLElkvtSLEEELT 720
Cdd:pfam05483  469 YLKEVEDLKTELeKEKLKNIELTahcdkllleNKELTQEASDMTlELKKHQEDIINCKKQEERMLKQIE----NLEEKEM 544

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   721 DLRVEKESLEKNLSERK-------KKSAQERSQAEEEI--------------DEIRKSYQEELDKLRQLLKKTRVSTDQA 779
Cdd:pfam05483  545 NLRDELESVREEFIQKGdevkcklDKSEENARSIEYEVlkkekqmkilenkcNNLKKQIENKNKNIEELHQENKALKKKG 624

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   780 AAEQLSLVQAELQTQweaKCEHLLASAK---DEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNE---QH- 852
Cdd:pfam05483  625 SAENKQLNAYEIKVN---KLELELASAKqkfEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDkrcQHk 701

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 578817219   853 IKE----LEKNKSQMSGVeAAASDPSEKVKKIMNQVFQSLRREFELEES 897
Cdd:pfam05483  702 IAEmvalMEKHKHQYDKI-IEERDSELGLYKNKEQEQSSAKAALEIELS 749
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
563-892 3.35e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 71.25  E-value: 3.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  563 IMSNIQRI-----IQENERLKQEILEKSNRIEEQNDKISELIERNQRyveqsnlmMEKRNNSLQTATENTQ-AK------ 630
Cdd:PRK03918  370 KKEELERLkkrltGLTPEKLEKELEELEKAKEEIEEEISKITARIGE--------LKKEIKELKKAIEELKkAKgkcpvc 441

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  631 ---VTEE-----LAAATAQVSHLQLKMTAHQKKETELQMQLTE------------SLKET-DLLRG--------QLTKVQ 681
Cdd:PRK03918  442 greLTEEhrkelLEEYTAELKRIEKELKEIEEKERKLRKELRElekvlkkeseliKLKELaEQLKEleeklkkyNLEELE 521

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  682 AKLSELQETSEQA------QSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQErsqAEEEIDEIR 755
Cdd:PRK03918  522 KKAEEYEKLKEKLiklkgeIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEE---LEERLKELE 598

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  756 KSYQE---------ELDKLRQLLKKTRVSTDQAAAEqLSLVQAELQtQWEAKCEHLLASAKDEhlqQYQEVcaqrdayQQ 826
Cdd:PRK03918  599 PFYNEylelkdaekELEREEKELKKLEEELDKAFEE-LAETEKRLE-ELRKELEELEKKYSEE---EYEEL-------RE 666

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817219  827 KLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDpSEKVKKIMNQVfQSLRREF 892
Cdd:PRK03918  667 EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE-LEKLEKALERV-EELREKV 730
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 191-309 1.80e-09

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 60.16  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  191 GPAVEVGDSLEVAYTGWLfqnhVLGQVFDSTANKDKLLRLKLGSgkVIKGWEDGMLGMKKGGKRLLIVPPACAVGSEGVI 270
Cdd:PRK10902  158 GEAPKDSDTVVVNYKGTL----IDGKEFDNSYTRGEPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVP 231

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 578817219  271 GWtqATDSILVFEVEVRRVKFARDSGSDGHSVSSRDSAA 309
Cdd:PRK10902  232 GI--PANSTLVFDVELLDVKPAPKADAKPEADAKAADSA 268
PHA03247 PHA03247
large tegument protein UL36; Provisional
 941-1154 9.07e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 9.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  941 RPRRPSQEQsasassgQPQAPLNRERPESPMVPSEQVVEEAVPLPPQALTTSQDGhrRKGDSEAEALSEIKDGSLPPELS 1020
Cdd:PHA03247 2907 RPPQPQAPP-------PPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGE--PSGAVPQPWLGALVPGRVAVPRF 2977

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219 1021 CIPSHRvlgPPTSIPPEPLGPVSMDSECEESLAASPMAAKPDNPSGKVCVRE-VAPDGPLQESSTRLSLTSDPEEGDPLA 1099
Cdd:PHA03247 2978 RVPQPA---PSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQtLWPPDDTEDSDADSLFDSDSERSDLEA 3054

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578817219 1100 LGPEsPGEPQPPQLKKDDVTSSTGPHKELSSTEAG--STVAGAAL--RPSHHSQRSSLS 1154
Cdd:PHA03247 3055 LDPL-PPEPHDPFAHEPDPATPEAGARESPSSQFGppPLSANAALsrRYVRSTGRSALA 3112
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 307-495 3.13e-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: 45.14  E-value: 3.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   307 SAAPSPIPGADNLSADPVVSPPTSIPFKSGEPALRTKSnslseqlAINTSPDAVKAKLISRMAKMgQPMLPILPPQldsn 386
Cdd:pfam03154  192 TQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHT-------LIQQTPTLHPQRLPSPHPPL-QPMTQPPPPS---- 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   387 dseiedvntlqgggQPVVTPSVQPSLHPAHPALPQMTSQAPqpsvTGLQAPSAAL-MQVSSLDSHSAVSGNAQSFQPYAG 465
Cdd:pfam03154  260 --------------QVSPQPLPQPSLHGQMPPMPHSLQTGP----SHMQHPVPPQpFPLTPQSSQSQVPPGPSPAAPGQS 321

                          170       180       190
                   ....*....|....*....|....*....|..
gi 578817219   466 MQAYAYPQASAVTSQLQPVR--PLYPAPLSQP 495
Cdd:pfam03154  322 QQRIHTPPSQSQLQSQQPPReqPLPPAPLSMP 353
AmmeMemoSam_B TIGR04336
AmmeMemoRadiSam system protein B; Members of this protein family belong to the same domain ...
 1004-1062 9.87e-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: 9.87e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817219  1004 AEALSEIKDGslPPELSCI--PSHRVLGPPTSIPPE-----PLGPVSMDSECEESLAASPMAAKPD 1062
Cdd:TIGR04336   55 AHAYAALKKG--RPETVVLlgPNHTGYGSGIALPPEgswetPLGDVPVDEELAEELLEHSPIIELD 118
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 645-797 1.19e-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: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  645 LQLKMTAHQKKETELQMQLTESLKE-TDLLRGQLTKVQAKLSELQEtseqAQSKFKSE-KQNRKQLELKVTSLEEELTD- 721
Cdd:cd22656    97 LELIDDLADATDDEELEEAKKTIKAlLDDLLKEAKKYQDKAAKVVD----KLTDFENQtEKDQTALETLEKALKDLLTDe 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  722 -LRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRqllKKTRVSTD-QAAAEQLSLVQA---------- 789
Cdd:cd22656   173 gGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLA---AALRLIADlTAADTDLDNLLAligpaipale 249


                  ....*...
gi 578817219  790 ELQTQWEA 797
Cdd:cd22656   250 KLQGAWQA 257
tig TIGR00115
trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first ...
 178-251 1.64e-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: 42.16  E-value: 1.64e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817219   178 LDAVLSQ--DLIVADGPAVEVGDSLEVAYTGwlfqnHVLGQVFDSTANKDklLRLKLGSGKVIKGWEDGMLGMKKG 251
Cdd:TIGR00115  131 LERLREQnaTLVPVERGAAEKGDRVTIDFEG-----FIDGEAFEGGKAEN--FSLELGSGQFIPGFEEQLVGMKAG 199
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 397-491 1.96e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.76  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  397 QGGGQPVVTPSVQPSLHPAHPALPQMTSQAPQPSVTGLQA------PSAALMQVSSLDSHSAVSGN-AQSFQPYAGMQAY 469
Cdd:PRK10263  738 DGPHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQyqqpqqPVAPQPQYQQPQQPVAPQPQyQQPQQPVAPQPQY 817

                          90       100
                  ....*....|....*....|....
gi 578817219  470 AYPQASAVTSQ--LQPVRPLYPAP 491
Cdd:PRK10263  818 QQPQQPVAPQPqyQQPQQPVAPQP 841
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 70-168 1.96e-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: 1.96e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219     70 STPTILVATAVHAYRYTNGQYVKQGKFGAAVLG---NHTAREYRILLYISQQQPVTVARIHVNFELMVRPNNYSTFYDDQ 146
Cdd:smart00461    3 SQCIILARAVVQLYDADTKKWVPTGEGGAANLVidkNQRSYFFRIVGIKGQDKVIWNQELYKNFKYNQATPTFHQWADDK 82

                            90       100
                    ....*....|....*....|..
gi 578817219    147 RQnWSIMFESEKAAVEFNKQVC 168
Cdd:smart00461   83 CV-YGLNFASEEEAKKFRKKVL 103
BAR smart00721
BAR domain;
576-769 7.44e-03

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 39.67  E-value: 7.44e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219    576 RLKQEILEKSNRIEEQndKISELIERnqryveqsnlmMEKRNNSLQTATENTQAKVTEELaaataQVSHLQLKMTAHQKK 655
Cdd:smart00721    8 RAKQKVGEKVGKAEKT--KLDEDFEE-----------LERRFDTTEAEIEKLQKDTKLYL-----QPNPAVRAKLASQKK 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219    656 ETELQMQLTESLKETDLLrGQLTKVQAKLSELQETSE---QAQSKFKSEKQNR------------KQLELKVTSLEEELT 720
Cdd:smart00721   70 LSKSLGEVYEGGDDGEGL-GADSSYGKALDKLGEALKkllQVEESLSQVKRTFilpllnfllgefKEIKKARKKLERKLL 148

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*....
gi 578817219    721 DLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLL 769
Cdd:smart00721  149 DYDSARHKLKKAKKSKEKKKDEKLAKAEEELRKAKQEFEESNAQLVEEL 197
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
193-286 1.16e-29

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 113.45  E-value: 1.16e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   193 AVEVGDSLEVAYTGWLFQnhvlGQVFDSTANKDKLLRLKLGSGKVIKGWEDGMLGMKKGGKRLLIVPPACAVGSEGVIGW 272
Cdd:pfam00254    4 KAKKGDRVTVHYTGTLED----GTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGP 79

                           90
                   ....*....|....
gi 578817219   273 TQATDSILVFEVEV 286
Cdd:pfam00254   80 VIPPNATLVFEVEL 93
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 184-286 1.93e-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: 1.93e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  184 QDLIVADGPAVEVGDSLEVAYTGWLFQnhvlGQVFDSTANKDKLLRLKLGSGKVIKGWEDGMLGMKKGGKRLLIVPPACA 263
Cdd:COG0545     4 KVLKEGTGAKPKAGDTVTVHYTGTLLD----GTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELA 79

                          90       100
                  ....*....|....*....|....*.
gi 578817219  264 VGSEG---VIGwtqaTDSILVFEVEV 286
Cdd:COG0545    80 YGERGaggVIP----PNSTLVFEVEL 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 578-884 2.32e-18

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 91.27  E-value: 2.32e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   578 KQEILEKSNRIEEQNDKISEL-IERNQRYVEQSNLMMEKRnnSLQTATENTQAKVTE---ELAAATAQVSHLQLKMTAHQ 653
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELeKALAELRKELEELEEELE--QLRKELEELSRQISAlrkDLARLEAEVEQLEERIAQLS 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   654 KKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNL 733
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   734 sERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTrvstdQAAAEQLSLVQAELQTQWEAKCEHL--LASAKDEHL 811
Cdd:TIGR02168  834 -AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-----ESELEALLNERASLEEALALLRSELeeLSEELRELE 907

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578817219   812 QQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQ-NEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQV 884
Cdd:TIGR02168  908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 563-817 5.79e-18

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 90.00  E-value: 5.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  563 IMSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQ--AKVTEELAAATA 640
Cdd:COG1196   258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEelAELEEELEELEE 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  641 QVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELT 720
Cdd:COG1196   338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  721 DLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSyQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWEakcE 800
Cdd:COG1196   418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL-EEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR---L 493

                         250
                  ....*....|....*..
gi 578817219  801 HLLASAKDEHLQQYQEV 817
Cdd:COG1196   494 LLLLEAEADYEGFLEGV 510
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 623-872 7.48e-18

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 89.61  E-value: 7.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  623 ATENTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEK 702
Cdd:COG1196   250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  703 QNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKtrvstdQAAAE 782
Cdd:COG1196   330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL------AAQLE 403

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  783 QLSLVQAELQTQWEAkcehlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQ 862
Cdd:COG1196   404 ELEEAEEALLERLER-----LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478

                         250
                  ....*....|
gi 578817219  863 MSGVEAAASD 872
Cdd:COG1196   479 LAELLEELAE 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 616-872 2.35e-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: 84.72  E-value: 2.35e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   616 RNNSLQTATENTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQ 695
Cdd:TIGR02168  243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   696 SKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKS-----------------AQERSQAEEEIDEIRKSY 758
Cdd:TIGR02168  323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELeelesrleeleeqletlRSKVAQLELQIASLNNEI 402

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   759 QEELDKLRQL---LKKTRVSTDQAAAEQLSLVQAELQTQWEAKCEHL--LASAKDEHLQQYQEVCAQRDAYQQKLVQLQE 833
Cdd:TIGR02168  403 ERLEARLERLedrRERLQQEIEELLKKLEEAELKELQAELEELEEELeeLQEELERLEEALEELREELEEAEQALDAAER 482

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 578817219   834 KCLALQAQITALTKQNEQH------IKELEKNKSQMSGVEAAASD 872
Cdd:TIGR02168  483 ELAQLQARLDSLERLQENLegfsegVKALLKNQSGLSGILGVLSE 527
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 533-848 5.95e-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: 83.58  E-value: 5.95e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   533 LMTKVEELQKHSagnSMLIPSMSV-TMETSMIMSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIErnqryveqsnl 611
Cdd:TIGR02169  693 LQSELRRIENRL---DELSQELSDaSRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS----------- 758

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   612 mMEKRNNSLQTATENTQAKVTEELAAATAQVSHLQLKmtahqkketELQMQLTESLKETDLLRGQLTKVQAKLSELQETS 691
Cdd:TIGR02169  759 -ELKELEARIEELEEDLHKLEEALNDLEARLSHSRIP---------EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   692 EQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLE----------KNLSERKKKSAQERSQAEEEIDEIRKSYQE- 760
Cdd:TIGR02169  829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEeeleeleaalRDLESRLGDLKKERDELEAQLRELERKIEEl 908

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   761 --ELDKLRQLLKKTRVsTDQAAAEQLS----------------LVQAELQTQWEAKCEHL--LASAKDEHLQQYQEVCAQ 820
Cdd:TIGR02169  909 eaQIEKKRKRLSELKA-KLEALEEELSeiedpkgedeeipeeeLSLEDVQAELQRVEEEIraLEPVNMLAIQEYEEVLKR 987

                          330       340
                   ....*....|....*....|....*...
gi 578817219   821 RDAYQQKLVQLQEKCLALQAQITALTKQ 848
Cdd:TIGR02169  988 LDELKEKRAKLEEERKAILERIEEYEKK 1015
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 566-892 7.26e-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: 83.18  E-value: 7.26e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   566 NIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATEntqakVTEELAAATAQVSHL 645
Cdd:TIGR02168  699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE-----LEAEIEELEERLEEA 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   646 QLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVE 725
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED 853

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   726 KESLEKNLSE----RKKKSAQ------ERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQ-TQ 794
Cdd:TIGR02168  854 IESLAAEIEEleelIEELESEleallnERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRlEG 933

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   795 WEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPS 874
Cdd:TIGR02168  934 LEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLT 1013

                          330       340       350
                   ....*....|....*....|....*....|..
gi 578817219   875 EKVKKIM--------------NQVFQSLRREF 892
Cdd:TIGR02168 1014 EAKETLEeaieeidrearerfKDTFDQVNENF 1045
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 560-912 9.90e-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: 82.81  E-value: 9.90e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   560 TSMI-MSNIQR--IIQE----------NERLKQEILEKSNRIEEQNDKISELI--------ERNQ--RY---------VE 607
Cdd:TIGR02169  145 TDFIsMSPVERrkIIDEiagvaefdrkKEKALEELEEVEENIERLDLIIDEKRqqlerlrrEREKaeRYqallkekreYE 224

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   608 QSNLMMEKRNNSLQ-TATENTQAKVTEELAAATAQVSHLQLKMTAHQKKETEL-----------QMQLTESLKEtdlLRG 675
Cdd:TIGR02169  225 GYELLKEKEALERQkEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkikdlgeeeQLRVKEKIGE---LEA 301

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   676 QLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIR 755
Cdd:TIGR02169  302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFA 381

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   756 ------KSYQEELDKLRQLLK--KTRVSTDQAAAEQLSLVQAELQTQweakcehlLASAKDEHLQQYQEVCAQRD---AY 824
Cdd:TIGR02169  382 etrdelKDYREKLEKLKREINelKRELDRLQEELQRLSEELADLNAA--------IAGIEAKINELEEEKEDKALeikKQ 453

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   825 QQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKimnqvfqslRREFELEESYNGRTIL 904
Cdd:TIGR02169  454 EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG---------GRAVEEVLKASIQGVH 524


                   ....*...
gi 578817219   905 GTIMNTIK 912
Cdd:TIGR02169  525 GTVAQLGS 532
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 567-852 2.04e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 81.52  E-value: 2.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  567 IQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYvEQSNLMMEKRNNSLQTAtentQAKVTEELAAATAQVSHLQ 646
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEEL-RLELEELELELEEAQAE----EYELLAELARLEQDIARLE 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  647 LKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEK 726
Cdd:COG1196   309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  727 ESLEKNLSERKKKSAQERSQAEEEIDEIRKsYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQtqweakcehlLASA 806
Cdd:COG1196   389 LEALRAAAELAAQLEELEEAEEALLERLER-LEEELEELEEALAELEEEEEEEEEALEEAAEEEAE----------LEEE 457

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 578817219  807 KDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQH 852
Cdd:COG1196   458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 567-898 2.05e-15

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: 81.65  E-value: 2.05e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   567 IQRIIQENERLKQEILEKSNRIEEQNDKISELIERnqryVEQSNLMMEKRnnslqtaTENTQAKVTEELAAATAQVSHLQ 646
Cdd:TIGR02169  239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQL----LEELNKKIKDL-------GEEEQLRVKEKIGELEAEIASLE 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   647 lkmtaHQKKETELQMQLTEslketdllrGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEK 726
Cdd:TIGR02169  308 -----RSIAEKERELEDAE---------ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL 373

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   727 ESLEKNLSERKKKSAQER---SQAEEEIDEIRKSYQEELDKLRQLlkKTRVSTDQAAAEQLSLVQAELQTQWEAKCEHLl 803
Cdd:TIGR02169  374 EEVDKEFAETRDELKDYReklEKLKREINELKRELDRLQEELQRL--SEELADLNAAIAGIEAKINELEEEKEDKALEI- 450

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   804 asAKDEhlQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALtkqnEQHIKELEKNKSQmSGVEAAASDPSEKVKKIMNQ 883
Cdd:TIGR02169  451 --KKQE--WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL----QRELAEAEAQARA-SEERVRGGRAVEEVLKASIQ 521

                          330
                   ....*....|....*.
gi 578817219   884 -VFQSLRREFELEESY 898
Cdd:TIGR02169  522 gVHGTVAQLGSVGERY 537
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 628-896 1.13e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 76.13  E-value: 1.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  628 QAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLteslketdlLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQ 707
Cdd:COG1196   208 QAEKAERYRELKEELKELEAELLLLKLRELEAELEE---------LEAELEELEAELEELEAELAELEAELEELRLELEE 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  708 LELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSyQEELDKLRQLLKKTRVSTDQAAAEQLSLV 787
Cdd:COG1196   279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL-EEELEELEEELEELEEELEEAEEELEEAE 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  788 QAELQtqweakcehlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVE 867
Cdd:COG1196   358 AELAE----------AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427

                         250       260
                  ....*....|....*....|....*....
gi 578817219  868 AAASDPSEKVKKIMNQVFQSLRREFELEE 896
Cdd:COG1196   428 EALAELEEEEEEEEEALEEAAEEEAELEE 456
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 556-880 3.15e-13

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: 74.29  E-value: 3.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   556 VTMETSMIMSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIER-NQRYVEQSNLMMEKRnnslqtatENTQAKVTEE 634
Cdd:TIGR04523  244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQlNQLKSEISDLNNQKE--------QDWNKELKSE 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   635 LaaataqvshlqlkmTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTS 714
Cdd:TIGR04523  316 L--------------KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS 381

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   715 LEEELTDLRVEKESLEKNLSERKKKSAQErsqaEEEIDEIRKSYqEELDKLRQLLKKTRVStDQAAAEQLSLVQAELQTQ 794
Cdd:TIGR04523  382 YKQEIKNLESQINDLESKIQNQEKLNQQK----DEQIKKLQQEK-ELLEKEIERLKETIIK-NNSEIKDLTNQDSVKELI 455

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   795 WEAkcehlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQN---EQHIKELEKNKSQM-SGVEAAA 870
Cdd:TIGR04523  456 IKN-----LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKkelEEKVKDLTKKISSLkEKIEKLE 530

                          330
                   ....*....|
gi 578817219   871 SDPSEKVKKI 880
Cdd:TIGR04523  531 SEKKEKESKI 540
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 563-895 5.44e-13

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: 73.52  E-value: 5.44e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   563 IMSNIQRIIQENERLKQEILEksnrIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTaTENTQAKVTEELAAATAQV 642
Cdd:TIGR04523  202 LLSNLKKKIQKNKSLESQISE----LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ-LKDEQNKIKKQLSEKQKEL 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   643 SHLQLKMTAHQKKETELQMQLTE--SLKETDL---LRGQLTKVQAKLSELQetSEQAQSkfkseKQNRKQLELKVTSLEE 717
Cdd:TIGR04523  277 EQNNKKIKELEKQLNQLKSEISDlnNQKEQDWnkeLKSELKNQEKKLEEIQ--NQISQN-----NKIISQLNEQISQLKK 349

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   718 ELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIrKSYQEELDKLRQLLKKtrvstdqaaAEQLSlvqAELQTQWEA 797
Cdd:TIGR04523  350 ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI-KNLESQINDLESKIQN---------QEKLN---QQKDEQIKK 416

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   798 kcehlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITAL--------------------TKQN-EQHIKEL 856
Cdd:TIGR04523  417 -----LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLdntresletqlkvlsrsinkIKQNlEQKQKEL 491

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 578817219   857 EKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFELE 895
Cdd:TIGR04523  492 KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 509-897 2.82e-12

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: 71.29  E-value: 2.82e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   509 MTEARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMLIPSMSVTMET--SMIMSNIQRIIQENERLK---QEILE 583
Cdd:pfam05483  309 MSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSleELLRTEQQRLEKNEDQLKiitMELQK 388

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   584 KSNRIEE----QNDKISELIERNQRYVEQSNLMMEKRN-NSLQTATENTQAKVTEELAAATAQVSHLQLKMTA------- 651
Cdd:pfam05483  389 KSSELEEmtkfKNNKEVELEELKKILAEDEKLLDEKKQfEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAiktseeh 468

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   652 HQKKETELQMQL-TESLKETDLL---------RGQLTKVQAKLS-ELQETSEQAQSKFKSEKQNRKQLElkvtSLEEELT 720
Cdd:pfam05483  469 YLKEVEDLKTELeKEKLKNIELTahcdkllleNKELTQEASDMTlELKKHQEDIINCKKQEERMLKQIE----NLEEKEM 544

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   721 DLRVEKESLEKNLSERK-------KKSAQERSQAEEEI--------------DEIRKSYQEELDKLRQLLKKTRVSTDQA 779
Cdd:pfam05483  545 NLRDELESVREEFIQKGdevkcklDKSEENARSIEYEVlkkekqmkilenkcNNLKKQIENKNKNIEELHQENKALKKKG 624

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   780 AAEQLSLVQAELQTQweaKCEHLLASAK---DEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNE---QH- 852
Cdd:pfam05483  625 SAENKQLNAYEIKVN---KLELELASAKqkfEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDkrcQHk 701

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 578817219   853 IKE----LEKNKSQMSGVeAAASDPSEKVKKIMNQVFQSLRREFELEES 897
Cdd:pfam05483  702 IAEmvalMEKHKHQYDKI-IEERDSELGLYKNKEQEQSSAKAALEIELS 749
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
563-892 3.35e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 71.25  E-value: 3.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  563 IMSNIQRI-----IQENERLKQEILEKSNRIEEQNDKISELIERNQRyveqsnlmMEKRNNSLQTATENTQ-AK------ 630
Cdd:PRK03918  370 KKEELERLkkrltGLTPEKLEKELEELEKAKEEIEEEISKITARIGE--------LKKEIKELKKAIEELKkAKgkcpvc 441

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  631 ---VTEE-----LAAATAQVSHLQLKMTAHQKKETELQMQLTE------------SLKET-DLLRG--------QLTKVQ 681
Cdd:PRK03918  442 greLTEEhrkelLEEYTAELKRIEKELKEIEEKERKLRKELRElekvlkkeseliKLKELaEQLKEleeklkkyNLEELE 521

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  682 AKLSELQETSEQA------QSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQErsqAEEEIDEIR 755
Cdd:PRK03918  522 KKAEEYEKLKEKLiklkgeIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEE---LEERLKELE 598

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  756 KSYQE---------ELDKLRQLLKKTRVSTDQAAAEqLSLVQAELQtQWEAKCEHLLASAKDEhlqQYQEVcaqrdayQQ 826
Cdd:PRK03918  599 PFYNEylelkdaekELEREEKELKKLEEELDKAFEE-LAETEKRLE-ELRKELEELEKKYSEE---EYEEL-------RE 666

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817219  827 KLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDpSEKVKKIMNQVfQSLRREF 892
Cdd:PRK03918  667 EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE-LEKLEKALERV-EELREKV 730
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 674-898 1.49e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 69.32  E-value: 1.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   674 RGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAE----- 748
Cdd:TIGR02168  669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqleer 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   749 --------EEIDEIRKSYQEELDKLRQLLKKTRvstdqAAAEQLSLVQAELQTQWEAkcehlLASAKDEHLQQYQEVCAQ 820
Cdd:TIGR02168  749 iaqlskelTELEAEIEELEERLEEAEEELAEAE-----AEIEELEAQIEQLKEELKA-----LREALDELRAELTLLNEE 818

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578817219   821 RDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFELEESY 898
Cdd:TIGR02168  819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 565-883 1.76e-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: 1.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  565 SNIQRIIQENERLKQEIL----EKSNRIEEQNDKISELIERNQRYVEQS--NLMMEKRNNSLQtatentqakvtEELAAA 638
Cdd:COG5185   253 DKLEKLVEQNTDLRLEKLgenaESSKRLNENANNLIKQFENTKEKIAEYtkSIDIKKATESLE-----------EQLAAA 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  639 TAQVSHLQLKMtahqKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNrKQLELKVTSLEEE 718
Cdd:COG5185   322 EAEQELEESKR----ETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFK-DTIESTKESLDEI 396

