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Conserved domains on  [gi|42572263|ref|NP_974227|]
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acyl-CoA binding protein 4 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
182-426 1.29e-28

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


:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 115.64  E-value: 1.29e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 182 PKARYEHGAAVIQDKMYIYGGNHNGRYLGDLHVLDLKSWTWSRVetkvatesqeTSTPTllAPCAGHSLIAWDNKLLSIG 261
Cdd:COG3055  10 PTPRSEAAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTWSEL----------APLPG--PPRHHAAAVAQDGKLYVFG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 262 GHTKDPSESMQVK---VFDPHTITWSMLktyGKPPVSRGGQSVTMVGKTLVIFGGQDAKRSLlNDLHILDLDTMTWDEID 338
Cdd:COG3055  78 GFTGANPSSTPLNdvyVYDPATNTWTKL---APMPTPRGGATALLLDGKIYVVGGWDDGGNV-AWVEVYDPATGTWTQLA 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 339 AVgvsPSPRSDHAAAVHAERFLLIFGG------------------------------------GSHATcFDDLHVLDLQT 382
Cdd:COG3055 154 PL---PTPRDHLAAAVLPDGKILVIGGrngsgfsntwttlaplptaraghaaavlggkilvfgGESGF-SDEVEAYDPAT 229

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 42572263 383 MEWSrpaQQGDAPTPRAGHAGVTIGENWFIVGGGDNKSGASESV 426
Cdd:COG3055 230 NTWT---ALGELPTPRHGHAAVLTDGKVYVIGGETKPGVRTPLV 270
ACBP pfam00887
Acyl CoA binding protein;
14-97 6.35e-23

Acyl CoA binding protein;


:

Pssm-ID: 459982  Cd Length: 76  Bit Score: 92.66  E-value: 6.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263    14 ERFYAAASYVgldgsdssaKNVISKFPDDTALLLYALYQQATVGPCNTPKPSAWRPVEQSKWKSWQGLGTMPSIEAMRLF 93
Cdd:pfam00887   2 EKFEAAAEFV---------KKLKSKPSNEEKLELYGLYKQATVGDCNTPRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKY 72


                  ....
gi 42572263    94 VKIL 97
Cdd:pfam00887  73 VELV 76
Crescentin super family cl41192
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 552-647 2.07e-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: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263   552 KSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELR----QKLQTLETLQKE 627
Cdd:pfam19220  47 KSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRielrDKTAQAEALERQ 126

                          90       100
                  ....*....|....*....|....*...
gi 42572263   628 L--------ELLQRQKAASEQAAMNAKR 647
Cdd:pfam19220 127 LaaeteqnrALEEENKALREEAQAAEKA 154
NanM super family cl34543
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
392-481 2.22e-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: 2.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 392 GDAPTPRAGHAGVTIGENWFIVGGGDNKSGASESVVLNMSTLAWSVVASvqgrVPLASEGLSLVVsSYNGEdVLVaFGGY 471
Cdd:COG3055   7 PDLPTPRSEAAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTWSELAP----LPGPPRHHAAAV-AQDGK-LYV-FGGF 79

                        90
                ....*....|
gi 42572263 472 NGRYNNEINL 481
Cdd:COG3055  80 TGANPSSTPL 89
 
Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
182-426 1.29e-28

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 115.64  E-value: 1.29e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 182 PKARYEHGAAVIQDKMYIYGGNHNGRYLGDLHVLDLKSWTWSRVetkvatesqeTSTPTllAPCAGHSLIAWDNKLLSIG 261
Cdd:COG3055  10 PTPRSEAAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTWSEL----------APLPG--PPRHHAAAVAQDGKLYVFG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 262 GHTKDPSESMQVK---VFDPHTITWSMLktyGKPPVSRGGQSVTMVGKTLVIFGGQDAKRSLlNDLHILDLDTMTWDEID 338
Cdd:COG3055  78 GFTGANPSSTPLNdvyVYDPATNTWTKL---APMPTPRGGATALLLDGKIYVVGGWDDGGNV-AWVEVYDPATGTWTQLA 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 339 AVgvsPSPRSDHAAAVHAERFLLIFGG------------------------------------GSHATcFDDLHVLDLQT 382
Cdd:COG3055 154 PL---PTPRDHLAAAVLPDGKILVIGGrngsgfsntwttlaplptaraghaaavlggkilvfgGESGF-SDEVEAYDPAT 229

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 42572263 383 MEWSrpaQQGDAPTPRAGHAGVTIGENWFIVGGGDNKSGASESV 426
Cdd:COG3055 230 NTWT---ALGELPTPRHGHAAVLTDGKVYVIGGETKPGVRTPLV 270
ACBP pfam00887
Acyl CoA binding protein;
14-97 6.35e-23

