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Conserved domains on  [gi|145338880|ref|NP_189040|]
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BLISTER [Arabidopsis thaliana]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
357-523 4.92e-08

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


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 56.61  E-value: 4.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   357 DDFTALEQHIEDLTQEKFSLQRDLDASRALAESLASENSSMTDTYNQQRglVNQLKDDMERLYQQIQAQMGELESVRVEY 436
Cdd:TIGR02169  744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEARLREIEQKL 821
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   437 ANAQLECNAADERSQILASEVISLED--KALRLRSNEL-----KLERELEKAQTEMLSYKKKLQSLEKDRQDLQSTIKAL 509
Cdd:TIGR02169  822 NRLTLEKEYLEKEIQELQEQRIDLKEqiKSIEKEIENLngkkeELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
                          170
                   ....*....|....
gi 145338880   510 QEEKKVLQTMVQKA 523
Cdd:TIGR02169  902 ERKIEELEAQIEKK 915
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
376-695 3.46e-06

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 3.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 376 LQRDLDASRALAESLASENSSMTDTYNQQRGLVNQLKDDMERLYQQIQAQMGELESVRVEYANAQLECNAADERSQILAS 455
Cdd:COG1196  237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 456 EVISLEDKALRLRSNELKLERELEKAQTEMLSYKKKLQSLEKDRQDLQstiKALQEEKKVLQTMVQKASSGGKSTDLSKN 535
Cdd:COG1196  317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE---EALLEAEAELAEAEEELEELAEELLEALR 393
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 536 STSRKNVSTSTEGLAISDTTPESSNQETDSTTLLESDSSNTAIIPETRQLTLEGFslsvpADQMRVIHNINTLIAELAIE 615
Cdd:COG1196  394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA-----EEEAELEEEEEALLELLAEL 468
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 616 KEELVQALSSELSRSAHVQELNKELSRKLEAQTQRLELVTAQKMAIDNVSPEKQQPDTHVVQERTPIADEGDEVVERVLG 695
Cdd:COG1196  469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
357-523 4.92e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 56.61  E-value: 4.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   357 DDFTALEQHIEDLTQEKFSLQRDLDASRALAESLASENSSMTDTYNQQRglVNQLKDDMERLYQQIQAQMGELESVRVEY 436
Cdd:TIGR02169  744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEARLREIEQKL 821
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   437 ANAQLECNAADERSQILASEVISLED--KALRLRSNEL-----KLERELEKAQTEMLSYKKKLQSLEKDRQDLQSTIKAL 509
Cdd:TIGR02169  822 NRLTLEKEYLEKEIQELQEQRIDLKEqiKSIEKEIENLngkkeELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
                          170
                   ....*....|....
gi 145338880   510 QEEKKVLQTMVQKA 523
Cdd:TIGR02169  902 ERKIEELEAQIEKK 915
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
356-518 5.61e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 5.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 356 NDDFTALEQHIEDLTQEKFSLQRDLDASRALAESLASENSSMTDTYNQQRGLVNQLKDDMERLYQQIQAQMGELESVRVE 435
Cdd:COG1196  238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 436 YANAQLECNAADERSQILASEVISLEDKALRLRSNELKLERELEKAQTEMLSYKKKLQSLEKDRQDLQSTIKALQEEKKV 515
Cdd:COG1196  318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397

                 ...
gi 145338880 516 LQT 518
Cdd:COG1196  398 LAA 400
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
376-695 3.46e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 3.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 376 LQRDLDASRALAESLASENSSMTDTYNQQRGLVNQLKDDMERLYQQIQAQMGELESVRVEYANAQLECNAADERSQILAS 455
Cdd:COG1196  237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 456 EVISLEDKALRLRSNELKLERELEKAQTEMLSYKKKLQSLEKDRQDLQstiKALQEEKKVLQTMVQKASSGGKSTDLSKN 535
Cdd:COG1196  317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE---EALLEAEAELAEAEEELEELAEELLEALR 393
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 536 STSRKNVSTSTEGLAISDTTPESSNQETDSTTLLESDSSNTAIIPETRQLTLEGFslsvpADQMRVIHNINTLIAELAIE 615
Cdd:COG1196  394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA-----EEEAELEEEEEALLELLAEL 468
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 616 KEELVQALSSELSRSAHVQELNKELSRKLEAQTQRLELVTAQKMAIDNVSPEKQQPDTHVVQERTPIADEGDEVVERVLG 695
Cdd:COG1196  469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
410-657 2.74e-05

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: 47.74  E-value: 2.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   410 QLKDDMERLyqQIQAQMGELESVRVEYANAQLECNAADERSQILASEVISLEDKALRLRSNELKLERELEKAQTEMLSYK 489
Cdd:TIGR02168  217 ELKAELREL--ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA 294
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   490 KKLQSLEKDRQDLQSTIKALQEEKKVLQTMVQKASSggKSTDLSKNSTSRKNVSTSTEGL---------AISDTTPESSN 560
Cdd:TIGR02168  295 NEISRLEQQKQILRERLANLERQLEELEAQLEELES--KLDELAEELAELEEKLEELKEElesleaeleELEAELEELES 372
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   561 QETDSTTLLESDSSntAIIPETRQLTLEGFSLSVPADQM-RVIHNINTLIAELAIEKEELVQALSSELS-RSAHVQELNK 638
Cdd:TIGR02168  373 RLEELEEQLETLRS--KVAQLELQIASLNNEIERLEARLeRLEDRRERLQQEIEELLKKLEEAELKELQaELEELEEELE 450
                          250
                   ....*....|....*....
gi 145338880   639 ELSRKLEAQTQRLELVTAQ 657
Cdd:TIGR02168  451 ELQEELERLEEALEELREE 469
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
357-511 5.81e-05

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe Cdc15, and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Schizosaccharomyces pombe Cdc15 and Imp2, and similar proteins. These proteins contain an N-terminal F-BAR domain and a C-terminal SH3 domain. S. pombe Cdc15 and Imp2 play both distinct and overlapping roles in the maintenance and strengthening of the contractile ring at the division site, which is required in cell division. Cdc15 is a component of the actomyosin ring and is required in normal cytokinesis. Imp2 colocalizes with the medial ring during septation and is required for normal septation. 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: 153335 [Multi-domain]  Cd Length: 236  Bit Score: 44.99  E-value: 5.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 357 DDFTALEQHIEDLTQEkfsLQRDLDASRALAESLASENSS-MTDTYNQQRGLVNQLKDDMERLYQQIQAQMGELESVRVE 435
Cdd:cd07651   53 SEEGGLKNSLDTLRLE---TESMAKSHLKFAKQIRQDLEEkLAAFASSYTQKRKKIQSHMEKLLKKKQDQEKYLEKAREK 129
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145338880 436 YanaQLECNaadersQIlasevisledKALRLRSNeLKLERELEKAQtemLSYKKKLQSLEKDRQDLQSTIKALQE 511
Cdd:cd07651  130 Y---EADCS------KI----------NSYTLQSQ-LTWGKELEKNN---AKLNKAQSSINSSRRDYQNAVKALRE 182
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
388-685 4.32e-04

