NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2468055594|ref|NP_001405912|]
View 

acyl-CoA-binding domain-containing protein 6 [Oryza sativa Japonica Group]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
169-481 8.14e-28

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 113.33  E-value: 8.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 169 EWTPLsvnGQRPKPRYEHGATVVQDKMYIFGGNHNGRYLSDLQALDLKSLTWSKIdAKFQAGSTdssksaqvsscAGHSL 248
Cdd:COG3055     2 TWSSL---PDLPTPRSEAAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTWSEL-APLPGPPR-----------HHAAA 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 249 ISWGNKFFSVAGHTKDPSENI---TVKEFDPHTCTWSivkTYGKPPVSRGGQSVTLVGTTLVLFGGEDAKRClLNDLHIL 325
Cdd:COG3055    67 VAQDGKLYVFGGFTGANPSSTplnDVYVYDPATNTWT---KLAPMPTPRGGATALLLDGKIYVVGGWDDGGN-VAWVEVY 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 326 DLETMTWDDVDAIgtPPPRSDHAAACHADRYLLIFgGGSHATCFNDlhvldlqtmEWSRPKQqglAPSPRAGHAGATVGE 405
Cdd:COG3055   143 DPATGTWTQLAPL--PTPRDHLAAAVLPDGKILVI-GGRNGSGFSN---------TWTTLAP---LPTARAGHAAAVLGG 207

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468055594 406 NWYIVGGGNNKSgvSETLVLNMSTLTWSVVssveGRVPLASEGMTLVhsNYNGDDYLISFGGYNGRYSNEVFALKL 481
Cdd:COG3055   208 KILVFGGESGFS--DEVEAYDPATNTWTAL----GELPTPRHGHAAV--LTDGKVYVIGGETKPGVRTPLVTSAEV 275
ACBP pfam00887
Acyl CoA binding protein;
27-93 4.74e-19

Acyl CoA binding protein;


:

Pssm-ID: 459982  Cd Length: 76  Bit Score: 81.87  E-value: 4.74e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468055594  27 TSSSAISRFQNDVALLLYGLYQQATVGPCNVPKPRAWNPVEQSKWTSWHGLGSMPSAEAMRLFVKIL 93
Cdd:pfam00887  10 FVKKLKSKPSNEEKLELYGLYKQATVGDCNTPRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKYVELV 76
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 471-637 4.36e-11

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: 66.11  E-value: 4.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 471 RYSNEVFALKLTLKSDLQSKTKEHASDGTSSVLEPEVELSH-DGKIREIAMDSADSDLKKDDANELLVALKAEKEELEAA 549
Cdd:COG1196   224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAElEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 550 LNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRCFKLEVDVAELRQKLQSMDALEREVELLRRQKAASEQA 629
Cdd:COG1196   304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383


                  ....*...
gi 2468055594 630 ALEAKQRQ 637
Cdd:COG1196   384 LAEELLEA 391
 
Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
169-481 8.14e-28

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 113.33  E-value: 8.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 169 EWTPLsvnGQRPKPRYEHGATVVQDKMYIFGGNHNGRYLSDLQALDLKSLTWSKIdAKFQAGSTdssksaqvsscAGHSL 248
Cdd:COG3055     2 TWSSL---PDLPTPRSEAAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTWSEL-APLPGPPR-----------HHAAA 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 249 ISWGNKFFSVAGHTKDPSENI---TVKEFDPHTCTWSivkTYGKPPVSRGGQSVTLVGTTLVLFGGEDAKRClLNDLHIL 325
Cdd:COG3055    67 VAQDGKLYVFGGFTGANPSSTplnDVYVYDPATNTWT---KLAPMPTPRGGATALLLDGKIYVVGGWDDGGN-VAWVEVY 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 326 DLETMTWDDVDAIgtPPPRSDHAAACHADRYLLIFgGGSHATCFNDlhvldlqtmEWSRPKQqglAPSPRAGHAGATVGE 405
Cdd:COG3055   143 DPATGTWTQLAPL--PTPRDHLAAAVLPDGKILVI-GGRNGSGFSN---------TWTTLAP---LPTARAGHAAAVLGG 207

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468055594 406 NWYIVGGGNNKSgvSETLVLNMSTLTWSVVssveGRVPLASEGMTLVhsNYNGDDYLISFGGYNGRYSNEVFALKL 481
Cdd:COG3055   208 KILVFGGESGFS--DEVEAYDPATNTWTAL----GELPTPRHGHAAV--LTDGKVYVIGGETKPGVRTPLVTSAEV 275
ACBP pfam00887
Acyl CoA binding protein;
27-93 4.74e-19

Acyl CoA binding protein;


Pssm-ID: 459982  Cd Length: 76  Bit Score: 81.87  E-value: 4.74e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468055594  27 TSSSAISRFQNDVALLLYGLYQQATVGPCNVPKPRAWNPVEQSKWTSWHGLGSMPSAEAMRLFVKIL 93
Cdd:pfam00887  10 FVKKLKSKPSNEEKLELYGLYKQATVGDCNTPRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKYVELV 76
ACBP cd00435
Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a ...
 37-95 7.95e-18

Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a one-to-one binding mode with high specificity and affinity. Acyl-CoAs are important intermediates in fatty lipid synthesis and fatty acid degradation and play a role in regulation of intermediary metabolism and gene regulation. The suggested role of ACBP is to act as a intracellular acyl-CoA transporter and pool former. ACBPs are present in a large group of eukaryotic species and several tissue-specific isoforms have been detected.


Pssm-ID: 238248  Cd Length: 85  Bit Score: 78.52  E-value: 7.95e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2468055594  37 NDVALLLYGLYQQATVGPCNVPKPRAWNPVEQSKWTSWHGLGSMPSAEAMRLFVKILEE 95
Cdd:cd00435    21 NEEKLQLYSLYKQATVGDCNTERPGMFDLKGRAKWDAWNSLKGMSKEDAMKAYIAKVEE 79
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 471-637 4.36e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.11  E-value: 4.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 471 RYSNEVFALKLTLKSDLQSKTKEHASDGTSSVLEPEVELSH-DGKIREIAMDSADSDLKKDDANELLVALKAEKEELEAA 549
Cdd:COG1196   224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAElEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 550 LNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRCFKLEVDVAELRQKLQSMDALEREVELLRRQKAASEQA 629
Cdd:COG1196   304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383


                  ....*...
gi 2468055594 630 ALEAKQRQ 637
Cdd:COG1196   384 LAEELLEA 391
PLN02153 PLN02153
epithiospecifier protein
 163-479 5.28e-11

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 64.62  E-value: 5.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 163 AVSVHEEWTPLSVNGQR-PKPRYEHGATVVQDKMYIFGGNhngryLSDLQALDlksltwskidakfqagstdssksaqvs 241
Cdd:PLN02153    2 APTLQGGWIKVEQKGGKgPGPRCSHGIAVVGDKLYSFGGE-----LKPNEHID--------------------------- 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 242 scaghsliswgnkffsvaghtKDpsenitVKEFDPHTCTWSIVKTYGKPP-VSRGGQSVTLVGTTLVLFGGEDAKRClLN 320
Cdd:PLN02153   50 ---------------------KD------LYVFDFNTHTWSIAPANGDVPrISCLGVRMVAVGTKLYIFGGRDEKRE-FS 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 321 DLHILDLETMTWD---DVDAIGTPPPRSDHAAACHaDRYLLIFGGGSHA------TCFNDLHVLDLQTMEWSRPKQQGLA 391
Cdd:PLN02153  102 DFYSYDTVKNEWTfltKLDEEGGPEARTFHSMASD-ENHVYVFGGVSKGglmktpERFRTIEAYNIADGKWVQLPDPGEN 180

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 392 PSPRAGHAGATV-GENWYIVG-------GGNNKSGVSETLVLNMSTLTWSVVSSVeGRVPLASEgmtlVHSNYNGDDYLI 463
Cdd:PLN02153  181 FEKRGGAGFAVVqGKIWVVYGfatsilpGGKSDYESNAVQFFDPASGKWTEVETT-GAKPSARS----VFAHAVVGKYII 255

                         330       340
                  ....*....|....*....|....*.
gi 2468055594 464 SFGG-----YNGRY-----SNEVFAL 479
Cdd:PLN02153  256 IFGGevwpdLKGHLgpgtlSNEGYAL 281
ACB COG4281
Acyl-CoA-binding protein [Lipid transport and metabolism];
33-96 3.74e-09

Acyl-CoA-binding protein [Lipid transport and metabolism];


Pssm-ID: 443422  Cd Length: 87  Bit Score: 54.09  E-value: 3.74e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468055594  33 SRFQNDVALLLYGLYQQATVGPCNVPKPRAWNPVEQSKWTSWHGLGSMPSAEAMRLFVKILEEE 96
Cdd:COG4281    20 ERPDNDTLLKLYALYKQATEGDVTGKRPGMTDFVGRAKYDAWAQLKGMSKDEAMQQYIDLVNSL 83
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 528-634 6.16e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.22  E-value: 6.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  528 KKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRCFKLEVDVAELRQKLQ 607
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410

                           90       100
                   ....*....|....*....|....*..
gi 2468055594  608 SmdaLEREVELLRRQKAASEQAALEAK 634
Cdd:TIGR02168  411 R---LEDRRERLQQEIEELLKKLEEAE 434
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 182-223 9.08e-08

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 48.76  E-value: 9.08e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2468055594 182 PRYEHGATVVQDKMYIFGGNHNGRYLSDLQALDLKSLTWSKI 223
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSKL 42
PTZ00458 PTZ00458
acyl CoA binding protein; Provisional
 37-100 1.06e-07

acyl CoA binding protein; Provisional


Pssm-ID: 185637  Cd Length: 90  Bit Score: 49.82  E-value: 1.06e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468055594  37 NDVALLLYGLYQQATVGPCNVPKPRAWNPVEQSKWTSWHGLGSMPSAEAMRLFVKILEEEDPGW 100
Cdd:PTZ00458   23 VEIKLDLYKYYKQSTVGNCNIKEPSMFKYQDRKKYEAWKSIENLNREDAKKRYVEIVTELFPNW 86
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 495-641 2.58e-06