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  719 LTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLK-KTRVSTDQAAAEQLSLVQA------EL 791
Cdd:COG5185   397 PQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISeLNKVMREADEESQSRLEEAydeinrSV 476

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  792 QTQWEAKCEHL------LASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKC-LALQAQITALTKQNEQHIKELEKNKSQMS 864
Cdd:COG5185   477 RSKKEDLNEELtqiesrVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLkDFMRARGYAHILALENLIPASELIQASNA 556

                         330
                  ....*....|....*....
gi 578817219  865 GVEAAASDPSEKVKKIMNQ 883
Cdd:COG5185   557 KTDGQAANLRTAVIDELTQ 575
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 537-794 3.46e-11

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: 67.79  E-value: 3.46e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   537 VEELQKHSAGNSMLIPSMSVTMEtsmimSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKr 616
Cdd:TIGR02169  246 LASLEEELEKLTEEISELEKRLE-----EIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELED- 319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   617 nnslqtaTENTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQA-------KLSELQE 689
Cdd:TIGR02169  320 -------AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKefaetrdELKDYRE 392

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   690 TSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLE---KNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLR 766
Cdd:TIGR02169  393 KLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEakiNELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY 472

                          250       260
                   ....*....|....*....|....*...
gi 578817219   767 QLLKKTRVSTDQAAAEQLSLVQAELQTQ 794
Cdd:TIGR02169  473 DLKEEYDRVEKELSKLQRELAEAEAQAR 500
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
629-856 3.76e-11

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 67.63  E-value: 3.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  629 AKVTEELAAATAQVSHLQLKMTAHQKKETELQM--QLTESLKETDLLRGQLTKVQAKLSELqetsEQAQSKFKSEKQNRK 706
Cdd:COG4913   620 AELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERL----DASSDDLAALEEQLE 695

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  707 QLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVStdQAAAEQLSL 786
Cdd:COG4913   696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVE--RELRENLEE 773

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578817219  787 VQAELQTQwEAKCEHLLASAKDEHLQQYQEVCAQRDA-------YQQKLVQLQEKCL-ALQAQI-TALTKQNEQHIKEL 856
Cdd:COG4913   774 RIDALRAR-LNRAEEELERAMRAFNREWPAETADLDAdleslpeYLALLDRLEEDGLpEYEERFkELLNENSIEFVADL 851
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 640-899 7.24e-11

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: 67.02  E-value: 7.24e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   640 AQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEEL 719
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   720 TDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEqlslVQAELQtqwEAKC 799
Cdd:TIGR02169  754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE----IEQKLN---RLTL 826

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   800 EHLLASAKDEHLQQYQEVC-AQRDAYQQKLVQLQEKCLALQAQItaltKQNEQHIKELEKNKSqmsgveaaasDPSEKVK 878
Cdd:TIGR02169  827 EKEYLEKEIQELQEQRIDLkEQIKSIEKEIENLNGKKEELEEEL----EELEAALRDLESRLG----------DLKKERD 892

                          250       260
                   ....*....|....*....|.
gi 578817219   879 KIMNQVFQSLRREFELEESYN 899
Cdd:TIGR02169  893 ELEAQLRELERKIEELEAQIE 913
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
613-891 7.76e-11

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 65.31  E-value: 7.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  613 MEKRNNSLQTATENTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSE 692
Cdd:COG4372    18 LRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  693 QAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEknlsERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKT 772
Cdd:COG4372    98 QAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLE----AQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  773 RVSTDQAAAEQLslvqAELQTQWEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQH 852
Cdd:COG4372   174 QALSEAEAEQAL----DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 578817219  853 IKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRRE 891
Cdd:COG4372   250 ELLEEVILKEIEELELAILVEKDTEEEELEIAALELEAL 288
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 673-878 2.14e-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: 64.01  E-value: 2.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  673 LRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLserkKKSAQERSQAEEEID 752
Cdd:COG4942    25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL----AELEKEIAELRAELE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  753 EIRKSYQEELDKL-----------------------RQLLKKTRVSTDQAAAEQLSLVQAELQTQweakcEHLLASAKDE 809
Cdd:COG4942   101 AQKEELAELLRALyrlgrqpplalllspedfldavrRLQYLKYLAPARREQAEELRADLAELAAL-----RAELEAERAE 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578817219  810 HLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVK 878
Cdd:COG4942   176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 635-851 2.77e-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: 63.63  E-value: 2.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  635 LAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQskfksekQNRKQLELKVTS 714
Cdd:COG4942    15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE-------QELAALEAELAE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  715 LEEELTDLRVEKESLEKNLSERKKK--------------SAQERSQA--------------EEEIDEIRKSyQEELDKLR 766
Cdd:COG4942    88 LEKEIAELRAELEAQKEELAELLRAlyrlgrqpplalllSPEDFLDAvrrlqylkylaparREQAEELRAD-LAELAALR 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  767 QLLkktrvstdQAAAEQLSLVQAELQTQWEAkcehlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALT 846
Cdd:COG4942   167 AEL--------EAERAELEALLAELEEERAA-----LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233


                  ....*
gi 578817219  847 KQNEQ 851
Cdd:COG4942   234 AEAAA 238
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 518-898 3.57e-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: 64.36  E-value: 3.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   518 EIRMAVSKVADKMDHLMTKVEELQKHsAGNSMLipSMSVTMETSMimSNIQRIIQE-----NERLKQ------EILEKSN 586
Cdd:pfam05483  180 ETRQVYMDLNNNIEKMILAFEELRVQ-AENARL--EMHFKLKEDH--EKIQHLEEEykkeiNDKEKQvsllliQITEKEN 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   587 R-------IEEQNDKISELIERNQRYVEQSNLMMEKRNN----------SLQTATeNTQAKVTEELAAATAQVSHLqlkm 649
Cdd:pfam05483  255 KmkdltflLEESRDKANQLEEKTKLQDENLKELIEKKDHltkeledikmSLQRSM-STQKALEEDLQIATKTICQL---- 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   650 tahqKKETELQMQLTESLKETDLLrgQLTKVQAKLSELQETSEQAQSKFKSEKQNRK--QLELKVTSLE-EELTDLR--- 723
Cdd:pfam05483  330 ----TEEKEAQMEELNKAKAAHSF--VVTEFEATTCSLEELLRTEQQRLEKNEDQLKiiTMELQKKSSElEEMTKFKnnk 403

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   724 -VEKESLEKNLSERKK---------KSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVStDQAAAEQLSLVQAELQ- 792
Cdd:pfam05483  404 eVELEELKKILAEDEKlldekkqfeKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTS-EEHYLKEVEDLKTELEk 482

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   793 -----TQWEAKCEHLLASAKD---------EHLQQYQEVCAQRDAYQQKLVQ----LQEKCLALQAQITALTKQNEQHIK 854
Cdd:pfam05483  483 eklknIELTAHCDKLLLENKEltqeasdmtLELKKHQEDIINCKKQEERMLKqienLEEKEMNLRDELESVREEFIQKGD 562

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*...
gi 578817219   855 E----LEKNKSQMSGVEAAASdPSEKVKKIMNQVFQSLRREFELEESY 898
Cdd:pfam05483  563 EvkckLDKSEENARSIEYEVL-KKEKQMKILENKCNNLKKQIENKNKN 609
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 573-863 3.65e-10

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: 64.28  E-value: 3.65e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   573 ENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQAKVTEELAAATAQVSHLQLKMTAH 652
Cdd:pfam05667  223 EEEWNSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTH 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   653 QKKET---ELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESL 729
Cdd:pfam05667  303 TEKLQftnEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEEL 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   730 EKNLsERKKKSAQERSQAEEEIdeirksyqeelDKLRQLLkktrvstdQAAAEQLslvqAELQTQWEAKCEHLLasakdE 809
Cdd:pfam05667  383 EKQY-KVKKKTLDLLPDAEENI-----------AKLQALV--------DASAQRL----VELAGQWEKHRVPLI-----E 433

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 578817219   810 HLQQYQEVCA-QRDAYQQKLVQLQ---EKCLalqaQITALTKQNEQHIKELEKNKSQM 863
Cdd:pfam05667  434 EYRALKEAKSnKEDESQRKLEEIKelrEKIK----EVAEEAKQKEELYKQLVAEYERL 487
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
566-892 4.32e-10

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 64.02  E-value: 4.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  566 NIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRnNSLQTATENTQAKVTEELAAATAQVSHL 645
Cdd:COG4717   126 QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQ-EELEELLEQLSLATEEELQDLAEELEEL 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  646 QLKMTAHQKKETELQMQLTESLKETDLLRGQLT--KVQAKLSELQET--------------------------------- 690
Cdd:COG4717   205 QQRLAELEEELEEAQEELEELEEELEQLENELEaaALEERLKEARLLlliaaallallglggsllsliltiagvlflvlg 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  691 ------------SEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVeKESLEKNLSERKKKSAQERSQAEEEIDEIRKSY 758
Cdd:COG4717   285 llallflllareKASLGKEAEELQALPALEELEEEELEELLAALGL-PPDLSPEELLELLDRIEELQELLREAEELEEEL 363

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  759 QEE--LDKLRQLLKKTRVSTD-------------QAAAEQLSLVQAELQTQWEAKCEHLLASAKDEHLQQYQEVCAQRDA 823
Cdd:COG4717   364 QLEelEQEIAALLAEAGVEDEeelraaleqaeeyQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEE 443

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578817219  824 YQQKLVQLQEKCLALQAQITALTKQNE-----QHIKELEKNKSQMsgVEAAASDpsEKVKKIMNQVFQSLRREF 892
Cdd:COG4717   444 LEEELEELREELAELEAELEQLEEDGElaellQELEELKAELREL--AEEWAAL--KLALELLEEAREEYREER 513
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 567-771 4.34e-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: 64.27  E-value: 4.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   567 IQRIIQENERLKQEI--LEKS------------NRIEEQNDKISEL---IERNQRYVEQSNLMMEKRNNSLQTATENTQa 629
Cdd:TIGR04523  428 IERLKETIIKNNSEIkdLTNQdsvkeliiknldNTRESLETQLKVLsrsINKIKQNLEQKQKELKSKEKELKKLNEEKK- 506

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   630 KVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKE-----TDLLRGQLTKV----QAKLSELQET---SEQAQSK 697
Cdd:TIGR04523  507 ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDElnkddFELKKENLEKEidekNKEIEELKQTqksLKKKQEE 586

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   698 FK-------SEKQN-RKQLELK---VTSLEEELTDLRVEKESLE---KNLSERKKKSAQERSQAEEEIDEIRKSYQEELD 763
Cdd:TIGR04523  587 KQelidqkeKEKKDlIKEIEEKekkISSLEKELEKAKKENEKLSsiiKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIK 666


                   ....*...
gi 578817219   764 KLRQLLKK 771
Cdd:TIGR04523  667 KIKESKTK 674
PTZ00121 PTZ00121
MAEBL; Provisional
 575-855 5.71e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.01  E-value: 5.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  575 ERLKQEILEKSNRIEEQNDKiseliernqRYVEQSNLMMEKRNNSLQTATENTQAKvtEELAAATAQVSHLQLKMTAHQK 654
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAEEK---------KKAEEAKKAEEDKNMALRKAEEAKKAE--EARIEEVMKLYEEEKKMKAEEA 1612

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  655 KETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQ------------AQSKFKSEKQNRKQLELKVtslEEEltDL 722
Cdd:PTZ00121 1613 KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElkkaeeenkikaAEEAKKAEEDKKKAEEAKK---AEE--DE 1687

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  723 RVEKESLEKNlSERKKKSAQERSQAEEEI---DEIRKSYQEELDKLRQLLKKTRvsTDQAAAEQLSLVQAElqtqwEAKC 799
Cdd:PTZ00121 1688 KKAAEALKKE-AEEAKKAEELKKKEAEEKkkaEELKKAEEENKIKAEEAKKEAE--EDKKKAEEAKKDEEE-----KKKI 1759

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578817219  800 EHLlasaKDEHLQQYQEVCAQRDAY-QQKLVQLQEKCLALQAQITALTKQNEQHIKE 855
Cdd:PTZ00121 1760 AHL----KKEEEKKAEEIRKEKEAViEEELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 568-880 1.56e-09

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 62.45  E-value: 1.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   568 QRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEkRNNSL------QTATENTQAKvTEELAAATAQ 641
Cdd:pfam17380  299 ERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME-RERELerirqeERKRELERIR-QEEIAMEISR 376

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   642 VSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQetseqaqsKFKSEKQNRKQLELKVTSLEEELTD 721
Cdd:pfam17380  377 MRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEME--------QIRAEQEEARQREVRRLEEERAREM 448

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   722 LRVEKESLEKNLS-ERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQ---LSLVQAELQTQWEA 797
Cdd:pfam17380  449 ERVRLEEQERQQQvERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEerkRKLLEKEMEERQKA 528

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   798 KCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKclalqAQITALTKQNE--QHIKELEKNKSqmsgvEAAASDPSE 875
Cdd:pfam17380  529 IYEEERRREAEEERRKQQEMEERRRIQEQMRKATEER-----SRLEAMEREREmmRQIVESEKARA-----EYEATTPIT 598


                   ....*
gi 578817219   876 KVKKI 880
Cdd:pfam17380  599 TIKPI 603
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 191-309 1.80e-09

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 60.16  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  191 GPAVEVGDSLEVAYTGWLfqnhVLGQVFDSTANKDKLLRLKLGSgkVIKGWEDGMLGMKKGGKRLLIVPPACAVGSEGVI 270
Cdd:PRK10902  158 GEAPKDSDTVVVNYKGTL----IDGKEFDNSYTRGEPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVP 231

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 578817219  271 GWtqATDSILVFEVEVRRVKFARDSGSDGHSVSSRDSAA 309
Cdd:PRK10902  232 GI--PANSTLVFDVELLDVKPAPKADAKPEADAKAADSA 268
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
654-871 1.88e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 62.09  E-value: 1.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  654 KKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQaqskfksekqnRKQLELKVTSLEEELTDLRVEKESLEKnl 733
Cdd:COG4717    64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE-----------LEELEAELEELREELEKLEKLLQLLPL-- 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  734 serkkksAQERSQAEEEIDEirksYQEELDKLRQllKKTRVSTDQAAAEQLSLVQAELQTQWEAKCEHLLASAKDE---H 810
Cdd:COG4717   131 -------YQELEALEAELAE----LPERLEELEE--RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdL 197

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817219  811 LQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALtkQNEQHIKELEKNKSQMSGVEAAAS 871
Cdd:COG4717   198 AEELEELQQRLAELEEELEEAQEELEELEEELEQL--ENELEAAALEERLKEARLLLLIAA 256
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 567-896 3.54e-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: 61.19  E-value: 3.54e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   567 IQRIIQENER---LKQEILEKSNRIEEQNDKISELIE---------------RNQRYVEQSNLMMEKRNNSLQTATENTQ 628
Cdd:TIGR04523   67 EEKINNSNNKikiLEQQIKDLNDKLKKNKDKINKLNSdlskinseikndkeqKNKLEVELNKLEKQKKENKKNIDKFLTE 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   629 AKVTE-ELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTK-----------------VQAKLSELQET 690
Cdd:TIGR04523  147 IKKKEkELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKlelllsnlkkkiqknksLESQISELKKQ 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   691 SEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKksaqERSQAEEEIDEIRKSYQEELDKLRQLLK 770
Cdd:TIGR04523  227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQK----ELEQNNKKIKELEKQLNQLKSEISDLNN 302

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   771 KTRVSTDQAAAEQLSLVQ---AELQTQWeAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKclalQAQITALTK 847
Cdd:TIGR04523  303 QKEQDWNKELKSELKNQEkklEEIQNQI-SQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEK----QNEIEKLKK 377

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 578817219   848 QNEQHIKELEKNKSQMSGVEAAASDpSEKVKKIMNQVFQSLRREFELEE 896
Cdd:TIGR04523  378 ENQSYKQEIKNLESQINDLESKIQN-QEKLNQQKDEQIKKLQQEKELLE 425
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
564-895 3.92e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 61.23  E-value: 3.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  564 MSNIQRIIQENERLKQEILEKSNRIEEQNDKISElIERNQRYVEQSNLMMEKRNNSLqtatentqakvtEELAAATAQVS 643
Cdd:PRK03918  178 IERLEKFIKRTENIEELIKEKEKELEEVLREINE-ISSELPELREELEKLEKEVKEL------------EELKEEIEELE 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  644 HLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQ--AQSKFKSEKQNRKQlelkvtSLEEELTD 721
Cdd:PRK03918  245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELR------EIEKRLSR 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  722 LRVEKESLEKNLSERKKKSAqERSQAEEEIDEIRKSYQE------ELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQW 795
Cdd:PRK03918  319 LEEEINGIEERIKELEEKEE-RLEELKKKLKELEKRLEEleerheLYEEAKAKKEELERLKKRLTGLTPEKLEKELEELE 397

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  796 EAKCEHLLASAK-DEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITaltkqnEQHIKEL-EKNKSQMSGVEaaasdp 873
Cdd:PRK03918  398 KAKEEIEEEISKiTARIGELKKEIKELKKAIEELKKAKGKCPVCGRELT------EEHRKELlEEYTAELKRIE------ 465

                         330       340
                  ....*....|....*....|..
gi 578817219  874 sEKVKKIMNQVFQSLRREFELE 895
Cdd:PRK03918  466 -KELKEIEEKERKLRKELRELE 486
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 573-892 5.30e-09

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: 60.75  E-value: 5.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   573 ENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQ-TATENTQAKVTEELAAA----TAQVSHLQL 647
Cdd:TIGR00618  436 QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQeTRKKAVVLARLLELQEEpcplCGSCIHPNP 515

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   648 KMTAHQKKETeLQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKE 727
Cdd:TIGR00618  516 ARQDIDNPGP-LTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITV 594

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   728 SLEKnlsERKKKSAQERSQAEEEIDEIRKSyQEELDKLRQLLKKTRVSTDQAAAEqLSLVQAELQTQWEAKCEHLLASAK 807
Cdd:TIGR00618  595 RLQD---LTEKLSEAEDMLACEQHALLRKL-QPEQDLQDVRLHLQQCSQELALKL-TALHALQLTLTQERVREHALSIRV 669

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   808 DEhLQQYQEVCAQRDAYQQKLVQLQEKCLALqAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQS 887
Cdd:TIGR00618  670 LP-KELLASRQLALQKMQSEKEQLTYWKEML-AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKE 747


                   ....*
gi 578817219   888 LRREF 892
Cdd:TIGR00618  748 LMHQA 752
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 649-822 5.31e-09

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 58.01  E-value: 5.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  649 MTAHQKKETELQmqltESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDL--RVEK 726
Cdd:COG1579     2 MPEDLRALLDLQ----ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVeaRIKK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  727 --------------ESLEK---NLSERKKKSAQERSQAEEEIDEIRKSY---QEELDKLRQLLKKTRVSTDQAAAEqlsl 786
Cdd:COG1579    78 yeeqlgnvrnnkeyEALQKeieSLKRRISDLEDEILELMERIEELEEELaelEAELAELEAELEEKKAELDEELAE---- 153

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 578817219  787 VQAELQTQwEAKCEHLLASAKDEHLQQYQEVCAQRD 822
Cdd:COG1579   154 LEAELEEL-EAEREELAAKIPPELLALYERIRKRKN 188
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 525-904 6.91e-09

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: 60.37  E-value: 6.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   525 KVADKMDHLMTKVEELQKHSAGNSMLIPSMSVTmETSMIMSNIQRIIQENERL--KQEILEKSNRIEEQNDKISELIERN 602
Cdd:pfam02463  630 KDTELTKLKESAKAKESGLRKGVSLEEGLAEKS-EVKASLSELTKELLEIQELqeKAESELAKEEILRRQLEIKKKEQRE 708

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   603 QRYVEQSNLMMEKRNNSLQTATENTQAKVTEELaaataqvshlqlkmtahQKKETELQMQLTESLKEtdllrgQLTKVQA 682
Cdd:pfam02463  709 KEELKKLKLEAEELLADRVQEAQDKINEELKLL-----------------KQKIDEEEEEEEKSRLK------KEEKEEE 765

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   683 KLSELQETSEQAQSKFKSEKQ-NRKQLELKVTSLEEELTdlrvEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEE 761
Cdd:pfam02463  766 KSELSLKEKELAEEREKTEKLkVEEEKEEKLKAQEEELR----ALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALE 841

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   762 L--DKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWEAKCEHLLASAKDEHLQQYQEvcaqrdayQQKLVQLQEKCLALQ 839
Cdd:pfam02463  842 LkeEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEE--------KKELEEESQKLNLLE 913

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578817219   840 AQITALTKQNEQHIKELEKNKSQ---MSGVEAAASDPSEKVKKIMNQVFQSLRREFELEESYNGRTIL 904
Cdd:pfam02463  914 EKENEIEERIKEEAEILLKYEEEpeeLLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIE 981
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
609-843 1.16e-08

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 59.26  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  609 SNLMMEKRNNSLQTATENTQAKVTEELAAATAQVSHLQLKMTAHQKKE--TELQMQLTESLKETDLLRGQLTKVQAKLSE 686
Cdd:COG3206   158 AEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAE 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  687 LQETSEQAQSKFKSEKQNRKQL--ELKVTSLEEELTDLRVEKESLEKNLSERkkksAQERSQAEEEIDEIRKSYQEELDK 764
Cdd:COG3206   238 AEARLAALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAELAELSARYTPN----HPDVIALRAQIAALRAQLQQEAQR 313

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578817219  765 LRQLLkKTRVSTDQAAAEQLSLVQAELQTQWEAkcehlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEkcLALQAQIT 843
Cdd:COG3206   314 ILASL-EAELEALQAREASLQAQLAQLEARLAE-----LPELEAELRRLEREVEVARELYESLLQRLEE--ARLAEALT 384
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 648-793 1.27e-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: 56.45  E-value: 1.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   648 KMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQaqskFKSEKQNRKQLELKVTSLEEELTDLRVEKE 727
Cdd:pfam13851   34 EIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLEN----YEKDKQSLKNLKARLKVLEKELKDLKWEHE 109

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817219   728 SLEknlsERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKtRVstdQAAAEQLSLVQAELQT 793
Cdd:pfam13851  110 VLE----QRFEKVERERDELYDKFEAAIQDVQQKTGLKNLLLEK-KL---QALGETLEKKEAQLNE 167
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 563-795 1.38e-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: 1.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  563 IMSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLM------MEKRNNSLQTATENTQAKVTEELA 636
Cdd:COG4942    32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeaelaeLEKEIAELRAELEAQKEELAELLR 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  637 AA--TAQVSHLQLKMTAHQKKETELQMQLTESLKETDllRGQLTKVQAKLSELQetseqaqskfksekQNRKQLELKVTS 714
Cdd:COG4942   112 ALyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPAR--REQAEELRADLAELA--------------ALRAELEAERAE 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  715 LEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEElDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQ 794
Cdd:COG4942   176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA-EELEALIARLEAEAAAAAERTPAAGFAALKGK 254


                  .
gi 578817219  795 W 795
Cdd:COG4942   255 L 255
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
577-797 1.43e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 59.01  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  577 LKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATEnTQAKVTEELAAATAQVSHLQlkmtaHQKKE 656
Cdd:COG4717    47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQE-ELEELEEELEELEAELEELR-----EELEK 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  657 TELQMQLTESLKETDLLRGQLTKVQAKLSELQEtseqaqskfksEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSER 736
Cdd:COG4717   121 LEKLLQLLPLYQELEALEAELAELPERLEELEE-----------RLEELRELEEELEELEAELAELQEELEELLEQLSLA 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817219  737 KKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWEA 797
Cdd:COG4717   190 TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
631-883 1.51e-08

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 57.61  E-value: 1.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  631 VTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLEL 710
Cdd:COG1340     6 LSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  711 KVTSLEEELTDLRVEKESLEKNLSERKKKSAQ----ERSQ------AEEE---IDEIRKsYQEELDKLRQLLKKTR-VST 776
Cdd:COG1340    86 KLNELREELDELRKELAELNKAGGSIDKLRKEierlEWRQqtevlsPEEEkelVEKIKE-LEKELEKAKKALEKNEkLKE 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  777 DQAAAEQLSLVQAELQTQWEAKCEhLLASAKDEHLQQYQ---EVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHI 853
Cdd:COG1340   165 LRAELKELRKEAEEIHKKIKELAE-EAQELHEEMIELYKeadELRKEADELHKEIVEAQEKADELHEEIIELQKELRELR 243

                         250       260       270
                  ....*....|....*....|....*....|..
gi 578817219  854 KELE--KNKSQMSGVEAAASDPSEKVKKIMNQ 883
Cdd:COG1340   244 KELKklRKKQRALKREKEKEELEEKAEEIFEK 275
PRK11281 PRK11281
mechanosensitive channel MscK;
618-857 2.17e-08

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 58.77  E-value: 2.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  618 NSLQTATENTQAKVTEELAAATAQVSHLQLKMTAHQKKETE-LQMQLTESLKetdllrgQLTKVQAKLSELQEtSEQAQS 696
Cdd:PRK11281   43 AQLDALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEqLKQQLAQAPA-------KLRQAQAELEALKD-DNDEET 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  697 KFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSerKKKSAQERSQAeeEIDEirksYQEELDKLRQLLKKTRVST 776
Cdd:PRK11281  115 RETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLV--SLQTQPERAQA--ALYA----NSQRLQQIRNLLKGGKVGG 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  777 DQAAAEQLSLVQAELQtqweakcehlLASAKDEHLQQ-----------YQevcAQRDAYQQKLVQLQEKCLALQAQITA- 844
Cdd:PRK11281  187 KALRPSQRVLLQAEQA----------LLNAQNDLQRKslegntqlqdlLQ---KQRDYLTARIQRLEHQLQLLQEAINSk 253