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 43.56  E-value: 4.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880  388 ESLASENSSMTDTYNQQRGLVNQLKDDMERLYQQIQAQM-------GELESVRVEYANAQLECNAADERSQilasevisl 460
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEekemnlrDELESVREEFIQKGDEVKCKLDKSE--------- 572
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880  461 edkalrlrSNELKLERELEKAQTEMLSYKKKLQSLEKDRQDLQSTIKALQEEKKVLQTMVQKASSGGKSTDLSKNSTSRK 540
Cdd:pfam05483 573 --------ENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELE 644
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880  541 NVSTSTEGLAISDT-TPESSNQETDSTTLLESDSSNTAIIPETRQLTLEgfslsvpaDQMRVIHNINTLIAELAIEK--- 616
Cdd:pfam05483 645 LASAKQKFEEIIDNyQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKE--------IDKRCQHKIAEMVALMEKHKhqy 716
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145338880  617 EELVQALSSELS--RSAHVQELNKELSRKLEAQTQRLELVTAQKMAidNVSPEKQQPDTHVVQERTPIADE 685
Cdd:pfam05483 717 DKIIEERDSELGlyKNKEQEQSSAKAALEIELSNIKAELLSLKKQL--EIEKEEKEKLKMEAKENTAILKD 785
PRK11281 PRK11281
mechanosensitive channel MscK;
354-520 4.86e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 43.75  E-value: 4.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880  354 KQNDDFTALEQHIEDLTQEKFSLQRDLDA-SRALAESLASENSSMTDTYNQQRglVNQLKDDMerlyQQIQAQMGELESV 432
Cdd:PRK11281   77 RQKEETEQLKQQLAQAPAKLRQAQAELEAlKDDNDEETRETLSTLSLRQLESR--LAQTLDQL----QNAQNDLAEYNSQ 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880  433 RVEYAN----AQLECNAADERSQILASEVISLED--KALRL-RSNELKLERELEKAQTEM----LSYKKKLQSLEKDRQD 501
Cdd:PRK11281  151 LVSLQTqperAQAALYANSQRLQQIRNLLKGGKVggKALRPsQRVLLQAEQALLNAQNDLqrksLEGNTQLQDLLQKQRD 230
                         170       180
                  ....*....|....*....|
gi 145338880  502 LQST-IKALQEEKKVLQTMV 520
Cdd:PRK11281  231 YLTArIQRLEHQLQLLQEAI 250
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
610-663 1.06e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 42.35  E-value: 1.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 145338880  610 AELAIEKEELVQALSSELSRSAHVQ-ELNKELSRKLEAQTQRLELVTAQKMAIDN 663
Cdd:PRK10929  239 AERALESTELLAEQSGDLPKSIVAQfKINRELSQALNQQAQRMDLIASQQRQAAS 293
V_ATPase_I pfam01496
V-type ATPase 116kDa subunit family; This family consists of the 116kDa V-type ATPase ...
404-517 3.38e-03

V-type ATPase 116kDa subunit family; This family consists of the 116kDa V-type ATPase (vacuolar (H+)-ATPases) subunits, as well as V-type ATP synthase subunit i. The V-type ATPases family are proton pumps that acidify intracellular compartments in eukaryotic cells for example yeast central vacuoles, clathrin-coated and synaptic vesicles. They have important roles in membrane trafficking processes. The 116kDa subunit (subunit a) in the V-type ATPase is part of the V0 functional domain responsible for proton transport. The a subunit is a transmembrane glycoprotein with multiple putative transmembrane helices it has a hydrophilic amino terminal and a hydrophobic carboxy terminal. It has roles in proton transport and assembly of the V-type ATPase complex. This subunit is encoded by two homologous gene in yeast VPH1 and STV1.


Pssm-ID: 460232 [Multi-domain]  Cd Length: 748  Bit Score: 40.92  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880  404 QRGLVNQLK--DDMERLYQQIQAQMGELESVRVEYanaqleCNAADERSQILASEVISLEDKALrlrsnelKLERELeka 481
Cdd:pfam01496  22 QRTFVNEIRrcDEMERKLRFFEEEIEKLDIIPIKD------TLDLETPEAPSPREIDELEEKLE-------KLENEL--- 85
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 145338880  482 qTEMLSYkkkLQSLEKDRQDLQstikalqEEKKVLQ 517
Cdd:pfam01496  86 -RELNEN---YETLKRNYNELT-------ELRHVLR 110
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
357-523 4.92e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 56.61  E-value: 4.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   357 DDFTALEQHIEDLTQEKFSLQRDLDASRALAESLASENSSMTDTYNQQRglVNQLKDDMERLYQQIQAQMGELESVRVEY 436
Cdd:TIGR02169  744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEARLREIEQKL 821
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   437 ANAQLECNAADERSQILASEVISLED--KALRLRSNEL-----KLERELEKAQTEMLSYKKKLQSLEKDRQDLQSTIKAL 509
Cdd:TIGR02169  822 NRLTLEKEYLEKEIQELQEQRIDLKEqiKSIEKEIENLngkkeELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
                          170
                   ....*....|....
gi 145338880   510 QEEKKVLQTMVQKA 523
Cdd:TIGR02169  902 ERKIEELEAQIEKK 915
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
356-518 5.61e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 5.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 356 NDDFTALEQHIEDLTQEKFSLQRDLDASRALAESLASENSSMTDTYNQQRGLVNQLKDDMERLYQQIQAQMGELESVRVE 435
Cdd:COG1196  238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 436 YANAQLECNAADERSQILASEVISLEDKALRLRSNELKLERELEKAQTEMLSYKKKLQSLEKDRQDLQSTIKALQEEKKV 515
Cdd:COG1196  318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397

                 ...
gi 145338880 516 LQT 518
Cdd:COG1196  398 LAA 400
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
354-653 4.01e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.23  E-value: 4.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 354 KQNDDFTALEQHIEDLTQEKFSLQRDLDASRALAESLASEnSSMTDTYNQQRGLVNQLKDDMERL------YQQIQAQMG 427
Cdd:COG4717   85 EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL-LQLLPLYQELEALEAELAELPERLeeleerLEELRELEE 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 428 ELESVRVEYANAQLECNAA-DERSQILASEVISLEDKALRLRSNELKLERELEKAQTEmlsykkkLQSLEKDRQDLQSTI 506
Cdd:COG4717  164 ELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE-------LEELEEELEQLENEL 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 507 KALQEEKKVLQTMVQKASSG------GKSTDLSKNSTSRKNVSTSTEGLAI-----SDTTPESSNQETDSTTLLESDSSN 575
Cdd:COG4717  237 EAAALEERLKEARLLLLIAAallallGLGGSLLSLILTIAGVLFLVLGLLAllfllLAREKASLGKEAEELQALPALEEL 316
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 576 TAIIpETRQLTLEGFSLSVPADQ----MRVIHNINTLIAELAIEKEEL----VQALSSELSRSAHVQELnKELSRKLEAQ 647
Cdd:COG4717  317 EEEE-LEELLAALGLPPDLSPEEllelLDRIEELQELLREAEELEEELqleeLEQEIAALLAEAGVEDE-EELRAALEQA 394

