NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|42563520|ref|NP_187193|]
View 

acyl-CoA binding protein 4 [Arabidopsis thaliana]

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];
181-425 1.43e-28

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


:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 115.64  E-value: 1.43e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 181 PKARYEHGAAVIQDKMYIYGGNHNGRYLGDLHVLDLKSWTWSRVetkvatesqeTSTPTllAPCAGHSLIAWDNKLLSIG 260
Cdd:COG3055  10 PTPRSEAAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTWSEL----------APLPG--PPRHHAAAVAQDGKLYVFG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 261 GHTKDPSESMQVK---VFDPHTITWSMLktyGKPPVSRGGQSVTMVGKTLVIFGGQDAKRSLlNDLHILDLDTMTWDEID 337
Cdd:COG3055  78 GFTGANPSSTPLNdvyVYDPATNTWTKL---APMPTPRGGATALLLDGKIYVVGGWDDGGNV-AWVEVYDPATGTWTQLA 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 338 AVgvsPSPRSDHAAAVHAERFLLIFGG------------------------------------GSHATcFDDLHVLDLQT 381
Cdd:COG3055 154 PL---PTPRDHLAAAVLPDGKILVIGGrngsgfsntwttlaplptaraghaaavlggkilvfgGESGF-SDEVEAYDPAT 229

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 42563520 382 MEWSrpaQQGDAPTPRAGHAGVTIGENWFIVGGGDNKSGASESV 425
Cdd:COG3055 230 NTWT---ALGELPTPRHGHAAVLTDGKVYVIGGETKPGVRTPLV 270
ACBP pfam00887
Acyl CoA binding protein;
14-97 6.28e-23

Acyl CoA binding protein;


:

Pssm-ID: 459982  Cd Length: 76  Bit Score: 92.66  E-value: 6.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520    14 ERFYAAASYVgldgsdssaKNVISKFPDDTALLLYALYQQATVGPCNTPKPSAWRPVEQSKWKSWQGLGTMPSIEAMRLF 93
Cdd:pfam00887   2 EKFEAAAEFV---------KKLKSKPSNEEKLELYGLYKQATVGDCNTPRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKY 72


                  ....
gi 42563520    94 VKIL 97
Cdd:pfam00887  73 VELV 76
Crescentin super family cl41192
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 551-646 1.89e-08

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


The actual alignment was detected with superfamily member pfam19220:

Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 57.00  E-value: 1.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520   551 KSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELR----QKLQTLETLQKE 626
Cdd:pfam19220  47 KSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRielrDKTAQAEALERQ 126

                          90       100
                  ....*....|....*....|....*...
gi 42563520   627 L--------ELLQRQKAASEQAAMNAKR 646
Cdd:pfam19220 127 LaaeteqnrALEEENKALREEAQAAEKA 154
NanM super family cl34543
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
391-480 2.32e-05

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


The actual alignment was detected with superfamily member COG3055:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 46.69  E-value: 2.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 391 GDAPTPRAGHAGVTIGENWFIVGGGDNKSGASESVVLNMSTLAWSVVASvqgrVPLASEGLSLVVsSYNGEdVLVaFGGY 470
Cdd:COG3055   7 PDLPTPRSEAAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTWSELAP----LPGPPRHHAAAV-AQDGK-LYV-FGGF 79

                        90
                ....*....|
gi 42563520 471 NGRYNNEINL 480
Cdd:COG3055  80 TGANPSSTPL 89
 
Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
181-425 1.43e-28

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 115.64  E-value: 1.43e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 181 PKARYEHGAAVIQDKMYIYGGNHNGRYLGDLHVLDLKSWTWSRVetkvatesqeTSTPTllAPCAGHSLIAWDNKLLSIG 260
Cdd:COG3055  10 PTPRSEAAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTWSEL----------APLPG--PPRHHAAAVAQDGKLYVFG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 261 GHTKDPSESMQVK---VFDPHTITWSMLktyGKPPVSRGGQSVTMVGKTLVIFGGQDAKRSLlNDLHILDLDTMTWDEID 337
Cdd:COG3055  78 GFTGANPSSTPLNdvyVYDPATNTWTKL---APMPTPRGGATALLLDGKIYVVGGWDDGGNV-AWVEVYDPATGTWTQLA 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 338 AVgvsPSPRSDHAAAVHAERFLLIFGG------------------------------------GSHATcFDDLHVLDLQT 381
Cdd:COG3055 154 PL---PTPRDHLAAAVLPDGKILVIGGrngsgfsntwttlaplptaraghaaavlggkilvfgGESGF-SDEVEAYDPAT 229

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 42563520 382 MEWSrpaQQGDAPTPRAGHAGVTIGENWFIVGGGDNKSGASESV 425
Cdd:COG3055 230 NTWT---ALGELPTPRHGHAAVLTDGKVYVIGGETKPGVRTPLV 270
ACBP pfam00887
Acyl CoA binding protein;
14-97 6.28e-23

Acyl CoA binding protein;


Pssm-ID: 459982  Cd Length: 76  Bit Score: 92.66  E-value: 6.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520    14 ERFYAAASYVgldgsdssaKNVISKFPDDTALLLYALYQQATVGPCNTPKPSAWRPVEQSKWKSWQGLGTMPSIEAMRLF 93
Cdd:pfam00887   2 EKFEAAAEFV---------KKLKSKPSNEEKLELYGLYKQATVGDCNTPRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKY 72


                  ....
gi 42563520    94 VKIL 97
Cdd:pfam00887  73 VELV 76
ACBP cd00435
Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a ...
 14-99 2.62e-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: 80.06  E-value: 2.62e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  14 ERFYAAASYVgldgsdssaKNVISKFPDDTALLLYALYQQATVGPCNTPKPSAWRPVEQSKWKSWQGLGTMPSIEAMRLF 93
Cdd:cd00435   3 EEFEAAAEKV---------KKLKTKPSNEEKLQLYSLYKQATVGDCNTERPGMFDLKGRAKWDAWNSLKGMSKEDAMKAY 73


                ....*.
gi 42563520  94 VKILEE 99
Cdd:cd00435  74 IAKVEE 79
PLN02153 PLN02153
epithiospecifier protein
 170-415 6.84e-13

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 70.40  E-value: 6.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  170 QW-TAPQTSGQRPKARYEHGAAVIQDKMYIYGGN--HNGRYLGDLHVLDLKSWTWS-------------------RVETK 227
Cdd:PLN02153   8 GWiKVEQKGGKGPGPRCSHGIAVVGDKLYSFGGElkPNEHIDKDLYVFDFNTHTWSiapangdvprisclgvrmvAVGTK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  228 VA------------------TESQETSTPTLLAPCAG------HSLIAWDNKL-----LSIGGHTKDPSESMQVKVFDPH 278
Cdd:PLN02153  88 LYifggrdekrefsdfysydTVKNEWTFLTKLDEEGGpeartfHSMASDENHVyvfggVSKGGLMKTPERFRTIEAYNIA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  279 TITWSMLKTYGKPPVSRGGQSVTMV-GKTLVIFG--------GQDAKRSllNDLHILDLDTMTWDEIDAVGVSPSPRSDH 349
Cdd:PLN02153 168 DGKWVQLPDPGENFEKRGGAGFAVVqGKIWVVYGfatsilpgGKSDYES--NAVQFFDPASGKWTEVETTGAKPSARSVF 245