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 48.91  E-value: 2.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 495 ASDGTSSVLEPEVELshDGKIREiamdsADSDLKKddANELLVALKAEKEELEAALNREQVQTIQLKEEIAEA-EARNAE 573
Cdd:pfam04012  13 IHEGLDKAEDPEKML--EQAIRD-----MQSELVK--ARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAAlTKGNEE 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468055594 574 LTKE----LQTVRGQLAAEQSRCFKLEVDVAELRQKLQsmdALEREVELLRRQK---AASEQAALEAKQRQSSSG 641
Cdd:pfam04012  84 LAREalaeKKSLEKQAEALETQLAQQRSAVEQLRKQLA---ALETKIQQLKAKKnllKARLKAAKAQEAVQTSLG 155
PRK09039 PRK09039
peptidoglycan -binding protein;
513-640 5.98e-05

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 45.73  E-value: 5.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 513 GKIREIAMDSADSDLKKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRgQLAAEQsrc 592
Cdd:PRK09039   60 SQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEK-QVSARA--- 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2468055594 593 fklevdvaeLRQklqsMDALEREVELLRRQKAASEQAALEAKQRQSSS 640
Cdd:PRK09039  136 ---------LAQ----VELLNQQIAALRRQLAALEAALDASEKRDRES 170
 
Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
169-481 8.14e-28

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 113.33  E-value: 8.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 169 EWTPLsvnGQRPKPRYEHGATVVQDKMYIFGGNHNGRYLSDLQALDLKSLTWSKIdAKFQAGSTdssksaqvsscAGHSL 248
Cdd:COG3055     2 TWSSL---PDLPTPRSEAAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTWSEL-APLPGPPR-----------HHAAA 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 249 ISWGNKFFSVAGHTKDPSENI---TVKEFDPHTCTWSivkTYGKPPVSRGGQSVTLVGTTLVLFGGEDAKRClLNDLHIL 325
Cdd:COG3055    67 VAQDGKLYVFGGFTGANPSSTplnDVYVYDPATNTWT---KLAPMPTPRGGATALLLDGKIYVVGGWDDGGN-VAWVEVY 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 326 DLETMTWDDVDAIgtPPPRSDHAAACHADRYLLIFgGGSHATCFNDlhvldlqtmEWSRPKQqglAPSPRAGHAGATVGE 405
Cdd:COG3055   143 DPATGTWTQLAPL--PTPRDHLAAAVLPDGKILVI-GGRNGSGFSN---------TWTTLAP---LPTARAGHAAAVLGG 207

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468055594 406 NWYIVGGGNNKSgvSETLVLNMSTLTWSVVssveGRVPLASEGMTLVhsNYNGDDYLISFGGYNGRYSNEVFALKL 481
Cdd:COG3055   208 KILVFGGESGFS--DEVEAYDPATNTWTAL----GELPTPRHGHAAV--LTDGKVYVIGGETKPGVRTPLVTSAEV 275
ACBP pfam00887
Acyl CoA binding protein;
27-93 4.74e-19

Acyl CoA binding protein;


Pssm-ID: 459982  Cd Length: 76  Bit Score: 81.87  E-value: 4.74e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468055594  27 TSSSAISRFQNDVALLLYGLYQQATVGPCNVPKPRAWNPVEQSKWTSWHGLGSMPSAEAMRLFVKIL 93
Cdd:pfam00887  10 FVKKLKSKPSNEEKLELYGLYKQATVGDCNTPRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKYVELV 76
ACBP cd00435
Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a ...
 37-95 7.95e-18

Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a one-to-one binding mode with high specificity and affinity. Acyl-CoAs are important intermediates in fatty lipid synthesis and fatty acid degradation and play a role in regulation of intermediary metabolism and gene regulation. The suggested role of ACBP is to act as a intracellular acyl-CoA transporter and pool former. ACBPs are present in a large group of eukaryotic species and several tissue-specific isoforms have been detected.


Pssm-ID: 238248  Cd Length: 85  Bit Score: 78.52  E-value: 7.95e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2468055594  37 NDVALLLYGLYQQATVGPCNVPKPRAWNPVEQSKWTSWHGLGSMPSAEAMRLFVKILEE 95
Cdd:cd00435    21 NEEKLQLYSLYKQATVGDCNTERPGMFDLKGRAKWDAWNSLKGMSKEDAMKAYIAKVEE 79
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 471-637 4.36e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.11  E-value: 4.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 471 RYSNEVFALKLTLKSDLQSKTKEHASDGTSSVLEPEVELSH-DGKIREIAMDSADSDLKKDDANELLVALKAEKEELEAA 549
Cdd:COG1196   224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAElEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 550 LNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRCFKLEVDVAELRQKLQSMDALEREVELLRRQKAASEQA 629
Cdd:COG1196   304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383


                  ....*...
gi 2468055594 630 ALEAKQRQ 637
Cdd:COG1196   384 LAEELLEA 391
PLN02153 PLN02153
epithiospecifier protein
 163-479 5.28e-11

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 64.62  E-value: 5.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 163 AVSVHEEWTPLSVNGQR-PKPRYEHGATVVQDKMYIFGGNhngryLSDLQALDlksltwskidakfqagstdssksaqvs 241
Cdd:PLN02153    2 APTLQGGWIKVEQKGGKgPGPRCSHGIAVVGDKLYSFGGE-----LKPNEHID--------------------------- 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 242 scaghsliswgnkffsvaghtKDpsenitVKEFDPHTCTWSIVKTYGKPP-VSRGGQSVTLVGTTLVLFGGEDAKRClLN 320
Cdd:PLN02153   50 ---------------------KD------LYVFDFNTHTWSIAPANGDVPrISCLGVRMVAVGTKLYIFGGRDEKRE-FS 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 321 DLHILDLETMTWD---DVDAIGTPPPRSDHAAACHaDRYLLIFGGGSHA------TCFNDLHVLDLQTMEWSRPKQQGLA 391
Cdd:PLN02153  102 DFYSYDTVKNEWTfltKLDEEGGPEARTFHSMASD-ENHVYVFGGVSKGglmktpERFRTIEAYNIADGKWVQLPDPGEN 180

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 392 PSPRAGHAGATV-GENWYIVG-------GGNNKSGVSETLVLNMSTLTWSVVSSVeGRVPLASEgmtlVHSNYNGDDYLI 463
Cdd:PLN02153  181 FEKRGGAGFAVVqGKIWVVYGfatsilpGGKSDYESNAVQFFDPASGKWTEVETT-GAKPSARS----VFAHAVVGKYII 255

                         330       340
                  ....*....|....*....|....*.
gi 2468055594 464 SFGG-----YNGRY-----SNEVFAL 479
Cdd:PLN02153  256 IFGGevwpdLKGHLgpgtlSNEGYAL 281
PLN02193 PLN02193
nitrile-specifier protein
 162-477 3.56e-10

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 62.67  E-value: 3.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 162 SAVSVHEEWTPLSVNGQRPKPRYEHGATVVQDKMYIFGGNHNGRYLSD--LQALDLKSLTWSKidakfqagstdSSKSAQ 239
Cdd:PLN02193  145 STPKLLGKWIKVEQKGEGPGLRCSHGIAQVGNKIYSFGGEFTPNQPIDkhLYVFDLETRTWSI-----------SPATGD 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 240 VS--SCAGHSLISWGNKFFSVAGhtKDPSENIT-VKEFDPHTCTWSIVKTYGKPPVSRGGQSVTLVGTTLVLFGGEDAkR 316
Cdd:PLN02193  214 VPhlSCLGVRMVSIGSTLYVFGG--RDASRQYNgFYSFDTTTNEWKLLTPVEEGPTPRSFHSMAADEENVYVFGGVSA-T 290

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 317 CLLNDLHILDLETMTWDDVDAIG-TPPPRSDHAAACHADRYLLIFGggshatcFN-----DLHVLDLQTMEWSRPKQQGL 390
Cdd:PLN02193  291 ARLKTLDSYNIVDKKWFHCSTPGdSFSIRGGAGLEVVQGKVWVVYG-------FNgcevdDVHYYDPVQDKWTQVETFGV 363

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 391 APSPRAGHAGATVGENWYIVGG------------GNNKSGvseTLVLNMSTLTWSVVSSV--EGRVPlASEGMTL-VHSN 455
Cdd:PLN02193  364 RPSERSVFASAAVGKHIVIFGGeiamdplahvgpGQLTDG---TFALDTETLQWERLDKFgeEEETP-SSRGWTAsTTGT 439

                         330       340
                  ....*....|....*....|....*
gi 2468055594 456 YNGDDYLISFGG---YNGRYSNEVF 477
Cdd:PLN02193  440 IDGKKGLVMHGGkapTNDRFDDLFF 464
PLN02153 PLN02153
epithiospecifier protein
 165-362 7.54e-10

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 61.16  E-value: 7.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 165 SVHEEW---TPLSVNGQrPKPRYEHGATVVQDKMYIFGGNHNG------RYLSDLQALDLKSLTWSKIdakfqagsTDSS 235
Cdd:PLN02153  108 TVKNEWtflTKLDEEGG-PEARTFHSMASDENHVYVFGGVSKGglmktpERFRTIEAYNIADGKWVQL--------PDPG 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 236 KSAQVSSCAGHSLISwgNKFFSVAGHT-------KDPSENITVKEFDPHTCTWSIVKTYGKPPVSRGGQSVTLVGTTLVL 308
Cdd:PLN02153  179 ENFEKRGGAGFAVVQ--GKIWVVYGFAtsilpggKSDYESNAVQFFDPASGKWTEVETTGAKPSARSVFAHAVVGKYIII 256