                         250
                  ....*....|...
gi 578817219  845 LTKQNEQHIKELE 857
Cdd:PRK11281  254 RLTLSEKTVQEAQ 266
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
568-897 2.93e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.86  E-value: 2.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  568 QRIIQENERLKQEILEKSNRIEEQNDKISELiERNQRYVEQSNLMMEKRNnslQTATENTQAkvtEELAAATAQVSHLQL 647
Cdd:COG4717    91 AELQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEA---ELAELPERL---EELEERLEELRELEE 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  648 KMTAHQKKETELQMQLTESLKETDL-LRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRvEK 726
Cdd:COG4717   164 ELEELEAELAELQEELEELLEQLSLaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA-LE 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  727 ESLEKN-------------------------------------------LSERKKKSAQERSQAEEEIDEIRKSYQEELD 763
Cdd:COG4717   243 ERLKEArlllliaaallallglggsllsliltiagvlflvlgllallflLLAREKASLGKEAEELQALPALEELEEEELE 322

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  764 KLRQLLKKTRVSTDQAAAEQLSLVQA--ELQTQW------------EAKCEHLLASAKDEHLQQYQEVCAQRDAYQqklv 829
Cdd:COG4717   323 ELLAALGLPPDLSPEELLELLDRIEElqELLREAeeleeelqleelEQEIAALLAEAGVEDEEELRAALEQAEEYQ---- 398

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817219  830 QLQEKCLALQAQITALTKQNEQHIKELEKN--KSQMSGVEAAASDPSEKVKKIMNQVfQSLRREFE-LEES 897
Cdd:COG4717   399 ELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREEL-AELEAELEqLEED 468
Filament pfam00038
Intermediate filament protein;
588-869 3.23e-08

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 56.85  E-value: 3.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   588 IEEQNDKISELIERnQRYVEQSNLMMEkrnnslqtatentqAKVTEELAAATAQVSHLQLkmtAHQKKETELQMQLtesl 667
Cdd:pfam00038    6 LQELNDRLASYIDK-VRFLEQQNKLLE--------------TKISELRQKKGAEPSRLYS---LYEKEIEDLRRQL---- 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   668 ketDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRkqlelkvTSLEEELTDLR--VEKESLEKNLSERKKKSAQErs 745
Cdd:pfam00038   64 ---DTLTVERARLQLELDNLRLAAEDFRQKYEDELNLR-------TSAENDLVGLRkdLDEATLARVDLEAKIESLKE-- 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   746 qaeeEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQA--ELQTQWEAKCEHLLASAKDEHLQQYQEVCAQRD- 822
Cdd:pfam00038  132 ----ELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSAlaEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAAr 207

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578817219   823 ------AYQQKLVQLQEKCLALQAQITALTKQN-----------EQHIKELEKNKSQMSGVEAA 869
Cdd:pfam00038  208 ngdalrSAKEEITELRRTIQSLEIELQSLKKQKaslerqlaeteERYELQLADYQELISELEAE 271
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
635-861 3.93e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.00  E-value: 3.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  635 LAAATAQVSHLQLKMTAHQKKETELQmQLtESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKsekqnrkqlELKVTS 714
Cdd:COG4913   224 FEAADALVEHFDDLERAHEALEDARE-QI-ELLEPIRELAERYAAARERLAELEYLRAALRLWFA---------QRRLEL 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  715 LEEELTDLRVEKESLEknlsERKKKSAQERSQAEEEIDEIRKSYQE----ELDKLRQLLKktrvstdqAAAEQLSLVQAE 790
Cdd:COG4913   293 LEAELEELRAELARLE----AELERLEARLDALREELDELEAQIRGnggdRLEQLEREIE--------RLERELEERERR 360

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578817219  791 LQtQWEAKCEHL---LASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQH---IKELEKNKS 861
Cdd:COG4913   361 RA-RLEALLAALglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELeaeIASLERRKS 436
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 625-771 5.75e-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: 54.93  E-value: 5.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  625 ENTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSE-QA-QSKFKSEK 702
Cdd:COG1579    23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyEAlQKEIESLK 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578817219  703 QNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKK 771
Cdd:COG1579   103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
555-783 6.68e-08

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 55.69  E-value: 6.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  555 SVTMETSMIMSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQAK--VT 632
Cdd:COG1340     5 ELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERdeLN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  633 EELAAATAQVSHLQLKMTAHQKKETELQ-----------MQLTESL---KETDL------LRGQLTKVQAKL---SELQE 689
Cdd:COG1340    85 EKLNELREELDELRKELAELNKAGGSIDklrkeierlewRQQTEVLspeEEKELvekikeLEKELEKAKKALeknEKLKE 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  690 TSEQAQSKFKSEKQNRKQLE----------LKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKsYQ 759
Cdd:COG1340   165 LRAELKELRKEAEEIHKKIKelaeeaqelhEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE-LR 243

                         250       260
                  ....*....|....*....|....
gi 578817219  760 EELDKLRQLLKKTRVSTDQAAAEQ 783
Cdd:COG1340   244 KELKKLRKKQRALKREKEKEELEE 267
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 653-896 6.86e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.99  E-value: 6.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   653 QKKETELQMQLTEslkeTDLLRGQ--LTKVQAKLSELQETSEQAQsKFKSEKQNRKQLELKVTsleeeLTDLRVEKESLE 730
Cdd:TIGR02168  173 RRKETERKLERTR----ENLDRLEdiLNELERQLKSLERQAEKAE-RYKELKAELRELELALL-----VLRLEELREELE 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   731 KNLSErKKKSAQERSQAEEEIDEirksYQEELDKLRqlLKKTRVSTDQAAAeqlslvQAELQTQWEAKcehllaSAKDEH 810
Cdd:TIGR02168  243 ELQEE-LKEAEEELEELTAELQE----LEEKLEELR--LEVSELEEEIEEL------QKELYALANEI------SRLEQQ 303

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   811 LQQYQEvcaqrdayqqKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRR 890
Cdd:TIGR02168  304 KQILRE----------RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR 373


                   ....*.
gi 578817219   891 EFELEE 896
Cdd:TIGR02168  374 LEELEE 379
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
565-904 8.01e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 57.00  E-value: 8.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  565 SNIQRIIQENE----RLKQEILEKSNRIEEQNDKISELIERNQRY------VEQSNLMMEKRNNSLQTATE---NTQAKV 631
Cdd:PRK03918  189 ENIEELIKEKEkeleEVLREINEISSELPELREELEKLEKEVKELeelkeeIEELEKELESLEGSKRKLEEkirELEERI 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  632 TE------ELAAATAQVSHLQLKMTAHQKKEtELQMQLTESL----KETDLLRGQLTKVQAKLSELQETSEQAQSKFKSE 701
Cdd:PRK03918  269 EElkkeieELEEKVKELKELKEKAEEYIKLS-EFYEEYLDELreieKRLSRLEEEINGIEERIKELEEKEERLEELKKKL 347

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  702 KQNRKQLElKVTSLEEELTDLRVEKESLEKnlsERKKKSAQERSQAEEEIDEIRKS---YQEELDKLRQLLK--KTRVST 776
Cdd:PRK03918  348 KELEKRLE-ELEERHELYEEAKAKKEELER---LKKRLTGLTPEKLEKELEELEKAkeeIEEEISKITARIGelKKEIKE 423

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  777 DQAAAEQLS-------LVQAELQtqwEAKCEHLLASAKDEH---LQQYQEVCAQRDAYQQKLVQLqEKCLALQAQITALT 846
Cdd:PRK03918  424 LKKAIEELKkakgkcpVCGRELT---EEHRKELLEEYTAELkriEKELKEIEEKERKLRKELREL-EKVLKKESELIKLK 499

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578817219  847 KQNEQhIKELEK--NKSQMSGVEAAASDpSEKVKKIMNQV---FQSLRREFELEESYNGRTIL 904
Cdd:PRK03918  500 ELAEQ-LKELEEklKKYNLEELEKKAEE-YEKLKEKLIKLkgeIKSLKKELEKLEELKKKLAE 560
CCCAP pfam15964
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ...
 572-896 1.35e-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: 56.07  E-value: 1.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   572 QENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATEntqaKVTEELAAATAQVSHLQLKMTA 651
Cdd:pfam15964  367 RQKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVE----KVTREKNSLVSQLEEAQKQLAS 442

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   652 HQKKET----ELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSE-KQNRKQLE-------------LKVT 713
Cdd:pfam15964  443 QEMDVTkvcgEMRYQLNQTKMKKDEAEKEHREYRTKTGRQLEIKDQEIEKLGLElSESKQRLEqaqqdaarareecLKLT 522

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   714 SL----EEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEideirksyqeeldkLRQLLKKTRVSTDQAAAEQLSLV-- 787
Cdd:pfam15964  523 ELlgesEHQLHLTRLEKESIQQSFSNEAKAQALQAQQREQE--------------LTQKMQQMEAQHDKTVNEQYSLLts 588

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   788 QAELQTQWEAKCeHLLASAKDEHLQQYQEVCAQrdaYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVE 867
Cdd:pfam15964  589 QNTFIAKLKEEC-CTLAKKLEEITQKSRSEVEQ---LSQEKEYLQDRLEKLQKRNEELEEQCVQHGRMHERMKQRLRQLD 664

                          330       340
                   ....*....|....*....|....*....
gi 578817219   868 AAASDPSEKVKKIMNQVFQSLRREFELEE 896
Cdd:pfam15964  665 KHCQATAQQLVQLLSKQNQLFKERQNLTE 693
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 572-893 2.13e-07

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 55.57  E-value: 2.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   572 QENERLKQEILEKSNRIEEQNDKISELIERnqryVEQSNLMMEKRNNSLQTATENTQAKVTEElaaaTAQVSHLQLKMTA 651
Cdd:pfam01576  422 SESERQRAELAEKLSKLQSELESVSSLLNE----AEGKNIKLSKDVSSLESQLQDTQELLQEE----TRQKLNLSTRLRQ 493

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   652 HQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQ----------ETSEQAQSKFKSEKQN-RKQLELKV-------- 712
Cdd:pfam01576  494 LEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKkkleedagtlEALEEGKKRLQRELEAlTQQLEEKAaaydklek 573

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   713 --TSLEEELTDLRVEKESLEKNLS--ERKKKS---------------AQERSQAE------------------------E 749
Cdd:pfam01576  574 tkNRLQQELDDLLVDLDHQRQLVSnlEKKQKKfdqmlaeekaisaryAEERDRAEaeareketralslaraleealeakE 653

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   750 EIDEIRKSYQEELDKL----------RQLLKKTRVSTDQAAAE---QLSLVQAELQTQWEAK--CEHLLASAKDEHLQQY 814
Cdd:pfam01576  654 ELERTNKQLRAEMEDLvsskddvgknVHELERSKRALEQQVEEmktQLEELEDELQATEDAKlrLEVNMQALKAQFERDL 733

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   815 QevcAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHI---KELEKN-KSQMSGVEAAASDPSEKVK--KIMNQVFQSL 888
Cdd:pfam01576  734 Q---ARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVaakKKLELDlKELEAQIDAANKGREEAVKqlKKLQAQMKDL 810


                   ....*
gi 578817219   889 RREFE 893
Cdd:pfam01576  811 QRELE 815
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
573-791 2.16e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.69  E-value: 2.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  573 ENERLKQEILEksnRIEEQNDKISEL---IERNQRYVEQSNL-MMEKRNNSLQTATENTQakvtEELAAATAQVSHLQLK 648
Cdd:COG4913   245 EDAREQIELLE---PIRELAERYAAArerLAELEYLRAALRLwFAQRRLELLEAELEELR----AELARLEAELERLEAR 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  649 MTAHQKKETELQMQLTES-LKETDLLRGQLTKVQAKLSELQETSEQAQSKFKsekqnrkQLELKVTSLEEELTDLRveke 727
Cdd:COG4913   318 LDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLA-------ALGLPLPASAEEFAALR---- 386

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578817219  728 sleKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQL------LKKTRVSTDQ-------AAAEQLSLVQAEL 791
Cdd:COG4913   387 ---AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELeaeiasLERRKSNIPArllalrdALAEALGLDEAEL 460
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 621-875 2.28e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 54.45  E-value: 2.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  621 QTATENTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQET-SEQAQSKFK 699
Cdd:COG3883    18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERARALYR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  700 SEKQNrKQLELKVTSleEELTDLrVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKtrVSTDQA 779
Cdd:COG3883    98 SGGSV-SYLDVLLGS--ESFSDF-LDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE--LEAAKA 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  780 AAEQLSLVQAELQTQweakcehlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKN 859
Cdd:COG3883   172 ELEAQQAEQEALLAQ--------LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243

                         250
                  ....*....|....*.
gi 578817219  860 KSQMSGVEAAASDPSE 875
Cdd:COG3883   244 ASAAGAGAAGAAGAAA 259
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 571-896 2.36e-07

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: 54.15  E-value: 2.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   571 IQENERLKQEILEKSNRIEEQndkiseliernqryveqsnlMMEKRNNSLQTATENTQAKVTEELAAATAqvshLQLKMT 650
Cdd:pfam13868   28 IAEKKRIKAEEKEEERRLDEM--------------------MEEERERALEEEEEKEEERKEERKRYRQE----LEEQIE 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   651 AHQKKEtelQMQLTESLKETDLLRGQLTKVQAKlselqetsEQAQSKFKSEKQNRKQLELKVTSleeELTDLRVEKESLE 730
Cdd:pfam13868   84 EREQKR---QEEYEEKLQEREQMDEIVERIQEE--------DQAEAEEKLEKQRQLREEIDEFN---EEQAEWKELEKEE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   731 KNLSERK-----KKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRvsTDQAAAEQL--SLVQAELQTQW-------E 796
Cdd:pfam13868  150 EREEDERileylKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQ--DEKAERDELraKLYQEEQERKErqkereeA 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   797 AKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQhiKELEKNKSQMSGVEAAASDPSEK 876
Cdd:pfam13868  228 EKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAE--KRRMKRLEHRRELEKQIEEREEQ 305

                          330       340
                   ....*....|....*....|
gi 578817219   877 VKKIMNQVFQSLRREFELEE 896
Cdd:pfam13868  306 RAAEREEELEEGERLREEEA 325
PRK11281 PRK11281
mechanosensitive channel MscK;
566-795 2.53e-07

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 55.30  E-value: 2.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  566 NIQRIIQENERLKQEILEKSNRIEEQNDKISELIERN-----QRYVEQSNLMMEKRNNSLQTATENTQakvtEELAAATA 640
Cdd:PRK11281   74 KIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNdeetrETLSTLSLRQLESRLAQTLDQLQNAQ----NDLAEYNS 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  641 QVSHLQLK-------MTAHQKKETELQMQLTESLKETDLLRG-QLTKVQAKLS------ELQETSEQAQSKFKS--EKQn 704
Cdd:PRK11281  150 QLVSLQTQperaqaaLYANSQRLQQIRNLLKGGKVGGKALRPsQRVLLQAEQAllnaqnDLQRKSLEGNTQLQDllQKQ- 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  705 RKQLELKVTSLEEELTDLRvekESL-EKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAaeq 783
Cdd:PRK11281  229 RDYLTARIQRLEHQLQLLQ---EAInSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLLKATEKLN--- 302

                         250
                  ....*....|...
gi 578817219  784 lSLVQAELQT-QW 795
Cdd:PRK11281  303 -TLTQQNLRVkNW 314
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 562-893 3.25e-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: 54.80  E-value: 3.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   562 MIMSNIQRIIQENERLKQEiLEKSNRIEEqndkiSELIERNQRYVEQSNLMMEKRNNslqtatentQAKVTEELAAATAQ 641
Cdd:pfam01576  187 AMISDLEERLKKEEKGRQE-LEKAKRKLE-----GESTDLQEQIAELQAQIAELRAQ---------LAKKEEELQAALAR 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   642 VSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKV-----------QAKLSELQET--SEQAQSKFKSEKQN---- 704
Cdd:pfam01576  252 LEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAekqrrdlgeelEALKTELEDTldTTAAQQELRSKREQevte 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   705 -RKQLELKVTSLEEELTDLRVE------------------KESLEKNL----SERKKKSAQERS--QAEEEIDEIRKSYQ 759
Cdd:pfam01576  332 lKKALEEETRSHEAQLQEMRQKhtqaleelteqleqakrnKANLEKAKqaleSENAELQAELRTlqQAKQDSEHKRKKLE 411

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   760 EELDKLRQLLKKT-RVSTDqaAAEQLSLVQAELQT------QWEAKCEHLL--ASAKDEHLQQYQEVCA----QRDAYQQ 826
Cdd:pfam01576  412 GQLQELQARLSESeRQRAE--LAEKLSKLQSELESvssllnEAEGKNIKLSkdVSSLESQLQDTQELLQeetrQKLNLST 489

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578817219   827 KLVQLQEKCLALQAQI-------TALTKQNEQHIKELEKNKSQMSGvEAAASDPSEKVKKIMNQVFQSLRREFE 893
Cdd:pfam01576  490 RLRQLEDERNSLQEQLeeeeeakRNVERQLSTLQAQLSDMKKKLEE-DAGTLEALEEGKKRLQRELEALTQQLE 562
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 662-876 3.50e-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: 3.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  662 QLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERkKKSA 741
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER-ARAL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  742 QERSQAEEEIDEI--RKSYQEELDKLRQLlkKTRVSTDQAAAEQLSLVQAELQTQweakcEHLLASAKDEHLQQYQEVCA 819
Cdd:COG3883    96 YRSGGSVSYLDVLlgSESFSDFLDRLSAL--SKIADADADLLEELKADKAELEAK-----KAELEAKLAELEALKAELEA 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578817219  820 QRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEK 876
Cdd:COG3883   169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
PTZ00121 PTZ00121
MAEBL; Provisional
 573-903 4.15e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.76  E-value: 4.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  573 ENERLKQEILE-KSNRIEEQNDKISELIERNQRYVEQSNLMMEKRN-NSLQTATENTQAKVTEELAAATAQVSHLQLKMT 650
Cdd:PTZ00121 1246 EEERNNEEIRKfEEARMAHFARRQAAIKAEEARKADELKKAEEKKKaDEAKKAEEKKKADEAKKKAEEAKKADEAKKKAE 1325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  651 AHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQN-----------RKQLELKVTSLEEEL 719
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKadaakkkaeekKKADEAKKKAEEDKK 1405

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  720 TDLRVEKESLEKNLSERKKKSAQERSQAEE---EIDEIRKSYQ-----EELDKLRQLLKKtrvSTDQAAAEQLSLVQAEL 791
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKAEEKKKADEakkKAEEAKKADEakkkaEEAKKAEEAKKK---AEEAKKADEAKKKAEEA 1482

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  792 QTQWEAKCEHLLASAKDEHLQQYQEvcAQRDAyqQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQmSGVEAAAS 871
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAE--AKKKA--DEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD-ELKKAEEL 1557

                         330       340       350
                  ....*....|....*....|....*....|..
gi 578817219  872 DPSEKVKKIMNQVFQSLRREFELEESYNGRTI 903
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA 1589
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 567-773 4.65e-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: 54.59  E-value: 4.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   567 IQRIIQENERLKQEILEKSNRIEEQNDKISELIERnqryvEQSNLMMEKRNNSLQTATENTQAKVTEELAaaTAQVSHLQ 646
Cdd:pfam02463  814 AELLEEEQLLIEQEEKIKEEELEELALELKEEQKL-----EKLAEEELERLEEEITKEELLQELLLKEEE--LEEQKLKD 886

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   647 LKMTAHQKKETELQMQLTESLKETDLLRGQLTK----------------VQAKLSELQETSEQAQ-SKFKSEKQNRKQLE 709
Cdd:pfam02463  887 ELESKEEKEKEEKKELEEESQKLNLLEEKENEIeerikeeaeillkyeeEPEELLLEEADEKEKEeNNKEEEEERNKRLL 966

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578817219   710 LKVTSLEEEltDLRVEKESLEKNLSERKKKSAQERsqAEEEIDEIRksyQEELDKLRQLLKKTR 773
Cdd:pfam02463  967 LAKEELGKV--NLMAIEEFEEKEERYNKDELEKER--LEEEKKKLI---RAIIEETCQRLKEFL 1023
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 497-865 5.36e-07

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 54.35  E-value: 5.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   497 HFQGSGDMASFLMTEARQHNTEIRMAVSKVADKMDHLMTKVEE-----LQKHSagnsmlipsmsvtmetsmimSNIQRII 571
Cdd:pfam15921  214 HFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNkiellLQQHQ--------------------DRIEQLI 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   572 QENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQAKVTEELAAATAQVSHLQLKMTA 651
Cdd:pfam15921  274 SEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVL 353

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   652 HQKKETELQMQLTESLKETDLLRGQLTKVQAKL----SELQETSEQAQSKFKSEKQNrkqlELKVTSLEEELTDLRVEKE 727
Cdd:pfam15921  354 ANSELTEARTERDQFSQESGNLDDQLQKLLADLhkreKELSLEKEQNKRLWDRDTGN----SITIDHLRRELDDRNMEVQ 429

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   728 SLEKNLS----------ERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLL-----KKTRVSTDQAAAEQLSLVQAELQ 792
Cdd:pfam15921  430 RLEALLKamksecqgqmERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVeeltaKKMTLESSERTVSDLTASLQEKE 509

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578817219   793 TQWEAKCEHL--LASAKDEHLQQYQEVCAQRDayqqKLVQLQEKCLALQAQITALTKQNEQHIKELEkNKSQMSG 865
Cdd:pfam15921  510 RAIEATNAEItkLRSRVDLKLQELQHLKNEGD----HLRNVQTECEALKLQMAEKDKVIEILRQQIE-NMTQLVG 579
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 619-884 5.63e-07

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 54.07  E-value: 5.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   619 SLQTATEnTQAKVTEELAAATAQVSHLQLKMT----AHQKKETELQMQLTESLKEtdllrgQLTKVQAKLSELQETSEQA 694
Cdd:pfam12128  612 ALQSARE-KQAAAEEQLVQANGELEKASREETfartALKNARLDLRRLFDEKQSE------KDKKNKALAERKDSANERL 684

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   695 QSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNL-SERKKKSAQ-------ERSQAEEEIDEIRKSYQEELDKLr 766
Cdd:pfam12128  685 NSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVeGALDAQLALlkaaiaaRRSGAKAELKALETWYKRDLASL- 763

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   767 qllkktrvSTDQAAAEQLSLVQAELQTQWE--AKCEHLLASAKDEHLQQYQEvcaQRDAYQQKLVQLQEKCLALQAQITA 844
Cdd:pfam12128  764 --------GVDPDVIAKLKREIRTLERKIEriAVRRQEVLRYFDWYQETWLQ---RRPRLATQLSNIERAISELQQQLAR 832

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 578817219   845 LTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQV 884
Cdd:pfam12128  833 LIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKL 872
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
575-877 7.99e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.51  E-value: 7.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  575 ERLKQEILEKSN-----RIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQAKvtEELAAATAQVSHLQLKM 649
Cdd:PRK02224  190 DQLKAQIEEKEEkdlheRLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR--EELETLEAEIEDLRETI 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  650 TA------------HQKKET--ELQMQLTESLKETDL-------LRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQL 708
Cdd:PRK02224  268 AEterereelaeevRDLRERleELEEERDDLLAEAGLddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL 347

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  709 ELKVTSLEEELTDLRVEKESLEKNLSERK---KKSAQERSQAEEEIDEIRKSYQ------EELDKLRQLLKKTRvstdQA 779
Cdd:PRK02224  348 REDADDLEERAEELREEAAELESELEEAReavEDRREEIEELEEEIEELRERFGdapvdlGNAEDFLEELREER----DE 423

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  780 AAEQLSLVQAELQTQWE--AKCEHLLASAKDEHLQQYQE----VCAQRDaYQQKLVQLQEKCLALQAQITALTKQNEQhI 853
Cdd:PRK02224  424 LREREAELEATLRTARErvEEAEALLEAGKCPECGQPVEgsphVETIEE-DRERVEELEAELEDLEEEVEEVEERLER-A 501

                         330       340
                  ....*....|....*....|....
gi 578817219  854 KELEKNKSQMSGVEAAASDPSEKV 877
Cdd:PRK02224  502 EDLVEAEDRIERLEERREDLEELI 525
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 598-918 1.04e-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: 53.22  E-value: 1.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   598 LIERNQRYVEQSNLMMEKRNNSLQTATENTQAKVTEELAAATAQVSHLQLKMTAHQKketelqmQLTESLKETDLLRGQL 677
Cdd:pfam07111  134 LEEGSQRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAK-------QLAEAQKEAELLRKQL 206

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   678 TKVQAKLsELQET---------SEQAQSKFKSE--KQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQ 746
Cdd:pfam07111  207 SKTQEEL-EAQVTlveslrkyvGEQVPPEVHSQtwELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEE 285

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   747 AEEEIDEIRKSYQEELDKLRQLLKKTRvstDQAAAEQLSLVQAELQTQWEAK-CEHLLASAKDEHLQQYQEVCAQRDAYQ 825
Cdd:pfam07111  286 LTRKIQPSDSLEPEFPKKCRSLLNRWR---EKVFALMVQLKAQDLEHRDSVKqLRGQVAELQEQVTSQSQEQAILQRALQ 362

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   826 QKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKS---QMSGVEAAASDPSEKVKKIMNQVFQSLRREFELEE--SYNG 900
Cdd:pfam07111  363 DKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASaeeQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNrlSYAV 442

                          330       340
                   ....*....|....*....|.
gi 578817219   901 R---TILGTIMNTIKMVTLQL 918
Cdd:pfam07111  443 RkvhTIKGLMARKVALAQLRQ 463
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 578-858 1.25e-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: 53.03  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  578 KQEILEKSNRIEEQNDKISELIERnQRYVEQSNLMMEKRNNSLQTAT------ENTQAKVtEELAAATAQvSHLQLKMTA 651
Cdd:COG3096   298 RRQLAEEQYRLVEMARELEELSAR-ESDLEQDYQAASDHLNLVQTALrqqekiERYQEDL-EELTERLEE-QEEVVEEAA 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  652 HQKKETELQMQLTEslKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQL---ELKVTSLEEELTDLRVEKES 728
Cdd:COG3096   375 EQLAEAEARLEAAE--EEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALCglpDLTPENAEDYLAAFRAKEQQ 452

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  729 LEKNLSERKkksaQERSQAEEEIDEIRKSYQ------------EELDKLRQLLKKTRVSTDQAA-----------AEQLS 785
Cdd:COG3096   453 ATEEVLELE----QKLSVADAARRQFEKAYElvckiageversQAWQTARELLRRYRSQQALAQrlqqlraqlaeLEQRL 528