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42563520  350 AAAVhAERFLLIFGG------GSH---ATCFDDLHVLDLQTMEWSRPAQQGDAPTPRAGHAGVTI---GENWFIVGGG 415
Cdd:PLN02153 246 AHAV-VGKYIIIFGGevwpdlKGHlgpGTLSNEGYALDTETLVWEKLGECGEPAMPRGWTAYTTAtvyGKNGLLMHGG 322
ACB COG4281
Acyl-CoA-binding protein [Lipid transport and metabolism];
14-99 7.33e-11

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


Pssm-ID: 443422  Cd Length: 87  Bit Score: 58.71  E-value: 7.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  14 ERFYAAASYVgldgsdssaKNVISKFPDDTALLLYALYQQATVGPCNTPKPSAWRPVEQSKWKSWQGLGTMPSIEAMRLF 93
Cdd:COG4281   6 AAFEAAVARV---------KTLTERPDNDTLLKLYALYKQATEGDVTGKRPGMTDFVGRAKYDAWAQLKGMSKDEAMQQY 76


                ....*.
gi 42563520  94 VKILEE 99
Cdd:COG4281  77 IDLVNS 82
PTZ00458 PTZ00458
acyl CoA binding protein; Provisional
 40-104 5.84e-09

acyl CoA binding protein; Provisional


Pssm-ID: 185637  Cd Length: 90  Bit Score: 53.67  E-value: 5.84e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42563520   40 PDDTALLLYALYQQATVGPCNTPKPSAWRPVEQSKWKSWQGLGTMPSIEAMRLFVKILEEDDPGW 104
Cdd:PTZ00458  22 SVEIKLDLYKYYKQSTVGNCNIKEPSMFKYQDRKKYEAWKSIENLNREDAKKRYVEIVTELFPNW 86
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 551-646 1.89e-08

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 57.00  E-value: 1.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520   551 KSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELR----QKLQTLETLQKE 626
Cdd:pfam19220  47 KSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRielrDKTAQAEALERQ 126

                          90       100
                  ....*....|....*....|....*...
gi 42563520   627 L--------ELLQRQKAASEQAAMNAKR 646
Cdd:pfam19220 127 LaaeteqnrALEEENKALREEAQAAEKA 154
Kelch_3 pfam13415
Galactose oxidase, central domain;
304-354 6.30e-08

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 49.21  E-value: 6.30e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 42563520   304 GKTLVIFGGQDAKRS-LLNDLHILDLDTMTWDEIdavGVSPSPRSDHAAAVH 354
Cdd:pfam13415   1 GDKLYIFGGLGFDGQtRLNDLYVYDLDTNTWTQI---GDLPPPRSGHSATYI 49
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
484-647 4.60e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.23  E-value: 4.60e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 484 SHKSTLQtKTLEAPLPGSLSAvnnattrdiESEVEVSQEGRVREIVMDNVNPGS---KVEGNSERIIATIKSEKEELEAS 560
Cdd:COG4717  34 AGKSTLL-AFIRAMLLERLEK---------EADELFKPQGRKPELNLKELKELEeelKEAEEKEEEYAELQEELEELEEE 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 561 LN--KERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLETLQKELELLQRQKAASE 638
Cdd:COG4717 104 LEelEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELL 183


                ....*....
gi 42563520 639 QAAMNAKRQ 647
Cdd:COG4717 184 EQLSLATEE 192
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
391-480 2.32e-05

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 46.69  E-value: 2.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 391 GDAPTPRAGHAGVTIGENWFIVGGGDNKSGASESVVLNMSTLAWSVVASvqgrVPLASEGLSLVVsSYNGEdVLVaFGGY 470
Cdd:COG3055   7 PDLPTPRSEAAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTWSELAP----LPGPPRHHAAAV-AQDGK-LYV-FGGF 79

                        90
                ....*....|
gi 42563520 471 NGRYNNEINL 480
Cdd:COG3055  80 TGANPSSTPL 89
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
538-631 1.39e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  538 KVEGNSERIIATIKSEKEELEASLNKERMQTLQLRQELGEA--------ELRN--TDLYKELQSVRGQLAAEQSRCFKLE 607
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLekevkeleELKEeiEELEKELESLEGSKRKLEEKIRELE 265

                         90       100
                 ....*....|....*....|....
gi 42563520  608 VDVAELRQKLQTLETLQKELELLQ 631
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELK 289
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 544-649 1.99e-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: 44.66  E-value: 1.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520    544 ERIIATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSvrgqLAAEQSRcfkLEVDVAELRQKLQTLETL 623
Cdd:TIGR02168  245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA----LANEISR---LEQQKQILRERLANLERQ 317

                           90       100       110
                   ....*....|....*....|....*....|.
gi 42563520    624 QKELE-----LLQRQKAASEQAAMNAKRQGS 649
Cdd:TIGR02168  318 LEELEaqleeLESKLDELAEELAELEEKLEE 348
 
Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
181-425 1.43e-28

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 115.64  E-value: 1.43e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 181 PKARYEHGAAVIQDKMYIYGGNHNGRYLGDLHVLDLKSWTWSRVetkvatesqeTSTPTllAPCAGHSLIAWDNKLLSIG 260
Cdd:COG3055  10 PTPRSEAAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTWSEL----------APLPG--PPRHHAAAVAQDGKLYVFG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 261 GHTKDPSESMQVK---VFDPHTITWSMLktyGKPPVSRGGQSVTMVGKTLVIFGGQDAKRSLlNDLHILDLDTMTWDEID 337
Cdd:COG3055  78 GFTGANPSSTPLNdvyVYDPATNTWTKL---APMPTPRGGATALLLDGKIYVVGGWDDGGNV-AWVEVYDPATGTWTQLA 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 338 AVgvsPSPRSDHAAAVHAERFLLIFGG------------------------------------GSHATcFDDLHVLDLQT 381
Cdd:COG3055 154 PL---PTPRDHLAAAVLPDGKILVIGGrngsgfsntwttlaplptaraghaaavlggkilvfgGESGF-SDEVEAYDPAT 229

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 42563520 382 MEWSrpaQQGDAPTPRAGHAGVTIGENWFIVGGGDNKSGASESV 425
Cdd:COG3055 230 NTWT---ALGELPTPRHGHAAVLTDGKVYVIGGETKPGVRTPLV 270
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
235-476 7.83e-26

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 107.55  E-value: 7.83e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 235 TSTPTLLAPCAGHSLIAWDNKLLSIGGHTKDpSESMQVKVFDPHTITWSMLKTYgkpPVSRGGQSVTMV--GKTLVI--F 310
Cdd:COG3055   4 SSLPDLPTPRSEAAAALLDGKVYVAGGLSGG-SASNSFEVYDPATNTWSELAPL---PGPPRHHAAAVAqdGKLYVFggF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 311 GGQDAKRSLLNDLHILDLDTMTWDEIdavGVSPSPRSDHAAAVHAERfLLIFGGGSHATCFDDLHVLDLQTMEWSrpaQQ 390
Cdd:COG3055  80 TGANPSSTPLNDVYVYDPATNTWTKL---APMPTPRGGATALLLDGK-IYVVGGWDDGGNVAWVEVYDPATGTWT---QL 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 391 GDAPTPRAGHAGVTIGENWFIVGGGDNKSGASEsvvlnmstlAWSVVAsvqgrvPLASEGLSLVVSSYNGEdvLVAFGGY 470
Cdd:COG3055 153 APLPTPRDHLAAAVLPDGKILVIGGRNGSGFSN---------TWTTLA------PLPTARAGHAAAVLGGK--ILVFGGE 215