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468055594 309 FGGE---DAKR-----CLLNDLHILDLETMTWDDVDAIGTPP-PR---SDHAAACHADRYLLIFGG 362
Cdd:PLN02153  257 FGGEvwpDLKGhlgpgTLSNEGYALDTETLVWEKLGECGEPAmPRgwtAYTTATVYGKNGLLMHGG 322
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 513-639 1.37e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.49  E-value: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 513 GKIREIAMDSADSDLKKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRc 592
Cdd:COG1196   288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA- 366

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2468055594 593 fkLEVDVAELRQKLQSMDALEREVELLRRQKAASEQAALEAKQRQSS 639
Cdd:COG1196   367 --LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
ACB COG4281
Acyl-CoA-binding protein [Lipid transport and metabolism];
33-96 3.74e-09

Acyl-CoA-binding protein [Lipid transport and metabolism];


Pssm-ID: 443422  Cd Length: 87  Bit Score: 54.09  E-value: 3.74e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468055594  33 SRFQNDVALLLYGLYQQATVGPCNVPKPRAWNPVEQSKWTSWHGLGSMPSAEAMRLFVKILEEE 96
Cdd:COG4281    20 ERPDNDTLLKLYALYKQATEGDVTGKRPGMTDFVGRAKYDAWAQLKGMSKDEAMQQYIDLVNSL 83
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 526-636 5.76e-09

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 56.86  E-value: 5.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 526 DLKKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLaaeqsrcfklevdvAELRQK 605
Cdd:COG1579    16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI--------------KKYEEQ 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2468055594 606 LQS------MDALEREVELLRRQKAASEQAALEAKQR 636
Cdd:COG1579    82 LGNvrnnkeYEALQKEIESLKRRISDLEDEILELMER 118
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 508-638 7.02e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 7.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 508 ELSHDGKIREIAMDSADSDLKKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAA 587
Cdd:COG1196   290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2468055594 588 EQSRcfkLEVDVAELRQKLQSMDALEREVELLRRQKAASEQAALEAKQRQS 638
Cdd:COG1196   370 AEAE---LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 514-637 9.89e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.79  E-value: 9.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 514 KIREIAMDSADSDLKKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRCF 593
Cdd:COG1196   310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2468055594 594 KLEVDVAELRQKLQSMDALEREvELLRRQKAASEQAALEAKQRQ 637
Cdd:COG1196   390 EALRAAAELAAQLEELEEAEEA-LLERLERLEEELEELEEALAE 432
PLN02153 PLN02153
epithiospecifier protein
 191-413 2.86e-08

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 56.15  E-value: 2.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 191 VQDKMYIFGGNHNGRYLSDLQALDLKSLTWSKIDAKFQAGSTDSSKSAQVSSCAGHSLISWGnkfFSVAGHTKDPSENIT 270
Cdd:PLN02153   84 VGTKLYIFGGRDEKREFSDFYSYDTVKNEWTFLTKLDEEGGPEARTFHSMASDENHVYVFGG---VSKGGLMKTPERFRT 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 271 VKEFDPHTCTWSIVKTYGKPPVSRGGQSVTLVG---------TTLVLFGGEDAKRCllNDLHILDLETMTWDDVDAIGTP 341
Cdd:PLN02153  161 IEAYNIADGKWVQLPDPGENFEKRGGAGFAVVQgkiwvvygfATSILPGGKSDYES--NAVQFFDPASGKWTEVETTGAK 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 342 PPRSDHAAACHADRYLLIFGG------GSH---ATCFNDLHVLDLQTMEWSRPKQQGLAPSPRA--GHAGATV-GENWYI 409
Cdd:PLN02153  239 PSARSVFAHAVVGKYIIIFGGevwpdlKGHlgpGTLSNEGYALDTETLVWEKLGECGEPAMPRGwtAYTTATVyGKNGLL 318


                  ....
gi 2468055594 410 VGGG 413
Cdd:PLN02153  319 MHGG 322
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 514-639 4.10e-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: 4.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 514 KIREIAMDSADSDLKKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRCF 593
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2468055594 594 KLEVDVAELRQKLQS----MDALEREVELLRRQKAASEQAALEAKQRQSS 639
Cdd:COG1196   397 ELAAQLEELEEAEEAllerLERLEEELEELEEALAELEEEEEEEEEALEE 446
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
513-637 5.88e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.93  E-value: 5.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 513 GKIREI---AMDSADSDLKK-DDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEA--RNAELTKELQTVRGQLA 586
Cdd:COG4717    63 GRKPELnlkELKELEEELKEaEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELA 142

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2468055594 587 AEQSRCFKLEVDVAELRQKLQSMDALEREVELLRRQKAASEQAALEAKQRQ 637
Cdd:COG4717   143 ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE 193
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
515-639 6.02e-08

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 55.79  E-value: 6.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 515 IREIAMDSADSDLKKDdanelLVALKAEKEELEAALNREQVQTIQLKEEIAEAEAR-NAELTKELQTVRGQLAAEQSRCF 593
Cdd:COG3206   256 LPELLQSPVIQQLRAQ-----LAELEAELAELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILASLEAELEALQAREA 330

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2468055594 594 KLEVDVAELRQKLQSMDALEREVELLRRQKAASEQ--AALEAKQRQSS 639
Cdd:COG3206   331 SLQAQLAQLEARLAELPELEAELRRLEREVEVARElyESLLQRLEEAR 378
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 528-634 6.16e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.22  E-value: 6.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  528 KKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRCFKLEVDVAELRQKLQ 607
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410

                           90       100
                   ....*....|....*....|....*..
gi 2468055594  608 SmdaLEREVELLRRQKAASEQAALEAK 634
Cdd:TIGR02168  411 R---LEDRRERLQQEIEELLKKLEEAE 434
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 182-223 9.08e-08

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 48.76  E-value: 9.08e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2468055594 182 PRYEHGATVVQDKMYIFGGNHNGRYLSDLQALDLKSLTWSKI 223
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSKL 42
PTZ00458 PTZ00458
acyl CoA binding protein; Provisional
 37-100 1.06e-07

acyl CoA binding protein; Provisional


Pssm-ID: 185637  Cd Length: 90  Bit Score: 49.82  E-value: 1.06e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468055594  37 NDVALLLYGLYQQATVGPCNVPKPRAWNPVEQSKWTSWHGLGSMPSAEAMRLFVKILEEEDPGW 100
Cdd:PTZ00458   23 VEIKLDLYKYYKQSTVGNCNIKEPSMFKYQDRKKYEAWKSIENLNREDAKKRYVEIVTELFPNW 86
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 538-637 1.08e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 538 ALKAEKEELEA---ALNREQVQTIQ--LKEEIAEAEARNAELTKELQTVRGQLAAEQSRCFKLEVDVAELRQKL----QS 608
Cdd:COG1196   217 ELKEELKELEAellLLKLRELEAELeeLEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellAE 296

                          90       100
                  ....*....|....*....|....*....
gi 2468055594 609 MDALEREVELLRRQKAASEQAALEAKQRQ 637
Cdd:COG1196   297 LARLEQDIARLEERRRELEERLEELEEEL 325
PHA03098 PHA03098
kelch-like protein; Provisional
 121-435 2.68e-07

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 53.62  E-value: 2.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 121 KEDPKVILASTNGTSVPEPKTISENGSS--VETQDKVVILEGLSAVSVHEEWTPLSVNGQRpkprYEHGATVVQDKMYIF 198
Cdd:PHA03098  225 NKRCIKIIYSKKYNLNKILPRSSTFGSIiyIHITMSIFTYNYITNYSPLSEINTIIDIHYV----YCFGSVVLNNVIYFI 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 199 GG-NHNGRYLSDLQALDLKSLTWSKI-----DAKFQAGSTDSsksaqvsscaghsliswgNKFFSVAGHTKDPSENiTVK 272
Cdd:PHA03098  301 GGmNKNNLSVNSVVSYDTKTKSWNKVpeliyPRKNPGVTVFN------------------NRIYVIGGIYNSISLN-TVE 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 273 EFDPHTCTWSIVKTYGKPpvsRGGQSVTLVGTTLVLFGGEDAKRCLLNDLHILDLETMTWDDVDAigTPPPRSDHAAACH 352
Cdd:PHA03098  362 SWKPGESKWREEPPLIFP---RYNPCVVNVNNLIYVIGGISKNDELLKTVECFSLNTNKWSKGSP--LPISHYGGCAIYH 436

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 353 aDRYLLIFGGGSHAT---CFNDLHVLDLQTMEWSRpkqqgLAPS--PRAGHAGATVGENWYIVGGGNNKSGVSETLVLNM 427
Cdd:PHA03098  437 -DGKIYVIGGISYIDnikVYNIVESYNPVTNKWTE-----LSSLnfPRINASLCIFNNKIYVVGGDKYEYYINEIEVYDD 510


                  ....*...
gi 2468055594 428 STLTWSVV 435
Cdd:PHA03098  511 KTNTWTLF 518
Kelch_3 pfam13415
Galactose oxidase, central domain;
354-401 4.57e-07

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 46.90  E-value: 4.57e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2468055594 354 DRYLLIFGG--GSHATCFNDLHVLDLQTMEWSRPKQQglaPSPRAGHAGA 401
Cdd:pfam13415   1 GDKLYIFGGlgFDGQTRLNDLYVYDLDTNTWTQIGDL---PPPRSGHSAT 47
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
520-639 7.15e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.83  E-value: 7.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 520 MDSADSDLkkDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRCFKLEVDV 599
Cdd:COG4372    40 LDKLQEEL--EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2468055594 600 AEL---RQKL-QSMDALEREVELLRRQKAASEQAALEAKQRQSS 639
Cdd:COG4372   118 EELqkeRQDLeQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
508-640 7.29e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.61  E-value: 7.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  508 ELSHDGKIREIAmdSADSDLKK-DDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLA 586
Cdd:COG4913    660 EIDVASAEREIA--ELEAELERlDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2468055594  587 AEQSRCFKLEVDVAELRQKLQSMDALEREVellrRQKAASEQAALEAKQRQSSS 640
Cdd:COG4913    738 AAEDLARLELRALLEERFAAALGDAVEREL----RENLEERIDALRARLNRAEE 787
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 499-634 8.75e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 52.38  E-value: 8.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  499 TSSVLEPEVELSH-DGKIREIAMDSADSDLKKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKE 577
Cdd:TIGR02169  293 KEKIGELEAEIASlERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468055594  578 LQTVRGQLAAeqsrcfkLEVDVAELRQKLqsmDALEREVELLRR---------QKAASEQAALEAK 634
Cdd:TIGR02169  373 LEEVDKEFAE-------TRDELKDYREKL---EKLKREINELKReldrlqeelQRLSEELADLNAA 428
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 508-637 9.45e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 9.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 508 ELSHDGKIREIAMDSADSDLKKDDANELLVALKAEKEELEAALNREQvqtiQLKEEIAEAEARNAELTKELQTVRGQLAA 587
Cdd:COG1196   217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELA----ELEAELEELRLELEELELELEEAQAEEYE 292