                 ....*.
gi 145338880 648 TQRLEL 653
Cdd:COG4717  395 EEYQEL 400
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
362-657 4.70e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 4.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 362 LEQHIEDLTQEK------FSLQRDLDasRALAESLASENSSMTDTYNQQRGLVNQLKDDMERLYQQIQAQMGELESVRVE 435
Cdd:COG1196  198 LERQLEPLERQAekaeryRELKEELK--ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 436 YANAQLECNAADERSQILASEVISLEDKALRLRSNELKLERELEKAQTEMLSYKKKLQSLEKDRQDLQSTIKALQEEKKV 515
Cdd:COG1196  276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 516 LQTMVQKASSggkstDLSKNSTSRKNVSTSTEGLAISDTTPES--SNQETDSTTLLESDSSNtaiipETRQLTLEgfsls 593
Cdd:COG1196  356 AEAELAEAEE-----ALLEAEAELAEAEEELEELAEELLEALRaaAELAAQLEELEEAEEAL-----LERLERLE----- 420
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145338880 594 vpadqmRVIHNINTLIAELAIEKEELVQALSSELSRSAHVQELNKELSRKLEAQTQRLELVTAQ 657
Cdd:COG1196  421 ------EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
376-695 3.46e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 3.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 376 LQRDLDASRALAESLASENSSMTDTYNQQRGLVNQLKDDMERLYQQIQAQMGELESVRVEYANAQLECNAADERSQILAS 455
Cdd:COG1196  237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 456 EVISLEDKALRLRSNELKLERELEKAQTEMLSYKKKLQSLEKDRQDLQstiKALQEEKKVLQTMVQKASSGGKSTDLSKN 535
Cdd:COG1196  317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE---EALLEAEAELAEAEEELEELAEELLEALR 393
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 536 STSRKNVSTSTEGLAISDTTPESSNQETDSTTLLESDSSNTAIIPETRQLTLEGFslsvpADQMRVIHNINTLIAELAIE 615
Cdd:COG1196  394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA-----EEEAELEEEEEALLELLAEL 468
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 616 KEELVQALSSELSRSAHVQELNKELSRKLEAQTQRLELVTAQKMAIDNVSPEKQQPDTHVVQERTPIADEGDEVVERVLG 695
Cdd:COG1196  469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
354-525 4.14e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 4.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   354 KQNDDFTALEQHIEDLTQEKFSLQRDLDASRALAESLASENSSMTDTYNQQRGLVNQLKddmerlyQQIQAQMGELEsvr 433
Cdd:TIGR02168  334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE-------LQIASLNNEIE--- 403
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   434 veYANAQLEcnAADERSQILASEVISLEDKALRLRSNELK-----LERELEKAQTEMLSYKKKLQSLEK-------DRQD 501
Cdd:TIGR02168  404 --RLEARLE--RLEDRRERLQQEIEELLKKLEEAELKELQaeleeLEEELEELQEELERLEEALEELREeleeaeqALDA 479
                          170       180
                   ....*....|....*....|....
gi 145338880   502 LQSTIKALQEEKKVLQTMVQKASS 525
Cdd:TIGR02168  480 AERELAQLQARLDSLERLQENLEG 503
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
369-654 5.77e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 5.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   369 LTQEKFSLQRDLDASRALAESLASENSSMTDTYNQQRGLVNQLKDDMERLYQQIQAQMGELEsvrveyaNAQLECNAADE 448
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY-------ALANEISRLEQ 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   449 RSQILASEVISLEDKALRLRSNELKLERELEKAQTEMLSYKKKLQSLEKDRQDLQSTIKALQEEKKVLQTmvqkassggK 528
Cdd:TIGR02168  303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES---------R 373
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   529 STDLSKNSTSRKNVSTSTEgLAISDTTPESSNQETDsttlLESDSSNTAIIPETRQLTLEGFSLSVPADQMRVIHNINTL 608
Cdd:TIGR02168  374 LEELEEQLETLRSKVAQLE-LQIASLNNEIERLEAR----LERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEE 448
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 145338880   609 IAELAIEKEELVQALSSELSRSAHVQELNKELSRKLEAQTQRLELV 654
Cdd:TIGR02168  449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
354-514 8.45e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.61  E-value: 8.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 354 KQNDDFTALEQHIEDLTQEKFSLQRDLDASRA-LAESLASenSSMTDTYNQQRGLVNQ--------LKDDMERLYQQIQA 424
Cdd:COG4942   73 ALEQELAALEAELAELEKEIAELRAELEAQKEeLAELLRA--LYRLGRQPPLALLLSPedfldavrRLQYLKYLAPARRE 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 425 QMGELESVRVEYANAQLECNAADERSQILASEvisLEDKALRLRSNELKLERELEKAQTEMLSYKKKLQSLEKDRQDLQS 504
Cdd:COG4942  151 QAEELRADLAELAALRAELEAERAELEALLAE---LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
                        170
                 ....*....|
gi 145338880 505 TIKALQEEKK 514
Cdd:COG4942  228 LIARLEAEAA 237
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
355-517 9.30e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 9.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   355 QNDDFTALEQHIEDLTQEKFSLQR---DLDASRALAESLASENSSMTDTYNQQRG----LVNQLKDDMERLYQQIQAQMG 427
Cdd:TIGR02168  731 LRKDLARLEAEVEQLEERIAQLSKeltELEAEIEELEERLEEAEEELAEAEAEIEeleaQIEQLKEELKALREALDELRA 810
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   428 ELESVRVEYANAQLECN--------------AADERSQILASEVISLEDKALRLRSNELKLERELEKAQTEMLSYKKKLQ 493
Cdd:TIGR02168  811 ELTLLNEEAANLRERLEslerriaaterrleDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
                          170       180
                   ....*....|....*....|....
gi 145338880   494 SLEKDRQDLQSTIKALQEEKKVLQ 517
Cdd:TIGR02168  891 LLRSELEELSEELRELESKRSELR 914
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
347-525 1.06e-05