                ....*.
gi 42563520 471 NGRYNN 476
Cdd:COG3055 216 SGFSDE 221
ACBP pfam00887
Acyl CoA binding protein;
14-97 6.28e-23

Acyl CoA binding protein;


Pssm-ID: 459982  Cd Length: 76  Bit Score: 92.66  E-value: 6.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520    14 ERFYAAASYVgldgsdssaKNVISKFPDDTALLLYALYQQATVGPCNTPKPSAWRPVEQSKWKSWQGLGTMPSIEAMRLF 93
Cdd:pfam00887   2 EKFEAAAEFV---------KKLKSKPSNEEKLELYGLYKQATVGDCNTPRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKY 72


                  ....
gi 42563520    94 VKIL 97
Cdd:pfam00887  73 VELV 76
ACBP cd00435
Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a ...
 14-99 2.62e-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: 80.06  E-value: 2.62e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  14 ERFYAAASYVgldgsdssaKNVISKFPDDTALLLYALYQQATVGPCNTPKPSAWRPVEQSKWKSWQGLGTMPSIEAMRLF 93
Cdd:cd00435   3 EEFEAAAEKV---------KKLKTKPSNEEKLQLYSLYKQATVGDCNTERPGMFDLKGRAKWDAWNSLKGMSKEDAMKAY 73


                ....*.
gi 42563520  94 VKILEE 99
Cdd:cd00435  74 IAKVEE 79
PLN02153 PLN02153
epithiospecifier protein
 170-415 6.84e-13

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 70.40  E-value: 6.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  170 QW-TAPQTSGQRPKARYEHGAAVIQDKMYIYGGN--HNGRYLGDLHVLDLKSWTWS-------------------RVETK 227
Cdd:PLN02153   8 GWiKVEQKGGKGPGPRCSHGIAVVGDKLYSFGGElkPNEHIDKDLYVFDFNTHTWSiapangdvprisclgvrmvAVGTK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  228 VA------------------TESQETSTPTLLAPCAG------HSLIAWDNKL-----LSIGGHTKDPSESMQVKVFDPH 278
Cdd:PLN02153  88 LYifggrdekrefsdfysydTVKNEWTFLTKLDEEGGpeartfHSMASDENHVyvfggVSKGGLMKTPERFRTIEAYNIA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  279 TITWSMLKTYGKPPVSRGGQSVTMV-GKTLVIFG--------GQDAKRSllNDLHILDLDTMTWDEIDAVGVSPSPRSDH 349
Cdd:PLN02153 168 DGKWVQLPDPGENFEKRGGAGFAVVqGKIWVVYGfatsilpgGKSDYES--NAVQFFDPASGKWTEVETTGAKPSARSVF 245

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42563520  350 AAAVhAERFLLIFGG------GSH---ATCFDDLHVLDLQTMEWSRPAQQGDAPTPRAGHAGVTI---GENWFIVGGG 415
Cdd:PLN02153 246 AHAV-VGKYIIIFGGevwpdlKGHlgpGTLSNEGYALDTETLVWEKLGECGEPAMPRGWTAYTTAtvyGKNGLLMHGG 322
PLN02193 PLN02193
nitrile-specifier protein
 162-415 1.61e-12

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 69.98  E-value: 1.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  162 SNTVSVYNQWTAPQTSGQRPKARYEHGAAVIQDKMYIYGGNHNGRYLGD--LHVLDLKSWTWS----------------- 222
Cdd:PLN02193 144 PSTPKLLGKWIKVEQKGEGPGLRCSHGIAQVGNKIYSFGGEFTPNQPIDkhLYVFDLETRTWSispatgdvphlsclgvr 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  223 -----------------------------RVETKVATESQETSTPTllapcAGHSLIAWDNKLLSIGGhtkdPSESMQVK 273
Cdd:PLN02193 224 mvsigstlyvfggrdasrqyngfysfdttTNEWKLLTPVEEGPTPR-----SFHSMAADEENVYVFGG----VSATARLK 294

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  274 VFDPHTI---TWSMLKTYGKPPVSRGGQSVTMV-GKTLVIFGGQDAKrslLNDLHILDLDTMTWDEIDAVGVSPSPRSDH 349
Cdd:PLN02193 295 TLDSYNIvdkKWFHCSTPGDSFSIRGGAGLEVVqGKVWVVYGFNGCE---VDDVHYYDPVQDKWTQVETFGVRPSERSVF 371

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  350 AAAVHAeRFLLIFGGG------SH---ATCFDDLHVLDLQTMEWSRPAQQG---DAPTPR---AGHAGVTIGENWFIVGG 414
Cdd:PLN02193 372 ASAAVG-KHIVIFGGEiamdplAHvgpGQLTDGTFALDTETLQWERLDKFGeeeETPSSRgwtASTTGTIDGKKGLVMHG 450


                 .
gi 42563520  415 G 415
Cdd:PLN02193 451 G 451
PHA03098 PHA03098
kelch-like protein; Provisional
 184-437 4.26e-11

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 65.94  E-value: 4.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  184 RYEHGAAVIQDKMYIYGG-NHNGRYLGDLHVLDLKSwtwsrvetkvateSQETSTPTLLAPCAGHSLIAWDNKLLSIGGH 262
Cdd:PHA03098 285 VYCFGSVVLNNVIYFIGGmNKNNLSVNSVVSYDTKT-------------KSWNKVPELIYPRKNPGVTVFNNRIYVIGGI 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  263 TKDPSESmQVKVFDPHTITWSMLKTYGKPpvsRGGQSVTMVGKTLVIFGGQDAKRSLLNDLHILDLDTMTWDEIDAvgvS 342
Cdd:PHA03098 352 YNSISLN-TVESWKPGESKWREEPPLIFP---RYNPCVVNVNNLIYVIGGISKNDELLKTVECFSLNTNKWSKGSP---L 424

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  343 PSPRSDHAAAVHAErFLLIFGGGSHAT---CFDDLHVLDLQTMEWSRPAQQGdapTPRaGHAGVTIGENWFIVGGGD-NK 418
Cdd:PHA03098 425 PISHYGGCAIYHDG-KIYVIGGISYIDnikVYNIVESYNPVTNKWTELSSLN---FPR-INASLCIFNNKIYVVGGDkYE 499

                        250
                 ....*....|....*....
gi 42563520  419 SGASESVVLNMSTLAWSVV 437
Cdd:PHA03098 500 YYINEIEVYDDKTNTWTLF 518
ACB COG4281
Acyl-CoA-binding protein [Lipid transport and metabolism];
14-99 7.33e-11

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


Pssm-ID: 443422  Cd Length: 87  Bit Score: 58.71  E-value: 7.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  14 ERFYAAASYVgldgsdssaKNVISKFPDDTALLLYALYQQATVGPCNTPKPSAWRPVEQSKWKSWQGLGTMPSIEAMRLF 93
Cdd:COG4281   6 AAFEAAVARV---------KTLTERPDNDTLLKLYALYKQATEGDVTGKRPGMTDFVGRAKYDAWAQLKGMSKDEAMQQY 76


                ....*.
gi 42563520  94 VKILEE 99
Cdd:COG4281  77 IDLVNS 82
PLN02153 PLN02153
epithiospecifier protein
 147-364 4.40e-10