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2468055594 588 EQSRCFKLEVDVAELRQKLQsmDALEREVELLRRQKAASEQAALEAKQRQ 637
Cdd:COG1196   293 LLAELARLEQDIARLEERRR--ELEERLEELEEELAELEEELEELEEELE 340
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
536-632 1.22e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.56  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 536 LVALKAEKEELEAALNREqvqtiqLKEEIAEAEARNAELTKELQTVRGQLAAEQSRcfklevdVAELRQKLQSMDALERE 615
Cdd:COG3206   293 VIALRAQIAALRAQLQQE------AQRILASLEAELEALQAREASLQAQLAQLEAR-------LAELPELEAELRRLERE 359

                          90       100
                  ....*....|....*....|....*
gi 2468055594 616 VE--------LLRRQKAASEQAALE 632
Cdd:COG3206   360 VEvarelyesLLQRLEEARLAEALT 384
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 528-632 1.60e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.92  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 528 KKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRCFKLEVDVAELRQKLq 607
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL- 99

                          90       100
                  ....*....|....*....|....*.
gi 2468055594 608 smDALEREV-ELLRRQKAASEQAALE 632
Cdd:COG4942   100 --EAQKEELaELLRALYRLGRQPPLA 123
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 530-637 2.50e-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: 50.83  E-value: 2.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  530 DDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRCFKLEVDVAELRQKLQSM 609
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759

                           90       100
                   ....*....|....*....|....*...
gi 2468055594  610 DAlEREVELLRRQKAASEQAALEAKQRQ 637
Cdd:TIGR02168  760 EA-EIEELEERLEEAEEELAEAEAEIEE 786
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 495-641 2.58e-06

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 48.91  E-value: 2.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 495 ASDGTSSVLEPEVELshDGKIREiamdsADSDLKKddANELLVALKAEKEELEAALNREQVQTIQLKEEIAEA-EARNAE 573
Cdd:pfam04012  13 IHEGLDKAEDPEKML--EQAIRD-----MQSELVK--ARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAAlTKGNEE 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468055594 574 LTKE----LQTVRGQLAAEQSRCFKLEVDVAELRQKLQsmdALEREVELLRRQK---AASEQAALEAKQRQSSSG 641
Cdd:pfam04012  84 LAREalaeKKSLEKQAEALETQLAQQRSAVEQLRKQLA---ALETKIQQLKAKKnllKARLKAAKAQEAVQTSLG 155
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 486-636 3.21e-06

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 50.28  E-value: 3.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 486 DLQSKTKEHASDGTSSVLEP----EVELSHDGKIREIAMDSADSDLKKDDANELLVALKAEKEELEAALNREQVQTIQLK 561
Cdd:pfam07888  98 ELEEKYKELSASSEELSEEKdallAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQ 177

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468055594 562 EEIAEAEARNAELTKELQTVRGQLAAEQSRCFKLEVDVAELRQKLQSMDALEREVELLRRQkAASEQAALEAKQR 636
Cdd:pfam07888 178 AKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEE-LRSLQERLNASER 251
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 528-637 3.68e-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: 3.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  528 KKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRCFKLEVDVAELRQKLQ 607
Cdd:TIGR02168  352 ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2468055594  608 S--MDALEREVELLRRQKaASEQAALEAKQRQ 637
Cdd:TIGR02168  432 EaeLKELQAELEELEEEL-EELQEELERLEEA 462
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
483-637 3.69e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.02  E-value: 3.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 483 LKSDLQSKTKEhaSDGTSSVLEPEVElshdgKIREiAMDSADSDLKKDDANELLVALKAEKEELEAALNREQVQTIQLKE 562
Cdd:COG3206   162 LEQNLELRREE--ARKALEFLEEQLP-----ELRK-ELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARA 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 563 EIAEAEARNAELTKELQTVRGQLAAE---------QSRCFKLEVDVAELRQKLQ----SMDALEREVELLRRQKAASEQA 629
Cdd:COG3206   234 ELAEAEARLAALRAQLGSGPDALPELlqspviqqlRAQLAELEAELAELSARYTpnhpDVIALRAQIAALRAQLQQEAQR 313


                  ....*...
gi 2468055594 630 ALEAKQRQ 637
Cdd:COG3206   314 ILASLEAE 321
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 504-634 3.96e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.45  E-value: 3.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  504 EPEVELSHDgKIREIamdsadsDLKKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELT-------K 576
Cdd:TIGR02169  783 DLEARLSHS-RIPEI-------QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKeqiksieK 854

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2468055594  577 ELQTVRGQLAAEQSRCFKLEVDVAELRQKLQSmdaLEREVELLRRQKAASEQAALEAK 634
Cdd:TIGR02169  855 EIENLNGKKEELEEELEELEAALRDLESRLGD---LKKERDELEAQLRELERKIEELE 909
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
514-633 4.18e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.52  E-value: 4.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 514 KIREIAMDSADSDLKKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRCF 593
Cdd:COG4372    81 ELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE 160

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2468055594 594 KLEVDVAELRQKLQSMDALEREVELLRRQKAASEQAALEA 633
Cdd:COG4372   161 SLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEE 200
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 530-641 4.36e-06

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 50.34  E-value: 4.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  530 DDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTK------ELQTVRGQLaAEQSRC-FKLEVDVAEL 602
Cdd:COG3096    553 EELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAArapawlAAQDALERL-REQSGEaLADSQEVTAA 631

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2468055594  603 RQKLqsmdaLEREVELLR-RQKAASEQAALEAKQRQSSSG 641
Cdd:COG3096    632 MQQL-----LEREREATVeRDELAARKQALESQIERLSQP 666
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 528-637 4.47e-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: 4.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  528 KKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQtvrgQLAAEQSRcfkLEVDVAELRQKLQ 607
Cdd:TIGR02168  240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY----ALANEISR---LEQQKQILRERLA 312

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2468055594  608 SMDA-LEREVELLRRQKAASEQAALEAKQRQ 637
Cdd:TIGR02168  313 NLERqLEELEAQLEELESKLDELAEELAELE 343
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
532-637 4.68e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.13  E-value: 4.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 532 ANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSrcfKLEVDVAELRQKLQSMDA 611
Cdd:COG4372    29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNE---QLQAAQAELAQAQEELES 105

                          90       100
                  ....*....|....*....|....*...
gi 2468055594 612 LEREVELLRRQ--KAASEQAALEAKQRQ 637
Cdd:COG4372   106 LQEEAEELQEEleELQKERQDLEQQRKQ 133
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 544-637 5.14e-06

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


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 48.07  E-value: 5.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 544 EELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRcfklevdVAELRQKLQSMDALEREVELLRRQK 623
Cdd:pfam12795  81 EELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQR-------LQQIRNRLNGPAPPGEPLSEAQRWA 153

                          90
                  ....*....|....
gi 2468055594 624 AASEQAALEAKQRQ 637
Cdd:pfam12795 154 LQAELAALKAQIDM 167
Kelch_4 pfam13418
Galactose oxidase, central domain;
182-226 6.56e-06

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 43.37  E-value: 6.56e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2468055594 182 PRYEHGATVVQDKM-YIFGG-NHNGRYLSDLQALDLKSLTWSKIDAK 226
Cdd:pfam13418   1 PRAYHTSTSIPDDTiYLFGGeGEDGTLLSDLWVFDLSTNEWTRLGSL 47
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
551-639 6.95e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.53  E-value: 6.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  551 NREQVQTI-----QLKEEIAEAEARNAELTKELQTVRGQLAAEQsRCFKL---EVDV-------AELRQKLQSMDA---- 611
Cdd:COG4913    608 NRAKLAALeaelaELEEELAEAEERLEALEAELDALQERREALQ-RLAEYswdEIDVasaereiAELEAELERLDAssdd 686

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2468055594  612 ---LEREVELLRRQKAASEQAALEAKQRQSS 639
Cdd:COG4913    687 laaLEEQLEELEAELEELEEELDELKGEIGR 717
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 534-639 8.08e-06

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 49.40  E-value: 8.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  534 ELLVALKAEKEELEAALNR---EQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRCFKLEVDVAELRQKLQsmD 610
Cdd:pfam01576  233 ELRAQLAKKEEELQAALARleeETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELE--D 310

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2468055594  611 AL-------------EREVELLRR----QKAASEQAALEAKQRQSS 639
Cdd:pfam01576  311 TLdttaaqqelrskrEQEVTELKKaleeETRSHEAQLQEMRQKHTQ 356
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
511-636 1.12e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 1.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  511 HDGKIREI--AMDSADSDlKKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAE 588
Cdd:COG4913    321 LREELDELeaQIRGNGGD-RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEE 399

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2468055594  589 QSRC----FKLEVDVAELRQKLqsmDALEREVELLRRQKAASEQAALEAKQR 636
Cdd:COG4913    400 LEALeealAEAEAALRDLRREL---RELEAEIASLERRKSNIPARLLALRDA 448
Kelch_4 pfam13418
Galactose oxidase, central domain;
343-394 1.13e-05