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578817219  786 LVQAELQTQWEAKCEHL---LASAKD-EHLQQYQEvcAQRDAYQQKLVQLQEKCLALQAQitalTKQNEQHIKELEK 858
Cdd:COG3096   529 RQQQNAERLLEEFCQRIgqqLDAAEElEELLAELE--AQLEELEEQAAEAVEQRSELRQQ----LEQLRARIKELAA 599
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 589-898 1.33e-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: 53.05  E-value: 1.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   589 EEQNDKISELIERNQryVEQSNLMMEKRNNSLQTATENTQAKVTEELAAATAQVShlqlkmTAHQKKETelqmqLTESLK 668
Cdd:TIGR00618  163 KEKKELLMNLFPLDQ--YTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPD------TYHERKQV-----LEKELK 229

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   669 etdllrgQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAE 748
Cdd:TIGR00618  230 -------HLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAV 302

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   749 EEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSL-VQAELQTQWEAKCehllasakdEHLQQYQEVCAQRDAYQQK 827
Cdd:TIGR00618  303 TQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIeEQRRLLQTLHSQE---------IHIRDAHEVATSIREISCQ 373

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817219   828 LVQLQEKCLALQAQITALTKQNEQHIKELEKNKSqmsgvEAAASDPSEKVKKIMNQVFQSLRREFELEESY 898
Cdd:TIGR00618  374 QHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQR-----EQATIDTRTSAFRDLQGQLAHAKKQQELQQRY 439
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 658-855 1.39e-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: 52.38  E-value: 1.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   658 ELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLElkvtSLEEEL-------TDLRVEKESLE 730
Cdd:pfam05622   18 ELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLE----QLQEENfrletarDDYRIKCEELE 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   731 KNLSERK------KKSAQERSQAEEEIDEIRKS-------------YQEELDKLRQLLKKTRVSTDQAAaeqlSLVQAEL 791
Cdd:pfam05622   94 KEVLELQhrneelTSLAEEAQALKDEMDILRESsdkvkkleatvetYKKKLEDLGDLRRQVKLLEERNA----EYMQRTL 169

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578817219   792 QTQWEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKE 855
Cdd:pfam05622  170 QLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIE 233
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 575-767 1.57e-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: 50.69  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  575 ERLKQEILEKSNRIEEQNDKISEL---IERNQRYVEQSNLMMEKRNNSLQTATENtqakvtEELAAATAQVSHLQLKMTA 651
Cdd:COG1579    34 AELEDELAALEARLEAAKTELEDLekeIKRLELEIEEVEARIKKYEEQLGNVRNN------KEYEALQKEIESLKRRISD 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  652 HQKKETELQMQLTEslketdlLRGQLTKVQAKLSELQEtseqaqskfksekqnrkQLELKVTSLEEELTDLRVEKESLEK 731
Cdd:COG1579   108 LEDEILELMERIEE-------LEEELAELEAELAELEA-----------------ELEEKKAELDEELAELEAELEELEA 163

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 578817219  732 nlserkkksaqERSQAEEEIDE-IRKSYqeelDKLRQ 767
Cdd:COG1579   164 -----------EREELAAKIPPeLLALY----ERIRK 185
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 683-802 1.65e-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: 48.84  E-value: 1.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   683 KLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRV-------EKESLEKNLSERKKK---SAQERSQA----- 747
Cdd:pfam12718    1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHknqqleeEVEKLEEQLKEAKEKaeeSEKLKTNNenltr 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578817219   748 -----EEEIDEIRKSYQEELDKLRQllkktrvsTDQAAAEQLSLVQAELQT--QWEAKCEHL 802
Cdd:pfam12718   81 kiqllEEELEESDKRLKETTEKLRE--------TDVKAEHLERKVQALEQErdEWEKKYEEL 134
mukB PRK04863
chromosome partition protein MukB;
575-863 1.67e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 52.65  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  575 ERLKQEIleksNRIEEQNDKISELIERNQRYVEQSNLMMekrNNSLQTATENTQAkvtEELAAATAQVSHLQLKMTAHQK 654
Cdd:PRK04863  789 EQLRAER----EELAERYATLSFDVQKLQRLHQAFSRFI---GSHLAVAFEADPE---AELRQLNRRRVELERALADHES 858

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  655 KETELQMQLTESLKETDLLRGQLTKV--------QAKLSELQETSEQAQSKFKSEKQNRKQLELkvtsLEEELTDLRVEK 726
Cdd:PRK04863  859 QEQQQRSQLEQAKEGLSALNRLLPRLnlladetlADRVEEIREQLDEAEEAKRFVQQHGNALAQ----LEPIVSVLQSDP 934

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  727 ESLEK-----NLSERKKKSAQERSQAEEEIDEIRK--SYQEEL----------DKLRQLLK---------KTRVSTDQAA 780
Cdd:PRK04863  935 EQFEQlkqdyQQAQQTQRDAKQQAFALTEVVQRRAhfSYEDAAemlaknsdlnEKLRQRLEqaeqertraREQLRQAQAQ 1014

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  781 AEQLSLVQAELQTQWEAKCEhLLASAKDEhLQQY---------QEVCAQRDAYQQKLVQLQEKCLALQAQIT----ALTK 847
Cdd:PRK04863 1015 LAQYNQVLASLKSSYDAKRQ-MLQELKQE-LQDLgvpadsgaeERARARRDELHARLSANRSRRNQLEKQLTfceaEMDN 1092

                         330
                  ....*....|....*.
gi 578817219  848 QNEQhIKELEKNKSQM 863
Cdd:PRK04863 1093 LTKK-LRKLERDYHEM 1107
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 623-901 2.61e-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: 52.10  E-value: 2.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   623 ATENTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQL---TESLKETDLLRGQL-----------TKVQAKLSELQ 688
Cdd:pfam01576    9 AKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLqaeTELCAEAEEMRARLaarkqeleeilHELESRLEEEE 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   689 ETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKN----------LSERKKKSAQERSQAEEEIDEIRKSY 758
Cdd:pfam01576   89 ERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKikkleedillLEDQNSKLSKERKLLEERISEFTSNL 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   759 QEELDKLRQLLKktrvstdqaaaeqlslvqaeLQTQWEAKCEHLLASAKDEHlQQYQEVCAQRDAYQQKLVQLQEKCLAL 838
Cdd:pfam01576  169 AEEEEKAKSLSK--------------------LKNKHEAMISDLEERLKKEE-KGRQELEKAKRKLEGESTDLQEQIAEL 227

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578817219   839 QAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQsLRREFELEESYNGR 901
Cdd:pfam01576  228 QAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISE-LQEDLESERAARNK 289
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 633-858 2.71e-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: 51.88  E-value: 2.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  633 EELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKV--------QAKLSELQETSEQAQSKFKSEKQN 704
Cdd:COG3096   836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAnlladetlADRLEELREELDAAQEAQAFIQQH 915

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  705 RKQLELkvtsLEEELTDLRVEKESLEkNLSERKKKSAQERSQAEEEIDEI-----RK---SYQEEL----------DKLR 766
Cdd:COG3096   916 GKALAQ----LEPLVAVLQSDPEQFE-QLQADYLQAKEQQRRLKQQIFALsevvqRRphfSYEDAVgllgensdlnEKLR 990

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  767 QLLK-------KTRVSTDQAAAE--QLSLVQAELQTQWEAKCEhLLASAKDEhLQQY-------QEVCAQ--RDAYQQKL 828
Cdd:COG3096   991 ARLEqaeearrEAREQLRQAQAQysQYNQVLASLKSSRDAKQQ-TLQELEQE-LEELgvqadaeAEERARirRDELHEEL 1068

                         250       260       270
                  ....*....|....*....|....*....|
gi 578817219  829 VQLQEKCLALQAQITALTKQNEQHIKELEK 858
Cdd:COG3096  1069 SQNRSRRSQLEKQLTRCEAEMDSLQKRLRK 1098
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 646-873 2.73e-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: 49.99  E-value: 2.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   646 QLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQL-------------ELKV 712
Cdd:pfam12795    1 KLDELEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALqakaeaapkeilaSLSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   713 TSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAE---EEIDEIRKsyqeELDKLRQLLKKTRVSTDQAAAEQLSLVQA 789
Cdd:pfam12795   81 EELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPEraqQQLSEARQ----RLQQIRNRLNGPAPPGEPLSEAQRWALQA 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   790 ELQtqweakcehlLASAKDEHLQQYQEVC--------AQRDAYQQKLVQLQEKCLALQAQItaltkqNEQHIKELEKN-- 859
Cdd:pfam12795  157 ELA----------ALKAQIDMLEQELLSNnnrqdllkARRDLLTLRIQRLEQQLQALQELL------NEKRLQEAEQAva 220

                          250
                   ....*....|....
gi 578817219   860 KSQMSGVEAAASDP 873
Cdd:pfam12795  221 QTEQLAEEAAGDHP 234
PTZ00121 PTZ00121
MAEBL; Provisional
 575-878 2.99e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 2.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  575 ERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRN-NSLQTATENTQAKVTEELAAATAQVSHLQLKMTAHQ 653
Cdd:PTZ00121 1442 EAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKaDEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA 1521

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  654 KKETELQMqlTESLKETDLLRGQLTKVQA----KLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEK--- 726
Cdd:PTZ00121 1522 KKADEAKK--AEEAKKADEAKKAEEKKKAdelkKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEvmk 1599

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  727 --ESLEKNLSERKKKSAQERSQAEE---------EIDEIRKSYQEELDKLRQLlKKTRVSTDQAAAEQLSLVQAELQTQW 795
Cdd:PTZ00121 1600 lyEEEKKMKAEEAKKAEEAKIKAEElkkaeeekkKVEQLKKKEAEEKKKAEEL-KKAEEENKIKAAEEAKKAEEDKKKAE 1678

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  796 EAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQmsgVEAAASDPSE 875
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK---AEEAKKDEEE 1755


                  ...
gi 578817219  876 KVK 878
Cdd:PTZ00121 1756 KKK 1758
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 654-769 3.19e-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: 47.63  E-value: 3.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   654 KKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQN----RKQL-ELK--VTSLEEELTDLRVEK 726
Cdd:pfam07926    1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVLhaedIKALqALReeLNELKAEIAELKAEA 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 578817219   727 ESLEKNLSERKKKSAQERSQAEEEIDEIRKSYqEELDKLRQLL 769
Cdd:pfam07926   81 ESAKAELEESEESWEEQKKELEKELSELEKRI-EDLNEQNKLL 122
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 685-896 3.57e-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: 51.51  E-value: 3.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   685 SELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLrvEKEslEKNLSERKKKSAQERSQAEEEI-DEIRKSYQEELD 763
Cdd:pfam02463  165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKL--KEQ--AKKALEYYQLKEKLELEEEYLLyLDYLKLNEERID 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   764 KLRQLLKKTRVSTDQAAAEQlslvQAELQTQWEAKCEHLLASAKDEHLQQYQEVCA-QRDAYQQKLVQLQEKCLALQAQI 842
Cdd:pfam02463  241 LLQELLRDEQEEIESSKQEI----EKEEEKLAQVLKENKEEEKEKKLQEEELKLLAkEEEELKSELLKLERRKVDDEEKL 316

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 578817219   843 TALTKQNEQHIKELEKNKSQMS---GVEAAASDPSEKVKKIMNQVFQSLRREFELEE 896
Cdd:pfam02463  317 KESEKEKKKAEKELKKEKEEIEeleKELKELEIKREAEEEEEEELEKLQEKLEQLEE 373
PLN02939 PLN02939
transferase, transferring glycosyl groups
 585-875 3.69e-06

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 51.44  E-value: 3.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  585 SNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENT----QAKVTeelaaATAQVSHLQLKMTAHQKKETELQ 660
Cdd:PLN02939  102 MQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNIlllnQARLQ-----ALEDLEKILTEKEALQGKINILE 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  661 MQLTESlketdllrGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELK-VTSLEEELTDLRVEKESLEKNLSERKkk 739
Cdd:PLN02939  177 MRLSET--------DARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLcVHSLSKELDVLKEENMLLKDDIQFLK-- 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  740 saqersqaeEEIDEIRKSYQE--ELDKLRQLLKKT------RVSTDQAAAEQLSLVQAELqtqWEAKCE---HLLASAKD 808
Cdd:PLN02939  247 ---------AELIEVAETEERvfKLEKERSLLDASlrelesKFIVAQEDVSKLSPLQYDC---WWEKVEnlqDLLDRATN 314

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  809 --EH----LQQYQEV--------------------CAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELE----- 857
Cdd:PLN02939  315 qvEKaalvLDQNQDLrdkvdkleaslkeanvskfsSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQdtlsk 394

                         330       340
                  ....*....|....*....|
gi 578817219  858 -KNKSQMSGVEAAASD-PSE 875
Cdd:PLN02939  395 lKEESKKRSLEHPADDmPSE 414
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 571-861 3.94e-06

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: 51.59  E-value: 3.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   571 IQENE-RLKQEILEKSNRIEEQNDKISELIERNQryvEQSNLMMEKRNNSLQTATENTQAKVTEELAAATAQVSHLQLKM 649
Cdd:TIGR00606  370 IQSLAtRLELDGFERGPFSERQIKNFHTLVIERQ---EDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKK 446

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   650 TAHQKKETELQ------MQLTESLKETDLLRGQLTKVQAKLSELQETS--EQAQSKFKSEKQNRKQLELKVTSLEEELTD 721
Cdd:TIGR00606  447 EILEKKQEELKfvikelQQLEGSSDRILELDQELRKAERELSKAEKNSltETLKKEVKSLQNEKADLDRKLRKLDQEMEQ 526

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   722 LRVEKESLEKNLSERKKKsaqerSQAEEEIDEIRKSYQEEL--------------DKLRQLLKKTRVSTDQAAAEQLSLV 787
Cdd:TIGR00606  527 LNHHTTTRTQMEMLTKDK-----MDKDEQIRKIKSRHSDELtsllgyfpnkkqleDWLHSKSKEINQTRDRLAKLNKELA 601

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   788 QAE-LQTQWEAKCEhllasAKDEHLQQYQ----EVCAQRDaYQQKLVQLQ---EKCLALQAQITALTKQNEQHIKEL-EK 858
Cdd:TIGR00606  602 SLEqNKNHINNELE-----SKEEQLSSYEdklfDVCGSQD-EESDLERLKeeiEKSSKQRAMLAGATAVYSQFITQLtDE 675


                   ...
gi 578817219   859 NKS 861
Cdd:TIGR00606  676 NQS 678
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 530-855 4.79e-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: 50.66  E-value: 4.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   530 MDHLMTKVEELQKHSAGNSML--IPSMSVtmetsmimsnIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVE 607
Cdd:pfam07888    3 LDELVTLEEESHGEEGGTDMLlvVPRAEL----------LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   608 QSNLMMEKRNNSLQTATENTQAKvTEELAAATAQVSHLQLKMTAHQ----KKETELQMQLTESLKETDLLRGQLTKVQAK 683
Cdd:pfam07888   73 RQRRELESRVAELKEELRQSREK-HEELEEKYKELSASSEELSEEKdallAQRAAHEARIRELEEDIKTLTQRVLERETE 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   684 LSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSER----------------KKKSAQERSQA 747
Cdd:pfam07888  152 LERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRdtqvlqlqdtittltqKLTTAHRKEAE 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   748 EEEIDEIRKSYQEEL-------DKLRQLLKKTRVSTDQAAAE----------------QLSLVQAELQTQWEAKCEHLLA 804
Cdd:pfam07888  232 NEALLEELRSLQERLnaserkvEGLGEELSSMAAQRDRTQAElhqarlqaaqltlqlaDASLALREGRARWAQERETLQQ 311

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578817219   805 SAKDEH---------LQQYQEVCAQRDAYQQKL------------VQLQEKCLALQ---AQITALTKQNEQHIKE 855
Cdd:pfam07888  312 SAEADKdrieklsaeLQRLEERLQEERMEREKLevelgrekdcnrVQLSESRRELQelkASLRVAQKEKEQLQAE 386
DUF4618 pfam15397
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ...
 678-877 6.57e-06

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: 49.18  E-value: 6.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   678 TKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKEsleknlSERKKKSAQeRSQAEEEIDEIRKS 757
Cdd:pfam15397   63 KQLQQAKAELQEWEEKEESKLNKLEQQLEQLNAKIQKTQEELNFLSTYKD------KEYPVKAVQ-IANLVRQLQQLKDS 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   758 YQEELDKLRQLLKKTRvstdqaaaeqlslvqAELQTQWEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLvqlqEKCLA 837
Cdd:pfam15397  136 QQDELDELEEMRRMVL---------------ESLSRKIQKKKEKILSSLAEKTLSPYQESLLQKTRDNQVM----LKEIE 196

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 578817219   838 lqaqitaltkQNEQHIKELEKN----KSQMSGVEAAASDPSEKV 877
Cdd:pfam15397  197 ----------QFREFIDELEEEipklKAEVQQLQAQRQEPREVI 230
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 194-265 6.98e-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: 6.98e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578817219  194 VEVGDSLEVAYTGWLfqnhVLGQVFDSTANKDKLLrLKLGSGKVIKGWEDGMLGMKKGGKRLLIVPPACAVG 265
Cdd:COG1047     1 IEKGDVVTLHYTLKL----EDGEVFDSTFEGEPLE-FLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG 67
PHA03247 PHA03247
large tegument protein UL36; Provisional
 941-1154 9.07e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 9.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  941 RPRRPSQEQsasassgQPQAPLNRERPESPMVPSEQVVEEAVPLPPQALTTSQDGhrRKGDSEAEALSEIKDGSLPPELS 1020
Cdd:PHA03247 2907 RPPQPQAPP-------PPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGE--PSGAVPQPWLGALVPGRVAVPRF 2977

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219 1021 CIPSHRvlgPPTSIPPEPLGPVSMDSECEESLAASPMAAKPDNPSGKVCVRE-VAPDGPLQESSTRLSLTSDPEEGDPLA 1099
Cdd:PHA03247 2978 RVPQPA---PSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQtLWPPDDTEDSDADSLFDSDSERSDLEA 3054

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578817219 1100 LGPEsPGEPQPPQLKKDDVTSSTGPHKELSSTEAG--STVAGAAL--RPSHHSQRSSLS 1154
Cdd:PHA03247 3055 LDPL-PPEPHDPFAHEPDPATPEAGARESPSSQFGppPLSANAALsrRYVRSTGRSALA 3112
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 518-773 9.59e-06

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: 50.44  E-value: 9.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   518 EIRMAVSKVADKMDHLMTKVEELQKHSAG--NSM--LIPSMSVTMETSMIMSNIQRIIQENERLKQEILEKSNRIEEQND 593
Cdd:TIGR01612 1115 KIKDDIKNLDQKIDHHIKALEEIKKKSENyiDEIkaQINDLEDVADKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKK 1194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   594 KISELIErnqryVEQSNLMMEKRNNSLQTATENTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETdll 673
Cdd:TIGR01612 1195 LLNEIAE-----IEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEM--- 1266

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   674 rGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLE------LKVTSLEEELTDLRVEKESLEKNLSERKKKSAQ----- 742
Cdd:TIGR01612 1267 -GIEMDIKAEMETFNISHDDDKDHHIISKKHDENISdireksLKIIEDFSEESDINDIKKELQKNLLDAQKHNSDinlyl 1345

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 578817219   743 --------------------ERSQAEEEIDEIRKSYQEELDKLRQLLKKTR 773
Cdd:TIGR01612 1346 neianiynilklnkikkiidEVKEYTKEIEENNKNIKDELDKSEKLIKKIK 1396
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 575-771 1.13e-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: 47.75  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   575 ERLKQEILEKSNRIEEQNDKISELIERNQRYVeqsnlmmekrnnslqtatentqaKVTEELAAATAQVshlqlkMTAHQK 654
Cdd:pfam05010   11 EKARNEIEEKELEINELKAKYEELRRENLEMR-----------------------KIVAEFEKTIAQM------IEEKQK 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   655 KETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEeltdlRVEKEslEKNLS 734
Cdd:pfam05010   62 QKELEHAEIQKVLEEKDQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLA-----RIKKE--EQRYQ 134

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 578817219   735 ERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKK 771
Cdd:pfam05010  135 ALKAHAEEKLDQANEEIAQVRSKAKAETAALQASLRK 171
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 653-844 1.42e-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: 49.30  E-value: 1.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   653 QKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQ---ETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESL 729
Cdd:pfam05622  303 RERLTELQQLLEDANRRKNELETQNRLANQRILELQqqvEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKK 382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   730 EKNLSERKKKSAQERSQAEEEIDEIRKSYQEE-----------LDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQwEAK 798
Cdd:pfam05622  383 KEQIEELEPKQDSNLAQKIDELQEALRKKDEDmkameerykkyVEKAKSVIKTLDPKQNPASPPEIQALKNQLLEK-DKK 461

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817219   799 CEHLLASAKDEHLQQYQE------------VCAQRDAYQQKLVQLQ---EKCLALQAQITA 844
Cdd:pfam05622  462 IEHLERDFEKSKLQREQEeklivtawynmgMALHRKAIEERLAGLSspgQSFLARQRQATN 522
mukB PRK04863
chromosome partition protein MukB;
652-872 1.84e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 49.19  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  652 HQKKETELQMQLTESLKETDLLRGQLTKVQAKLSEL--QETSEQAQSKFKSEKQNR--------KQLELKVTSLEEeLTD 721
Cdd:PRK04863  284 HLEEALELRRELYTSRRQLAAEQYRLVEMARELAELneAESDLEQDYQAASDHLNLvqtalrqqEKIERYQADLEE-LEE 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  722 LRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKS---YQEELDKLR----------QLLKKTRVSTDQA--AAEQLSL 786
Cdd:PRK04863  363 RLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQladYQQALDVQQtraiqyqqavQALERAKQLCGLPdlTADNAED 442

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  787 VQAELQTQWEAKCEHLLA---------SAKDEHLQQYQEVCA-----QRDAYQQKLVQL-----QEKCLALQAQitaltk 847
Cdd:PRK04863  443 WLEEFQAKEQEATEELLSleqklsvaqAAHSQFEQAYQLVRKiagevSRSEAWDVARELlrrlrEQRHLAEQLQ------ 516

                         250       260
                  ....*....|....*....|....*
gi 578817219  848 QNEQHIKELEKNKSQMSGVEAAASD 872
Cdd:PRK04863  517 QLRMRLSELEQRLRQQQRAERLLAE 541
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 568-884 1.87e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.86  E-value: 1.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   568 QRIIQENERLKQEILEKSNRIEEqndkiselIERNQryveqsNLMMEKRNNSlqtateNTQAKVTEelaaatAQVSHLQL 647
Cdd:TIGR04523   36 KQLEKKLKTIKNELKNKEKELKN--------LDKNL------NKDEEKINNS------NNKIKILE------QQIKDLND 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   648 KMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLS----ELQETSEQaQSKFKSEKQNrkqLELKVTSLEEELTDLR 723
Cdd:TIGR04523   90 KLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNklekQKKENKKN-IDKFLTEIKK---KEKELEKLNNKYNDLK 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   724 VEKESLEKNLSERKKksaqERSQAEEEIDEIRKsyqeeldKLRQLLKKtrvstdqaaaeqLSLVQAELQtqweakcEHLL 803
Cdd:TIGR04523  166 KQKEELENELNLLEK----EKLNIQKNIDKIKN-------KLLKLELL------------LSNLKKKIQ-------KNKS 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   804 ASAKDEHL-QQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMN 882
Cdd:TIGR04523  216 LESQISELkKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKS 295


                   ..
gi 578817219   883 QV 884
Cdd:TIGR04523  296 EI 297
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 566-870 2.12e-05

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 49.03  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  566 NIQRIIQENERLKQEILEKSNRIEEQNDKISE---LIERNQRYVEqsnlmMEKRNNSLQTATENTQAKVTEELAAATAQV 642
Cdd:PRK10246  448 AIQNVTQEQTQRNAALNEMRQRYKEKTQQLADvktICEQEARIKD-----LEAQRAQLQAGQPCPLCGSTSHPAVEAYQA 522

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  643 shlqLKMTAHQKKETELQMQLTESLKETDLLRGQLtkvQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSL------E 716
Cdd:PRK10246  523 ----LEPGVNQSRLDALEKEVKKLGEEGAALRGQL---DALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLnitlqpQ 595

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  717 EELTDLRVEKESLEKNL---SERKKKSAQERSQAEEEIdeirkSYQEELDKLRQLLkktrvsTDQAAAEQLSLVQAELQT 793
Cdd:PRK10246  596 DDIQPWLDAQEEHERQLrllSQRHELQGQIAAHNQQII-----QYQQQIEQRQQQL------LTALAGYALTLPQEDEEA 664

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  794 QWeakcehllASAKDEHLQQYQEVCAQRDAYQQKLVQL----------------------------QEKCLALQAQITAL 845
Cdd:PRK10246  665 SW--------LATRQQEAQSWQQRQNELTALQNRIQQLtplletlpqsddlphseetvaldnwrqvHEQCLSLHSQLQTL 736

                         330       340
                  ....*....|....*....|....*
gi 578817219  846 TKQNEQHIKELEKNKSQMSGVEAAA 870
Cdd:PRK10246  737 QQQDVLEAQRLQKAQAQFDTALQAS 761
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 580-744 2.34e-05

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


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 48.90  E-value: 2.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   580 EILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATEN-----TQAKVTEELAAataqvsHLQLKMTAHQK 654
Cdd:pfam05911  664 EIPSDGPLVSGSNDLKTEENKRLKEEFEQLKSEKENLEVELASCTENlestkSQLQESEQLIA------ELRSELASLKE 737

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   655 K----ETELQMQlTESLKETDLlrgQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTdlRVEKESLE 730
Cdd:pfam05911  738 SnslaETQLKCM-AESYEDLET---RLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLE--RNEKKESS 811

                          170
                   ....*....|....*
gi 578817219   731 KNL-SERKKKSAQER 744
Cdd:pfam05911  812 NCDaDQEDKKLQQEK 826
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 607-816 2.72e-05

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: 48.41  E-value: 2.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   607 EQSNLMMEKRNNSLQTA--TENTQAK--VTEELAAATAQVSHLQLKMTAHQKKETELQMQLTEslketdllrgqltkVQA 682
Cdd:pfam15709  287 EESQVSIDGRSSPTQTFvvTGNMESEeeRSEEDPSKALLEKREQEKASRDRLRAERAEMRRLE--------------VER 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   683 KLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEE--LTDLRVEKESLEKNLSERKK----KSAQERSQAEEEidEIRK 756
Cdd:pfam15709  353 KRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEirLRKQRLEEERQRQEEEERKQrlqlQAAQERARQQQE--EFRR 430