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 61.93  E-value: 4.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  147 GRLAETQDKDVVSEDSntvsVYNQWTAPQTSGQR--PKARYEHGAAVIQDKMYIYGGNHNG---------RYLGDLHVLD 215
Cdd:PLN02153  93 GRDEKREFSDFYSYDT----VKNEWTFLTKLDEEggPEARTFHSMASDENHVYVFGGVSKGglmktperfRTIEAYNIAD 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  216 LKswtWsrVETKVATESQETSTPTLLAPCAGHSLIAWDNKLLSIGGhTKDPSESMQVKVFDPHTITWSMLKTYGKPPVSR 295
Cdd:PLN02153 169 GK---W--VQLPDPGENFEKRGGAGFAVVQGKIWVVYGFATSILPG-GKSDYESNAVQFFDPASGKWTEVETTGAKPSAR 242

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  296 GGQSVTMVGKTLVIFGGQ---DAKR-----SLLNDLHILDLDTMTWDEIDAVGVSPSPR---SDHAAAVHAERFLLIFGG 364
Cdd:PLN02153 243 SVFAHAVVGKYIIIFGGEvwpDLKGhlgpgTLSNEGYALDTETLVWEKLGECGEPAMPRgwtAYTTATVYGKNGLLMHGG 322
PLN02193 PLN02193
nitrile-specifier protein
 230-414 1.25e-09

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 61.12  E-value: 1.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  230 TESQETSTPTLLAPcaGHSLIAWDNKLLSIGGHTKDPSESMQVKVFDPHTI----TWSMLKTYGKPPVSRGGQSVTMVGK 305
Cdd:PLN02193  99 TYKGKTSHPIEKRP--GVKFVLQGGKIVGFHGRSTDVLHSLGAYISLPSTPkllgKWIKVEQKGEGPGLRCSHGIAQVGN 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  306 TLVIFGGQ-DAKRSLLNDLHILDLDTMTWDEIDAVGVSPSPRSDHAAAVHAERFLLIFGGGSHATCFDDLHVLDLQTMEW 384
Cdd:PLN02193 177 KIYSFGGEfTPNQPIDKHLYVFDLETRTWSISPATGDVPHLSCLGVRMVSIGSTLYVFGGRDASRQYNGFYSFDTTTNEW 256

                        170       180       190
                 ....*....|....*....|....*....|..
gi 42563520  385 S--RPAQQGdaPTPRAGHAGVTIGENWFIVGG 414
Cdd:PLN02193 257 KllTPVEEG--PTPRSFHSMAADEENVYVFGG 286
PTZ00458 PTZ00458
acyl CoA binding protein; Provisional
 40-104 5.84e-09

acyl CoA binding protein; Provisional


Pssm-ID: 185637  Cd Length: 90  Bit Score: 53.67  E-value: 5.84e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42563520   40 PDDTALLLYALYQQATVGPCNTPKPSAWRPVEQSKWKSWQGLGTMPSIEAMRLFVKILEEDDPGW 104
Cdd:PTZ00458  22 SVEIKLDLYKYYKQSTVGNCNIKEPSMFKYQDRKKYEAWKSIENLNREDAKKRYVEIVTELFPNW 86
PLN02193 PLN02193
nitrile-specifier protein
 141-374 9.22e-09

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 58.04  E-value: 9.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  141 TISTENGRLAETQDKDVVSEDSNTvsvyNQWTAPQTSGQRPKARYEHGAAVIQDKMYIYGGNHNGRYLGDLHVLDLKSWT 220
Cdd:PLN02193 230 TLYVFGGRDASRQYNGFYSFDTTT----NEWKLLTPVEEGPTPRSFHSMAADEENVYVFGGVSATARLKTLDSYNIVDKK 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  221 WSrvetkvatesqETSTP-TLLAPCAGHSLIAWDNKLLSIGGHtkDPSESMQVKVFDPHTITWSMLKTYGKPPVSRGGQS 299
Cdd:PLN02193 306 WF-----------HCSTPgDSFSIRGGAGLEVVQGKVWVVYGF--NGCEVDDVHYYDPVQDKWTQVETFGVRPSERSVFA 372

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  300 VTMVGKTLVIFGGQDAKR--------SLLNDLHILDLDTMTWDEIDAVGV---SPSPR---SDHAAAVHAERFLLIFGGG 365
Cdd:PLN02193 373 SAAVGKHIVIFGGEIAMDplahvgpgQLTDGTFALDTETLQWERLDKFGEeeeTPSSRgwtASTTGTIDGKKGLVMHGGK 452

                        250
                 ....*....|
gi 42563520  366 SHAT-CFDDL 374
Cdd:PLN02193 453 APTNdRFDDL 462
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 551-646 1.89e-08

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 57.00  E-value: 1.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520   551 KSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELR----QKLQTLETLQKE 626
Cdd:pfam19220  47 KSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRielrDKTAQAEALERQ 126

                          90       100
                  ....*....|....*....|....*...
gi 42563520   627 L--------ELLQRQKAASEQAAMNAKR 646
Cdd:pfam19220 127 LaaeteqnrALEEENKALREEAQAAEKA 154
Kelch_3 pfam13415
Galactose oxidase, central domain;
304-354 6.30e-08

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 49.21  E-value: 6.30e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 42563520   304 GKTLVIFGGQDAKRS-LLNDLHILDLDTMTWDEIdavGVSPSPRSDHAAAVH 354
Cdd:pfam13415   1 GDKLYIFGGLGFDGQtRLNDLYVYDLDTNTWTQI---GDLPPPRSGHSATYI 49
Kelch_3 pfam13415
Galactose oxidase, central domain;
356-405 3.27e-07

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 47.28  E-value: 3.27e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 42563520   356 ERFLLIFGG--GSHATCFDDLHVLDLQTMEWSRPaqqGDAPTPRAGHAGVTI 405
Cdd:pfam13415   1 GDKLYIFGGlgFDGQTRLNDLYVYDLDTNTWTQI---GDLPPPRSGHSATYI 49
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 183-224 4.02e-07

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: 46.84  E-value: 4.02e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 42563520   183 ARYEHGAAVIQDKMYIYGGNHNGRYLGDLHVLDLKSWTWSRV 224
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSKL 42
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
484-647 4.60e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.23  E-value: 4.60e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 484 SHKSTLQtKTLEAPLPGSLSAvnnattrdiESEVEVSQEGRVREIVMDNVNPGS---KVEGNSERIIATIKSEKEELEAS 560
Cdd:COG4717  34 AGKSTLL-AFIRAMLLERLEK---------EADELFKPQGRKPELNLKELKELEeelKEAEEKEEEYAELQEELEELEEE 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 561 LN--KERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLETLQKELELLQRQKAASE 638
Cdd:COG4717 104 LEelEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELL 183


                ....*....
gi 42563520 639 QAAMNAKRQ 647
Cdd:COG4717 184 EQLSLATEE 192
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 511-641 7.83e-07

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: 52.20  E-value: 7.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520   511 RDIESEVEVSQEGRVREIVMDNVNPGSKV---EGNSERIIATIK---SEKEELEAslnkERMQtLQLRQELGEAELRNtd 584
Cdd:pfam07888 117 KDALLAQRAAHEARIRELEEDIKTLTQRVlerETELERMKERAKkagAQRKEEEA----ERKQ-LQAKLQQTEEELRS-- 189