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 42.98  E-value: 1.13e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2468055594 343 PRSDHAAACHADRYLLIFGG-GSHATCFNDLHVLDLQTMEWSRpkqqgLAPSP 394
Cdd:pfam13418   1 PRAYHTSTSIPDDTIYLFGGeGEDGTLLSDLWVFDLSTNEWTR-----LGSLP 48
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 534-645 1.31e-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: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 534 ELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRcfkLEVDVAELRQKLQSMDALE 613
Cdd:COG4942   150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE---LAELAAELAELQQEAEELE 226

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2468055594 614 REVELLRRQKAASEQAAlEAKQRQSSSGMWGW 645
Cdd:COG4942   227 ALIARLEAEAAAAAERT-PAAGFAALKGKLPW 257
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 530-656 1.48e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.90  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 530 DDANELLVALKAEKEELEAalnreqvQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRCFKLEVDVAELRQKLQSM 609
Cdd:COG3883   129 DADADLLEELKADKAELEA-------KKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAEL 201

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2468055594 610 DALEREVELLRRQKAASEQAALEAKQRQSSSGMWGWLVGTPPDKSES 656
Cdd:COG3883   202 EAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 536-629 1.86e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.45  E-value: 1.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 536 LVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRCFKLEVDVAELRQKLQsmdALERE 615
Cdd:COG4942    15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA---ELEKE 91

                          90
                  ....*....|....
gi 2468055594 616 VELLRRQKAASEQA 629
Cdd:COG4942    92 IAELRAELEAQKEE 105
Kelch_3 pfam13415
Galactose oxidase, central domain;
305-350 1.87e-05

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 42.28  E-value: 1.87e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2468055594 305 TLVLFGGEDAKRC-LLNDLHILDLETMTWDDVDAIgtPPPRSDHAAA 350
Cdd:pfam13415   3 KLYIFGGLGFDGQtRLNDLYVYDLDTNTWTQIGDL--PPPRSGHSAT 47
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 512-637 2.55e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 46.07  E-value: 2.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 512 DGKIREIAMDSADSDLKKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELT---------KELQTVR 582
Cdd:COG1579    16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlgnvrnnKEYEALQ 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2468055594 583 GQLAAEQSRCFKLEVDVAELRQKLqsmDALEREVELLRRQKAAsEQAALEAKQRQ 637
Cdd:COG1579    96 KEIESLKRRISDLEDEILELMERI---EELEEELAELEAELAE-LEAELEEKKAE 146
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 512-637 2.78e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.75  E-value: 2.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 512 DGKIREIAMDSADSDLKKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAA---- 587
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErara 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2468055594 588 --EQSRCF-KLEV-----DVAELRQKLQSMDAL-EREVELLRRQKAAseQAALEAKQRQ 637
Cdd:COG3883    95 lyRSGGSVsYLDVllgseSFSDFLDRLSALSKIaDADADLLEELKAD--KAELEAKKAE 151
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 526-640 2.97e-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: 47.36  E-value: 2.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  526 DLKKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEArnaeltkELQTVRGQLAAEQSRCFKLEVDVAELRQK 605
Cdd:TIGR02168  767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA-------ELTLLNEEAANLRERLESLERRIAATERR 839

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2468055594  606 LQsMDALEREVELLRRQKAASEQAALEAKQRQSSS 640
Cdd:TIGR02168  840 LE-DLEEQIEELSEDIESLAAEIEELEELIEELES 873
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 514-616 3.00e-05

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 47.38  E-value: 3.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 514 KIReIAMDSADSDLkkDDANELLVALKAEKEELE----------AALNREQVQtiQLKEEIAEAEARNA---ELTKELQT 580
Cdd:COG0542   401 RVR-MEIDSKPEEL--DELERRLEQLEIEKEALKkeqdeasferLAELRDELA--ELEEELEALKARWEaekELIEEIQE 475

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2468055594 581 VRGQLAAEQSRCFKLEVDVAELRQKLQSMDALEREV 616
Cdd:COG0542   476 LKEELEQRYGKIPELEKELAELEEELAELAPLLREE 511
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 527-637 3.18e-05

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 46.45  E-value: 3.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 527 LKKDDANELLVALKAEKEE--LEAALNREQVQtiQLKEEIAEAEARNAELtKELQtvrgqlaAEQSRcfKLEVDVAE-LR 603
Cdd:pfam13868  95 EKLQEREQMDEIVERIQEEdqAEAEEKLEKQR--QLREEIDEFNEEQAEW-KELE-------KEEER--EEDERILEyLK 162

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2468055594 604 QKLQSMDALEREVELLRRQKAAsEQAALEAKQRQ 637
Cdd:pfam13868 163 EKAEREEEREAEREEIEEEKER-EIARLRAQQEK 195
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 514-615 3.55e-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: 3.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 514 KIREIAMDSADSDLKKDDANELLVALKAEKE------ELEAALNREQV---QTIQLKEEIAEAEARNAELTKELQTVRGQ 584
Cdd:COG1579    60 EIKRLELEIEEVEARIKKYEEQLGNVRNNKEyealqkEIESLKRRISDledEILELMERIEELEEELAELEAELAELEAE 139

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2468055594 585 LAAEQSRcfkLEVDVAELRQKLQSMDAlERE 615
Cdd:COG1579   140 LEEKKAE---LDEELAELEAELEELEA-ERE 166
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 523-652 3.64e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.36  E-value: 3.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 523 ADSDLKK-DDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRCFKLEvdvAE 601
Cdd:COG3883   128 ADADADLlEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE---AE 204

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2468055594 602 LRQKLQSMDALEREVELLRRQKAASEQAALEAKQRQSSSGMWGWLVGTPPD 652
Cdd:COG3883   205 LAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAA 255
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
515-637 3.96e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 3.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  515 IREIAMDSADSDLKKDDANELLVALKAEKEELEAALNREQVQTIQ-----LKEEIAEAEARNAELTKELQTVRGQ----- 584
Cdd:COG4913    257 IRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRaelarLEAELERLEARLDALREELDELEAQirgng 336

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2468055594  585 ------LAAEQSRcfkLEVDVAELRQKLQSMDALEREVELlrrqKAASEQAALEAKQRQ 637
Cdd:COG4913    337 gdrleqLEREIER---LERELEERERRRARLEALLAALGL----PLPASAEEFAALRAE 388
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 528-651 4.66e-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: 46.30  E-value: 4.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 528 KKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAeqsrcfkLEVDVAELRQKLQ 607
Cdd:COG4942   158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE-------LQQEAEELEALIA 230

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2468055594 608 SmdaLEREVELLRRQKAASEQAALEAK--------------QRQSSSGMW-GWLVGTPP 651
Cdd:COG4942   231 R---LEAEAAAAAERTPAAGFAALKGKlpwpvsgrvvrrfgERDGGGGRNkGIDIAAPP 286
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 510-635 5.73e-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: 46.59  E-value: 5.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  510 SHDGKIREIAMDSADSDLKKDDANELLVALKAEKEELEAALN--REQVQTIQ-----LKEEIAEAE-------ARNAELT 575
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSelEEEIEELQkelyaLANEISRLEqqkqilrERLANLE 315

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468055594  576 KELQTVRGQLAAEQSRCFKLEVDVAELRQKLQS----MDALEREVELLRRQKAASEQAALEAKQ 635
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEEKLEElkeeLESLEAELEELEAELEELESRLEELEE 379
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 530-637 5.78e-05

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 45.68  E-value: 5.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 530 DDANELLVALKAEKEELEAALNREQVQTIQLKEE-----IAEAEARNAELTKELQTVRGQLAAEQSRcfKLEVDvaELRQ 604
Cdd:pfam13868 133 DEFNEEQAEWKELEKEEEREEDERILEYLKEKAEreeerEAEREEIEEEKEREIARLRAQQEKAQDE--KAERD--ELRA 208

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2468055594 605 KLQsMDALEREvellRRQKAAsEQAALEAKQRQ 637
Cdd:pfam13868 209 KLY-QEEQERK----ERQKER-EEAEKKARQRQ 235
PRK09039 PRK09039
peptidoglycan -binding protein;
513-640 5.98e-05

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 45.73  E-value: 5.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 513 GKIREIAMDSADSDLKKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRgQLAAEQsrc 592
Cdd:PRK09039   60 SQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEK-QVSARA--- 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2468055594 593 fklevdvaeLRQklqsMDALEREVELLRRQKAASEQAALEAKQRQSSS 640
Cdd:PRK09039  136 ---------LAQ----VELLNQQIAALRRQLAALEAALDASEKRDRES 170
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 534-636 7.12e-05

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


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 44.13  E-value: 7.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 534 ELLVALKAEKEELEA--ALNREQVQTIQ-----LKEEIAEAEARNAELTKELQT---VRGQLAAEQSRCFKLEVDVAELR 603
Cdd:pfam13851  26 ELIKSLKEEIAELKKkeERNEKLMSEIQqenkrLTEPLQKAQEEVEELRKQLENyekDKQSLKNLKARLKVLEKELKDLK 105

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2468055594 604 Q----KLQSMDALEREV-ELLRRQkaasEQAALEAKQR 636
Cdd:pfam13851 106 WehevLEQRFEKVERERdELYDKF----EAAIQDVQQK 139
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 180-217 7.52e-05

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 433528 [Multi-domain]  Cd Length: 41  Bit Score: 40.24  E-value: 7.52e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2468055594 180 PKPRYEHGATVVQDKMYIFGGNH--NGRYLSDLQALDLKS 217
Cdd:pfam13854   1 PVPRYGHCAVTVGDYIYLYGGYTggEGQPSDDVYVLSLPT 40
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
534-637 8.95e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 8.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 534 ELLVALKAEKEELEAALNREQvqtiQLKEEIAEAEARNAELTKELQTVRGQLAaeqsrcfKLEVDVAELRQKLQSMDALE 613
Cdd:PRK03918  169 EVIKEIKRRIERLEKFIKRTE----NIEELIKEKEKELEEVLREINEISSELP-------ELREELEKLEKEVKELEELK 237