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578817219   757 SYQEeldkLRQllKKTRVSTDQAAAEQLSlvQAELQTQWEAKCEHLLASAKD---EHLQQYQE 816
Cdd:pfam15709  431 KLQE----LQR--KKQQEEAERAEAEKQR--QKELEMQLAEEQKRLMEMAEEerlEYQRQKQE 485
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 569-852 2.87e-05

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 48.20  E-value: 2.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   569 RIIQ-ENERLKQEILEKSNRIEEQNdKISELIERNQRYVEqsnlmmekRNNSLQTATENTQAKVTEELAAATAQVSHLQL 647
Cdd:pfam05557   10 RLSQlQNEKKQMELEHKRARIELEK-KASALKRQLDRESD--------RNQELQKRIRLLEKREAEAEEALREQAELNRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   648 K---MTAHQKKETELQMQLTESLKETDLLRGQLT-----------KVQAKLSELQETSEQ---AQSKFKSEKQNRKQLEL 710
Cdd:pfam05557   81 KkkyLEALNKKLNEKESQLADAREVISCLKNELSelrrqiqraelELQSTNSELEELQERldlLKAKASEAEQLRQNLEK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   711 KVTSL---EEELTDLRVEKESLEKNLSERKKKSAQ---------ERSQAEEEIDEIRKS------YQEELDKLRQLLKKT 772
Cdd:pfam05557  161 QQSSLaeaEQRIKELEFEIQSQEQDSEIVKNSKSElaripelekELERLREHNKHLNENienkllLKEEVEDLKRKLERE 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   773 RVSTDQAAAEQLSL--VQAELQtQWE----AKCEHL----LASAKDEHLQQYQEVCAQRD--------AYQQKLVQLQEK 834
Cdd:pfam05557  241 EKYREEAATLELEKekLEQELQ-SWVklaqDTGLNLrspeDLSRRIEQLQQREIVLKEENssltssarQLEKARRELEQE 319

                          330
                   ....*....|....*...
gi 578817219   835 CLALQAQITALTKQNEQH 852
Cdd:pfam05557  320 LAQYLKKIEDLNKKLKRH 337
Filament pfam00038
Intermediate filament protein;
572-767 3.01e-05

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 47.61  E-value: 3.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   572 QENERLKQEILEKSN---RIEEQNDKISELIER-NQRYVEQSNLmmekrnnslQTATENTQAKVTEELAAATAQVSHLQL 647
Cdd:pfam00038   54 KEIEDLRRQLDTLTVeraRLQLELDNLRLAAEDfRQKYEDELNL---------RTSAENDLVGLRKDLDEATLARVDLEA 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   648 KMTA-----------HQKKETELQMQLTES--LKETDLLRGQ-LTKV-----------------------QAKLSELQET 690
Cdd:pfam00038  125 KIESlkeelaflkknHEEEVRELQAQVSDTqvNVEMDAARKLdLTSAlaeiraqyeeiaaknreeaeewyQSKLEELQQA 204

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578817219   691 SEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIrksyQEELDKLRQ 767
Cdd:pfam00038  205 AARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISEL----EAELQETRQ 277
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 625-746 3.11e-05

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


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 44.94  E-value: 3.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   625 ENTQAKVTEELAAATAQVSHLQLKM--------TAHQKKETELQMQlTESLKETDLLRGQLTKVQAKLSELQETSEQAQS 696
Cdd:pfam07926    7 QSEIKRLKEEAADAEAQLQKLQEDLekqaeiarEAQQNYERELVLH-AEDIKALQALREELNELKAEIAELKAEAESAKA 85

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 578817219   697 KFKSEKQnrkqlelkvtSLEEEltdlrveKESLEKNLSERKKKSAQERSQ 746
Cdd:pfam07926   86 ELEESEE----------SWEEQ-------KKELEKELSELEKRIEDLNEQ 118
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 563-749 3.12e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.90  E-value: 3.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  563 IMSNIQRIIQENERLKQEILEKSNRIEEQNDKISEL---IERNQRYVEQSNLMMEKRNNSLQTATENTQAKVT----EEL 635
Cdd:COG3883    35 AQAELDALQAELEELNEEYNELQAELEALQAEIDKLqaeIAEAEAEIEERREELGERARALYRSGGSVSYLDVllgsESF 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  636 AAATAQVSHLQlKMTAHQKKETELQMQLTESLKET-DLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTS 714
Cdd:COG3883   115 SDFLDRLSALS-KIADADADLLEELKADKAELEAKkAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 578817219  715 LEEELTDLRVEKESLEKNLSERKKKSAQERSQAEE 749
Cdd:COG3883   194 AEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
Macoilin pfam09726
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ...
 626-847 3.25e-05

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: 48.31  E-value: 3.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   626 NTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNR 705
Cdd:pfam09726  388 NNQLSKPDALVRLEQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTV 467

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   706 KQLELKvtsLEEEltdlRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQllkktrvstdqaAAEQLS 785
Cdd:pfam09726  468 QQLEKR---LKAE----QEARASAEKQLAEEKKRKKEEEATAARAVALAAASRGECTESLKQ------------RKRELE 528

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578817219   786 LVQAELQTQWEAKCEHLLA-SAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTK 847
Cdd:pfam09726  529 SEIKKLTHDIKLKEEQIRElEIKVQELRKYKESEKDTEVLMSALSAMQDKNQHLENSLSAETR 591
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 529-860 3.42e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 48.19  E-value: 3.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   529 KMDHLMTKVEELQKHSA-------GNSMLIPSMSVTMETSMIMSNIQRIIQEnerLKQEILEKSNRIEEQNDKISELIER 601
Cdd:pfam15921  449 QMAAIQGKNESLEKVSSltaqlesTKEMLRKVVEELTAKKMTLESSERTVSD---LTASLQEKERAIEATNAEITKLRSR 525

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   602 -NQRYVEQSNLMMEKRN-NSLQTATENTQAKVTEE---LAAATAQVSHLQLKMTAH-------QKKETELQMQLTE---S 666
Cdd:pfam15921  526 vDLKLQELQHLKNEGDHlRNVQTECEALKLQMAEKdkvIEILRQQIENMTQLVGQHgrtagamQVEKAQLEKEINDrrlE 605

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   667 LKETDLLR----GQLTKVQAKLSELQ--------ETSEQAQSkFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLs 734
Cdd:pfam15921  606 LQEFKILKdkkdAKIRELEARVSDLElekvklvnAGSERLRA-VKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNF- 683

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   735 erkKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAeqlslVQAELQTQWEAKcehllasakdehlqqy 814
Cdd:pfam15921  684 ---RNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMK-----VAMGMQKQITAK---------------- 739

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 578817219   815 qevCAQRDAYQQKLVQLQEkclalqaqitALTKQN-EQHIKELEKNK 860
Cdd:pfam15921  740 ---RGQIDALQSKIQFLEE----------AMTNANkEKHFLKEEKNK 773
PLN02939 PLN02939
transferase, transferring glycosyl groups
 515-783 4.24e-05

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 47.97  E-value: 4.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  515 HNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMLIPSMSVTMETSMIMSN---------IQRIIQENERLKQEILEKS 585
Cdd:PLN02939   97 HNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNqarlqaledLEKILTEKEALQGKINILE 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  586 NRIEEQNDKIsELIERNQRYVEQSNLMMEKRNNSLQTATENTQAKVT---EELAaaTAQVSHLQLKMTAHQKKETELQMQ 662
Cdd:PLN02939  177 MRLSETDARI-KLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHslsKELD--VLKEENMLLKDDIQFLKAELIEVA 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  663 LTESL-----KETDLLRGQLTKVQAKLSELQE--------------------------TSEQAQSKFKSEKQNRkQLELK 711
Cdd:PLN02939  254 ETEERvfkleKERSLLDASLRELESKFIVAQEdvsklsplqydcwwekvenlqdlldrATNQVEKAALVLDQNQ-DLRDK 332

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578817219  712 VTSLEEELTDLRVEKESLEK-NLSERKKKSAQERSQA-EEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQ 783
Cdd:PLN02939  333 VDKLEASLKEANVSKFSSYKvELLQQKLKLLEERLQAsDHEIHSYIQLYQESIKEFQDTLSKLKEESKKRSLEH 406
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
568-861 4.62e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.73  E-value: 4.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  568 QRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQsnlMMEKRNNSLQTATENTQAKVTEELAAATAQVshLQL 647
Cdd:PRK02224  240 DEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEE---VRDLRERLEELEEERDDLLAEAGLDDADAEA--VEA 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  648 KMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKfksekqnRKQLELKVTSLEEELTDLRVEKE 727
Cdd:PRK02224  315 RREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREE-------AAELESELEEAREAVEDRREEIE 387

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  728 SLEK---NLSERKKKSAQERSQAEEEIDEIRksyqEELDKLRQLLKKTRVSTdQAAAEQLSLVQAELQtqwEAKCEHLLA 804
Cdd:PRK02224  388 ELEEeieELRERFGDAPVDLGNAEDFLEELR----EERDELREREAELEATL-RTARERVEEAEALLE---AGKCPECGQ 459

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  805 SAKD-EHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALT--KQNEQHIKELEKNKS 861
Cdd:PRK02224  460 PVEGsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEdlVEAEDRIERLEERRE 519
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 686-889 4.92e-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: 48.02  E-value: 4.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  686 ELQETSEQ-AQSKFKSEKQNR--KQLELKVTSL---------EEELTDLRVEKESLEKNLSERKKKSAQERSQAEeeide 753
Cdd:COG3096   793 ERDELAEQyAKASFDVQKLQRlhQAFSQFVGGHlavafapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLD----- 867

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  754 irkSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWEAK------CEHLlaSAKDEHLQQYQEVCAQRDAYQQK 827
Cdd:COG3096   868 ---QLKEQLQLLNKLLPQANLLADETLADRLEELREELDAAQEAQafiqqhGKAL--AQLEPLVAVLQSDPEQFEQLQAD 942

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  828 LVQLQEKCLALQAQITALTK--QNEQHI------------KEL-EKNKSQMSGVEAAASDPSEKVKKI------MNQVFQ 886
Cdd:COG3096   943 YLQAKEQQRRLKQQIFALSEvvQRRPHFsyedavgllgenSDLnEKLRARLEQAEEARREAREQLRQAqaqysqYNQVLA 1022


                  ...
gi 578817219  887 SLR 889
Cdd:COG3096  1023 SLK 1025
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
704-858 5.87e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 5.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  704 NRKQLELK---VTSLEEELTDLRVEKESLE---KNLSERKK---------------KSAQER-SQAEEEIDEIRKSyQEE 761
Cdd:COG4913   608 NRAKLAALeaeLAELEEELAEAEERLEALEaelDALQERREalqrlaeyswdeidvASAEREiAELEAELERLDAS-SDD 686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  762 LDKLRQLLKKTRVSTDQAAAE--QLSLVQAELQTQWEA------KCEHLLASAKDEHLQQYQEVCAQRdaYQQKLVQLQE 833
Cdd:COG4913   687 LAALEEQLEELEAELEELEEEldELKGEIGRLEKELEQaeeeldELQDRLEAAEDLARLELRALLEER--FAAALGDAVE 764

                         170       180
                  ....*....|....*....|....*..
gi 578817219  834 KCL--ALQAQITALTKQNEQHIKELEK 858
Cdd:COG4913   765 RELreNLEERIDALRARLNRAEEELER 791
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 555-875 6.26e-05

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: 47.06  E-value: 6.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   555 SVTMETSMIMSNIQRIIQENERLKQEI-LEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQAKvte 633
Cdd:pfam09731  173 AEISREKATDSALQKAEALAEKLKEVInLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYK--- 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   634 ELAAATAQVSHLQLKmtahqKKETELQMQLTE-SLKETDLLRGQLTKVQAKLSELQEtsEQAQSKfkseKQNRKQLELKV 712
Cdd:pfam09731  250 ELVASERIVFQQELV-----SIFPDIIPVLKEdNLLSNDDLNSLIAHAHREIDQLSK--KLAELK----KREEKHIERAL 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   713 TSLEEELTDLRVE-KESLEKNLSERKKksaQERSQAEEEIDEIRKSYQEELdklrqllkktrvstdqaaaeqlslvQAEL 791
Cdd:pfam09731  319 EKQKEELDKLAEElSARLEEVRAADEA---QLRLEFEREREEIRESYEEKL-------------------------RTEL 370

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   792 QTQWEAKCEHLlasaKDEHLQQYQEvcaqrdayqqklvqLQEKclALQAQITALTKQNEQHIKELEKNKSQMSGVEAAAS 871
Cdd:pfam09731  371 ERQAEAHEEHL----KDVLVEQEIE--------------LQRE--FLQDIKEKVEEERAGRLLKLNELLANLKGLEKATS 430


                   ....
gi 578817219   872 DPSE 875
Cdd:pfam09731  431 SHSE 434
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 514-896 7.05e-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: 47.35  E-value: 7.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   514 QHNTEIRMAVSKVADKMDHLMTKVEELQ-----KHSAGNSMLIPSMSVTMETSMIMSNIQRIIQENERLKQEILEKSNRI 588
Cdd:TIGR00606  688 QTEAELQEFISDLQSKLRLAPDKLKSTEselkkKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI 767

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   589 EEQN-----------------------DKISELIERNQRYVEQ--SNLMMEKRNNSLQTATENTQAKvTEELAAATAQVS 643
Cdd:TIGR00606  768 EEQEtllgtimpeeesakvcltdvtimERFQMELKDVERKIAQqaAKLQGSDLDRTVQQVNQEKQEK-QHELDTVVSKIE 846

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   644 HLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQlelkVTSLEEELTDLR 723
Cdd:TIGR00606  847 LNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQ----DSPLETFLEKDQ 922

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   724 VEKESLEKNLSERKKKSAQERSQAEEEIDEI---RKSYQEELDKLRQLLKKTRVSTDQAAAEQLSlvqaELQTQWEAKCE 800
Cdd:TIGR00606  923 QEKEELISSKETSNKKAQDKVNDIKEKVKNIhgyMKDIENKIQDGKDDYLKQKETELNTVNAQLE----ECEKHQEKINE 998

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   801 HLLASAKDEHLQQYQEvcaqrdayqqKLVQLQEKCLALQAQITALTKQNEQHIKELekNKSQMSGVEAAASDPSEKVKKI 880
Cdd:TIGR00606  999 DMRLMRQDIDTQKIQE----------RWLQDNLTLRKRENELKEVEEELKQHLKEM--GQMQVLQMKQEHQKLEENIDLI 1066

                          410
                   ....*....|....*.
gi 578817219   881 MNQVFQSLRREFELEE 896
Cdd:TIGR00606 1067 KRNHVLALGRQKGYEK 1082
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 568-882 7.38e-05

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: 46.77  E-value: 7.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   568 QRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQT---ATENTQAKVTEELAAATAQVSH 644
Cdd:pfam06160   85 KKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLAnrfSYGPAIDELEKQLAEIEEEFSQ 164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   645 LQLKMTAHQKKETElqMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSekqNRKQLE-----LKVTSLEEEL 719
Cdd:pfam06160  165 FEELTESGDYLEAR--EVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKE---GYREMEeegyaLEHLNVDKEI 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   720 TDLRVEKESLEKNLSERKKKSAQERSQA-EEEIDEI----------RKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQ 788
Cdd:pfam06160  240 QQLEEQLEENLALLENLELDEAEEALEEiEERIDQLydllekevdaKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQ 319

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   789 A-ELQTQWEAKCEHLlasakDEHLQ----QYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEknksQM 863
Cdd:pfam06160  320 SyTLNENELERVRGL-----EKQLEelekRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQ----SL 390

                          330
                   ....*....|....*....
gi 578817219   864 SGVEAAASDPSEKVKKIMN 882
Cdd:pfam06160  391 RKDELEAREKLDEFKLELR 409
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 640-804 7.93e-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: 47.35  E-value: 7.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   640 AQVSHLQLKMTAHQK-KETELQMQLTESLKETDL-LRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLE---LKVTS 714
Cdd:TIGR00606  187 ALETLRQVRQTQGQKvQEHQMELKYLKQYKEKACeIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEhnlSKIMK 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   715 LEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIR-------KSYQEELDKLRQLLKKTRVSTDQAAAEQLSLV 787
Cdd:TIGR00606  267 LDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYhnhqrtvREKERELVDCQRELEKLNKERRLLNQEKTELL 346

                          170
                   ....*....|....*....
gi 578817219   788 --QAELQTQWEAKCEHLLA 804
Cdd:TIGR00606  347 veQGRLQLQADRHQEHIRA 365
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
567-798 8.85e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.43  E-value: 8.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  567 IQRIIQENERLKQEILEKSNRIEEQNDKISELIERnqryveqsnlmMEKRNNSLQTATENTQaKVTEELAAATAQVSHLQ 646
Cdd:COG4372    61 LEQLEEELEQARSELEQLEEELEELNEQLQAAQAE-----------LAQAQEELESLQEEAE-ELQEELEELQKERQDLE 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  647 LKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSE-----QAQSKFKSEKQNRKQLELKVTSLEEELTD 721
Cdd:COG4372   129 QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalseaEAEQALDELLKEANRNAEKEEELAEAEKL 208

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578817219  722 LRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWEAK 798
Cdd:COG4372   209 IESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALEL 285
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
696-883 9.38e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 45.67  E-value: 9.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  696 SKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKsYQEELDKLRQLLKKTRVS 775
Cdd:COG1340     1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQE-LREKRDELNEKVKELKEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  776 TDQaAAEQLSLVQAELQtqwEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLV-------QLQEKCLALQAQITALTKQ 848
Cdd:COG1340    80 RDE-LNEKLNELREELD---ELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVlspeeekELVEKIKELEKELEKAKKA 155

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 578817219  849 NEQHiKELEKNKSQMSGVEAAASDPSEKVKKIMNQ 883
Cdd:COG1340   156 LEKN-EKLKELRAELKELRKEAEEIHKKIKELAEE 189
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 693-879 1.04e-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: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  693 QAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEK---NLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLL 769
Cdd:COG3883    13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEeynELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  770 K---KTRVSTD-----------QAAAEQLSLV-------QAELQTQWEAKCEhlLASAKDEHLQQYQEVCAQRDAYQQKL 828
Cdd:COG3883    93 RalyRSGGSVSyldvllgsesfSDFLDRLSALskiadadADLLEELKADKAE--LEAKKAELEAKLAELEALKAELEAAK 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578817219  829 VQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKK 879
Cdd:COG3883   171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
PTZ00121 PTZ00121
MAEBL; Provisional
 572-1001 1.11e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  572 QENERLKQEILEKSNRIEEQNDKISEliERNQRYVEQSNLMMEKRN-NSLQTATENTQAKVTEELAAATAQVSHLQLKMT 650
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKAEAAEKKKE--EAKKKADAAKKKAEEKKKaDEAKKKAEEDKKKADELKKAAAAKKKADEAKKK 1426

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  651 AHQKKETELQMQLTESLKETDllrgQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLEL-KVTSLEEELTDLRVEKESL 729
Cdd:PTZ00121 1427 AEEKKKADEAKKKAEEAKKAD----EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAkKADEAKKKAEEAKKKADEA 1502

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  730 EKnlSERKKKSAQERSQAEE--EIDEIRKSyqEELDKLRQLLK--KTRVSTDQAAAEQLSLVQAELQTQWEAKCEH--LL 803
Cdd:PTZ00121 1503 KK--AAEAKKKADEAKKAEEakKADEAKKA--EEAKKADEAKKaeEKKKADELKKAEELKKAEEKKKAEEAKKAEEdkNM 1578

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  804 ASAKDEHLQQYQEvcaQRDAYQQKLVQLQEKCLALQAQitaltKQNEQHIK--ELEKNKSQMSGVEAAASDPSEKVKKIm 881
Cdd:PTZ00121 1579 ALRKAEEAKKAEE---ARIEEVMKLYEEEKKMKAEEAK-----KAEEAKIKaeELKKAEEEKKKVEQLKKKEAEEKKKA- 1649

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  882 nqvfQSLRREFEleesyngrtilgtiMNTIKMVTLQllnqqeQEKEESSSEEEEEKAEERPRRPSQEQSASASSGQPQAP 961
Cdd:PTZ00121 1650 ----EELKKAEE--------------ENKIKAAEEA------KKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 578817219  962 LNRERPESPMVPSEQV--VEEAVPLPPQALTTSQDGHRRKGD 1001
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELkkAEEENKIKAEEAKKEAEEDKKKAE 1747
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
567-766 1.18e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.57  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  567 IQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQsnlMMEKRNNSlQTATENTQaKVTEELAAATAQVSHLq 646
Cdd:PRK02224  511 IERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE---AEEKREAA-AEAEEEAE-EAREEVAELNSKLAEL- 584

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  647 lkmtahqKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFkSEKQNRKQlelkvtSLEEELTDLRVEK 726
Cdd:PRK02224  585 -------KERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERL-AEKRERKR------ELEAEFDEARIEE 650

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 578817219  727 esleknlserkkksAQERSQ-AEEEIDEIrksyQEELDKLR 766
Cdd:PRK02224  651 --------------AREDKErAEEYLEQV----EEKLDELR 673
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 662-869 1.23e-04

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 46.48  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  662 QLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSlEEELTDLRVEKESLEKNLSERKKKSA 741
Cdd:COG3096   499 ELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDA-AEELEELLAELEAQLEELEEQAAEAV 577

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  742 QERSQAEEEIDEIRKSYQEeldkLRQLLKKTRVStdQAAAEQLslvqaelqtqweakCEHLlasakDEHLQQYQEVcaqr 821
Cdd:COG3096   578 EQRSELRQQLEQLRARIKE----LAARAPAWLAA--QDALERL--------------REQS-----GEALADSQEV---- 628

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578817219  822 DAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELeknkSQMSGVEAA 869
Cdd:COG3096   629 TAAMQQLLEREREATVERDELAARKQALESQIERL----SQPGGAEDP 672
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 660-893 1.27e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 45.98  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  660 QMQLT-ESLKETDLLRGQLTKVQA-KLSELQETSEQA-----QSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKn 732
Cdd:PRK04778   55 KLNLTgQSEEKFEEWRQKWDEIVTnSLPDIEEQLFEAeelndKFRFRKAKHEINEIESLLDLIEEDIEQILEELQELLE- 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  733 lSErkKKSAQERSQAEEEIDEIRK-------SYQEELDKLRQLLKKTRVSTDQ-----------AAAEQLSLVQAELqTQ 794
Cdd:PRK04778  134 -SE--EKNREEVEQLKDLYRELRKsllanrfSFGPALDELEKQLENLEEEFSQfveltesgdyvEAREILDQLEEEL-AA 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  795 WEAKCEH---LLASAKDEHLQQYQEVcaqRDAYQQKLVQ---LQEkcLALQAQITALTKQ---NEQHIKELEknksqmsg 865
Cdd:PRK04778  210 LEQIMEEipeLLKELQTELPDQLQEL---KAGYRELVEEgyhLDH--LDIEKEIQDLKEQideNLALLEELD-------- 276

                         250       260       270
                  ....*....|....*....|....*....|.
gi 578817219  866 VEAAasdpSEKVKKI---MNQVFQSLRREFE 893
Cdd:PRK04778  277 LDEA----EEKNEEIqerIDQLYDILEREVK 303
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 647-772 1.32e-04

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


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 45.49  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  647 LKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSekqnrkqLELKVTSLEEELTDLRVEK 726
Cdd:COG4026   121 LKSLQNIPEYNELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKK-------LREENSILEEEFDNIKSEY 193

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 578817219  727 ESLEKNLSERKKKSAQERSQAEEEIDEIrksYQEELDKLRQLLKKT 772
Cdd:COG4026   194 SDLKSRFEELLKKRLLEVFSLEELWKEL---FPEELPEEDFIYFAT 236
mukB PRK04863
chromosome partition protein MukB;
611-845 1.34e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.49  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  611 LMMEKRNNSLQTAteNTQ-AKVTEELAAATAQVSHLQlkmtAHQK-KETELQmqltesLKETDLLRGQLTKVQAKLSELQ 688
Cdd:PRK04863  459 LSLEQKLSVAQAA--HSQfEQAYQLVRKIAGEVSRSE----AWDVaRELLRR------LREQRHLAEQLQQLRMRLSELE 526

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  689 ETSEQAQSKFKSEKQNRKQLELKVTSlEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEideirksyQEELDKLRQL 768
Cdd:PRK04863  527 QRLRQQQRAERLLAEFCKRLGKNLDD-EDELEQLQEELEARLESLSESVSEARERRMALRQQ--------LEQLQARIQR 597

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  769 LKKTRVS--TDQAAAEQLSlvqaelqtqwEAKCEHLLASAK-DEHLQQYQEvcaQRDAYQQKLVQLQEKCLALQAQITAL 845
Cdd:PRK04863  598 LAARAPAwlAAQDALARLR----------EQSGEEFEDSQDvTEYMQQLLE---RERELTVERDELAARKQALDEEIERL 664
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 584-897 1.38e-04

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: 46.50  E-value: 1.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   584 KSNRIEEQNDK-ISELIErnqrYVEQSNLMMEKRNNSLQTATEnTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQ 662
Cdd:pfam02463  143 KIEIIAMMKPErRLEIEE----EAAGSRLKRKKKEALKKLIEE-TENLAELIIDLEELKLQELKLKEQAKKALEYYQLKE 217

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   663 LTESLKETdllrgqlTKVQAKLSELQETSEQAQSKfKSEKQNRKQLELKVTSLEEELTD----LRVEKESLEKNLSERKK 738
Cdd:pfam02463  218 KLELEEEY-------LLYLDYLKLNEERIDLLQEL-LRDEQEEIESSKQEIEKEEEKLAqvlkENKEEEKEKKLQEEELK 289

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   739 KSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQA--ELQTQWEAKCEHLLASAKDEHLQQYQE 816
Cdd:pfam02463  290 LLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELekELKELEIKREAEEEEEEELEKLQEKLE 369

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   817 VCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFELEE 896
Cdd:pfam02463  370 QLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEE 449


                   .
gi 578817219   897 S 897
Cdd:pfam02463  450 K 450
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
518-764 1.40e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 45.29  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  518 EIRMAVSKVADKMDHLmtkVEELQKHSAGNSMLIPSMSVTMETsmiMSNIQRIIQENERLKQEILEKSNRIEE-----QN 592
Cdd:COG1340    54 ELREEAQELREKRDEL---NEKVKELKEERDELNEKLNELREE---LDELRKELAELNKAGGSIDKLRKEIERlewrqQT 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  593 DKISelIERNQRYVEQSNLMMEKrnnsLQTATEntQAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDL 672
Cdd:COG1340   128 EVLS--PEEEKELVEKIKELEKE----LEKAKK--ALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIE 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  673 LRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNlsERKKKSAQERSQAEEE-- 750
Cdd:COG1340   200 LYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKRE--KEKEELEEKAEEIFEKlk 277