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42563520   585 LYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQT-------LETLQKELELLQRQKAASEQAA 641
Cdd:pfam07888 190 LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTahrkeaeNEALLEELRSLQERLNASERKV 253
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
547-647 9.97e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.44  E-value: 9.97e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 547 IATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLETLQKE 626
Cdd:COG4372  54 LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ 133

                        90       100
                ....*....|....*....|....*
gi 42563520 627 LE----LLQRQKAASEQAAMNAKRQ 647
Cdd:COG4372 134 LEaqiaELQSEIAEREEELKELEEQ 158
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
547-647 2.71e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.90  E-value: 2.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 547 IATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTL----ET 622
Cdd:COG4372  40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELqeelEE 119

                        90       100
                ....*....|....*....|....*
gi 42563520 623 LQKELELLQRQKAASEQAAMNAKRQ 647
Cdd:COG4372 120 LQKERQDLEQQRKQLEAQIAELQSE 144
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 181-219 5.84e-06

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: 43.32  E-value: 5.84e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 42563520   181 PKARYEHGAAVIQDKMYIYGGNH--NGRYLGDLHVLDLKSW 219
Cdd:pfam13854   1 PVPRYGHCAVTVGDYIYLYGGYTggEGQPSDDVYVLSLPTF 41
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 544-647 1.18e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 1.18e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 544 ERIIATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRcfkLEVDVAELRQKLQTLETL 623
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD---IARLEERRRELEERLEEL 321

                        90       100
                ....*....|....*....|....
gi 42563520 624 QKELELLQRQKAASEQAAMNAKRQ 647
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEE 345
PHA03098 PHA03098
kelch-like protein; Provisional
 154-385 1.50e-05

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 48.23  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  154 DKDVVSEDSNTvsvyNQW-TAPQTSgqrpKARYEHGAAVIQDKMYIYGGNHNGRYLgdlhvldlkswtwSRVETKVATES 232
Cdd:PHA03098 310 VNSVVSYDTKT----KSWnKVPELI----YPRKNPGVTVFNNRIYVIGGIYNSISL-------------NTVESWKPGES 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  233 QETSTPTLLAPCAGHSLIAWDNKLLSIGGHTKDPSESMQVKVFDPHTITWSMLKTYgkpPVSRGGQSVTMVGKTLVIFGG 312
Cdd:PHA03098 369 KWREEPPLIFPRYNPCVVNVNNLIYVIGGISKNDELLKTVECFSLNTNKWSKGSPL---PISHYGGCAIYHDGKIYVIGG 445

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42563520  313 ----QDAKRslLNDLHILDLDTMTWDEIDAVGVspsPRSDhAAAVHAERFLLIFGGGSHATCFDDLHVLDLQTMEWS 385
Cdd:PHA03098 446 isyiDNIKV--YNIVESYNPVTNKWTELSSLNF---PRIN-ASLCIFNNKIYVVGGDKYEYYINEIEVYDDKTNTWT 516
Kelch_6 pfam13964
Kelch motif;
297-336 1.76e-05

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 42.32  E-value: 1.76e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 42563520   297 GQSVTMVGKTLVIFGGQDAKRSLLNDLHILDLDTMTWDEI 336
Cdd:pfam13964   4 FHSVVSVGGYIYVFGGYTNASPALNKLEVYNPLTKSWEEL 43
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 543-640 1.82e-05

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: 48.25  E-value: 1.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520    543 SERIiATIKSEK------EELEAslnkermqtlqLRQELgEAELRNTDLYKELQSVRGQLAAEQSRCFK-----LEVDVA 611
Cdd:pfam01576  282 SERA-ARNKAEKqrrdlgEELEA-----------LKTEL-EDTLDTTAAQQELRSKREQEVTELKKALEeetrsHEAQLQ 348

                           90       100       110
                   ....*....|....*....|....*....|
gi 42563520    612 ELRQK-LQTLETLQKELELLQRQKAASEQA 640
Cdd:pfam01576  349 EMRQKhTQALEELTEQLEQAKRNKANLEKA 378
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
391-480 2.32e-05

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 46.69  E-value: 2.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 391 GDAPTPRAGHAGVTIGENWFIVGGGDNKSGASESVVLNMSTLAWSVVASvqgrVPLASEGLSLVVsSYNGEdVLVaFGGY 470
Cdd:COG3055   7 PDLPTPRSEAAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTWSELAP----LPGPPRHHAAAV-AQDGK-LYV-FGGF 79

                        90
                ....*....|
gi 42563520 471 NGRYNNEINL 480
Cdd:COG3055  80 TGANPSSTPL 89
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 538-650 4.27e-05

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: 45.06  E-value: 4.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520   538 KVEGNSERIIATIKSEKEELEAslNKERMQTLQLRQEL----GEAELRNTDLYkELQSVRGQLAAEQSRCFKLEVDVAEL 613
Cdd:pfam04012  40 KARQALAQTIARQKQLERRLEQ--QTEQAKKLEEKAQAaltkGNEELAREALA-EKKSLEKQAEALETQLAQQRSAVEQL 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 42563520   614 RQKLQTLETLQKELE-----LLQRQKAASEQAAMNAKRQGSG 650
Cdd:pfam04012 117 RKQLAALETKIQQLKakknlLKARLKAAKAQEAVQTSLGSLS 158
Kelch_4 pfam13418
Galactose oxidase, central domain;
183-227 1.31e-04

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 39.90  E-value: 1.31e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 42563520   183 ARYEHGAAVIQDKM-YIYGG-NHNGRYLGDLHVLDLKSWTWSRVETK 227
Cdd:pfam13418   1 PRAYHTSTSIPDDTiYLFGGeGEDGTLLSDLWVFDLSTNEWTRLGSL 47
Kelch_4 pfam13418
Galactose oxidase, central domain;
345-386 1.39e-04

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 39.90  E-value: 1.39e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 42563520   345 PRSDHAAAVHAERFLLIFGG-GSHATCFDDLHVLDLQTMEWSR 386
Cdd:pfam13418   1 PRAYHTSTSIPDDTIYLFGGeGEDGTLLSDLWVFDLSTNEWTR 43
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
538-631 1.39e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  538 KVEGNSERIIATIKSEKEELEASLNKERMQTLQLRQELGEA--------ELRN--TDLYKELQSVRGQLAAEQSRCFKLE 607
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLekevkeleELKEeiEELEKELESLEGSKRKLEEKIRELE 265

                         90       100
                 ....*....|....*....|....
gi 42563520  608 VDVAELRQKLQTLETLQKELELLQ 631
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELK 289
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
513-639 1.44e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  513 IESEVEvSQEGR---VREIVmdNVNPGSKVEGNSERIIATIKSEKEELEaslnKERMQTLQLRQELGEAELRNTDLYKEL 589
Cdd:PRK03918 137 IDAILE-SDESRekvVRQIL--GLDDYENAYKNLGEVIKEIKRRIERLE----KFIKRTENIEELIKEKEKELEEVLREI 209

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 42563520  590 QSVRGQLAaeqsrcfKLEVDVAELRQKLQTLETLQKELELLQRQKAASEQ 639
Cdd:PRK03918 210 NEISSELP-------ELREELEKLEKEVKELEELKEEIEELEKELESLEG 252
Kelch_3 pfam13415
Galactose oxidase, central domain;
194-251 1.46e-04