                          90       100
                  ....*....|....*....|....*.
gi 2468055594 614 REVELLRRQKAASEQ--AALEAKQRQ 637
Cdd:PRK03918  238 EEIEELEKELESLEGskRKLEEKIRE 263
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
517-638 1.03e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 517 EIAMDSADSDLKKDDANELLVALKAEKEELEAALNREqvqtiqLKEEIAEAEARN-AELTKELQTVRGQLAAEQSRCFKL 595
Cdd:COG4717   378 EAGVEDEEELRAALEQAEEYQELKEELEELEEQLEEL------LGELEELLEALDeEELEEELEELEEELEELEEELEEL 451

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2468055594 596 EVDVAELRQKLQSMDALEREVELLRRQKAASEQAALEAKQRQS 638
Cdd:COG4717   452 REELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAA 494
PRK09039 PRK09039
peptidoglycan -binding protein;
529-640 1.09e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 44.96  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 529 KDDAnelLVALKAEKEELEAALNREQVQTIQLKEEIAE--AEARNAELTKE-LQTVRGQLAAEQSRcfkLEVDVAELRQK 605
Cdd:PRK09039   51 KDSA---LDRLNSQIAELADLLSLERQGNQDLQDSVANlrASLSAAEAERSrLQALLAELAGAGAA---AEGRAGELAQE 124

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2468055594 606 LQSMDAL----EREVELLRRQKAA------SEQAALEAKQRQSSS 640
Cdd:PRK09039  125 LDSEKQVsaraLAQVELLNQQIAAlrrqlaALEAALDASEKRDRE 169
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 517-637 1.12e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.55  E-value: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  517 EIAMDSADSDLKKDdanellvALKAEKEELEAalnreqvQTIQLKEEIAEaEARNAELTKE--------LQTVRGQLAAE 588
Cdd:pfam01576  865 ELADEIASGASGKS-------ALQDEKRRLEA-------RIAQLEEELEE-EQSNTELLNDrlrkstlqVEQLTTELAAE 929

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2468055594  589 QSRCFK-------LEVDVAELRQKLQSMDALEREvellrRQKAASeqAALEAKQRQ 637
Cdd:pfam01576  930 RSTSQKsesarqqLERQNKELKAKLQEMEGTVKS-----KFKSSI--AALEAKIAQ 978
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 474-636 1.20e-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: 1.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  474 NEVFALKLTLkSDLQSKTKEHASDGtsSVLEPEVElshdgKIREIAMDSADSDLKKDDANEllvALKAEKEELEAALNRE 553
Cdd:TIGR02169  702 NRLDELSQEL-SDASRKIGEIEKEI--EQLEQEEE-----KLKERLEELEEDLSSLEQEIE---NVKSELKELEARIEEL 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  554 QVQTIQLKEEIAEAEARNA-----ELTKELQTVRGQLAAEQSRCFKLEVDVAELRQKLQ----SMDALEREVELLRRQKA 624
Cdd:TIGR02169  771 EEDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEylekEIQELQEQRIDLKEQIK 850

                          170
                   ....*....|....
gi 2468055594  625 A--SEQAALEAKQR 636
Cdd:TIGR02169  851 SieKEIENLNGKKE 864
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 536-636 1.59e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 1.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  536 LVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQ-------TVRGQLAAEQSRCFKLEVDVAELRQKLQs 608
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEallneraSLEEALALLRSELEELSEELRELESKRS- 911

                           90       100
                   ....*....|....*....|....*...
gi 2468055594  609 mdALEREVELLRRQKAASEQAALEAKQR 636
Cdd:TIGR02168  912 --ELRRELEELREKLAQLELRLEGLEVR 937
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 540-637 1.63e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.14  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 540 KAEKEELEAALNREQVQTIQLKEEIAEAEARnAELTKELQTVRGQLAAEQSRCFKLEVDVAE-----LRQKLQSMDALER 614
Cdd:pfam13868 200 KAERDELRAKLYQEEQERKERQKEREEAEKK-ARQRQELQQAREEQIELKERRLAEEAEREEeeferMLRKQAEDEEIEQ 278

                          90       100
                  ....*....|....*....|....*..
gi 2468055594 615 EVELLRRQKAASEQAALEA----KQRQ 637
Cdd:pfam13868 279 EEAEKRRMKRLEHRRELEKqieeREEQ 305
Kelch_4 pfam13418
Galactose oxidase, central domain;
294-343 1.91e-04

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 39.52  E-value: 1.91e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2468055594 294 RGGQSVTLVG-TTLVLFGGEDAKRCLLNDLHILDLETMTWDDvdaIGTPPP 343
Cdd:pfam13418   2 RAYHTSTSIPdDTIYLFGGEGEDGTLLSDLWVFDLSTNEWTR---LGSLPS 49
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
528-636 2.44e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 528 KKDDANELLVALKAEKEELEAALNR--EQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRCFK---LEVDVAEL 602
Cdd:COG4717    96 ELEELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEEleeLEAELAEL 175

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2468055594 603 RQKL------------QSMDALEREVELLRRQKAASEQAALEAKQR 636
Cdd:COG4717   176 QEELeelleqlslateEELQDLAEELEELQQRLAELEEELEEAQEE 221
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 530-636 2.57e-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: 2.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  530 DDANELLVALKAEKEELEAALNREQvqtiqlkEEIAEAEARNAELTK-------ELQTVRGQLAAEQSRCFKLEVDVAEL 602
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAE-------EELAEAEAEIEELEAqieqlkeELKALREALDELRAELTLLNEEAANL 822

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2468055594  603 RQKLQS----MDALEREVELLRRQKA-ASEQAALEAKQR 636
Cdd:TIGR02168  823 RERLESlerrIAATERRLEDLEEQIEeLSEDIESLAAEI 861
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 533-641 2.65e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.60  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 533 NELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRCFKLEVDVAELRQKLQsmdAL 612
Cdd:COG4942   142 KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA---EL 218

                          90       100
                  ....*....|....*....|....*....
gi 2468055594 613 EREVELLRRQKAASEQAALEAKQRQSSSG 641
Cdd:COG4942   219 QQEAEELEALIARLEAEAAAAAERTPAAG 247
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 513-622 2.96e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 2.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 513 GKIREIAMDSADSDLKKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRC 592
Cdd:COG1196   665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2468055594 593 FK-LEVDVAELRQKLQSMDALEREVELLRRQ 622
Cdd:COG1196   745 EElLEEEALEELPEPPDLEELERELERLERE 775
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 392-429 3.07e-04

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 433528 [Multi-domain]  Cd Length: 41  Bit Score: 38.70  E-value: 3.07e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2468055594 392 PSPRAGHAGATVGENWYIVGG--GNNKSGVSETLVLNMST 429
Cdd:pfam13854   1 PVPRYGHCAVTVGDYIYLYGGytGGEGQPSDDVYVLSLPT 40
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 523-636 3.19e-04

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


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 42.67  E-value: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 523 ADSDLKKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAA--------EQSRCFK 594
Cdd:pfam12795  74 ILASLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGpappgeplSEAQRWA 153

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2468055594 595 LEVDVA-------ELRQKLQSMDALeREVELLRRQKAASEQAALEAKQR 636
Cdd:pfam12795 154 LQAELAalkaqidMLEQELLSNNNR-QDLLKARRDLLTLRIQRLEQQLQ 201
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
529-637 3.26e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 3.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 529 KDDANEL---LVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRcfKLEVDVAELRQK 605
Cdd:COG4372   107 QEEAEELqeeLEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE--LQALSEAEAEQA 184

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2468055594 606 LQSMDALEREVELLRRQKAASEQAALEAKQRQ 637
Cdd:COG4372   185 LDELLKEANRNAEKEEELAEAEKLIESLPREL 216
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 528-625 4.24e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 4.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 528 KKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRCFKLEVDVAELRQKLQ 607
Cdd:COG4942    35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALY 114

                          90
                  ....*....|....*...
gi 2468055594 608 SMDALEREVELLRRQKAA 625
Cdd:COG4942   115 RLGRQPPLALLLSPEDFL 132
Kelch_6 pfam13964
Kelch motif;
182-223 4.36e-04

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 38.47  E-value: 4.36e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2468055594 182 PRYEHGATVVQDKMYIFGGNHN-GRYLSDLQALDLKSLTWSKI 223
Cdd:pfam13964   1 PRTFHSVVSVGGYIYVFGGYTNaSPALNKLEVYNPLTKSWEEL 43
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 341-379 5.07e-04

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 433528 [Multi-domain]  Cd Length: 41  Bit Score: 37.93  E-value: 5.07e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2468055594 341 PPPRSDHaAACHADRYLLIFGGGSHAT--CFNDLHVLDLQT 379
Cdd:pfam13854   1 PVPRYGH-CAVTVGDYIYLYGGYTGGEgqPSDDVYVLSLPT 40
Kelch_6 pfam13964
Kelch motif;
296-341 5.68e-04

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 38.09  E-value: 5.68e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2468055594 296 GQSVTLVGTTLVLFGGEDAKRCLLNDLHILDLETMTWDDVDAIGTP 341
Cdd:pfam13964   4 FHSVVSVGGYIYVFGGYTNASPALNKLEVYNPLTKSWEELPPLPTP 49
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 514-639 5.71e-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: 42.83  E-value: 5.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 514 KIREIAMDSADSDLKKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAA------ 587
Cdd:COG4942    35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllraly 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468055594 588 EQSRCFKLEV--------------------------DVAELRQKLQSMDALEREVELLRRQKAASEQAALEAKQRQSS 639
Cdd:COG4942   115 RLGRQPPLALllspedfldavrrlqylkylaparreQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 540-621 6.57e-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: 41.83  E-value: 6.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 540 KAEKEELEAALNREQvqtiqLKEEIAEAEARNAELTKELQTVRGQLAAEQSrcfKLEVDVAELRQKLqsmDALEREV--E 617
Cdd:COG1579   107 DLEDEILELMERIEE-----LEEELAELEAELAELEAELEEKKAELDEELA---ELEAELEELEAER---EELAAKIppE 175


                  ....
gi 2468055594 618 LLRR 621
Cdd:COG1579   176 LLAL 179
KASH_CCD pfam14662
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ...
 544-640 7.32e-04

Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.