                         250       260
                  ....*....|....*....|
gi 578817219  751 ------IDEIRKSYQEELDK 764
Cdd:COG1340   278 kgekltTEELKLLQKSGLLE 297
Rabaptin pfam03528
Rabaptin;
653-860 1.40e-04

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 45.87  E-value: 1.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   653 QKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEqaqskfksEKQNRKQLELKVTslEEELTDLRVEKESLEKN 732
Cdd:pfam03528    7 QQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKE--------EDLKRQNAVLQEA--QVELDALQNQLALARAE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   733 LSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWE------AKCEHLLASA 806
Cdd:pfam03528   77 MENIKAVATVSENTKQEAIDEVKSQWQEEVASLQAIMKETVREYEVQFHRRLEQERAQWNQYREsaereiADLRRRLSEG 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 578817219   807 KDEHLQQYQEVCAQRDAYQQKLV--QLQEKCLALQAQITaltkQNEQHIKELEKNK 860
Cdd:pfam03528  157 QEEENLEDEMKKAQEDAEKLRSVvmPMEKEIAALKAKLT----EAEDKIKELEASK 208
PRK00106 PRK00106
ribonuclease Y;
629-790 1.44e-04

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 46.01  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  629 AKVTEELAAATAQvshlQLKMTAHQKKETELQMQLTESLKETDLLRGQLTkVQAKlSELQETSEQAQSKFKSEKQNRKQL 708
Cdd:PRK00106   29 AKEAAELTLLNAE----QEAVNLRGKAERDAEHIKKTAKRESKALKKELL-LEAK-EEARKYREEIEQEFKSERQELKQI 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  709 ELKVT----SL---EEELTDLRVEKESLEKNLSErKKKSAQERsqaEEEIDEIRKSYQEELDKLRQLlkktrvstDQAAA 781
Cdd:PRK00106  103 ESRLTeratSLdrkDENLSSKEKTLESKEQSLTD-KSKHIDER---EEQVEKLEEQKKAELERVAAL--------SQAEA 170


                  ....*....
gi 578817219  782 EQLSLVQAE 790
Cdd:PRK00106  171 REIILAETE 179
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 572-784 1.83e-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: 45.62  E-value: 1.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   572 QENERLKQEILEKSNRIEEQNDKISELIER-NQRYVeqsnlmmekrnnsLQTATENTQAKVTEELAAATAQVSHLQLKMT 650
Cdd:pfam06160  287 KYVEKNLPEIEDYLEHAEEQNKELKEELERvQQSYT-------------LNENELERVRGLEKQLEELEKRYDEIVERLE 353

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   651 AHQKKETELQMQLTESLKetdllrgQLTKVQAKLSELQetsEQAQSKFKSEKQNRKQLELKVTSLEEelTDLRVEKE--- 727
Cdd:pfam06160  354 EKEVAYSELQEELEEILE-------QLEEIEEEQEEFK---ESLQSLRKDELEAREKLDEFKLELRE--IKRLVEKSnlp 421

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578817219   728 SLEKNLSERKKKSAQERSQAEEE-------IDEIRKSYQEELDKLRQLLKKTRVSTDQAA-AEQL 784
Cdd:pfam06160  422 GLPESYLDYFFDVSDEIEDLADElnevplnMDEVNRLLDEAQDDVDTLYEKTEELIDNATlAEQL 486
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
 630-848 1.89e-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: 44.71  E-value: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   630 KVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQS-------KFKSEK 702
Cdd:pfam06008   16 KINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGhakelaeAIKNLI 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   703 QNRKQLELKVTSLEEELTDLRVEK-------------ESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLL 769
Cdd:pfam06008   96 DNIKEINEKVATLGENDFALPSSDlsrmlaeaqrmlgEIRSRDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALA 175

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578817219   770 KKTRvstdqaaaEQLSLVQAELQTQWEAKCEHLLASAKDEHLQqyQEVCAQRDAYQQKLVQLQEkclaLQAQITALTKQ 848
Cdd:pfam06008  176 NALR--------DSLAEYEAKLSDLRELLREAAAKTRDANRLN--LANQANLREFQRKKEEVSE----QKNQLEETLKT 240
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 703-880 1.90e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.59  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  703 QNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDK-LRQLLKKTRVSTDQAAA 781
Cdd:PRK00409  527 ELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEiIKELRQLQKGGYASVKA 606

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  782 EQLSLVQAELQTQWEAKCEHLLASAKDEH-LQQYQEVcaqrdayqqKLVQLQEKclalqAQITALTKQNE---Q------ 851
Cdd:PRK00409  607 HELIEARKRLNKANEKKEKKKKKQKEKQEeLKVGDEV---------KYLSLGQK-----GEVLSIPDDKEaivQagimkm 672

                         170       180       190
                  ....*....|....*....|....*....|.
gi 578817219  852 --HIKELEKNKSQmsgveaaasdPSEKVKKI 880
Cdd:PRK00409  673 kvPLSDLEKIQKP----------KKKKKKKP 693
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
 572-899 2.06e-04

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 45.98  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  572 QENERLKQEILEKSNRIEEQNDKISELIERN----QRYVEQSNLMMEKRNNSLQTATENT--QAKVTEELAAATAQVSHL 645
Cdd:PTZ00440  560 KLKRSMKNDIKNKIKYIEENVDHIKDIISLNdeidNIIQQIEELINEALFNKEKFINEKNdlQEKVKYILNKFYKGDLQE 639

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  646 QLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQ-ETSEQAQSKFKSEKQNRKQLE--------------- 709
Cdd:PTZ00440  640 LLDELSHFLDDHKYLYHEAKSKEDLQTLLNTSKNEYEKLEFMKsDNIDNIIKNLKKELQNLLSLKeniikkqlnnieqdi 719

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  710 --------LKVTSLEEELTDLRVEKESLE---KNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQ 778
Cdd:PTZ00440  720 snslnqytIKYNDLKSSIEEYKEEEEKLEvykHQIINRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTILNKENKISND 799

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  779 AAA--EQLSLVQAELQTqWEAKCEHLLASA--KDEHLQQYQEVCAQRDAyQQKLVQLQEKCLALQAQITALTKQNEQHIK 854
Cdd:PTZ00440  800 INIlkENKKNNQDLLNS-YNILIQKLEAHTekNDEELKQLLQKFPTEDE-NLNLKELEKEFNENNQIVDNIIKDIENMNK 877

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 578817219  855 ELEKNKSQMSGVEAAASDPS--EKVKKIMNQVFQSLRREFELEESYN 899
Cdd:PTZ00440  878 NINIIKTLNIAINRSNSNKQlvEHLLNNKIDLKNKLEQHMKIINTDN 924
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 559-830 2.08e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.91  E-value: 2.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   559 ETSMIMSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNnslqtatENTQAKVTEELAAA 638
Cdd:pfam13868   99 EREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERI-------LEYLKEKAEREEER 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   639 TAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLtkvqakLSELQETSEQAQSKFKSEKQNRKQLELKvtsleee 718
Cdd:pfam13868  172 EAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKL------YQEEQERKERQKEREEAEKKARQRQELQ------- 238

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   719 ltdlrvekESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWEAK 798
Cdd:pfam13868  239 --------QAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAER 310

                          250       260       270
                   ....*....|....*....|....*....|..
gi 578817219   799 cehllasakdEHLQQYQEVCAQRDAYQQKLVQ 830
Cdd:pfam13868  311 ----------EEELEEGERLREEEAERRERIE 332
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
665-773 2.16e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 45.62  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  665 ESLKEtdLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNR-KQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQE 743
Cdd:COG2433   376 LSIEE--ALEELIEKELPEEEPEAEREKEHEERELTEEEEEiRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEA 453

                          90       100       110
                  ....*....|....*....|....*....|..
gi 578817219  744 RSQAEEEIDEIRK--SYQEELDKLRQLLKKTR 773
Cdd:COG2433   454 RSEERREIRKDREisRLDREIERLERELEEER 485
EzrA COG4477
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ...
 511-864 2.23e-04

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


Pssm-ID: 443574 [Multi-domain]  Cd Length: 567  Bit Score: 45.22  E-value: 2.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  511 EARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMlipsmsvtmetsmimsNIQRIIQENERLKQEILEKSN---- 586
Cdd:COG4477   101 KAKKALDEIEQLLDEIEEEIEEILEELEELLESEEKNRE----------------EIEELKEKYRELRKTLLAHRHsfgp 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  587 ---RIEEQNDKISELIERNQRYVEQSNlMMEKRN--NSLQTATENTQAKVTE----------ELAAATAQVSHLQLKMTA 651
Cdd:COG4477   165 aaeELEKQLEELEPEFEEFEELTESGD-YLEAREilEQLEEELNALEELMEEippllkelqtELPDQLEELKSGYREMKE 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  652 ------HQKKETELQmQLTESLKET--DLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLR 723
Cdd:COG4477   244 qgyvleHLNIEKEIE-QLEEQLKEAleLLEELDLDEAEEELEEIEEEIDELYDLLEKEVEAKKYVDKNQEELEEYLEHLK 322

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  724 VEKESLEknlserkkksaqersqaeEEIDEIRKSYQ---EELDKLRQLLKktrvstdqaaaeQLSLVQAELQTqweakce 800
Cdd:COG4477   323 EQNRELK------------------EEIDRVQQSYRlneNELEKVRNLEK------------QIEELEKRYDE------- 365

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578817219  801 hlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKqNEQHIKE-LEKNKSQMS 864
Cdd:COG4477   366 --IDERIEEEKVAYSELQEELEEIEEQLEEIEEEQEEFSEKLKSLRK-DELEAREkLDELKKKLR 427
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
563-762 2.89e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  563 IMSNIQRIIQENERLKQEILEKS-NRIEEQNDKISELIERNQRYVEQSNLMMEKRnnslqtATENTQAKVTEELAAATAQ 641
Cdd:PRK03918  561 LEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKELE------REEKELKKLEEELDKAFEE 634

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  642 VSHLQLKMTAHQKKETELQMQLTES-----LKETDLLRGQLTKVQAKLSELQETSEQAQS---KFKSEKQNRKQLELKVT 713
Cdd:PRK03918  635 LAETEKRLEELRKELEELEKKYSEEeyeelREEYLELSRELAGLRAELEELEKRREEIKKtleKLKEELEEREKAKKELE 714

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578817219  714 SLEEELTDLRVEKESLeknlserKKKSAQERSQAEEEIDEIRKSYQEEL 762
Cdd:PRK03918  715 KLEKALERVEELREKV-------KKYKALLKERALSKVGEIASEIFEEL 756
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 307-495 3.13e-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: 45.14  E-value: 3.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   307 SAAPSPIPGADNLSADPVVSPPTSIPFKSGEPALRTKSnslseqlAINTSPDAVKAKLISRMAKMgQPMLPILPPQldsn 386
Cdd:pfam03154  192 TQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHT-------LIQQTPTLHPQRLPSPHPPL-QPMTQPPPPS---- 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   387 dseiedvntlqgggQPVVTPSVQPSLHPAHPALPQMTSQAPqpsvTGLQAPSAAL-MQVSSLDSHSAVSGNAQSFQPYAG 465
Cdd:pfam03154  260 --------------QVSPQPLPQPSLHGQMPPMPHSLQTGP----SHMQHPVPPQpFPLTPQSSQSQVPPGPSPAAPGQS 321

                          170       180       190
                   ....*....|....*....|....*....|..
gi 578817219   466 MQAYAYPQASAVTSQLQPVR--PLYPAPLSQP 495
Cdd:pfam03154  322 QQRIHTPPSQSQLQSQQPPReqPLPPAPLSMP 353
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 528-803 4.30e-04

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: 44.72  E-value: 4.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   528 DKMDHLMTKVEELQKHSAGNSMLIPSMSVTMEtsmimsNIQRIIQENERLKQEIL-EKSNRIEEQNDKISELIE------ 600
Cdd:pfam15921  541 DHLRNVQTECEALKLQMAEKDKVIEILRQQIE------NMTQLVGQHGRTAGAMQvEKAQLEKEINDRRLELQEfkilkd 614

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   601 ---RNQRYVEQ--SNLMMEK------RNNSLQTATENTQAK--VTEELAAATAQVSHLQ-----LKMTAHQKKE------ 656
Cdd:pfam15921  615 kkdAKIRELEArvSDLELEKvklvnaGSERLRAVKDIKQERdqLLNEVKTSRNELNSLSedyevLKRNFRNKSEemettt 694

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   657 TELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESL--EKN-L 733
Cdd:pfam15921  695 NKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLkeEKNkL 774

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578817219   734 SERKKKSAQERSQAEEEIDEIRKsyQEEldKLRQLLKKTRVSTDQAA---AEQLSLVQAELQTQWEAKCEHLL 803
Cdd:pfam15921  775 SQELSTVATEKNKMAGELEVLRS--QER--RLKEKVANMEVALDKASlqfAECQDIIQRQEQESVRLKLQHTL 843
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 653-774 4.47e-04

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 44.69  E-value: 4.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  653 QKKETELQMQLTESLKETDLLRGQ-LTKVQAKLSELQETSEQAQSKFKSEKQnrkqLELKVTSLEEELTDLRVEKESLEK 731
Cdd:COG0542   417 ERRLEQLEIEKEALKKEQDEASFErLAELRDELAELEEELEALKARWEAEKE----LIEEIQELKEELEQRYGKIPELEK 492

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  732 NLSERKKKSAQERSQAEEEIDE--------------IRKSYQEELDKLRQL---LKKtRV 774
Cdd:COG0542   493 ELAELEEELAELAPLLREEVTEediaevvsrwtgipVGKLLEGEREKLLNLeeeLHE-RV 551
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
 632-767 4.64e-04

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: 41.03  E-value: 4.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   632 TEELAAATAQVSHLQLKMTAHQKKetelqmqlTESLK--ETDLlrgqltkvqAKLSELQETSEQAQSKFKSEKQNRKQLE 709
Cdd:pfam18595    1 SSTLAEEKEELAELERKARELQAK--------IDALQvvEKDL---------RSCIKLLEEIEAELAKLEEAKKKLKELR 63

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 578817219   710 LKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIrksyQEELDKLRQ 767
Cdd:pfam18595   64 DALEEKEIELRELERREERLQRQLENAQEKLERLREQAEEKREAA----QARLEELRE 117
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 597-765 5.19e-04

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


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 42.23  E-value: 5.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   597 ELIERNQRYVEQSNLMmEKRNNSLQTATE----NTQAKVTEELAAATAQVSHLQLKMTAHQKketelqmQLTESLKETDL 672
Cdd:pfam08614    4 ELIDAYNRLLDRTALL-EAENAKLQSEPEsvlpSTSSSKLSKASPQSASIQSLEQLLAQLRE-------ELAELYRSRGE 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   673 LRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEEL-------TDLRVEKESLekNLserkkksaqERS 745
Cdd:pfam08614   76 LAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELrekrklnQDLQDELVAL--QL---------QLN 144

                          170       180
                   ....*....|....*....|
gi 578817219   746 QAEEEIDEIRKSYQEELDKL 765
Cdd:pfam08614  145 MAEEKLRKLEKENRELVERW 164
PRK11637 PRK11637
AmiB activator; Provisional
 577-790 6.01e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 43.91  E-value: 6.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  577 LKQEILEKSNRIEEQNDKISELIERNQryvEQSNLMMEKrNNSLQTaTENTQAKVTEELAAATAQVSHL----------- 645
Cdd:PRK11637   52 IQQDIAAKEKSVRQQQQQRASLLAQLK---KQEEAISQA-SRKLRE-TQNTLNQLNKQIDELNASIAKLeqqqaaqerll 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  646 --QLKMTAHQKKETELQMQLT--ESLKETDLLR--GQLTKV-QAKLSELQETSEQAQskfksekQNRKQLELKVTSLEEE 718
Cdd:PRK11637  127 aaQLDAAFRQGEHTGLQLILSgeESQRGERILAyfGYLNQArQETIAELKQTREELA-------AQKAELEEKQSQQKTL 199

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578817219  719 LTDLRVEKESLEKNLSERKKKSAQERSQAEEEideirksyQEELDKLRQllKKTRVSTDQAAAEQLSLVQAE 790
Cdd:PRK11637  200 LYEQQAQQQKLEQARNERKKTLTGLESSLQKD--------QQQLSELRA--NESRLRDSIARAEREAKARAE 261
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 655-895 6.14e-04

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: 43.73  E-value: 6.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   655 KETELQMQLTESLKEtdllRGQLTKVQAKLSELQETSEQAQSKFKSE-KQNRKQLELKVTSLEEELTDLRVEKESLEknl 733
Cdd:pfam07888   28 RAELLQNRLEECLQE----RAELLQAQEAANRQREKEKERYKRDREQwERQRRELESRVAELKEELRQSREKHEELE--- 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   734 sERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTrvstdQAAAEQLSLVQAELQTQWEaKCEHLLASAKDEHlqq 813
Cdd:pfam07888  101 -EKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDI-----KTLTQRVLERETELERMKE-RAKKAGAQRKEEE--- 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   814 yqevcAQRDAYQQKLVQLQEKCLALQaqitaltkqneqhiKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFE 893
Cdd:pfam07888  171 -----AERKQLQAKLQQTEEELRSLS--------------KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE 231


                   ..
gi 578817219   894 LE 895
Cdd:pfam07888  232 NE 233
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 558-858 6.27e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 44.06  E-value: 6.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  558 METSMIMSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIER-NQRYVEQSNLMMEKR------NNSLQTATENTQAK 630
Cdd:PRK04778  101 RKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQlKDLYRELRKSLLANRfsfgpaLDELEKQLENLEEE 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  631 VtEELAAATAQVSHLQLKMTAHQKKETELQM-QLTESLKEtdLLRGQLTKVQAKLSELQETSEQAqskfksEKQNRKqle 709
Cdd:PRK04778  181 F-SQFVELTESGDYVEAREILDQLEEELAALeQIMEEIPE--LLKELQTELPDQLQELKAGYREL------VEEGYH--- 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  710 LKVTSLEEELTDLRVEKESLEKNLSERKKKSAQER-SQAEEEIDEI----------RKSYQEELDKLRQLLKKTRVSTDQ 778
Cdd:PRK04778  249 LDHLDIEKEIQDLKEQIDENLALLEELDLDEAEEKnEEIQERIDQLydilerevkaRKYVEKNSDTLPDFLEHAKEQNKE 328

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  779 AAAEQLSLVQA------ELQTQWEAKCEhlLASAKDEHLQQYQEVCAQRDAYQqklvQLQEKCLALQAQITALTKQNEQ- 851
Cdd:PRK04778  329 LKEEIDRVKQSytlnesELESVRQLEKQ--LESLEKQYDEITERIAEQEIAYS----ELQEELEEILKQLEEIEKEQEKl 402


                  ....*....
gi 578817219  852 --HIKELEK 858
Cdd:PRK04778  403 seMLQGLRK 411
COG5022 COG5022
Myosin heavy chain [General function prediction only];
571-907 6.44e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 44.30  E-value: 6.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  571 IQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENtqAKVTEELAAATAQVSHLQLKMT 650
Cdd:COG5022   799 LQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRS--LKAKKRFSLLKKETIYLQSAQR 876

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  651 AhQKKETELQmQLTESLKETDLLRGQLTKVQAKLSEL---QETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKE 727
Cdd:COG5022   877 V-ELAERQLQ-ELKIDVKSISSLKLVNLELESEIIELkksLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLP 954

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  728 SLEKNLSERK--KKSAQERS----QAEEEIDEIRKSyQEELDKLRQLLKKTRVSTD--QAAAEQLSLVQAELQTQWEAkc 799
Cdd:COG5022   955 ELNKLHEVESklKETSEEYEdllkKSTILVREGNKA-NSELKNFKKELAELSKQYGalQESTKQLKELPVEVAELQSA-- 1031

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  800 EHLLASAKDEhLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITaLTKQNEQHIKELEKNKSQMSGVEAA--------AS 871
Cdd:COG5022  1032 SKIISSESTE-LSILKPLQKLKGLLLLENNQLQARYKALKLRRE-NSLLDDKQLYQLESTENLLKTINVKdlevtnrnLV 1109

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 578817219  872 DPSEKVKKImnqVFQSLRREFELEESYNGRTILGTI 907
Cdd:COG5022  1110 KPANVLQFI---VAQMIKLNLLQEISKFLSQLVNTL 1142
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 942-1111 6.55e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 43.91  E-value: 6.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  942 PRRPSQeqsasassgqPQAPLNRERPESPMVP--SEQVVEEAVPLPPQALTTSQDGHRRKGDSEAE-----ALSEIKDGS 1014
Cdd:PTZ00449  633 PKRPPP----------PQRPSSPERPEGPKIIksPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKEtkttvVLDESFESI 702

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219 1015 LPPELSCIPSHRVLGPPTSIPPEPLGPVSMDSECEESLAASPMAAKPDNP--SGKVCVREVAPDGPLQESSTRL----SL 1088
Cdd:PTZ00449  703 LKETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPpeEERTFFHETPADTPLPDILAEEfkeeDI 782

                         170       180
                  ....*....|....*....|....*
gi 578817219 1089 TSDPEEGDPLALGPESPGE--PQPP 1111
Cdd:PTZ00449  783 HAETGEPDEAMKRPDSPSEheDKPP 807
YkyA pfam10368
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ...
 679-858 8.18e-04

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: 41.81  E-value: 8.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   679 KVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQA-EEEIDEIRKS 757
Cdd:pfam10368    1 SPEEKIYDHLEEAVELEKPFEEQQEPLVELEKKEQELYEEIIELGMDEFDEIKKLSDEALENVEEREELlEKEKESIEEA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   758 YqEELDKLRQLLKKTRvstDQAAAEQLSLVQAELQTQWEAkceHllasakDEHLQQYQE-VCAQRDAY---QQKLVQLQE 833
Cdd:pfam10368   81 K-EEFKKIKEIIEEIE---DEELKKEAEELIDAMEERYEA---Y------DELYDAYKKaLELDKELYemlKDEDLTLEE 147

                          170       180
                   ....*....|....*....|....*
gi 578817219   834 kclaLQAQITALTKQNEQHIKELEK 858
Cdd:pfam10368  148 ----LQEQIEKINESYEEVKEANEQ 168
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 717-848 8.94e-04

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


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 40.70  E-value: 8.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   717 EELTDLRVEKESLEKNLS--ERKKKSAQERSQAEEEI-DEIRKSYQEELdklrqLLKKTRVSTDQAAAEQLSLVQAELQt 793
Cdd:pfam07926    1 AELSSLQSEIKRLKEEAAdaEAQLQKLQEDLEKQAEIaREAQQNYEREL-----VLHAEDIKALQALREELNELKAEIA- 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 578817219   794 QWEAKCEhllaSAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQ 848
Cdd:pfam07926   75 ELKAEAE----SAKAELEESEESWEEQKKELEKELSELEKRIEDLNEQNKLLHDQ 125
PHA03247 PHA03247
large tegument protein UL36; Provisional
 958-1194 9.55e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 9.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  958 PQAPLNRERPESPMVPSEQVVEeavPLPPQALTTSQDghrrkgdseAEALSEIKDGSLPPELscipshrvlgPPTSIPPE 1037
Cdd:PHA03247 2506 PDAPPAPSRLAPAILPDEPVGE---PVHPRMLTWIRG---------LEELASDDAGDPPPPL----------PPAAPPAA 2563

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219 1038 PlgpvsmdsecEESLAASPMAAKPDNPSgkVCVREVAPDGPLQESSTRLSLT---SDPEEGDPLALGPESPGEPQPPQLK 1114
Cdd:PHA03247 2564 P----------DRSVPPPRPAPRPSEPA--VTSRARRPDAPPQSARPRAPVDdrgDPRGPAPPSPLPPDTHAPDPPPPSP 2631

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219 1115 KDDVTSSTGPHKELSSTEAGSTVAGAALRPSHHSQRSSLS-GDEEDELFKGATLKALRPKAQPeeededeVSMKGRPPPT 1193
Cdd:PHA03247 2632 SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGrAAQASSPPQRPRRRAARPTVGS-------LTSLADPPPP 2704


                  .
gi 578817219 1194 P 1194
Cdd:PHA03247 2705 P 2705
AmmeMemoSam_B TIGR04336
AmmeMemoRadiSam system protein B; Members of this protein family belong to the same domain ...
 1004-1062 9.87e-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: 9.87e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817219  1004 AEALSEIKDGslPPELSCI--PSHRVLGPPTSIPPE-----PLGPVSMDSECEESLAASPMAAKPD 1062
Cdd:TIGR04336   55 AHAYAALKKG--RPETVVLlgPNHTGYGSGIALPPEgswetPLGDVPVDEELAEELLEHSPIIELD 118
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 1014-1194 1.13e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.24  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219 1014 SLPPELSCIPSHRVLGPPTSIPPEPLGPVSMDSECEESLAASPMAAKPDNPSGKVCVREVAPDGPLQESSTRLSLTSDPE 1093
Cdd:PHA03307   92 LSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQ 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219 1094 EGDPLALGPES---PGEPQPPQLKKDDVTSSTGPHKELSSTEAGSTVAGAALRPShhSQRSSLSGDEEDELfkgatlkal 1170
Cdd:PHA03307  172 AALPLSSPEETaraPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGR--SAADDAGASSSDSS--------- 240

                         170       180
                  ....*....|....*....|....
gi 578817219 1171 rpKAQPEEEDEDEVSMKGRPPPTP 1194
Cdd:PHA03307  241 --SSESSGCGWGPENECPLPRPAP 262
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 645-797 1.19e-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: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  645 LQLKMTAHQKKETELQMQLTESLKE-TDLLRGQLTKVQAKLSELQEtseqAQSKFKSE-KQNRKQLELKVTSLEEELTD- 721
Cdd:cd22656    97 LELIDDLADATDDEELEEAKKTIKAlLDDLLKEAKKYQDKAAKVVD----KLTDFENQtEKDQTALETLEKALKDLLTDe 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  722 -LRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRqllKKTRVSTD-QAAAEQLSLVQA---------- 789
Cdd:cd22656   173 gGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLA---AALRLIADlTAADTDLDNLLAligpaipale 249