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 39.97  E-value: 1.46e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520   194 DKMYIYGGNH--NGRYLGDLHVLDLKSWTWsrvetkvatesqeTSTPTLLAPCAGHSLIA 251
Cdd:pfam13415   2 DKLYIFGGLGfdGQTRLNDLYVYDLDTNTW-------------TQIGDLPPPRSGHSATY 48
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
547-645 1.46e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 1.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 547 IATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSV----------RGQLAAEQSrcfKLEVDVAELRQK 616
Cdd:COG4372  75 LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELqkerqdleqqRKQLEAQIA---ELQSEIAEREEE 151

                        90       100       110
                ....*....|....*....|....*....|...
gi 42563520 617 LQTLET----LQKELELLQRQKAASEQAAMNAK 645
Cdd:COG4372 152 LKELEEqlesLQEELAALEQELQALSEAEAEQA 184
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 544-649 1.99e-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: 44.66  E-value: 1.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520    544 ERIIATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSvrgqLAAEQSRcfkLEVDVAELRQKLQTLETL 623
Cdd:TIGR02168  245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA----LANEISR---LEQQKQILRERLANLERQ 317

                           90       100       110
                   ....*....|....*....|....*....|.
gi 42563520    624 QKELE-----LLQRQKAASEQAAMNAKRQGS 649
Cdd:TIGR02168  318 LEELEaqleeLESKLDELAEELAELEEKLEE 348
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 547-644 3.05e-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: 42.99  E-value: 3.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 547 IATIKSEKEELEASLNKermqtlqLRQELGEAElrntdlyKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLET---- 622
Cdd:COG1579  19 LDRLEHRLKELPAELAE-------LEDELAALE-------ARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgn 84

                        90       100       110
                ....*....|....*....|....*....|.
gi 42563520 623 ---------LQKELELLQRQKAASEQAAMNA 644
Cdd:COG1579  85 vrnnkeyeaLQKEIESLKRRISDLEDEILEL 115
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 547-647 3.06e-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: 3.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 547 IATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKL----QTLET 622
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELeeleEELEE 341

                        90       100
                ....*....|....*....|....*
gi 42563520 623 LQKELELLQRQKAASEQAAMNAKRQ 647
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEA 366
Kelch_6 pfam13964
Kelch motif;
243-295 3.08e-04

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 38.86  E-value: 3.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 42563520   243 PCAGHSLIAWDNKLLSIGGHTKDPSESMQVKVFDPHTITWsmlKTYGKPPVSR 295
Cdd:pfam13964   1 PRTFHSVVSVGGYIYVFGGYTNASPALNKLEVYNPLTKSW---EELPPLPTPR 50
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 549-647 3.25e-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: 3.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 549 TIKSEKEELEASLNKERMQTLQ-----LRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKL----QT 619
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEaeleeLEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellAE 296

                        90       100
                ....*....|....*....|....*...
gi 42563520 620 LETLQKELELLQRQKAASEQAAMNAKRQ 647
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEE 324
Kelch_4 pfam13418
Galactose oxidase, central domain;
295-336 4.03e-04

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 38.36  E-value: 4.03e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 42563520   295 RGGQSVTMVGK-TLVIFGGQDAKRSLLNDLHILDLDTMTWDEI 336
Cdd:pfam13418   2 RAYHTSTSIPDdTIYLFGGEGEDGTLLSDLWVFDLSTNEWTRL 44
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
550-646 4.11e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 4.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 550 IKSEKEELEASLNKERMQTLQLRQELGEAELRntdlyKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLETLQKELEL 629
Cdd:COG4717 400 LKEELEELEEQLEELLGELEELLEALDEEELE-----EELEELEEELEELEEELEELREELAELEAELEQLEEDGELAEL 474

                        90
                ....*....|....*..
gi 42563520 630 LQRQKAASEQAAMNAKR 646
Cdd:COG4717 475 LQELEELKAELRELAEE 491
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
547-643 5.02e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.47  E-value: 5.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 547 IATIKSEKEELEASLNKErmqtlqLRQELGEAELRNTDLYKELQSVRGQLAAEQSRcfklevdVAELRQKLQTLETLQKE 626
Cdd:COG3206 293 VIALRAQIAALRAQLQQE------AQRILASLEAELEALQAREASLQAQLAQLEAR-------LAELPELEAELRRLERE 359

                        90       100
                ....*....|....*....|....*
gi 42563520 627 LE--------LLQRQKAASEQAAMN 643
Cdd:COG3206 360 VEvarelyesLLQRLEEARLAEALT 384
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 537-647 5.20e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 5.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 537 SKVEGNSERIIATIKSEKEELEASLNKER---MQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAEL 613
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYellAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342

                        90       100       110
                ....*....|....*....|....*....|....
gi 42563520 614 RQKLQTLEtlqKELELLQRQKAASEQAAMNAKRQ 647
Cdd:COG1196 343 EEELEEAE---EELEEAEAELAEAEEALLEAEAE 373
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 550-647 5.29e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 5.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 550 IKSEKEELEASLN--KERMQTL-----QLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLET 622
Cdd:COG1196 293 LLAELARLEQDIArlEERRRELeerleELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                        90       100
                ....*....|....*....|....*
gi 42563520 623 LQKELELLQRQKAASEQAAMNAKRQ 647
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAE 397
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 552-641 5.40e-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: 5.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 552 SEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLETLQKELE--L 629
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRaeL 99

                        90
                ....*....|..
gi 42563520 630 LQRQKAASEQAA 641
Cdd:COG4942 100 EAQKEELAELLR 111
Kelch_6 pfam13964
Kelch motif;
183-224 6.20e-04

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 38.09  E-value: 6.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 42563520   183 ARYEHGAAVIQDKMYIYGGNHN-GRYLGDLHVLDLKSWTWSRV 224
Cdd:pfam13964   1 PRTFHSVVSVGGYIYVFGGYTNaSPALNKLEVYNPLTKSWEEL 43
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 555-645 8.37e-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: 41.52  E-value: 8.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520   555 EELEASLNKERMQTLQLRQELGEAElrntdlyKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLETLQKELELLQRQK 634
Cdd:pfam12795  81 EELEQRLLQTSAQLQELQNQLAQLN-------SQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWA 153

                          90
                  ....*....|.
gi 42563520   635 AASEQAAMNAK 645
Cdd:pfam12795 154 LQAELAALKAQ 164
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 547-647 8.45e-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: 8.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520    547 IATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQ-------- 618
Cdd:TIGR02168  360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaelkelq 439

                           90       100       110
                   ....*....|....*....|....*....|
gi 42563520    619 -TLETLQKELELLQRQKAASEQAAMNAKRQ 647
Cdd:TIGR02168  440 aELEELEEELEELQEELERLEEALEELREE 469
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 542-647 8.60e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 8.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 542 NSERIIATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRcfKLEVDVAELRQKLQTLE 621
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE--LAEAEEELEELAEELLE 390

                        90       100
                ....*....|....*....|....*.
gi 42563520 622 TLQKELELLQRQKAASEQAAMNAKRQ 647
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERL 416
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 547-647 8.67e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 8.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 547 IATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLETLQKE 626
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418