Pssm-ID: 405365 [Multi-domain]  Cd Length: 191  Bit Score: 41.32  E-value: 7.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 544 EELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRCFK---LEVDVAELRQKLQSMD-----ALERE 615
Cdd:pfam14662  11 EDLQANNQKLLQENSKLKATVETREETNAKLLEENLNLRKQAKSQQQAVQKeklLEEELEDLKLIVNSLEearrsLLAQN 90

                          90       100
                  ....*....|....*....|....*.
gi 2468055594 616 VELLR-RQKAASEQAALEAKQRQSSS 640
Cdd:pfam14662  91 KQLEKeNQSLLQEIESLQEENKKNQA 116
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 394-437 7.47e-04

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 37.59  E-value: 7.47e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2468055594 394 PRAGHAGATVGENWYIVGGGNNKSGVSETLVLNMSTLTWSVVSS 437
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSKLPS 44
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 539-636 7.73e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 42.65  E-value: 7.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  539 LKAEKEELEAALNREQvQTIQLKEEIAEAEARNAELTK-----ELQTVRGQLAAEQSRCFKLEVDVAELRQKLQSMDAlE 613
Cdd:TIGR00618  245 LTQKREAQEEQLKKQQ-LLKQLRARIEELRAQEAVLEEtqeriNRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMR-S 322

                           90       100
                   ....*....|....*....|...
gi 2468055594  614 REVELLRRQKAASEQAALEAKQR 636
Cdd:TIGR00618  323 RAKLLMKRAAHVKQQSSIEEQRR 345
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 543-637 7.85e-04

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 42.63  E-value: 7.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 543 KEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQ--------LAAEQSRCFKLEVDVAELRQKLQSMDALER 614
Cdd:pfam15709 397 EEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKkqqeeaerAEAEKQRQKELEMQLAEEQKRLMEMAEEER 476

                          90       100
                  ....*....|....*....|...
gi 2468055594 615 eVELLRRQKAASEQAALEAKQRQ 637
Cdd:pfam15709 477 -LEYQRQKQEAEEKARLEAEERR 498
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
 514-637 8.30e-04

flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.


Pssm-ID: 131526 [Multi-domain]  Cd Length: 141  Bit Score: 39.99  E-value: 8.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 514 KIREIAMDSADSDLKK-----DDANELLVALKAEKEELEAALNREQVQTIQlkeeIAEAEARNAELTKeLQTVRGQLAAE 588
Cdd:TIGR02473   9 DLREKEEEQAKLELAKaqaefERLETQLQQLIKYREEYEQQALEKVGAGTS----ALELSNYQRFIRQ-LDQRIQQQQQE 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2468055594 589 QSRcfkLEVDVAELRQKLQSMDALEREVELLRrQKAASEQAALEAKQRQ 637
Cdd:TIGR02473  84 LAL---LQQEVEAKRERLLEARRELKALEKLK-EKKQKEYRAEEAKREQ 128
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 495-639 8.53e-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: 42.74  E-value: 8.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  495 ASDGTSSVLEPEVElshdgkIREIAMDSADSDLKKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAEL 574
Cdd:TIGR02168  665 SAKTNSSILERRRE------IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468055594  575 TKELQTVRGQLAAEQSRCFKLEVDVAELRQKLQS----MDALEREVELLRRQKAASEQAALEAKQRQSS 639
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeeLAEAEAEIEELEAQIEQLKEELKALREALDE 807
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
482-634 1.00e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 482 TLKSDLQSKTKEHASDGTSSVLEPEVELSHDGKI--REIAMDSADSDLKkddanELLVALKAEKEELEAALnreqvqtiq 559
Cdd:PRK03918  567 ELEEELAELLKELEELGFESVEELEERLKELEPFynEYLELKDAEKELE-----REEKELKKLEEELDKAF--------- 632

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 560 lkEEIAEAEARNAELTKELQTVRGQLAAEQ-----SRCFKLEVDVAELRQKLQSM----DALEREVELLRRQKAASEQAA 630
Cdd:PRK03918  633 --EELAETEKRLEELRKELEELEKKYSEEEyeelrEEYLELSRELAGLRAELEELekrrEEIKKTLEKLKEELEEREKAK 710


                  ....
gi 2468055594 631 LEAK 634
Cdd:PRK03918  711 KELE 714
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 528-637 1.44e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.44  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 528 KKDDANELlvALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRcfklEVDVAELRQKLQ 607
Cdd:pfam13868 217 RKERQKER--EEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQ----EEAEKRRMKRLE 290

                          90       100       110
                  ....*....|....*....|....*....|
gi 2468055594 608 SMDALEREVELLRRQKAASEQAALEAKQRQ 637
Cdd:pfam13868 291 HRRELEKQIEEREEQRAAEREEELEEGERL 320
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 503-635 1.56e-03

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: 41.98  E-value: 1.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  503 LEPEVElSHDGKIREiaMDSADSDLKKD--DANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELqt 580
Cdd:TIGR02169  866 LEEELE-ELEAALRD--LESRLGDLKKErdELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK-- 940

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2468055594  581 vrGQLAAEQSRCFKLEVDVAELRQKLQSMDALErEVELLRRQKAASEQAA---LEAKQ 635
Cdd:TIGR02169  941 --GEDEEIPEEELSLEDVQAELQRVEEEIRALE-PVNMLAIQEYEEVLKRldeLKEKR 995
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 552-636 1.58e-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: 40.27  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 552 REQVQTIQ-LKEEIAEAEARNAELTKELQtvrgQLAAEQSRCF----KLEVDVAELRQKL-------QSMDALEREVELL 619
Cdd:pfam13851  22 RNNLELIKsLKEEIAELKKKEERNEKLMS----EIQQENKRLTeplqKAQEEVEELRKQLenyekdkQSLKNLKARLKVL 97

                          90
                  ....*....|....*..
gi 2468055594 620 RRQKAASEQAALEAKQR 636
Cdd:pfam13851  98 EKELKDLKWEHEVLEQR 114
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 526-636 1.68e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 526 DLKKddANELLVALKAEKEELEAALNREQVQT-IQLKEEIAEAEARNAELTKELQTvrgQLAAEqsrcfkLEVDVAE-LR 603
Cdd:pfam13868 236 ELQQ--AREEQIELKERRLAEEAEREEEEFERmLRKQAEDEEIEQEEAEKRRMKRL---EHRRE------LEKQIEErEE 304

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2468055594 604 QKLQSMDALEREVELLRRQKAASEQAALEAKQR 636
Cdd:pfam13868 305 QRAAEREEELEEGERLREEEAERRERIEEERQK 337
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 516-587 1.73e-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: 40.68  E-value: 1.73e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468055594 516 REIAMDSADSDLKKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAA 587
Cdd:COG1579    96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 515-590 1.89e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 1.89e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468055594 515 IREIAMDSADSDLKKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQS 590
Cdd:COG3883   142 KAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
538-637 1.90e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 538 ALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAE--QSRCFKLEVDVAELRQKLQSmdaLERE 615
Cdd:COG4717   364 QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELlgELEELLEALDEEELEEELEE---LEEE 440

                          90       100
                  ....*....|....*....|....
gi 2468055594 616 VELL--RRQKAASEQAALEAKQRQ 637
Cdd:COG4717   441 LEELeeELEELREELAELEAELEQ 464
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 343-384 1.94e-03

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 36.44  E-value: 1.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2468055594 343 PRSDHAAACHaDRYLLIFGGGSHATCFNDLHVLDLQTMEWSR 384
Cdd:pfam01344   1 RRSGAGVVVV-GGKIYVIGGFDGNQSLNSVEVYDPETNTWSK 41
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 512-636 2.49e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.31  E-value: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  512 DGKIREIAMDSADSDLKKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSR 591
Cdd:pfam01576  411 EGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTR 490

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2468055594  592 CFKLEVDVAELRQKLQ----SMDALEREVELLRRQ----------KAASEQAALEAKQR 636
Cdd:pfam01576  491 LRQLEDERNSLQEQLEeeeeAKRNVERQLSTLQAQlsdmkkkleeDAGTLEALEEGKKR 549
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
540-637 2.63e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 40.63  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 540 KAEKEELEAALNREQ-VQTIQlkeeIAEAEARNAEL--TKELQTVRGQLAAEQsrcfklEVDVAELRQKLQsmdaLEREV 616
Cdd:COG2268   218 QANREAEEAELEQEReIETAR----IAEAEAELAKKkaEERREAETARAEAEA------AYEIAEANAERE----VQRQL 283

                          90       100
                  ....*....|....*....|...
gi 2468055594 617 ELLRRQK--AASEQAALEAKQRQ 637
Cdd:COG2268   284 EIAEREReiELQEKEAEREEAEL 306
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
515-621 2.74e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.00  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 515 IREIAMDSADSDLKKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELtkelqtvRGQLAAEQSRCFK 594
Cdd:COG2433   373 IRGLSIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEEL-------EAELEEKDERIER 445

                          90       100
                  ....*....|....*....|....*..
gi 2468055594 595 LEVDVAELRQKLQSMDALEREVELLRR 621
Cdd:COG2433   446 LERELSEARSEERREIRKDREISRLDR 472
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 503-623 2.89e-03

Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.