                  ....*...
gi 578817219  790 ELQTQWEA 797
Cdd:cd22656   250 KLQGAWQA 257
46 PHA02562
endonuclease subunit; Provisional
 530-776 1.28e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.08  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  530 MDHLM-TKVEELQKHSAGNSMLIpsmsvtmetsmimSNIQRIIQENERLKQEILEKSN-RIEEQNDKISELIERNQRYV- 606
Cdd:PHA02562  168 MDKLNkDKIRELNQQIQTLDMKI-------------DHIQQQIKTYNKNIEEQRKKNGeNIARKQNKYDELVEEAKTIKa 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  607 EQSNLMMEKRNNSLQTA-TENTQAKVTEELAAATAQVSHLQLKMTAHQK----------------KETELQMQLTESLKE 669
Cdd:PHA02562  235 EIEELTDELLNLVMDIEdPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqqisegpdRITKIKDKLKELQHS 314

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  670 TDLLRGQLTKVQAKLSELQETSEQA---QSKFKSEKQNRKQLELKVTSLE---EELTDLRVEKESLEKNLSERKKKSAQE 743
Cdd:PHA02562  315 LEKLDTAIDELEEIMDEFNEQSKKLlelKNKISTNKQSLITLVDKAKKVKaaiEELQAEFVDNAEELAKLQDELDKIVKT 394

                         250       260       270
                  ....*....|....*....|....*....|...
gi 578817219  744 RSQAEEEIDeirksyqeELDKLRQLLKKTRVST 776
Cdd:PHA02562  395 KSELVKEKY--------HRGIVTDLLKDSGIKA 419
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 539-796 1.53e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 42.73  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  539 ELQKHSAGNSMLIPSMSVTMETSMIMsniQRIIQENERLkqeiLEKSNRIEEQNDK---ISELIerNQRYVEQSnlmmEK 615
Cdd:PRK10929   83 ELRQQLNNERDEPRSVPPNMSTDALE---QEILQVSSQL----LEKSRQAQQEQDRareISDSL--SQLPQQQT----EA 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  616 RNnSLQTATENTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQM-QLTESLKE------TDLLRGQLTKVQAKLSELQ 688
Cdd:PRK10929  150 RR-QLNEIERRLQTLGTPNTPLAQAQLTALQAESAALKALVDELELaQLSANNRQelarlrSELAKKRSQQLDAYLQALR 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  689 ET-SEQAQSKFKSEKQNRKQLELKVTSLEEELTD-LRVEKEsLEKNLSERKKK----SAQERsQAEEEIDEIRKS----- 757
Cdd:PRK10929  229 NQlNSQRQREAERALESTELLAEQSGDLPKSIVAqFKINRE-LSQALNQQAQRmdliASQQR-QAASQTLQVRQAlntlr 306

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  758 ---------------------------------------------YQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQ 792
Cdd:PRK10929  307 eqsqwlgvsnalgealraqvarlpempkpqqldtemaqlrvqrlrYEDLLNKQPQLRQIRQADGQPLTAEQNRILDAQLR 386


                  ....
gi 578817219  793 TQWE 796
Cdd:PRK10929  387 TQRE 390
tig TIGR00115
trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first ...
 178-251 1.64e-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: 42.16  E-value: 1.64e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817219   178 LDAVLSQ--DLIVADGPAVEVGDSLEVAYTGwlfqnHVLGQVFDSTANKDklLRLKLGSGKVIKGWEDGMLGMKKG 251
Cdd:TIGR00115  131 LERLREQnaTLVPVERGAAEKGDRVTIDFEG-----FIDGEAFEGGKAEN--FSLELGSGQFIPGFEEQLVGMKAG 199
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 595-924 1.71e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.85  E-value: 1.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   595 ISELIERNQRYvEQSNLMMEKrnnsLQTATENTQAKVTEELAAATAQVSHLQLKMtahQKKETELQMQLTESLKETdllr 674
Cdd:pfam01576  189 ISDLEERLKKE-EKGRQELEK----AKRKLEGESTDLQEQIAELQAQIAELRAQL---AKKEEELQAALARLEEET---- 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   675 GQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESL--------------EKNLSERKKKS 740
Cdd:pfam01576  257 AQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTldttaaqqelrskrEQEVTELKKAL 336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   741 AQERSQAEEEIDEIRKSYQEELDKLRQLL---KKTRVS---TDQAAAEQLSLVQAELQTQWEAKCEHLLASAKDEhlQQY 814
Cdd:pfam01576  337 EEETRSHEAQLQEMRQKHTQALEELTEQLeqaKRNKANlekAKQALESENAELQAELRTLQQAKQDSEHKRKKLE--GQL 414

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   815 QEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFEL 894
Cdd:pfam01576  415 QELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQL 494

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578817219   895 EESYNG-------------------RTILGTIMNTIKMVT-------------------LQLLNQQEQ 924
Cdd:pfam01576  495 EDERNSlqeqleeeeeakrnverqlSTLQAQLSDMKKKLEedagtlealeegkkrlqreLEALTQQLE 562
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 573-771 1.73e-03

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: 42.65  E-value: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   573 ENERLKQEILEKSNRIEEQNDKISELIERNQRY--------------VEQSNLMMEkrnnSLQTATENTQAKVTEELAAA 638
Cdd:TIGR00618  652 QLTLTQERVREHALSIRVLPKELLASRQLALQKmqsekeqltywkemLAQCQTLLR----ELETHIEEYDREFNEIENAS 727

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   639 TAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLrgQLTKVQAKLSELQETSEQAQSKFKSEKQNRkQLELKVTSLEEE 718
Cdd:TIGR00618  728 SSLGSDLAAREDALNQSLKELMHQARTVLKARTEA--HFNNNEEVTAALQTGAELSHLAAEIQFFNR-LREEDTHLLKTL 804

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578817219   719 LTDLRVEKESLEKNLSERKKKSAQERSQAEE----------EIDEIRKSYQEELDKLRQLLKK 771
Cdd:TIGR00618  805 EAEIGQEIPSDEDILNLQCETLVQEEEQFLSrleeksatlgEITHQLLKYEECSKQLAQLTQE 867
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 620-792 1.76e-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: 42.32  E-value: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   620 LQTATEnTQAKVTEELAA-ATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKF 698
Cdd:pfam05701  252 LETASA-LLLDLKAELAAyMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAAASLRSEL 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   699 KSEKQN---RKQLE----LKVTSLEEELTDLRVEKESL---EKNLSERKKKSAQERSQAEEEIDEIRKSYQeeldKLRQL 768
Cdd:pfam05701  331 EKEKAElasLRQREgmasIAVSSLEAELNRTKSEIALVqakEKEAREKMVELPKQLQQAAQEAEEAKSLAQ----AAREE 406

                          170       180
                   ....*....|....*....|....
gi 578817219   769 LKKTRVSTDQAAAEqLSLVQAELQ 792
Cdd:pfam05701  407 LRKAKEEAEQAKAA-ASTVESRLE 429
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 710-844 1.81e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 42.76  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  710 LKVTSLEEELTDLRVEKESLEKnlserkkksaqERSQAEEEIDEirkSYQEELDKLRQLLKKTRvstdqaaaEQLslvqA 789
Cdd:COG0542   404 MEIDSKPEELDELERRLEQLEI-----------EKEALKKEQDE---ASFERLAELRDELAELE--------EEL----E 457

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578817219  790 ELQTQWEAKCEHL--LASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITA 844
Cdd:COG0542   458 ALKARWEAEKELIeeIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE 514
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 397-491 1.96e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.76  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  397 QGGGQPVVTPSVQPSLHPAHPALPQMTSQAPQPSVTGLQA------PSAALMQVSSLDSHSAVSGN-AQSFQPYAGMQAY 469
Cdd:PRK10263  738 DGPHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQyqqpqqPVAPQPQYQQPQQPVAPQPQyQQPQQPVAPQPQY 817

                          90       100
                  ....*....|....*....|....
gi 578817219  470 AYPQASAVTSQ--LQPVRPLYPAP 491
Cdd:PRK10263  818 QQPQQPVAPQPqyQQPQQPVAPQP 841
WH1 smart00461
WASP homology region 1; Region of the Wiskott-Aldrich syndrome protein (WASp) that contains ...
 70-168 1.96e-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: 1.96e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219     70 STPTILVATAVHAYRYTNGQYVKQGKFGAAVLG---NHTAREYRILLYISQQQPVTVARIHVNFELMVRPNNYSTFYDDQ 146
Cdd:smart00461    3 SQCIILARAVVQLYDADTKKWVPTGEGGAANLVidkNQRSYFFRIVGIKGQDKVIWNQELYKNFKYNQATPTFHQWADDK 82

                            90       100
                    ....*....|....*....|..
gi 578817219    147 RQnWSIMFESEKAAVEFNKQVC 168
Cdd:smart00461   83 CV-YGLNFASEEEAKKFRKKVL 103
Tht1 pfam04163
Tht1-like nuclear fusion protein;
599-817 2.01e-03

Tht1-like nuclear fusion protein;


Pssm-ID: 282073  Cd Length: 595  Bit Score: 42.12  E-value: 2.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   599 IERN-QRYVEQSNLMMEKRNNSLQTATENTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQL 677
Cdd:pfam04163  193 MEQDfENFLDDLAQMFDKFDGEFNNATESNRIIIENDFKDFNFKVNDEIMGLVELENHEQEGMVLEKEIIEKIKQLKNEI 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   678 TKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKS 757
Cdd:pfam04163  273 DDIHHFFADFADELAGYKNDIIEKINDLKDDSENAIALSAIGKYTSEFSAFMEKNIKDLIEMSEDSLKESVQRNIDFVNS 352

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   758 YQEELDKLRQLLKKTRVSTDQAAAEQLSLvQAELQTQWEAKcehLLASAKDeHLQQYQEV 817
Cdd:pfam04163  353 GFQELEDFSIGLKEELGGLKKDLSEQQNL-EAEEILQWKSD---FLNILHD-HLKVLQQL 407
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 577-833 2.03e-03

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: 42.52  E-value: 2.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   577 LKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQAKvTEELAAATAQvsHLQL------KMT 650
Cdd:pfam12128  267 YKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKD-RSELEALEDQ--HGAFldadieTAA 343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   651 AHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSEL-QETSEQAQSKFKSEKQNR-KQLELKVTSLEEE---------- 718
Cdd:pfam12128  344 ADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRrSKIKEQNNRDIAGIKDKLaKIREARDRQLAVAeddlqalese 423

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   719 --------LTDLRVEKESLEKNLSERKKKSAQerSQAEEEIDEIRKSYQEELDKLRQLLkktrvstDQAAAEQLSLVQAE 790
Cdd:pfam12128  424 lreqleagKLEFNEEEYRLKSRLGELKLRLNQ--ATATPELLLQLENFDERIERAREEQ-------EAANAEVERLQSEL 494

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 578817219   791 LQtqweakcehlLASAKDEHLQQYQEVCAQRDAYQQKLVQLQE 833
Cdd:pfam12128  495 RQ----------ARKRRDQASEALRQASRRLEERQSALDELEL 527
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 564-744 2.06e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 40.89  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  564 MSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQsnlmMEKRNNSLQTATENTQAKVTE---ELAAATA 640
Cdd:cd00176    32 LESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE----IQERLEELNQRWEELRELAEErrqRLEEALD 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  641 QVSHLQlkmtahQKKETELQMQLTESLKETDLLRGQLTKVQA---KLSELQETSEQAQSKFKSEKQNRKQLELKVTS--- 714
Cdd:cd00176   108 LQQFFR------DADDLEQWLEEKEAALASEDLGKDLESVEEllkKHKELEEELEAHEPRLKSLNELAEELLEEGHPdad 181

                         170       180       190
                  ....*....|....*....|....*....|..
gi 578817219  715 --LEEELTDLRVEKESLEKNLSERKKKSAQER 744
Cdd:cd00176   182 eeIEEKLEELNERWEELLELAEERQKKLEEAL 213
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
 681-767 2.13e-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: 39.91  E-value: 2.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   681 QAKLSELQETSEQAQSKFKSEKQNRKQ----LELKVTSLEEELTDLRVEKESLEK-----------NLSERKKKSAQERS 745
Cdd:pfam09744   49 NVELEELREDNEQLETQYEREKALRKRaeeeLEEIEDQWEQETKDLLSQVESLEEenrrleadhvsRLEEKEAELKKEYS 128

                           90       100
                   ....*....|....*....|..
gi 578817219   746 QAEEEIDEIRKSYQEELDKLRQ 767
Cdd:pfam09744  129 KLHERETEVLRKLKEVVDRQRD 150
PTZ00121 PTZ00121
MAEBL; Provisional
 511-994 2.39e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  511 EARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMLIPSMSVTMETSMIMSNIQRIIQENERLKQEILEKSNRIEE 590
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  591 QNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQAKVTEELAAATAQVSHL-QLKMTAHQKKETELQMQLTESLKE 669
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAdEAKKKAEEAKKAEEAKKKAEEAKK 1471

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  670 TDLLRGQLTKVQaKLSELQETSEQAQSKF----KSEKQNRKQLELKVTSLEEELTDLRV--EKESLEKNLSERKKKSAQE 743
Cdd:PTZ00121 1472 ADEAKKKAEEAK-KADEAKKKAEEAKKKAdeakKAAEAKKKADEAKKAEEAKKADEAKKaeEAKKADEAKKAEEKKKADE 1550

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  744 RSQAEE--EIDEIRKSYQ---EELDK---------LRQLLKKTRVSTDQAAAEQLSLVQAELQTQWEA--KCEHLlasAK 807
Cdd:PTZ00121 1551 LKKAEElkKAEEKKKAEEakkAEEDKnmalrkaeeAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkiKAEEL---KK 1627

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  808 DEHLQQYQEVCAQRDAYQQK----LVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKImnq 883
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKkaeeLKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA--- 1704

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  884 vfQSLRREFELEESYNGRTILGTIMNTIKMVTLQllnqqeqekeeSSSEEEEEKAEERPRRPSQEQSASASSGQPQAPLN 963
Cdd:PTZ00121 1705 --EELKKKEAEEKKKAEELKKAEEENKIKAEEAK-----------KEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771

                         490       500       510
                  ....*....|....*....|....*....|.
gi 578817219  964 RERPESPMVPSEQVVEEAVPLPPQALTTSQD 994
Cdd:PTZ00121 1772 EIRKEKEAVIEEELDEEDEKRRMEVDKKIKD 1802
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 502-855 2.43e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 42.09  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  502 GDMASFLMTEARQH--------NTEIRMAVS-KVADKMDHLMTKVEELQKHSAGNSMLIPSMSVTMETSMimsniQRIIQ 572
Cdd:PRK10246  156 GQFAAFLNAKPKERaelleeltGTEIYGQISaMVFEQHKSARTELEKLQAQASGVALLTPEQVQSLTASL-----QVLTD 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  573 ENERL--KQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEK----------------------RNNSLQTATENTQ 628
Cdd:PRK10246  231 EEKQLltAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKaqpqlaalslaqparqlrphweRIQEQSAALAHTR 310

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  629 AKVTE---ELAAATAQVSHL-QLKMTAHQKKETELQmQLTESLKETDLLR-------------GQLTKVQAKLSELQETS 691
Cdd:PRK10246  311 QQIEEvntRLQSTMALRARIrHHAAKQSAELQAQQQ-SLNTWLAEHDRFRqwnnelagwraqfSQQTSDREQLRQWQQQL 389

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  692 EQAQSKFKS-----------------EKQNRKQ-LELKVTSLEEELTDLRVEKESLEKNLSerkkKSAQERSQAEEEIDE 753
Cdd:PRK10246  390 THAEQKLNAlpaitltltadevaaalAQHAEQRpLRQRLVALHGQIVPQQKRLAQLQVAIQ----NVTQEQTQRNAALNE 465

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  754 IRKSYQEeldKLRQLLKKTRVSTDQAAAEQLSLVQAELQTqweAKCEHLLASAKDEHLQQYQEVC-----AQRDAYQQKL 828
Cdd:PRK10246  466 MRQRYKE---KTQQLADVKTICEQEARIKDLEAQRAQLQA---GQPCPLCGSTSHPAVEAYQALEpgvnqSRLDALEKEV 539

                         410       420
                  ....*....|....*....|....*..
gi 578817219  829 VQLQEKCLALQAQITALTKQNEQHIKE 855
Cdd:PRK10246  540 KKLGEEGAALRGQLDALTKQLQRDESE 566
PRK01156 PRK01156
chromosome segregation protein; Provisional
 564-884 2.43e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 42.20  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  564 MSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQT-----ATENTQAKVTEELAAA 638
Cdd:PRK01156  182 ISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSAlnelsSLEDMKNRYESEIKTA 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  639 TAQVSHLQLKMTAHQKKETELqMQLT---------------------ESLKET-DLLRGQLTKVQA---KLSELQETSEQ 693
Cdd:PRK01156  262 ESDLSMELEKNNYYKELEERH-MKIIndpvyknrnyindyfkykndiENKKQIlSNIDAEINKYHAiikKLSVLQKDYND 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  694 AQSKfKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKsaQERSQAeeEIDEIRKSYQEELDKLRQLLKKTR 773
Cdd:PRK01156  341 YIKK-KSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKN--IERMSA--FISEILKIQEIDPDAIKKELNEIN 415

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  774 VSTDQAAAEqlslvQAELQTQWEAKCEHLLASAKDEHLQQYQEVCAQ-------------RDAYQQKLVQLQEKCLALQA 840
Cdd:PRK01156  416 VKLQDISSK-----VSSLNQRIRALRENLDELSRNMEMLNGQSVCPVcgttlgeeksnhiINHYNEKKSRLEEKIREIEI 490

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 578817219  841 QITALTKQNEQHIKELEK-NKSQMSGVEAA---ASDPSEKVKKIMNQV 884
Cdd:PRK01156  491 EVKDIDEKIVDLKKRKEYlESEEINKSINEynkIESARADLEDIKIKI 538
46 PHA02562
endonuclease subunit; Provisional
 502-736 2.84e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.92  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  502 GDMASFLMTEARQHNTEIRMavskVADKMDHLMTKV-------EELQKHSAGNsmlipsmsVTMETSMIMSN---IQRII 571
Cdd:PHA02562  166 SEMDKLNKDKIRELNQQIQT----LDMKIDHIQQQIktynkniEEQRKKNGEN--------IARKQNKYDELveeAKTIK 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  572 QENERLKQEILEKSNRIEEQNDKISELierNQRYVEQSNLM--------MEKRNNSLQTAT------ENTQAKVTEELAA 637
Cdd:PHA02562  234 AEIEELTDELLNLVMDIEDPSAALNKL---NTAAAKIKSKIeqfqkvikMYEKGGVCPTCTqqisegPDRITKIKDKLKE 310

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  638 ATAQVSHLQLKMTAHQKKE---TELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQnrkqlelKVTS 714
Cdd:PHA02562  311 LQHSLEKLDTAIDELEEIMdefNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAE-------ELAK 383

                         250       260
                  ....*....|....*....|..
gi 578817219  715 LEEELTDLRVEKESLEKNLSER 736
Cdd:PHA02562  384 LQDELDKIVKTKSELVKEKYHR 405
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
743-858 3.08e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  743 ERSQAEEEIDEIRKSYqEELDKLRQLLKKTRVSTD------------QAAAEQLSLVQAELQT--QWEA-KCEHLLASAK 807
Cdd:COG4913   219 EEPDTFEAADALVEHF-DDLERAHEALEDAREQIEllepirelaeryAAARERLAELEYLRAAlrLWFAqRRLELLEAEL 297

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578817219  808 DEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQ--------ITALTKQNEQHIKELEK 858
Cdd:COG4913   298 EELRAELARLEAELERLEARLDALREELDELEAQirgnggdrLEQLEREIERLERELEE 356
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
 716-802 3.59e-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: 40.04  E-value: 3.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   716 EEELTDLRVEKEslEKNLSERKKKSAQERSQAEEEiDEIRKsyqEELDKLRQLLKKTRvstdqAAAEQLSLVqAELQTQW 795
Cdd:pfam15927    5 EEEEERLRAEEE--EAERLEEERREEEEEERLAAE-QDRRA---EELEELKHLLEERK-----EALEKLRAE-AREEAEW 72


                   ....*....
gi 578817219   796 E--AKCEHL 802
Cdd:pfam15927   73 EryMRCDGL 81
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
 576-814 4.03e-03

BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different protein families. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysin, endophilin, BRAP and Nadrin. BAR domains are also frequently found alongside domains that determine lipid specificity, like pfam00169 and pfam00787 domains in beta centaurins and sorting nexins respectively.


Pssm-ID: 460810 [Multi-domain]  Cd Length: 235  Bit Score: 40.40  E-value: 4.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   576 RLKQEILEKSNRIEEqnDKISELIERnqryveqsnlmMEKRNNSLQTATENTQAKVTEELAAataqvshlQLKMTAHQKK 655
Cdd:pfam03114    7 RASQLLGEKVGGAEK--TKLDEDFEE-----------LERRFDTTEKEIKKLQKDTKGYLQP--------NPGARAKQTV 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   656 ETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELK-VTSLEEELTDLRVEKESLE---- 730
Cdd:pfam03114   66 LEQPEELLAESMIEAGKDLGEDSSFGKALEDYGEALKRLAQLLEQLDDRVETNFLDpLRNLLKEFKEIQKHRKKLErkrl 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   731 --KNLSERKKKSAQERS-------QAEEEIDEIRKSYQEELDKLRQLLKKTRVS-TDQAAAEQLSLVQAELQTQweAKCE 800
Cdd:pfam03114  146 dyDAAKTRVKKAKKKKSskakdesQAEEELRKAQAKFEESNEQLKALLPNLLSLeVEFVVNQLVAFVEAQLDFH--RQCY 223

                          250
                   ....*....|....
gi 578817219   801 HLLasakdEHLQQY 814
Cdd:pfam03114  224 QLL-----EQLQQQ 232
PRK01156 PRK01156
chromosome segregation protein; Provisional
 511-803 4.12e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.43  E-value: 4.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  511 EARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSA---GNSMlIPSMSVTMETSMIMSNIQRIIQENERLKQEILEKSNR 587
Cdd:PRK01156  413 EINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlnGQSV-CPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIE 491

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  588 IEEQNDKISELIERN--------QRYVEQSNLMMEKRNNSLQTA-TENTQAKVTEELAAATAQVSHLQLKMTaHQKKETE 658
Cdd:PRK01156  492 VKDIDEKIVDLKKRKeyleseeiNKSINEYNKIESARADLEDIKiKINELKDKHDKYEEIKNRYKSLKLEDL-DSKRTSW 570

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  659 LQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQnrkQLELKVTSLEEELtdlrvekeslekNLSERKK 738
Cdd:PRK01156  571 LNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKS---YIDKSIREIENEA------------NNLNNKY 635

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578817219  739 KSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQ--------WEAKCEHLL 803
Cdd:PRK01156  636 NEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDdakanrarLESTIEILR 708
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 679-856 4.41e-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: 39.55  E-value: 4.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   679 KVQAKLSELQETSEQAQSKFKSEKQNrkqlelKVTSLEEELTDLRvekESLEKNLSERKKKSAQERSQAEEEIdeirksy 758
Cdd:pfam01442    1 LLEDSLDELSTYAEELQEQLGPVAQE------LVDRLEKETEALR---ERLQKDLEEVRAKLEPYLEELQAKL------- 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   759 QEELDKLRQLLK------KTRVSTD-QAAAEQLSLVQAELQTQWEAKCEHLLAsakdeHLQQYQEvcAQRDAYQQKLVQL 831
Cdd:pfam01442   65 GQNVEELRQRLEpyteelRKRLNADaEELQEKLAPYGEELRERLEQNVDALRA-----RLAPYAE--ELRQKLAERLEEL 137

                          170       180
                   ....*....|....*....|....*
gi 578817219   832 QEKclaLQAQITALTKQNEQHIKEL 856
Cdd:pfam01442  138 KES---LAPYAEEVQAQLSQRLQEL 159
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 668-754 4.50e-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: 4.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   668 KETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESL-EKNLSE--RKKKSAQER 744
Cdd:TIGR04320  254 NSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTaQNNLATaqAALANAEAR 333

                           90
                   ....*....|.
gi 578817219   745 -SQAEEEIDEI 754
Cdd:TIGR04320  334 lAKAKEALANL 344
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 679-902 4.66e-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: 4.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   679 KVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELT--DLRVEKESLEKNLSERKKKSAQERSQAEEEIDEiRK 756
Cdd:TIGR02794   65 KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQaeQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAE-RK 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   757 SYQEELDKLRQLLKKTRVSTDQAAAEqlslvQAELQTQWEAKcehllasAKDEHLQQYQEVCAQRDAYQQKL---VQLQE 833
Cdd:TIGR02794  144 AKEEAAKQAEEEAKAKAAAEAKKKAE-----EAKKKAEAEAK-------AKAEAEAKAKAEEAKAKAEAAKAkaaAEAAA 211

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578817219   834 KCLALQAQITALTKQ------NEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFELEESYNGRT 902
Cdd:TIGR02794  212 KAEAEAAAAAAAEAErkadeaELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQNLYDDPSFRGKT 286
PRK12704 PRK12704
phosphodiesterase; Provisional
 627-794 4.73e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  627 TQAKVTEELAAATAQVSHLQLKmtaHQKKETELQMQlteslKETDLLRGQLTK-VQAKLSELQETSEQAQSKFKSEKQNR 705
Cdd:PRK12704   31 AKIKEAEEEAKRILEEAKKEAE---AIKKEALLEAK-----EEIHKLRNEFEKeLRERRNELQKLEKRLLQKEENLDRKL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  706 KQLELKVTSLEEELTDLRVEKESLEKnlserkkksaqersqAEEEIDEIRKSYQEELDKLRQLlkktrvSTDQAAAEQLS 785
Cdd:PRK12704  103 ELLEKREEELEKKEKELEQKQQELEK---------------KEEELEELIEEQLQELERISGL------TAEEAKEILLE 161


                  ....*....
gi 578817219  786 LVQAELQTQ 794
Cdd:PRK12704  162 KVEEEARHE 170
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 630-802 4.93e-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: 39.17  E-value: 4.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   630 KVTEELAAATAQVSHLQLKMTAHQKketELQMQLTeslKETDLLRGQLtkvQAKLSELQETSEQAQSKFKSE-KQNRKQL 708
Cdd:pfam01442    1 LLEDSLDELSTYAEELQEQLGPVAQ---ELVDRLE---KETEALRERL---QKDLEEVRAKLEPYLEELQAKlGQNVEEL 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   709 ELKVTSLEEELTD-LRVEKESLEKNLSErkkKSAQERSQAEEEIDEIRKSYQEELDKLRQL-------LKKTRVSTDQAA 780
Cdd:pfam01442   72 RQRLEPYTEELRKrLNADAEELQEKLAP---YGEELRERLEQNVDALRARLAPYAEELRQKlaerleeLKESLAPYAEEV 148

                          170       180
                   ....*....|....*....|..
gi 578817219   781 AEQLSLVQAELQTQWEAKCEHL 802
Cdd:pfam01442  149 QAQLSQRLQELREKLEPQAEDL 170
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 676-898 5.05e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 39.74  E-value: 5.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  676 QLTKVQAKLSELQETSEQAQSKFKSEK------QNRKQLElKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEE 749
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDygddleSVEALLK-KHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  750 EIDEIRKSYQEeldkLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWEAKCEHLLASakDEHLQQYQEVCAQrdayQQKLV 829
Cdd:cd00176    80 RLEELNQRWEE----LRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALAS--EDLGKDLESVEEL----LKKHK 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  830 QLQEKCLALQAQITALTKQNEQHIKEleknksQMSGVEAAASDPSEKVKKIMNQVFQSL-RREFELEESY 898
Cdd:cd00176   150 ELEEELEAHEPRLKSLNELAEELLEE------GHPDADEEIEEKLEELNERWEELLELAeERQKKLEEAL 213
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 614-769 5.26e-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: 39.17  E-value: 5.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   614 EKRNNSLQTATENTQAKVTEELAAATAQvshLQLKMTAHQKKET----ELQMQLTESLKEtdlLRGQLT--------KVQ 681
Cdd:pfam01442   14 EELQEQLGPVAQELVDRLEKETEALRER---LQKDLEEVRAKLEpyleELQAKLGQNVEE---LRQRLEpyteelrkRLN 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   682 AKLSELQETSEQAQSKFKSE-KQNRKQLELKVTSLEEELTDLRVEK-ESLEKNLSERKKKSaqeRSQAEEEIDEIRKSYQ 759
Cdd:pfam01442   88 ADAEELQEKLAPYGEELRERlEQNVDALRARLAPYAEELRQKLAERlEELKESLAPYAEEV---QAQLSQRLQELREKLE 164

                          170
                   ....*....|
gi 578817219   760 EELDKLRQLL 769
Cdd:pfam01442  165 PQAEDLREKL 174
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
 186-251 5.47e-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: 40.50  E-value: 5.47e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817219  186 LIVADGPAvEVGDSLEVAYTGWlfqnhVLGQVFDSTANKDklLRLKLGSGKVIKGWEDGMLGMKKG 251
Cdd:COG0544   151 LVPVERAA-EEGDRVTIDFEGT-----IDGEEFEGGKAED--YSLELGSGSFIPGFEEQLVGMKAG 208
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
 665-895 5.54e-03

SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.