                        90       100
                ....*....|....*....|.
gi 42563520 627 LELLQRQKAASEQAAMNAKRQ 647
Cdd:COG1196 419 LEEELEELEEALAELEEEEEE 439
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 544-655 1.28e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 1.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 544 ERIIATIKSEKEELEaslnkermqtlQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRC----FKLEVDVAELRQKLQT 619
Cdd:COG4942 149 REQAEELRADLAELA-----------ALRAELEAERAELEALLAELEEERAALEALKAERqkllARLEKELAELAAELAE 217

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 42563520 620 L----ETLQKELELLQRQKAASEQAAMNAKRQGSGGVWGW 655
Cdd:COG4942 218 LqqeaEELEALIARLEAEAAAAAERTPAAGFAALKGKLPW 257
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 547-647 1.31e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 1.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 547 IATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLE-TLQK 625
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEeAEEA 411

                        90       100
                ....*....|....*....|..
gi 42563520 626 ELELLQRQKAASEQAAMNAKRQ 647
Cdd:COG1196 412 LLERLERLEEELEELEEALAEL 433
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
547-647 1.47e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 1.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 547 IATIKSEKEELEASLNKE--RMQTLQLRQELGEAELRNTdLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLETLQ 624
Cdd:COG3206 272 LAELEAELAELSARYTPNhpDVIALRAQIAALRAQLQQE-AQRILASLEAELEALQAREASLQAQLAQLEARLAELPELE 350

                        90       100
                ....*....|....*....|....*
gi 42563520 625 KELELLQRQKAASEQA--AMNAKRQ 647
Cdd:COG3206 351 AELRRLEREVEVARELyeSLLQRLE 375
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 343-381 1.62e-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: 433528 [Multi-domain]  Cd Length: 41  Bit Score: 36.77  E-value: 1.62e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 42563520   343 PSPRSDHAAAVHAERfLLIFGGGSHAT--CFDDLHVLDLQT 381
Cdd:pfam13854   1 PVPRYGHCAVTVGDY-IYLYGGYTGGEgqPSDDVYVLSLPT 40
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 550-647 1.68e-03

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


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 41.58  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520   550 IKSEKEELEASLNK--ERMQTLQLRqeLGEAELRNTDLYKELQSVR--GQLAAEQSRCFK------------LEVDVAEL 613
Cdd:pfam05911 693 LKSEKENLEVELASctENLESTKSQ--LQESEQLIAELRSELASLKesNSLAETQLKCMAesyedletrlteLEAELNEL 770

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 42563520   614 RQKLQTLET-LQKE-----------LEL-LQRQKAASEQAAMNAKRQ 647
Cdd:pfam05911 771 RQKFEALEVeLEEEkncheeleakcLELqEQLERNEKKESSNCDADQ 817
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 542-633 1.88e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 1.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 542 NSERIIATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTL- 620
Cdd:COG4942  24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQk 103

                        90
                ....*....|...
gi 42563520 621 ETLQKELELLQRQ 633
Cdd:COG4942 104 EELAELLRALYRL 116
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 540-647 1.91e-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: 41.58  E-value: 1.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520    540 EGNSERIIATIKSEKEELEASLNKERMQTLQLRQELGEAElrntdlyKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQT 619
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE-------AEIEELEAQIEQLKEELKALREALDELRAELTL 814

                           90       100       110
                   ....*....|....*....|....*....|..
gi 42563520    620 LE----TLQKELELLQRQKAASEQAAMNAKRQ 647
Cdd:TIGR02168  815 LNeeaaNLRERLESLERRIAATERRLEDLEEQ 846
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 566-646 1.92e-03

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


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 39.53  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520   566 MQTLQLRQELGEAELRNT-------DLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQ-----------TLETLQKEL 627
Cdd:pfam08614  57 QLLAQLREELAELYRSRGelaqrlvDLNEELQELEKKLREDERRLAALEAERAQLEEKLKdreeelrekrkLNQDLQDEL 136

                          90
                  ....*....|....*....
gi 42563520   628 ELLQRQKAASEQAAMNAKR 646
Cdd:pfam08614 137 VALQLQLNMAEEKLRKLEK 155
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
547-640 1.96e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 1.96e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 547 IATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLETLQKE 626
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE 182

                        90
                ....*....|....
gi 42563520 627 LELLQRQKAASEQA 640
Cdd:COG4372 183 QALDELLKEANRNA 196
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 507-645 2.03e-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: 41.59  E-value: 2.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520    507 NATTRDIES-EVEVSQEGRVREIVMDNVNPGSKVEGNSERIIATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDL 585
Cdd:TIGR02169  290 LRVKEKIGElEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDL 369

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42563520    586 YKELQSVrgqlaaeqsrcfklEVDVAELRQKL----QTLETLQKELELLQR---------QKAASEQAAMNAK 645
Cdd:TIGR02169  370 RAELEEV--------------DKEFAETRDELkdyrEKLEKLKREINELKReldrlqeelQRLSEELADLNAA 428
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
544-634 2.14e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  544 ERIIATIKSEKEELEASLNK--ERMQTLQLRQELGEAELrnTDLYKELQSVRGQLAAEQSRC----FKLEVDVAELRQKl 617
Cdd:COG4913  344 EREIERLERELEERERRRARleALLAALGLPLPASAEEF--AALRAEAAALLEALEEELEALeealAEAEAALRDLRRE- 420

                         90
                 ....*....|....*..
gi 42563520  618 qtLETLQKELELLQRQK 634
Cdd:COG4913  421 --LRELEAEIASLERRK 435
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 544-647 2.17e-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: 41.21  E-value: 2.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520    544 ERIIATIKSEKEELEASLNK---------ERMQTLQLRQElgEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELR 614
Cdd:TIGR02169  804 EEEVSRIEARLREIEQKLNRltlekeyleKEIQELQEQRI--DLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLE 881

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 42563520    615 QKLQTLET----LQKELELLQR----QKAASEQAAMNAKRQ 647
Cdd:TIGR02169  882 SRLGDLKKerdeLEAQLRELERkieeLEAQIEKKRKRLSEL 922
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 540-640 2.69e-03

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: 41.09  E-value: 2.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  540 EGNSERIIATIKSEKEELEASLNKERMQTLQLRQELGEAE---------------LRNTDLYKELQSVRGQL-AAEQSRC 603
Cdd:COG3096  831 APDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKeqlqllnkllpqanlLADETLADRLEELREELdAAQEAQA 910

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 42563520  604 F---------KLEVDVAELRQKLQTLETLQKE-LELLQRQKAASEQA 640
Cdd:COG3096  911 FiqqhgkalaQLEPLVAVLQSDPEQFEQLQADyLQAKEQQRRLKQQI 957
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 544-647 2.85e-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: 41.20  E-value: 2.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520    544 ERIIATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSrcfKLEVDVAELRQKLQTLETL 623
Cdd:TIGR02168  336 AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL---QIASLNNEIERLEARLERL 412

                           90       100
                   ....*....|....*....|....
gi 42563520    624 QKELELLQRQKAASEQAAMNAKRQ 647
Cdd:TIGR02168  413 EDRRERLQQEIEELLKKLEEAELK 436
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 554-649 3.04e-03

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


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 40.83  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520   554 KEE---LEASLNKERMQTLQLRQELGEAELRNTDLYKelqsvrgqlAAEQSRCFKLEVDVaeLRQ------KL-QTLETL 623
Cdd:pfam05622  72 QEEnfrLETARDDYRIKCEELEKEVLELQHRNEELTS---------LAEEAQALKDEMDI--LREssdkvkKLeATVETY 140