Pssm-ID: 463102 [Multi-domain]  Cd Length: 140  Bit Score: 38.43  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 503 LEPEVELShdGKIREIAMdsadsdLKKDDANELLVALKAEKEELEAALNREQVQTIQLKEEiaeaearNAELTKELQTVR 582
Cdd:pfam10473  29 LERELEMS--EENQELAI------LEAENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSE-------KENLTKELQKKQ 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2468055594 583 GQLAAEQSRCFKLEVDVAELRQ-KLQSMDALEREVELLRRQK 623
Cdd:pfam10473  94 ERVSELESLNSSLENLLEEKEQeKVQMKEESKTAVEMLQTQL 135
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 512-639 2.98e-03

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: 40.82  E-value: 2.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  512 DGKIREIAMDSADSDLKKDDANELLVALKAEKEELEAALNRE------QVQT--IQLKEEIAEAEARNAELTKELQTVRG 583
Cdd:TIGR02169  243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlRVKEkiGELEAEIASLERSIAEKERELEDAEE 322

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468055594  584 QLAAEQSRCFKLEVDVAELRQKLQS-----------MDALEREVELLRRQKAASEQAALEAKQRQSS 639
Cdd:TIGR02169  323 RLAKLEAEIDKLLAEIEELEREIEEerkrrdklteeYAELKEELEDLRAELEEVDKEFAETRDELKD 389
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 514-610 3.29e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 3.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 514 KIREIAMDSADSDLKKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAaeqsrcf 593
Cdd:COG4942   158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA------- 230

                          90
                  ....*....|....*..
gi 2468055594 594 KLEVDVAELRQKLQSMD 610
Cdd:COG4942   231 RLEAEAAAAAERTPAAG 247
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 542-635 3.29e-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: 40.72  E-value: 3.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  542 EKEELEAALNREQVQTIQLKEEIAEAEARNAELTKE-LQTVRGQLAAEQSRCFKLEVDVAELRQKLQSMDALEREVELLR 620
Cdd:TIGR00618  638 SQELALKLTALHALQLTLTQERVREHALSIRVLPKElLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYD 717

                           90
                   ....*....|....*
gi 2468055594  621 RQKAASEQAALEAKQ 635
Cdd:TIGR00618  718 REFNEIENASSSLGS 732
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 514-637 3.44e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 40.29  E-value: 3.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 514 KIREIAMdSADSDLKKDDANELLVALKAEKEELEAALNREQVQtiQLKEEIAEAEARNAELTKELQTVRGQLAA-EQSRC 592
Cdd:pfam13868  14 KLLAAKC-NKERDAQIAEKKRIKAEEKEEERRLDEMMEEERER--ALEEEEEKEEERKEERKRYRQELEEQIEErEQKRQ 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2468055594 593 FKLEVDVAELRQKLQSMDALEREVELLRRQKAASEQAALEAKQRQ 637
Cdd:pfam13868  91 EEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEF 135
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 493-621 3.91e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.54  E-value: 3.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  493 EHASDGTSSVLEPEVELSHDGKIR---EIAMDSADSDLKKDDANELlvALKAEKEELEAALNREQVQTIQLKEEIAEAEA 569
Cdd:pfam01576  159 ERISEFTSNLAEEEEKAKSLSKLKnkhEAMISDLEERLKKEEKGRQ--ELEKAKRKLEGESTDLQEQIAELQAQIAELRA 236

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2468055594  570 RNAELTKELQTVRGQLAAE-------QSRCFKLEVDVAELRQKLQSMDALEREVELLRR 621
Cdd:pfam01576  237 QLAKKEEELQAALARLEEEtaqknnaLKKIRELEAQISELQEDLESERAARNKAEKQRR 295
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 482-644 3.92e-03

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: 40.44  E-value: 3.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  482 TLKSDLQSKTKEHAS--DGTSSVlepEVELshDGKIREIAMDSADSDLKKDDANEL---LVALKAEKEELEAALNREQVQ 556
Cdd:TIGR02169  368 DLRAELEEVDKEFAEtrDELKDY---REKL--EKLKREINELKRELDRLQEELQRLseeLADLNAAIAGIEAKINELEEE 442

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  557 TIQLKEEIAEAEarnaeltKELQTVRGQLAAEQSrcfklevdvaELRQKLQSMDALEREVEllrrqKAASEQAALEAKQR 636
Cdd:TIGR02169  443 KEDKALEIKKQE-------WKLEQLAADLSKYEQ----------ELYDLKEEYDRVEKELS-----KLQRELAEAEAQAR 500


                   ....*...
gi 2468055594  637 QSSSGMWG 644
Cdd:TIGR02169  501 ASEERVRG 508
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 528-604 4.43e-03

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 37.55  E-value: 4.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 528 KKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEAR--------------NAELTKELQTVRGQLAAEQSRCF 593
Cdd:pfam13863  18 KREEIERLEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKrrralkkaeeetklKKEKEKEIKKLTAQIEELKSEIS 97

                          90
                  ....*....|.
gi 2468055594 594 KLEVDVAELRQ 604
Cdd:pfam13863  98 KLEEKLEEYKP 108
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 524-637 4.66e-03

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 39.83  E-value: 4.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 524 DSDLKKDDANELLVALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRCFKLEVDVAELR 603
Cdd:TIGR02794  44 DPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEE 123

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2468055594 604 QKLQsmdaleREVELLRRQKAASEQAALEAKQRQ 637
Cdd:TIGR02794 124 AKAK------QAAEAKAKAEAEAERKAKEEAAKQ 151
Filament pfam00038
Intermediate filament protein;
520-636 4.85e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 39.52  E-value: 4.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 520 MDSAdsdlKKDDANELLVALKAEKEELeAALNREQV-QTIQLK-EEIAEAEARNAEltkELQTVRgqlaaeqsrcfkleV 597
Cdd:pfam00038 160 MDAA----RKLDLTSALAEIRAQYEEI-AAKNREEAeEWYQSKlEELQQAAARNGD---ALRSAK--------------E 217

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2468055594 598 DVAELRQKLQSmdaLEREVELLRRQKAASEQAALEAKQR 636
Cdd:pfam00038 218 EITELRRTIQS---LEIELQSLKKQKASLERQLAETEER 253
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
 561-639 5.47e-03

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


Pssm-ID: 465814 [Multi-domain]  Cd Length: 117  Bit Score: 37.18  E-value: 5.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 561 KEEIAEAEARNAELT----------KELQTVRGQL---AAEQSRCFKLEVDVAELRQKLQSMDA----LEREVELLRRQ- 622
Cdd:pfam18595   8 KEELAELERKARELQakidalqvveKDLRSCIKLLeeiEAELAKLEEAKKKLKELRDALEEKEIelreLERREERLQRQl 87

                          90
                  ....*....|....*..
gi 2468055594 623 KAASEQaaLEAKQRQSS 639
Cdd:pfam18595  88 ENAQEK--LERLREQAE 102
Kelch_3 pfam13415
Galactose oxidase, central domain;
193-229 5.74e-03

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 35.34  E-value: 5.74e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2468055594 193 DKMYIFGGNH--NGRYLSDLQALDLKSLTWSKIDAKFQA 229
Cdd:pfam13415   2 DKLYIFGGLGfdGQTRLNDLYVYDLDTNTWTQIGDLPPP 40
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 538-637 5.97e-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: 39.67  E-value: 5.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 538 ALKAEKEELEAALNREQVQTIQLKEEIAEAEARNAELTK---ELQTVRGQ---LAAEQSRCFKLEVDVAELRQKLQSMDA 611
Cdd:pfam05622  70 QLQEENFRLETARDDYRIKCEELEKEVLELQHRNEELTSlaeEAQALKDEmdiLRESSDKVKKLEATVETYKKKLEDLGD 149

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2468055594 612 LEREVELLRR----------------QKAASEQAALEAKQRQ 637
Cdd:pfam05622 150 LRRQVKLLEErnaeymqrtlqleeelKKANALRGQLETYKRQ 191
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 471-603 7.30e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 7.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594  471 RYSNEVFALKLTLKSdLQSKTKEHASDGTSSvlepevELSHDGKIREI-AMDSADSDLKKDDANELLVALKAEKEELEAA 549
Cdd:TIGR02168  383 TLRSKVAQLELQIAS-LNNEIERLEARLERL------EDRRERLQQEIeELLKKLEEAELKELQAELEELEEELEELQEE 455

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2468055594  550 LNREQVQTIQLKEEIAEAEArnaeltkELQTVRGQLAAEQSRCFKLEVDVAELR 603
Cdd:TIGR02168  456 LERLEEALEELREELEEAEQ-------ALDAAERELAQLQARLDSLERLQENLE 502
Filament pfam00038
Intermediate filament protein;
540-635 8.01e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 38.75  E-value: 8.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 540 KAEKEELEAALNREQVQTIqlKEEIAEAEARNAELTKELQTVRGQLAAeqsrcfkLEVDVAELRQKlqsmdaLEREVELL 619
Cdd:pfam00038 197 KLEELQQAAARNGDALRSA--KEEITELRRTIQSLEIELQSLKKQKAS-------LERQLAETEER------YELQLADY 261

                          90
                  ....*....|....*.
gi 2468055594 620 RRQKAASEQAALEAKQ 635
Cdd:pfam00038 262 QELISELEAELQETRQ 277
HAUS-augmin3 pfam14932
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found ...
 531-629 9.95e-03

HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found from Drosophila to humans. The HAUS-augmin complex is made up of eight subunits. The augmin complex interacts with gamma-TuRC, and attenuation of this interaction severely impairs spindle MT generation. Furthermore, we provide evidence that human augmin plays critical and non-redundant roles in the kinetochore-MT attachment and also central spindle formation during anaphase in human cells.The HAUS complex is required for mitotic spindle assembly and for maintenance of centrosome integrity.


Pssm-ID: 464384 [Multi-domain]  Cd Length: 261  Bit Score: 38.45  E-value: 9.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468055594 531 DANELLVALKAEKEELEAALNREQVQtiQLKEEIAEAEARNAELTKELQTVRGQLAAEQSRCFKLEVDVAELRQKLQSMD 610
Cdd:pfam14932  45 EGAALDEALKTISAESPGLLNQQDVE--ALEESLEEIREATEDLEAELQELQKTKQLKINRLNKLQAQASSLSQGLRALV 122

                          90       100
                  ....*....|....*....|....
gi 2468055594 611 ALEREV-----ELLRRQKAASEQA 629
Cdd:pfam14932 123 AEEEEAakqleELQEELAALNAKT 146
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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