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: 48.90  E-value: 1.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   347 FTDFSMPKQNDDFTALEQHIEDLTQEKFSLQRDLDASRALAESLASEnssmtdtYNQQRGLVNQLKDDMERLYQQIQAQM 426
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE-------LESLEAELEELEAELEELESRLEELE 378
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   427 GELESVRVEYANAQLECNAADERSQILASEVISLEDKALRLRSNELKLERELEKAQTEMLS-----YKKKLQSLEKDRQD 501
Cdd:TIGR02168  379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQaeleeLEEELEELQEELER 458
                          170       180
                   ....*....|....*....|....
gi 145338880   502 LQSTIKALQEEKKVLQTMVQKASS 525
Cdd:TIGR02168  459 LEEALEELREELEEAEQALDAAER 482
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
361-523 1.34e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.84  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 361 ALEQHIEDLTQEKFSLQRDLDASRALAESLASENSSMTDTYNQQRGLVNQLKDDMERLYQQIQAQMGEL----------- 429
Cdd:COG4942   38 ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaellralyrlg 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 430 ---------------ESVR----VEYANAQLECNAADERSQI--LASEVISLEDKALRLRSNELKLERELEKAQTEMLSY 488
Cdd:COG4942  118 rqpplalllspedflDAVRrlqyLKYLAPARREQAEELRADLaeLAALRAELEAERAELEALLAELEEERAALEALKAER 197
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 145338880 489 KKKLQSLEKDRQDLQSTIKALQEEKKVLQTMVQKA 523
Cdd:COG4942  198 QKLLARLEKELAELAAELAELQQEAEELEALIARL 232
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
354-520 2.54e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.76  E-value: 2.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   354 KQNDDFTALEQHIED-------LTQEKFSLQRDLDASRALAESLASENSSMTDTYNQQRGLVNQLKDDMERLyQQIQAQM 426
Cdd:TIGR02169  333 KLLAEIEELEREIEEerkrrdkLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL-KRELDRL 411
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   427 GElESVRVEYANAQLECNAADERSQILASEViSLEDKALRLRSNELKLER---ELEKAQTEMLSYKKKLQSLEKDRQDLQ 503
Cdd:TIGR02169  412 QE-ELQRLSEELADLNAAIAGIEAKINELEE-EKEDKALEIKKQEWKLEQlaaDLSKYEQELYDLKEEYDRVEKELSKLQ 489
                          170
                   ....*....|....*..
gi 145338880   504 STIKALQEEKKVLQTMV 520
Cdd:TIGR02169  490 RELAEAEAQARASEERV 506
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
410-657 2.74e-05

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: 47.74  E-value: 2.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   410 QLKDDMERLyqQIQAQMGELESVRVEYANAQLECNAADERSQILASEVISLEDKALRLRSNELKLERELEKAQTEMLSYK 489
Cdd:TIGR02168  217 ELKAELREL--ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA 294
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   490 KKLQSLEKDRQDLQSTIKALQEEKKVLQTMVQKASSggKSTDLSKNSTSRKNVSTSTEGL---------AISDTTPESSN 560
Cdd:TIGR02168  295 NEISRLEQQKQILRERLANLERQLEELEAQLEELES--KLDELAEELAELEEKLEELKEElesleaeleELEAELEELES 372
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   561 QETDSTTLLESDSSntAIIPETRQLTLEGFSLSVPADQM-RVIHNINTLIAELAIEKEELVQALSSELS-RSAHVQELNK 638
Cdd:TIGR02168  373 RLEELEEQLETLRS--KVAQLELQIASLNNEIERLEARLeRLEDRRERLQQEIEELLKKLEEAELKELQaELEELEEELE 450
                          250
                   ....*....|....*....
gi 145338880   639 ELSRKLEAQTQRLELVTAQ 657
Cdd:TIGR02168  451 ELQEELERLEEALEELREE 469
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
359-531 3.27e-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: 3.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880  359 FTALEQhIEDLTQEKFSLQRDLDASRALAESLASEnssmTDTYNQQRGLVNQLKddmERLYQQIqaqmgELESVRVEYAN 438
Cdd:COG4913   606 FDNRAK-LAALEAELAELEEELAEAEERLEALEAE----LDALQERREALQRLA---EYSWDEI-----DVASAEREIAE 672
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880  439 AQlecnaaDERSQILASevisledkalrlrSNELK-LERELEKAQTEMLSYKKKLQSLEKDRQDLQSTIKALQEEKKVLQ 517
Cdd:COG4913   673 LE------AELERLDAS-------------SDDLAaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
                         170
                  ....*....|....
gi 145338880  518 TMVQKASSGGKSTD 531
Cdd:COG4913   734 DRLEAAEDLARLEL 747
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
362-516 3.43e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 45.69  E-value: 3.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 362 LEQHIEDLTQEKFSLQRDLDASRALAESLASEnssmtdtYNQQRGLVNQLKDDMERLyqqiQAQMGELESVRvEYANAQL 441
Cdd:COG1579   29 LPAELAELEDELAALEARLEAAKTELEDLEKE-------IKRLELEIEEVEARIKKY----EEQLGNVRNNK-EYEALQK 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145338880 442 ECnaadersQILASEVISLEDKALRLRSNELKLERELEKAQTEMLSYKKKLQSLEKDRQ----DLQSTIKALQEEKKVL 516
Cdd:COG1579   97 EI-------ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDeelaELEAELEELEAEREEL 168
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
361-510 3.53e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 3.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880  361 ALEQHIEDLTQEKFSLQRDLDASRALAESLASENSSMTDTYNQQRGlvnqlkDDMERLYQQIQAQMGELESVRVEYANAQ 440
Cdd:COG4913   292 LLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG------DRLEQLEREIERLERELEERERRRARLE 365
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880  441 LECNAADERSQILASEVISLEDKALRLRSNELKLERELEKAQTEMlsyKKKLQSLEKDRQDLQSTIKALQ 510
Cdd:COG4913   366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEA---EAALRDLRRELRELEAEIASLE 432
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
410-651 4.20e-05

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: 46.97  E-value: 4.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   410 QLKDDMERLYQQIQAQMGELESVRVEYANAQLECNAADERSQILASEVISLEDKALRLRSNELKLERELEKAQTEMLSYK 489
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   490 KKLQSLEKDRQDLQSTIKALQEEKKVLQTMVQKASSGGKSTDLSKNSTSRKNVSTSTEGLAISDTTPESSNQETDSTTLL 569
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   570 ESDSSNTAIIPETRQ-LTLEGFSLSVPADQMRviHNINTLIAELAIEKEELVQALSSELSRSAHVQELNKELsRKLEAQT 648
Cdd:TIGR02168  841 EDLEEQIEELSEDIEsLAAEIEELEELIEELE--SELEALLNERASLEEALALLRSELEELSEELRELESKR-SELRREL 917

                   ...
gi 145338880   649 QRL 651
Cdd:TIGR02168  918 EEL 920
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
357-511 5.81e-05