                          90       100       110
                  ....*....|....*....|....*....|
gi 42563520   624 QKELE---LLQRQ-KAASEQAAMNAKRQGS 649
Cdd:pfam05622 141 KKKLEdlgDLRRQvKLLEERNAEYMQRTLQ 170
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 537-634 3.18e-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: 40.93  E-value: 3.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520    537 SKVEGNSERIIATIKSEKEELEASLNkermQTLQLRQELGEaelRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQK 616
Cdd:pfam01576  397 QQAKQDSEHKRKKLEGQLQELQARLS----ESERQRAELAE---KLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQ 469

                           90
                   ....*....|....*....
gi 42563520    617 LQ-TLETLQKElellQRQK 634
Cdd:pfam01576  470 LQdTQELLQEE----TRQK 484
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 345-386 3.91e-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: 35.67  E-value: 3.91e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 42563520   345 PRSDHAAAVHAERfLLIFGGGSHATCFDDLHVLDLQTMEWSR 386
Cdd:pfam01344   1 RRSGAGVVVVGGK-IYVIGGFDGNQSLNSVEVYDPETNTWSK 41
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 522-639 3.92e-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: 38.05  E-value: 3.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520   522 EGRVREIVMdnvnpgskVEGNSERII---ATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQsvrgqlaA 598
Cdd:pfam10473  27 ENLERELEM--------SEENQELAIleaENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSEKENLTKELQ-------K 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 42563520   599 EQSRCFKLEVDVAELRQKLQTLEtlQKELELLQRQKAASEQ 639
Cdd:pfam10473  92 KQERVSELESLNSSLENLLEEKE--QEKVQMKEESKTAVEM 130
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 504-651 3.97e-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: 3.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520    504 AVNNATTRDIESEVEVSQEGRVREIvmdnvnpgskveGNSERIIATIKSEKEELEASLNKERMQTLQLRQELGEAELRNT 583
Cdd:TIGR02169  377 DKEFAETRDELKDYREKLEKLKREI------------NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE 444

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42563520    584 DLYKELQSVRGQLAAEQSRCFKLEvdvAELRQKLQTLETLQKELELLQRQKAASEqAAMNAKRQGSGG 651
Cdd:TIGR02169  445 DKALEIKKQEWKLEQLAADLSKYE---QELYDLKEEYDRVEKELSKLQRELAEAE-AQARASEERVRG 508
Kelch_2 pfam07646
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 184-224 4.05e-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: 462220 [Multi-domain]  Cd Length: 47  Bit Score: 35.77  E-value: 4.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 42563520   184 RYEHGAAVIQDKMYIYGG--NHNGRYLGDLHVLDLKSWTWSRV 224
Cdd:pfam07646   2 RYPHASSVPGGKLYVVGGsdGLGDLSSSDVLVYDPETNVWTEV 44
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 537-648 4.37e-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: 40.43  E-value: 4.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520    537 SKVEGNSERIIATIKsEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQK 616
Cdd:TIGR02168  824 ERLESLERRIAATER-RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902

                           90       100       110
                   ....*....|....*....|....*....|..
gi 42563520    617 LQTLETLQKELElLQRQKAASEQAAMNAKRQG 648
Cdd:TIGR02168  903 LRELESKRSELR-RELEELREKLAQLELRLEG 933
Kelch_2 pfam07646
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 243-283 4.56e-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: 462220 [Multi-domain]  Cd Length: 47  Bit Score: 35.39  E-value: 4.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 42563520   243 PCAGHSLIAWDNKLLSIGGHTKDPSE-SMQVKVFDPHTITWS 283
Cdd:pfam07646   1 PRYPHASSVPGGKLYVVGGSDGLGDLsSSDVLVYDPETNVWT 42
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
544-647 5.10e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 5.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  544 ERIIATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRG----QLAAEQSRcfkLEVDVAELRQKLQT 619
Cdd:COG4913  287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGdrleQLEREIER---LERELEERERRRAR 363

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 42563520  620 LETLQKELEL--------LQRQKAASEQAAMNAKRQ 647
Cdd:COG4913  364 LEALLAALGLplpasaeeFAALRAEAAALLEALEEE 399
mukB PRK04863
chromosome partition protein MukB;
540-647 6.11e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 6.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520   540 EGNSERIIATIKSEKEELEASLNKERMQTLQLRQELGEAE---------------LRNTDLYKELQSVRGQLA-AEQSRC 603
Cdd:PRK04863  832 EADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKeglsalnrllprlnlLADETLADRVEEIREQLDeAEEAKR 911

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 42563520   604 F--KLEVDVAELRQKLQTLETLQKELELLQRQKAASEQAAMNAKRQ 647
Cdd:PRK04863  912 FvqQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQ 957
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 550-639 6.19e-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: 40.04  E-value: 6.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520    550 IKSEKEELEASLNKERMQTL-----QLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTL---- 620
Cdd:TIGR02168  218 LKAELRELELALLVLRLEELreeleELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALanei 297

                           90
                   ....*....|....*....
gi 42563520    621 ETLQKELELLQRQKAASEQ 639
Cdd:TIGR02168  298 SRLEQQKQILRERLANLER 316
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 555-634 6.91e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 39.72  E-value: 6.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520   555 EELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDvaELRQKLQTLETlqkELELLQRQK 634
Cdd:pfam05557 390 QKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVD--SLRRKLETLEL---ERQRLREQK 464
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 510-647 7.15e-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: 39.67  E-value: 7.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520    510 TRDIESEVEV--SQEGRVREIVMDnvnpgSKVEGNS-ERIIATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTD-- 584
Cdd:TIGR02169  718 IGEIEKEIEQleQEEEKLKERLEE-----LEEDLSSlEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHsr 792

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42563520    585 ---LYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLETLQKELEllQRQKAASEQAAMNAKRQ 647
Cdd:TIGR02169  793 ipeIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ--EQRIDLKEQIKSIEKEI 856
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 544-647 7.17e-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: 39.36  E-value: 7.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520 544 ERIIATIKSEKEELEASLNK------ERMQTLQLRQELGEAEL-----------RNTDLYKELQSVRGQLAAEqsrcfkL 606
Cdd:COG4942  82 EAELAELEKEIAELRAELEAqkeelaELLRALYRLGRQPPLALllspedfldavRRLQYLKYLAPARREQAEE------L 155

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 42563520 607 EVDVAELRQKLQTLETLQKELELLQRQKAAsEQAAMNAKRQ 647
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEE-ERAALEALKA 195
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
550-645 7.52e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 7.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  550 IKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQ-----SRCFKLEVDVAELRQKLQTLE--- 621
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelrEEYLELSRELAGLRAELEELEkrr 689

                         90       100
                 ....*....|....*....|....*
gi 42563520  622 -TLQKELELLQRQKAASEQAAMNAK 645
Cdd:PRK03918 690 eEIKKTLEKLKEELEEREKAKKELE 714
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
562-647 9.26e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 9.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563520  562 NKERMQTLQlrQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKL---------EVDV-------AELRQKLQTLETLQK 625
Cdd:COG4913  608 NRAKLAALE--AELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdEIDVasaereiAELEAELERLDASSD 685

                         90       100
                 ....*....|....*....|..
gi 42563520  626 ELELLQRQKAASEQAAMNAKRQ 647
Cdd:COG4913  686 DLAALEEQLEELEAELEELEEE 707
 
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