Pssm-ID: 293683 [Multi-domain]  Cd Length: 228  Bit Score: 39.72  E-value: 5.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   665 ESLKETDLlrgQLTKVQAKLSELQETSEQAQSKFKsekqnrkqlelkvtsleEELTDLRVEKESLEKNLsERKKKSAQEr 744
Cdd:pfam17078   13 DALTKTNL---QLTVQSQNLLSKLEIAQQKESKFL-----------------ENLASLKHENDNLSSML-NRKERRLKD- 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   745 sqAEEEIDEIRKSYQE---ELDKLRQLLKKTRvSTDQAAAEQLSLVQAelqtQWEAkcehLLASakdehlQQYQevcaqR 821
Cdd:pfam17078   71 --LEDQLSELKNSYEElteSNKQLKKRLENSS-ASETTLEAELERLQI----QYDA----LVDS------QNEY-----K 128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   822 DAYQQKLVQLQEkclALQAQITALTKQNEQHI-------KELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFEL 894
Cdd:pfam17078  129 DHYQQEINTLQE---SLEDLKLENEKQLENYQqrissndKDIDTKLDSYNNKFKNLDNIYVNKNNKLLTKLDSLAQLLDL 205


                   .
gi 578817219   895 E 895
Cdd:pfam17078  206 P 206
PHA03247 PHA03247
large tegument protein UL36; Provisional
 941-1111 5.55e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 5.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  941 RPRRPSQEQSASASSGQPQAPLNRERPesPMVPSEQVVEEAVPLPPQAlttSQDGHRRKGDSEAEALSEIKDGSLPPELS 1020
Cdd:PHA03247 2759 RPPTTAGPPAPAPPAAPAAGPPRRLTR--PAVASLSESRESLPSPWDP---ADPPAAVLAPAAALPPAASPAGPLPPPTS 2833

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219 1021 CIPSHRVLGPPTSIPPEPL-GPVSMDSECEESLAASPMAAKPDNPSGKVCVREVAPdgPLQESSTRLSLTSDPEEGDPla 1099
Cdd:PHA03247 2834 AQPTAPPPPPGPPPPSLPLgGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARP--AVSRSTESFALPPDQPERPP-- 2909

                         170
                  ....*....|..
gi 578817219 1100 lGPESPGEPQPP 1111
Cdd:PHA03247 2910 -QPQAPPPPQPQ 2920
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 563-784 5.68e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.97  E-value: 5.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  563 IMSNIQRIIQENERLKQEI-------LEKSNR-IEEQNDKISELIERN---QRYVEQSN-------LMMEKRNNSLQTAT 624
Cdd:PRK04778  254 IEKEIQDLKEQIDENLALLeeldldeAEEKNEeIQERIDQLYDILEREvkaRKYVEKNSdtlpdflEHAKEQNKELKEEI 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  625 E-------------NTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKetdllrgQLTKVQAKLSELQETs 691
Cdd:PRK04778  334 DrvkqsytlneselESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILK-------QLEEIEKEQEKLSEM- 405

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  692 eqAQSKFKSEKQNRKQLELKVTSLEEelTDLRVEKE---SLEKNLSERKKKSAQERSQAEEEIDEIR---KSYQEELDK- 764
Cdd:PRK04778  406 --LQGLRKDELEAREKLERYRNKLHE--IKRYLEKSnlpGLPEDYLEMFFEVSDEIEALAEELEEKPinmEAVNRLLEEa 481

                         250       260
                  ....*....|....*....|....
gi 578817219  765 ---LRQLLKKTRVSTDQAA-AEQL 784
Cdd:PRK04778  482 tedVETLEEETEELVENATlTEQL 505
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 572-761 5.70e-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: 5.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   572 QENERLKQEILEKSNRIEEQndkiselIERNQRYVEQSNLMMEKRNNSLQTATENTQAKvteelaaataqvSHLQLKMT- 650
Cdd:pfam15709  358 EEQRRLQQEQLERAEKMREE-------LELEQQRRFEEIRLRKQRLEEERQRQEEEERK------------QRLQLQAAq 418

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   651 --AHQKKEtelqmqlteslketdllrgqltKVQAKLSELQETSEQAQS-KFKSEKQNRKQLELKVT---------SLEEE 718
Cdd:pfam15709  419 erARQQQE----------------------EFRRKLQELQRKKQQEEAeRAEAEKQRQKELEMQLAeeqkrlmemAEEER 476

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 578817219   719 LTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEE 761
Cdd:pfam15709  477 LEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQ 519
NST1 pfam13945
Salt tolerance down-regulator; NST1 is a family of proteins that seem to be involved, directly ...
 701-762 5.82e-03

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: 39.48  E-value: 5.82e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578817219   701 EKQNRKQLELKVTslEEELTDL-RVEKESLEKNLSERKKKS------AQERSQAEEEIDEIRKSYQEEL 762
Cdd:pfam13945  106 ERENIKEFWLSLG--EEERRSLvKVEKEAVLKKMKEQQKHScsctvcGRKRTAIEEELEVLYDAYYEEL 172
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 658-771 5.83e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.97  E-value: 5.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  658 ELQMQLTESLKETDLLRGQltkVQAKLSELQETSEQAQSKFKSEKQNRKQlelkvtSLEEELTDLRVEKESLEKNLSERK 737
Cdd:PRK00409  527 ELERELEQKAEEAEALLKE---AEKLKEELEEKKEKLQEEEDKLLEEAEK------EAQQAIKEAKKEADEIIKELRQLQ 597

                          90       100       110
                  ....*....|....*....|....*....|....
gi 578817219  738 KKsaQERSQAEEEIDEIRKSYQEELDKLRQLLKK 771
Cdd:PRK00409  598 KG--GYASVKAHELIEARKRLNKANEKKEKKKKK 629
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 613-792 5.93e-03

The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively.


Pssm-ID: 153271 [Multi-domain]  Cd Length: 194  Bit Score: 39.35  E-value: 5.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  613 MEKRNNSLQTATENTQAKVTEELAAATAQVSHLQlKMTAHQKKETELQmqLTESLKetdllrgQLTKVQAKLSELQET-S 691
Cdd:cd07307     5 LEKLLKKLIKDTKKLLDSLKELPAAAEKLSEALQ-ELGKELPDLSNTD--LGEALE-------KFGKIQKELEEFRDQlE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  692 EQAQSKFKSEKQNRKQLELKVT-SLEEELTDLRVEKES-LEKNLSERKKKSAQER-SQAEEEIDEIRKSYQEELDKLRQL 768
Cdd:cd07307    75 QKLENKVIEPLKEYLKKDLKEIkKRRKKLDKARLDYDAaREKLKKLRKKKKDSSKlAEAEEELQEAKEKYEELREELIED 154

                         170       180
                  ....*....|....*....|....*
gi 578817219  769 LKKTRVSTDQAAAEQL-SLVQAELQ 792
Cdd:cd07307   155 LNKLEEKRKELFLSLLlSFIEAQSE 179
Kre28 pfam17097
Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore ...
 572-710 5.97e-03

Spindle pole body component; In Saccharomyces cerevisae Kre28 and Spc105 form a kinetochore microtubule binding complex, which bridges between centromeric heterochromatin and kinetochore MAPs (microtubule associated protein, such as Bim1, Bik1 and SIk19) and motors (Cin8, Kar3). It may be regulated by sumoylation.


Pssm-ID: 407241 [Multi-domain]  Cd Length: 360  Bit Score: 40.56  E-value: 5.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   572 QENERLKQEILEKSNRIEEQNDKISELiernqrYVEQSNLMME--KRNNSLQTATeNTQAKVTEELAAATAQVSHLQLKM 649
Cdd:pfam17097  140 QEIDQIKGDILQVAQEIADKQDQVNEL------CLETSNELDEcwELLNELERLR-DQRITVEEQTSNEKDTELDPVEET 212

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578817219   650 TAHQKKETELQMQLTESLKETDllrgQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLEL 710
Cdd:pfam17097  213 YEEWKSLQESLQQLEHLKEELD----QLQKQKDSLEKVDKSSINRTQNDEESIQNTVQLNL 269
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 571-811 6.32e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 40.68  E-value: 6.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  571 IQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSnlmMEKRNNSLqtatENTQAKVTEELAAATAQVSHLQLKMT 650
Cdd:PRK05771   45 LRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKS---LEELIKDV----EEELEKIEKEIKELEEEISELENEIK 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  651 AHQKKETELQMQLTESLKETDLLRGQLTKVQA------KLSELQETSEQAQSKFKSEKQNRK-----QLELKVTSLEEEL 719
Cdd:PRK05771  118 ELEQEIERLEPWGNFDLDLSLLLGFKYVSVFVgtvpedKLEELKLESDVENVEYISTDKGYVyvvvvVLKELSDEVEEEL 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  720 TDLRVEKESLEknlseRKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTrvstdqaaaEQLSLVQAELQTQWEAKC 799
Cdd:PRK05771  198 KKLGFERLELE-----EEGTPSELIREIKEELEEIEKERESLLEELKELAKKY---------LEELLALYEYLEIELERA 263

                         250
                  ....*....|..
gi 578817219  800 EHLLASAKDEHL 811
Cdd:PRK05771  264 EALSKFLKTDKT 275
46 PHA02562
endonuclease subunit; Provisional
 658-881 6.91e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.38  E-value: 6.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  658 ELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQA----QSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNL 733
Cdd:PHA02562  178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENiarkQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  734 SERKKKSAQERSQAeEEIDEIRKSYQE-------------ELDKLRQLlkKTRVSTDQAAAEQLSLVQAELQtqwEAKCE 800
Cdd:PHA02562  258 NKLNTAAAKIKSKI-EQFQKVIKMYEKggvcptctqqiseGPDRITKI--KDKLKELQHSLEKLDTAIDELE---EIMDE 331

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  801 HLLASAKdehlqqYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQ---NEQHIKELEKNKSQMSgveaaaSDPSEKV 877
Cdd:PHA02562  332 FNEQSKK------LLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEfvdNAEELAKLQDELDKIV------KTKSELV 399


                  ....
gi 578817219  878 KKIM 881
Cdd:PHA02562  400 KEKY 403
YkyA pfam10368
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ...
 571-693 7.05e-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: 39.11  E-value: 7.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   571 IQENERLKQEILEKSNRI-EEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATEN--------------TQAKVTEEL 635
Cdd:pfam10368   27 LVELEKKEQELYEEIIELgMDEFDEIKKLSDEALENVEEREELLEKEKESIEEAKEEfkkikeiieeiedeELKKEAEEL 106

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578817219   636 AAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDL----LRGQLTKVQAKLSELQETSEQ 693
Cdd:pfam10368  107 IDAMEERYEAYDELYDAYKKALELDKELYEMLKDEDLtleeLQEQIEKINESYEEVKEANEQ 168
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
 632-816 7.20e-03

SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.


Pssm-ID: 293683 [Multi-domain]  Cd Length: 228  Bit Score: 39.34  E-value: 7.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   632 TEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELK 711
Cdd:pfam17078   16 TKTNLQLTVQSQNLLSKLEIAQQKESKFLENLASLKHENDNLSSMLNRKERRLKDLEDQLSELKNSYEELTESNKQLKKR 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   712 V-------TSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQllkktRVSTDQAAAE-- 782
Cdd:pfam17078   96 LenssaseTTLEAELERLQIQYDALVDSQNEYKDHYQQEINTLQESLEDLKLENEKQLENYQQ-----RISSNDKDIDtk 170

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 578817219   783 ---------QLSLVQAELQTQWEAKCEHLLASAK-DEHLQQYQE 816
Cdd:pfam17078  171 ldsynnkfkNLDNIYVNKNNKLLTKLDSLAQLLDlPSWLNLYPE 214
BAR smart00721
BAR domain;
576-769 7.44e-03

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 39.67  E-value: 7.44e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219    576 RLKQEILEKSNRIEEQndKISELIERnqryveqsnlmMEKRNNSLQTATENTQAKVTEELaaataQVSHLQLKMTAHQKK 655
Cdd:smart00721    8 RAKQKVGEKVGKAEKT--KLDEDFEE-----------LERRFDTTEAEIEKLQKDTKLYL-----QPNPAVRAKLASQKK 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219    656 ETELQMQLTESLKETDLLrGQLTKVQAKLSELQETSE---QAQSKFKSEKQNR------------KQLELKVTSLEEELT 720
Cdd:smart00721   70 LSKSLGEVYEGGDDGEGL-GADSSYGKALDKLGEALKkllQVEESLSQVKRTFilpllnfllgefKEIKKARKKLERKLL 148

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*....
gi 578817219    721 DLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLL 769
Cdd:smart00721  149 DYDSARHKLKKAKKSKEKKKDEKLAKAEEELRKAKQEFEESNAQLVEEL 197
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 575-722 7.44e-03

Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 39.03  E-value: 7.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   575 ERLKQEILEKSNrIEEQNDKISELIERNQRYVEQSnlmmekrnnslqtaTENTQAKvTEELAAataQVSHLQLKMTAHQK 654
Cdd:pfam06785   58 EDALKEKFEKSF-LEEKEAKLTELDAEGFKILEET--------------LEELQSE-EERLEE---ELSQKEEELRRLTE 118

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578817219   655 KETELQMQLTESLKETDLLR----GQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDL 722
Cdd:pfam06785  119 ENQQLQIQLQQISQDFAEFRleseEQLAEKQLLINEYQQTIEEQRSVLEKRQDQIENLESKVRDLNYEIKTL 190
STAT5_CCD cd16855
Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family ...
 664-863 7.50e-03

Coiled-coil domain of Signal Transducer and Activator of Transcription 5 (STAT5); This family consists of the coiled-coil (alpha) domain of the STAT5 proteins (Signal Transducer and Activator of Transcription 5, or Signal Transduction And Transcription 5) which include STAT5A and STAT5B, both of which are >90% identical despite being encoded by separate genes. The coiled-coil domain (CCD) of STAT5A and STAT5B appears to be required for constitutive nuclear localization signals (NLS) function; small deletions within the CCD can abrogate nuclear import. Studies show that the CCD binds to the importin-alpha3 NLS adapter in most cells. STAT5A and STAT5B regulate erythropoiesis, lymphopoiesis, and the maintenance of the hematopoietic stem cell population. STAT5A and STAT5B have overlapping and redundant functions; both isoforms can be activated by the same set of cytokines, but some cytokines preferentially activate either STAT5A or STAT5B, e.g. during pregnancy and lactation, STAT5A rather than STAT5B is required for the production of luminal progenitor cells from mammary stem cells and is essential for the differentiation of milk producing alveolar cells during pregnancy. STAT5 has been found to be constitutively phosphorylated in cancer cells, and therefore constantly activated, either by aberrant cell signaling expression or by mutations. It differentially regulates cellular behavior in human mammary carcinoma. Prolactin (PRL) in the prostate gland can induce growth and survival of prostate cancer cells and tissues through the activation of STAT5, its downstream target; PRL expression and STAT5 activation correlates with disease severity. STAT5A and STAT5B are central signaling molecules in leukemias driven by Abelson fusion tyrosine kinases, displaying unique nuclear shuttling mechanisms and having a key role in resistance of leukemic cells against treatment with tyrosine kinase inhibitors (TKI). In addition, STAT5A and STAT5B promote survival of leukemic stem cells. STAT5 is a key transcription factor for IL-3-mediated inhibition of RANKL-induced osteoclastogenesis via the induction of the expression of Id genes. Autosomal recessive STAT5B mutations are associated with severe growth failure, insulin-like growth factor (IGF) deficiency and growth hormone insensitivity (GHI) syndrome. STAT5B deficiency can lead to potentially fatal primary immunodeficiency.


Pssm-ID: 341080 [Multi-domain]  Cd Length: 194  Bit Score: 39.17  E-value: 7.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  664 TESLKETDLLRGQLTKVQAKLSELQETSE------QAQSKFKSEKQNRKQLELkvTSLEEELTDLRVEKESLEKNLSERk 737
Cdd:cd16855     4 LEIRQQLEELRQRTQETENDLRNLQQKQEsfviqyQESQKIQAQLQQLQQQPQ--NERIELEQQLQQQKEQLEQLLNAK- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  738 kksAQERSQAEEEIDEIrksYQEELDKLRQLLKKtrvstdqaaaeqlslVQAELQTQWEAKcehllasakdehlQQYQEV 817
Cdd:cd16855    81 ---AQELLQLRMELADK---FKKTIQLLSKLQSR---------------VLDEELIQWKRQ-------------QQLAGN 126

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 578817219  818 CAQRDAyqqKLVQLQEKCLALqaqiTALTKQNEQHIKELEKNKSQM 863
Cdd:cd16855   127 GAPFES---NLDTIQEWCESL----AEIIWQNRQQIKRAERLKQKL 165
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 631-893 7.82e-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: 7.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   631 VTEELAaataQVSHLQLKMtahqkkETElqmQLTESLKE--TDLLRGQLTKVQAKLSELQETSEQaqSKFKSEKQNRKQL 708
Cdd:pfam06160   27 VQEELS----KVKKLNLTG------ETQ---EKFEEWRKkwDDIVTKSLPDIEELLFEAEELNDK--YRFKKAKKALDEI 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   709 ELKVTSLEEELTDLRvekESLeKNLSERKKKSAQERSQAEEEIDEIRKSY--------------QEELDKLRQLLKKTRV 774
Cdd:pfam06160   92 EELLDDIEEDIKQIL---EEL-DELLESEEKNREEVEELKDKYRELRKTLlanrfsygpaidelEKQLAEIEEEFSQFEE 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   775 STDQ----AAAEQLSLVQ---AELQTQWEaKCEHLLASAKDEHLQQYQEVcaqRDAYQqklvQLQEK-----CLALQAQI 842
Cdd:pfam06160  168 LTESgdylEAREVLEKLEeetDALEELME-DIPPLYEELKTELPDQLEEL---KEGYR----EMEEEgyaleHLNVDKEI 239

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 578817219   843 TALTKQNEQHIKELEKNksQMSGVEAAASDPSEKvkkiMNQVFQSLRREFE 893
Cdd:pfam06160  240 QQLEEQLEENLALLENL--ELDEAEEALEEIEER----IDQLYDLLEKEVD 284
Leu_zip pfam15294
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ...
 558-723 8.09e-03

Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).


Pssm-ID: 464620 [Multi-domain]  Cd Length: 276  Bit Score: 39.69  E-value: 8.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   558 METSMIMSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSL--QTATENTQAKVTEEL 635
Cdd:pfam15294   98 FEEREFTSSNKKPNFELNKPKLEPLNEGGGSALLHMEIERLKEENEKLKERLKTLESQATQALdeKSKLEKALKDLQKEQ 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219   636 AAATAQVSHLQlKMTAHQKKETELQMQLTESLKETDL----LRGQLTKVQAKLSELQETSEQAQS----KFKSEKQ--NR 705
Cdd:pfam15294  178 GAKKDVKSNLK-EISDLEEKMAALKSDLEKTLNASTAlqksLEEDLASTKHELLKVQEQLEMAEKelekKFQQTAAyrNM 256

                          170
                   ....*....|....*...
gi 578817219   706 KQLelkVTSLEEELTDLR 723
Cdd:pfam15294  257 KEM---LTKKNEQIKELR 271
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 692-767 8.44e-03

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


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 37.94  E-value: 8.44e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578817219   692 EQAQSKFKSEKQNRKQlelKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQ 767
Cdd:pfam03938   18 KAAQAQLEKKFKKRQA---ELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQ 90
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 580-794 8.46e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 8.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  580 EILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQ--TATENTQAKVTEELAAATAQVSHLQ--LKMTAHQKK 655
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAelEALQAEIDKLQAEIAEAEAEIEERReeLGERARALY 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  656 ETELQMQLTESLKE----TDLLRG-----QLTKVQAKL----SELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDL 722
Cdd:COG3883    97 RSGGSVSYLDVLLGsesfSDFLDRlsalsKIADADADLleelKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578817219  723 RVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQ 794
Cdd:COG3883   177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
F-BAR_GAS7 cd07649
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein ...
 581-831 8.67e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein 7; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Growth Arrest Specific protein 7 (GAS7) is mainly expressed in the brain and is required for neurite outgrowth. It may also play a role in the protection and migration of embryonic stem cells. Treatment-related acute myeloid leukemia (AML) has been reported resulting from mixed-lineage leukemia (MLL)-GAS7 translocations as a complication of primary cancer treatment. GAS7 contains an N-terminal SH3 domain, followed by a WW domain, and a central F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153333 [Multi-domain]  Cd Length: 233  Bit Score: 39.23  E-value: 8.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  581 ILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEK-RNNSLQTATENTQAKVTEELAAATAQVSHLQLKMTAHQKKETEL 659
Cdd:cd07649    10 LLQKQLKGKQMQKEMAEFIRERIKIEEEYAKNLSKlSQSSLAAQEEGTLGEAWAQVKKSLADEAEVHLKFSSKLQSEVEK 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  660 Q-MQLTESLKEtdllrgQLTKVQAKLSELQetsEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKEslekNLSERKK 738
Cdd:cd07649    90 PlLNFRENFKK------DMKKLDHHIADLR---KQLASRYAAVEKARKALLERQKDLEGKTQQLEIKLS----NKTEEDI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  739 KSAQERS-QAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQaelqtqweakcehllasakdEHLQQYQEV 817
Cdd:cd07649   157 KKARRKStQAGDDLMRCVDLYNQAQSKWFEEMVTTSLELERLEVERIEMIR--------------------QHLCQYTQL 216

                         250
                  ....*....|....
gi 578817219  818 CAQRDAYQQKLVQL 831
Cdd:cd07649   217 RHETDMFNQSTVEP 230
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
 528-912 9.43e-03

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 40.59  E-value: 9.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  528 DKMDHLMTKVEELQKhsagNSMLIPSMSVTMETSMI-MSNIQRIIQENERLKQEILEKSNRIE-----EQNDKI------ 595
Cdd:PTZ00440  863 QIVDNIIKDIENMNK----NINIIKTLNIAINRSNSnKQLVEHLLNNKIDLKNKLEQHMKIINtdniiQKNEKLnllnnl 938

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  596 ---SELIER--NQRYVEQSNLMMEKRNNSLQTATENTQAKVT---EELAAATAQVSHLQLKM----TAHQ---------- 653
Cdd:PTZ00440  939 nkeKEKIEKqlSDTKINNLKMQIEKTLEYYDKSKENINGNDGthlEKLDKEKDEWEHFKSEIdklnVNYNilnkkiddli 1018

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  654 KKETELQMQLTESLKeTDLLRGQLTKVQAKLSELQETSEQAQSKFKSE----------KQNRKQLELKVTSLEEELTDLR 723
Cdd:PTZ00440 1019 KKQHDDIIELIDKLI-KEKGKEIEEKVDQYISLLEKMKTKLSSFHFNIdikkyknpkiKEEIKLLEEKVEALLKKIDENK 1097

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  724 VEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSyqeeLDKLRQLLKKTRVSTDQAAAEQLSLVQA-ELQTQWEAKCEHL 802
Cdd:PTZ00440 1098 NKLIEIKNKSHEHVVNADKEKNKQTEHYNKKKKS----LEKIYKQMEKTLKELENMNLEDITLNEVnEIEIEYERILIDH 1173

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578817219  803 LASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITAL---------TKQNEQHIKELEKNKSQMSGvEAAASDP 873
Cdd:PTZ00440 1174 IVEQINNEAKKSKTIMEEIESYKKDIDQVKKNMSKERNDHLTTfeynayydkATASYENIEELTTEAKGLKG-EANRSTN 1252

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578817219  874 SEKVKKIMNQVFQSLRRE-----------------FELEESYNGRTILGTIMNTIK 912
Cdd:PTZ00440 1253 VDELKEIKLQVFSYLQQVikennkmenalheiknmYEFLISIDSEKILKEILNSTK 1308
 
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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