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe Cdc15, and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Schizosaccharomyces pombe Cdc15 and Imp2, and similar proteins. These proteins contain an N-terminal F-BAR domain and a C-terminal SH3 domain. S. pombe Cdc15 and Imp2 play both distinct and overlapping roles in the maintenance and strengthening of the contractile ring at the division site, which is required in cell division. Cdc15 is a component of the actomyosin ring and is required in normal cytokinesis. Imp2 colocalizes with the medial ring during septation and is required for normal septation. 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: 153335 [Multi-domain]  Cd Length: 236  Bit Score: 44.99  E-value: 5.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 357 DDFTALEQHIEDLTQEkfsLQRDLDASRALAESLASENSS-MTDTYNQQRGLVNQLKDDMERLYQQIQAQMGELESVRVE 435
Cdd:cd07651   53 SEEGGLKNSLDTLRLE---TESMAKSHLKFAKQIRQDLEEkLAAFASSYTQKRKKIQSHMEKLLKKKQDQEKYLEKAREK 129
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145338880 436 YanaQLECNaadersQIlasevisledKALRLRSNeLKLERELEKAQtemLSYKKKLQSLEKDRQDLQSTIKALQE 511
Cdd:cd07651  130 Y---EADCS------KI----------NSYTLQSQ-LTWGKELEKNN---AKLNKAQSSINSSRRDYQNAVKALRE 182
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
354-525 8.79e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 8.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   354 KQNDDFTALEQHIEDLTQEKFSLQRDLDASRALAESLASENSSMTDTYNQQRGLVNQLKDDMERL----YQQIQAQMGEL 429
Cdd:TIGR02169  220 KREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeQLRVKEKIGEL 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   430 ESvrvEYANAQLECNAADERSQILASEVISLEDKALRLRSNELKLERELEKAQTEMLSYKKKLQSLEKDRQDLQSTikaL 509
Cdd:TIGR02169  300 EA---EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE---L 373
                          170
                   ....*....|....*.
gi 145338880   510 QEEKKVLQTMVQKASS 525
Cdd:TIGR02169  374 EEVDKEFAETRDELKD 389
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
361-522 1.07e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.14  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 361 ALEQHIEDLTQEKFSLQRDLDASRALAESLASENSSMTDTYNQQRGLVNQLKDDMERLYQQIQAQMGELESVRVEYAN-- 438
Cdd:COG4942   31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEll 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 439 -AQLECNAADERSQILASEVISLEDKALR-LRSNELKLERELEKAQTEMLSYKKKLQSLEKDRQDLQSTIKALQEEKKVL 516
Cdd:COG4942  111 rALYRLGRQPPLALLLSPEDFLDAVRRLQyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190

                 ....*.
gi 145338880 517 QTMVQK 522
Cdd:COG4942  191 EALKAE 196
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
353-661 1.10e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 353 PKQNDDFTALEQHIEDLTQEKFSLQRDLDASRALAESLASENSSMTDTYNQQRGLVNQLKDDMERLYQQIQAQMGELESV 432
Cdd:COG4372   20 PKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQA 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 433 RVEYANAQLECNAADERSQILASEVISLEDKALRLRSNELKLERELEKAQTEMLSYKKKLQSLEKDRQDLQSTIKALQEE 512
Cdd:COG4372  100 QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 513 K--KVLQTMVQKASSGGKSTDLSKNSTSRKNVSTSTEGLAISDTTPESSNQETDSTTLLESDSSNTAIIPETRQLTLEGF 590
Cdd:COG4372  180 EaeQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145338880 591 SLSVPADQMRVIHNINTLIAELAIEKEELVQALSSELSRSAHVQELNKELSRKLEAQTQRLELVTAQKMAI 661
Cdd:COG4372  260 IEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLEL 330
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
362-514 1.42e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.44  E-value: 1.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   362 LEQHIEDLTQEKFSLQRDLDASRALAESLASE-----------NSSMTDTYNQQRGLVNQLKDdMERLYQQIQAQMgELE 430
Cdd:TIGR02169  838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEEleeleaalrdlESRLGDLKKERDELEAQLRE-LERKIEELEAQI-EKK 915
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   431 SVRVEYANAQLEcNAADERSQILA---------SEVISLEDKALRLRSNELKLER----------ELEKAQTEMLSYKKK 491
Cdd:TIGR02169  916 RKRLSELKAKLE-ALEEELSEIEDpkgedeeipEEELSLEDVQAELQRVEEEIRAlepvnmlaiqEYEEVLKRLDELKEK 994
                          170       180
                   ....*....|....*....|...
gi 145338880   492 LQSLEKDRQDLQSTIKALQEEKK 514
Cdd:TIGR02169  995 RAKLEEERKAILERIEEYEKKKR 1017
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
366-663 1.79e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 1.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 366 IEDLTQEKFSLQRDLDASRALAESLASENSSMTDTYNQQRGLVNQLKDDMERLYQQIQAQMGELESVRVEYANAQLECNA 445
Cdd:COG4372   26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 446 ADERSQILASEVISLEDKALRLRSNELKLERELEKAQTEMLSYKKKLQSLEKDRQDLQSTIKALQEEKKVLQTMVQKASS 525
Cdd:COG4372  106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 526 GGKSTDLSKNSTSRKNVSTSTEGLAISDTTPESSNQETDSTTLLESDSSNTAIIPETRQLTLEGFSLSVPADQMRVIHNI 605
Cdd:COG4372  186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 145338880 606 NTLIAELAIEKEELVQALSSELSRSAHVQELNKELSRKLEAQTQRLELVTAQKMAIDN 663
Cdd:COG4372  266 AILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
409-523 2.06e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 43.37  E-value: 2.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 409 NQLKDDMERLYQQIQAQMGELESVRVEYANAQLECNAADERSQILASEVISLEDKALRL--RSNELKLERELEKAQTEML 486
Cdd:COG1579   20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYeeQLGNVRNNKEYEALQKEIE 99
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 145338880 487 SYKKKLQSLEKDRQDLQSTIKALQEEKKVLQTMVQKA 523
Cdd:COG1579  100 SLKRRISDLEDEILELMERIEELEEELAELEAELAEL 136
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
364-525 2.68e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 2.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 364 QHIEDLTQEKFSLQRDLDASRALAESLASENSSMtdtyNQQRGLVNQLKDDMERLYQQIQAQM--GELESVRVEYANAQL 441
Cdd:COG4717   71 KELKELEEELKEAEEKEEEYAELQEELEELEEEL----EELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPE 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 442 ECNAADERSQilasEVISLEDKALRLRSNELKLERELEKAQTEM-LSYKKKLQSLEKDRQDLQSTIKALQEEKKVLQTMV 520
Cdd:COG4717  147 RLEELEERLE----ELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222

                 ....*
gi 145338880 521 QKASS 525
Cdd:COG4717  223 EELEE 227
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
354-511 2.71e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.28  E-value: 2.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   354 KQNDDFTALEQHIEDLTQEKFSLQRDLDASRALAESLASENSsmtdtynQQRGLVNQLKDDMERLYQQIQAQMGELESVR 433
Cdd:TIGR02168  807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE-------ELSEDIESLAAEIEELEELIEELESELEALL 879
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145338880   434 VEYANAQLECNAADERSQILASEVISLEDKALRLRsnelkleRELEKAQTEMLSYKKKLQSLEKDRQDLQSTIKALQE 511
Cdd:TIGR02168  880 NERASLEEALALLRSELEELSEELRELESKRSELR-------RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYS 950
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
356-496 3.79e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 3.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 356 NDDFTALEQHIEDLTQEKFSLQRDLDASRALAESLASENSSMTDT---------YNQQRGLVNQLKDDMERL-------- 418
Cdd:COG3206  211 SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDAlpellqspvIQQLRAQLAELEAELAELsarytpnh 290
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 419 --YQQIQAQMGELES-----VRVEYANAQLECNAADERSQILASEVISLEDKALRLRSNE---LKLERELEKAQTEMLSY 488
Cdd:COG3206  291 pdVIALRAQIAALRAqlqqeAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEaelRRLEREVEVARELYESL 370

                 ....*...
gi 145338880 489 KKKLQSLE 496
Cdd:COG3206  371 LQRLEEAR 378
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
388-685 4.32e-04

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 43.56  E-value: 4.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880  388 ESLASENSSMTDTYNQQRGLVNQLKDDMERLYQQIQAQM-------GELESVRVEYANAQLECNAADERSQilasevisl 460
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEekemnlrDELESVREEFIQKGDEVKCKLDKSE--------- 572
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880  461 edkalrlrSNELKLERELEKAQTEMLSYKKKLQSLEKDRQDLQSTIKALQEEKKVLQTMVQKASSGGKSTDLSKNSTSRK 540
Cdd:pfam05483 573 --------ENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELE 644
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880  541 NVSTSTEGLAISDT-TPESSNQETDSTTLLESDSSNTAIIPETRQLTLEgfslsvpaDQMRVIHNINTLIAELAIEK--- 616
Cdd:pfam05483 645 LASAKQKFEEIIDNyQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKE--------IDKRCQHKIAEMVALMEKHKhqy 716
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145338880  617 EELVQALSSELS--RSAHVQELNKELSRKLEAQTQRLELVTAQKMAidNVSPEKQQPDTHVVQERTPIADE 685
Cdd:pfam05483 717 DKIIEERDSELGlyKNKEQEQSSAKAALEIELSNIKAELLSLKKQL--EIEKEEKEKLKMEAKENTAILKD 785
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
350-679 4.72e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 4.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 350 FSMPKQNDDFTALEQHIEDLTQEKFSLQRDLDASRALAESLASENSSMTDTYNQQRGLVNQLKDDMERLYQQIQAQMGEL 429
Cdd:COG4372   38 FELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 430 ESVRVEYANAQLECNAADERSQILASEVISLEDKALRLRSNELKLERELEKAQTEMLSYKKklqslEKDRQDLQSTIKAL 509
Cdd:COG4372  118 EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE-----AEAEQALDELLKEA 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 510 QEEKKVLQTM-VQKASSGGKSTDLSKNSTSRKNVSTSTEGLAISDTTPESSNQETDSTTLLESDSSNTAIIPETRQLTLE 588
Cdd:COG4372  193 NRNAEKEEELaEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKD 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 589 GFSLSVPADQMRVIHNINTLIAELAIEKEELVQALSSELSRSAHVQELNKELSRKLEAQTQRLELVTAQKMAIDNVSPEK 668
Cdd:COG4372  273 TEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLD 352
                        330
                 ....*....|.
gi 145338880 669 QQPDTHVVQER 679
Cdd:COG4372  353 NDVLELLSKGA 363
PRK11281 PRK11281
mechanosensitive channel MscK;
354-520 4.86e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 43.75  E-value: 4.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880  354 KQNDDFTALEQHIEDLTQEKFSLQRDLDA-SRALAESLASENSSMTDTYNQQRglVNQLKDDMerlyQQIQAQMGELESV 432
Cdd:PRK11281   77 RQKEETEQLKQQLAQAPAKLRQAQAELEAlKDDNDEETRETLSTLSLRQLESR--LAQTLDQL----QNAQNDLAEYNSQ 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880  433 RVEYAN----AQLECNAADERSQILASEVISLED--KALRL-RSNELKLERELEKAQTEM----LSYKKKLQSLEKDRQD 501
Cdd:PRK11281  151 LVSLQTqperAQAALYANSQRLQQIRNLLKGGKVggKALRPsQRVLLQAEQALLNAQNDLqrksLEGNTQLQDLLQKQRD 230
                         170       180
                  ....*....|....*....|
gi 145338880  502 LQST-IKALQEEKKVLQTMV 520
Cdd:PRK11281  231 YLTArIQRLEHQLQLLQEAI 250
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
376-670 6.81e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 6.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 376 LQRDLDASRALAESLASENSSMTDTYNQQRGLVNQLKDDMERLYQQIQAQMGELESVRVEYANAQLECNAADERSQILAS 455
Cdd:COG4372   29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 456 EVISLEDKALRLRSNELKLERELEKAQTEMLSYKKKLQSLEKDRQDLQSTIKALQEEKKVLQTMVQKASSGGKSTDLSKN 535
Cdd:COG4372  109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 536 STSRKNVSTSTEGLAISDTTPESSNQETDSTTLLESDSSNTAIIPETRQLTLEGFSLSVPADQMRVIHNINTLIAELAIE 615
Cdd:COG4372  189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 145338880 616 KEELVQALSSELSRSAHVQELNKELSRKLEAQTQRLELVTAQKMAIDNVSPEKQQ 670
Cdd:COG4372  269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
610-663 1.06e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 42.35  E-value: 1.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 145338880  610 AELAIEKEELVQALSSELSRSAHVQ-ELNKELSRKLEAQTQRLELVTAQKMAIDN 663
Cdd:PRK10929  239 AERALESTELLAEQSGDLPKSIVAQfKINRELSQALNQQAQRMDLIASQQRQAAS 293
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
361-567 1.29e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 361 ALEQHIEDLTQEKFSLQRDLDASRALAESLASENSSMTDTYNQQRglvNQLKDDMERLYQQiQAQMGELESV-------- 432
Cdd:COG3883   41 ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR---EELGERARALYRS-GGSVSYLDVLlgsesfsd 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 433 ---RVEYANAQLECNAA-----DERSQILASEVISLEDKALRLRSNELKLERELEKAQTEMLSYKKKLQSLEKDRQDLQS 504
Cdd:COG3883  117 fldRLSALSKIADADADlleelKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEA 196
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145338880 505 TIKALQEEKKVLQTMVQKASSGGKSTDLSKNSTSRKNVSTSTEGLAISDTTPESSNQETDSTT 567
Cdd:COG3883  197 QLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAA 259
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
360-525 1.47e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 360 TALEQHIEDLTQEKFSLQRDLDASRALAESLAS--ENSSMTDTYNQQRGLVNQLKDDMERLYQQIQAQM--GELESVRVE 435
Cdd:COG4717  354 REAEELEEELQLEELEQEIAALLAEAGVEDEEElrAALEQAEEYQELKEELEELEEQLEELLGELEELLeaLDEEELEEE 433
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 436 YANAQLECNAADERSQILASEVisledKALRLRSNELKLERELEKAQTEMLSYKKKLQSLEKD-------RQDLQSTIKA 508
Cdd:COG4717  434 LEELEEELEELEEELEELREEL-----AELEAELEQLEEDGELAELLQELEELKAELRELAEEwaalklaLELLEEAREE 508
                        170
                 ....*....|....*..
gi 145338880 509 LQEEKkvLQTMVQKASS 525
Cdd:COG4717  509 YREER--LPPVLERASE 523
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
362-502 1.70e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 362 LEQHIEDLTQ-------EKFSLQRDLDASRALAESLASENSSMTDTYNQQRGlvnqlkdDMERLYQQIQAQMGELESVRV 434
Cdd:PRK02224 256 LEAEIEDLREtiaeterEREELAEEVRDLRERLEELEEERDDLLAEAGLDDA-------DAEAVEARREELEDRDEELRD 328
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145338880 435 EYANAQLECNAADERSQILASEVISLEDKALRLRSNELKLERELEKAQTEMLSYKKKLQSLEKDRQDL 502
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL 396
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
473-670 1.92e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 473 KLERELEKAQTEMLSYKKKLQSLEKDRQDLQSTIKALQEEKKVLQTMVQKASSGGKST--DLSKNSTS----RKNVSTST 546
Cdd:COG4942   24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeaELAELEKEiaelRAELEAQK 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 547 EGLAISDTTPESSNQETDSTTLLESDSSNTAIipetRQLTLegFSLSVPADQMRvIHNINTLIAELAIEKEELVQALSSE 626
Cdd:COG4942  104 EELAELLRALYRLGRQPPLALLLSPEDFLDAV----RRLQY--LKYLAPARREQ-AEELRADLAELAALRAELEAERAEL 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 145338880 627 LSRSAHVQELNKELSRKLEAQTQRLELVTAQKMAIDNVSPEKQQ 670
Cdd:COG4942  177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
437-663 2.19e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 437 ANAQLECNAADERSQILAsEVISLEDKALRLRSNELKLERELEKAQTEMLSYKKKLQSLEKDRQDLQSTIKALQEEKKVL 516
Cdd:COG4942   17 AQADAAAEAEAELEQLQQ-EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 517 QTMVQKassggKSTDLSKN-STSRKNVSTSTEGLAISdttPESSNQETDSTTLLEsdssntAIIPETRQLTlegfslsvp 595
Cdd:COG4942   96 RAELEA-----QKEELAELlRALYRLGRQPPLALLLS---PEDFLDAVRRLQYLK------YLAPARREQA--------- 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145338880 596 ADQMRVIHNINTLIAELAIEKEELVQALSSELSRSAHVQELNKE-------LSRKLEAQTQRLELVTAQKMAIDN 663
Cdd:COG4942  153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAErqkllarLEKELAELAAELAELQQEAEELEA 227
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
358-512 3.36e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880  358 DFTALEQHIEDLTQEKFSLQRDLDASRALAESLAsenssmtdtynqqrglvnQLKDDMERLYQQIQAQMGELESVRVEYA 437
Cdd:COG4913   662 DVASAEREIAELEAELERLDASSDDLAALEEQLE------------------ELEAELEELEEELDELKGEIGRLEKELE 723
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145338880  438 NAQLECNAADERsqilASEVISLEDKALRLRsnelkLERELEKAQTEmLSYKKKLQSLEKDRQDLQSTIKALQEE 512
Cdd:COG4913   724 QAEEELDELQDR----LEAAEDLARLELRAL-----LEERFAAALGD-AVERELRENLEERIDALRARLNRAEEE 788
V_ATPase_I pfam01496
V-type ATPase 116kDa subunit family; This family consists of the 116kDa V-type ATPase ...
404-517 3.38e-03

V-type ATPase 116kDa subunit family; This family consists of the 116kDa V-type ATPase (vacuolar (H+)-ATPases) subunits, as well as V-type ATP synthase subunit i. The V-type ATPases family are proton pumps that acidify intracellular compartments in eukaryotic cells for example yeast central vacuoles, clathrin-coated and synaptic vesicles. They have important roles in membrane trafficking processes. The 116kDa subunit (subunit a) in the V-type ATPase is part of the V0 functional domain responsible for proton transport. The a subunit is a transmembrane glycoprotein with multiple putative transmembrane helices it has a hydrophilic amino terminal and a hydrophobic carboxy terminal. It has roles in proton transport and assembly of the V-type ATPase complex. This subunit is encoded by two homologous gene in yeast VPH1 and STV1.


Pssm-ID: 460232 [Multi-domain]  Cd Length: 748  Bit Score: 40.92  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880  404 QRGLVNQLK--DDMERLYQQIQAQMGELESVRVEYanaqleCNAADERSQILASEVISLEDKALrlrsnelKLERELeka 481
Cdd:pfam01496  22 QRTFVNEIRrcDEMERKLRFFEEEIEKLDIIPIKD------TLDLETPEAPSPREIDELEEKLE-------KLENEL--- 85
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 145338880  482 qTEMLSYkkkLQSLEKDRQDLQstikalqEEKKVLQ 517
Cdd:pfam01496  86 -RELNEN---YETLKRNYNELT-------ELRHVLR 110
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
357-523 4.12e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 4.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880  357 DDFTALEQHIEDLTQEKFSLQRDLDASRALAESLASEnssmTDTYNQQRGLVnQLKDDMERL------YQQIQAQmgeLE 430
Cdd:COG4913   624 EELAEAEERLEALEAELDALQERREALQRLAEYSWDE----IDVASAEREIA-ELEAELERLdassddLAALEEQ---LE 695
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880  431 SVRVEYANAQLECNAADERSQILASEVISLEDKALRLRSNELKLERELEKAQTEMLsyKKKLQSLEKD------RQDLQS 504
Cdd:COG4913   696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL--EERFAAALGDaverelRENLEE 773
                         170
                  ....*....|....*....
gi 145338880  505 TIKALQEEKKVLQTMVQKA 523
Cdd:COG4913   774 RIDALRARLNRAEEELERA 792
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
362-512 4.55e-03

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


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 40.06  E-value: 4.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880  362 LEQHIEDLTQEKFSLQRDLDASRALAESLASENSSMTDT---YNQQRGLVNQLKDDMERLYQ-----QIQAQMGELESVR 433
Cdd:pfam05622  19 LDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGgkkYLLLQKQLEQLQEENFRLETarddyRIKCEELEKEVLE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880  434 VEYANAQLecnaadersQILASEVISLEDK--ALRLRSNEL-KLERELEkaqtemlSYKKKLQslekDRQDLQSTIKALQ 510
Cdd:pfam05622  99 LQHRNEEL---------TSLAEEAQALKDEmdILRESSDKVkKLEATVE-------TYKKKLE----DLGDLRRQVKLLE 158

                  ..
gi 145338880  511 EE 512
Cdd:pfam05622 159 ER 160
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
411-653 5.49e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 39.91  E-value: 5.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 411 LKDDMERLYQQIQ-AQMGELESVRVEYANAQLEcNAADERSQIlaSEVISLEDKALRLRSNELKLERELEKAQTEML--S 487
Cdd:PRK05771  14 LKSYKDEVLEALHeLGVVHIEDLKEELSNERLR-KLRSLLTKL--SEALDKLRSYLPKLNPLREEKKKVSVKSLEELikD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 488 YKKKLQSLEKDRQDLQSTIKALQEEKKVLQTMVQKASS-GGKSTDLSKNSTSRknVSTSTEGLAISDTTPESSNQETDST 566
Cdd:PRK05771  91 VEEELEKIEKEIKELEEEISELENEIKELEQEIERLEPwGNFDLDLSLLLGFK--YVSVFVGTVPEDKLEELKLESDVEN 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 567 TLLESDSSNTAII-------------PETRQLTLEGFSLSVPADQMRVIHNINTLIAELAIEKEELVQALSSELSRSAhv 633
Cdd:PRK05771 169 VEYISTDKGYVYVvvvvlkelsdeveEELKKLGFERLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYL-- 246
                        250       260
                 ....*....|....*....|
gi 145338880 634 qELNKELSRKLEAQTQRLEL 653
Cdd:PRK05771 247 -EELLALYEYLEIELERAEA 265
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
360-670 5.72e-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: 39.95  E-value: 5.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   360 TALEQHIEDLTQEKFSLQRDLDASRALAESLASENSSMtDTYNQQRglvNQLKDDMERLYQQIQAQMGELESVRVeyana 439
Cdd:TIGR00618  375 HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATI-DTRTSAF---RDLQGQLAHAKKQQELQQRYAELCAA----- 445
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   440 qlecnAADERSQILASEVISLEDKALRLRsnelKLERELEKAQTEMLSYKKKLQSLEKDRQDLQSTIKALQE-EKKVLQT 518
Cdd:TIGR00618  446 -----AITCTAQCEKLEKIHLQESAQSLK----EREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGsCIHPNPA 516
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   519 MVQKASSGGKSTDLSKNSTSRKNVSTSTE-----GLAISDTTPESSNQET----DSTTLLESDSSNTAIIPETRQLTLEg 589
Cdd:TIGR00618  517 RQDIDNPGPLTRRMQRGEQTYAQLETSEEdvyhqLTSERKQRASLKEQMQeiqqSFSILTQCDNRSKEDIPNLQNITVR- 595
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880   590 fslSVPADQMRVIHNInTLIAELAIEKEELVQALsSELSRSAHVQELNKELSRKLEAQTQRLELVTAQKMAIDNVSPEKQ 669
Cdd:TIGR00618  596 ---LQDLTEKLSEAED-MLACEQHALLRKLQPEQ-DLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVL 670

                   .
gi 145338880   670 Q 670
Cdd:TIGR00618  671 P 671
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
365-532 7.25e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 7.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 365 HIEDLTQEKfsLQRDLDASRALAESLASENSSMTDTYNQQRGLVNQLKDDMERLyqQIQAQMGELESVrVEYANAQLE-- 442
Cdd:COG4717  312 ALEELEEEE--LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAAL-LAEAGVEDEee 386
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 443 ----CNAADERSQILAsEVISLEDkalRLRSNELKLERELEKAQTEMLsyKKKLQSLEKDRQDLQSTIKALQEEKKVLQT 518
Cdd:COG4717  387 lraaLEQAEEYQELKE-ELEELEE---QLEELLGELEELLEALDEEEL--EEELEELEEELEELEEELEELREELAELEA 460
                        170
                 ....*....|....
gi 145338880 519 MVQKASSGGKSTDL 532
Cdd:COG4717  461 ELEQLEEDGELAEL 474
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
350-522 7.53e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.62  E-value: 7.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880  350 FSMPKQNDDFTALEQHIEDLTQEKFSLQRDLDASR----ALAESLASENSSMTDTYNQQRGLVNQLKD------------ 413
Cdd:TIGR04523 204 SNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQqeinEKTTEISNTQTQLNQLKDEQNKIKKQLSEkqkeleqnnkki 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880  414 -DMERLYQQIQAQMGELESVRVEYANAQLECNAADERSQI----------------LASEVISLEDKALRLRSNELKLER 476
Cdd:TIGR04523 284 kELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLeeiqnqisqnnkiisqLNEQISQLKKELTNSESENSEKQR 363
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 145338880  477 ELEKAQTEML-------SYKKKLQSLEKDRQDLQSTIKALQEEKKVLQTMVQK 522
Cdd:TIGR04523 364 ELEEKQNEIEklkkenqSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK 416
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
413-516 8.12e-03

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: 38.75  E-value: 8.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 413 DDMERLY--QQIQAQMGELESVRveyANAQLECNAADERSQILASEVISLEDKALRLRSNELKLERELEKAQTEMLSYKK 490
Cdd:COG1579    4 EDLRALLdlQELDSELDRLEHRL---KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
                         90       100
                 ....*....|....*....|....*...
gi 145338880 491 KLQSL--EKDRQDLQSTIKALQEEKKVL 516
Cdd:COG1579   81 QLGNVrnNKEYEALQKEIESLKRRISDL 108
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
357-524 8.46e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 8.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 357 DDFTALEQHIEDLTQEKFSLQRDLDASRALAESLA---SENSSMTDTYNQQRGLVNQLKDDMERL------YQQIQAQMG 427
Cdd:PRK03918 293 EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEeriKELEEKEERLEELKKKLKELEKRLEELeerhelYEEAKAKKE 372
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145338880 428 ELESVRVEYANAQLECNAADERSQILASEVISLEDKALRLRSNELKLER--------ELEKAQ----------TE----- 484
Cdd:PRK03918 373 ELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIkelkkaieELKKAKgkcpvcgrelTEehrke 452
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 145338880 485 -MLSYKKKLQSLEKDRQDLQSTIKALQEEKKVLQTMVQKAS 524
Cdd:PRK03918 453 lLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES 493
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
459-517 8.63e-03

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


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 37.96  E-value: 8.63e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145338880  459 SLEDKALRLRSNELKLERE--------------LEKAQTEMLSYKKKLQSLEKDRQDLQST---IKALQEEKKVLQ 517
Cdd:pfam13851  30 SLKEEIAELKKKEERNEKLmseiqqenkrltepLQKAQEEVEELRKQLENYEKDKQSLKNLkarLKVLEKELKDLK 105
 
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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