Acyl CoA binding protein;


Pssm-ID: 459982  Cd Length: 76  Bit Score: 92.66  E-value: 6.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263    14 ERFYAAASYVgldgsdssaKNVISKFPDDTALLLYALYQQATVGPCNTPKPSAWRPVEQSKWKSWQGLGTMPSIEAMRLF 93
Cdd:pfam00887   2 EKFEAAAEFV---------KKLKSKPSNEEKLELYGLYKQATVGDCNTPRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKY 72


                  ....
gi 42572263    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 2.65e-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: 2.65e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  14 ERFYAAASYVgldgsdssaKNVISKFPDDTALLLYALYQQATVGPCNTPKPSAWRPVEQSKWKSWQGLGTMPSIEAMRLF 93
Cdd:cd00435   3 EEFEAAAEKV---------KKLKTKPSNEEKLQLYSLYKQATVGDCNTERPGMFDLKGRAKWDAWNSLKGMSKEDAMKAY 73


                ....*.
gi 42572263  94 VKILEE 99
Cdd:cd00435  74 IAKVEE 79
PLN02153 PLN02153
epithiospecifier protein
 171-416 6.86e-13

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 70.40  E-value: 6.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  171 QW-TAPQTSGQRPKARYEHGAAVIQDKMYIYGGN--HNGRYLGDLHVLDLKSWTWS-------------------RVETK 228
Cdd:PLN02153   8 GWiKVEQKGGKGPGPRCSHGIAVVGDKLYSFGGElkPNEHIDKDLYVFDFNTHTWSiapangdvprisclgvrmvAVGTK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  229 VA------------------TESQETSTPTLLAPCAG------HSLIAWDNKL-----LSIGGHTKDPSESMQVKVFDPH 279
Cdd:PLN02153  88 LYifggrdekrefsdfysydTVKNEWTFLTKLDEEGGpeartfHSMASDENHVyvfggVSKGGLMKTPERFRTIEAYNIA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  280 TITWSMLKTYGKPPVSRGGQSVTMV-GKTLVIFG--------GQDAKRSllNDLHILDLDTMTWDEIDAVGVSPSPRSDH 350
Cdd:PLN02153 168 DGKWVQLPDPGENFEKRGGAGFAVVqGKIWVVYGfatsilpgGKSDYES--NAVQFFDPASGKWTEVETTGAKPSARSVF 245

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42572263  351 AAAVhAERFLLIFGG------GSH---ATCFDDLHVLDLQTMEWSRPAQQGDAPTPRAGHAGVTI---GENWFIVGGG 416
Cdd:PLN02153 246 AHAV-VGKYIIIFGGevwpdlKGHlgpGTLSNEGYALDTETLVWEKLGECGEPAMPRGWTAYTTAtvyGKNGLLMHGG 322
ACB COG4281
Acyl-CoA-binding protein [Lipid transport and metabolism];
14-99 7.56e-11

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


Pssm-ID: 443422  Cd Length: 87  Bit Score: 58.71  E-value: 7.56e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  14 ERFYAAASYVgldgsdssaKNVISKFPDDTALLLYALYQQATVGPCNTPKPSAWRPVEQSKWKSWQGLGTMPSIEAMRLF 93
Cdd:COG4281   6 AAFEAAVARV---------KTLTERPDNDTLLKLYALYKQATEGDVTGKRPGMTDFVGRAKYDAWAQLKGMSKDEAMQQY 76


                ....*.
gi 42572263  94 VKILEE 99
Cdd:COG4281  77 IDLVNS 82
PTZ00458 PTZ00458
acyl CoA binding protein; Provisional
 40-104 5.85e-09

acyl CoA binding protein; Provisional


Pssm-ID: 185637  Cd Length: 90  Bit Score: 53.67  E-value: 5.85e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42572263   40 PDDTALLLYALYQQATVGPCNTPKPSAWRPVEQSKWKSWQGLGTMPSIEAMRLFVKILEEDDPGW 104
Cdd:PTZ00458  22 SVEIKLDLYKYYKQSTVGNCNIKEPSMFKYQDRKKYEAWKSIENLNREDAKKRYVEIVTELFPNW 86
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 552-647 2.07e-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: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263   552 KSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELR----QKLQTLETLQKE 627
Cdd:pfam19220  47 KSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRielrDKTAQAEALERQ 126

                          90       100
                  ....*....|....*....|....*...
gi 42572263   628 L--------ELLQRQKAASEQAAMNAKR 647
Cdd:pfam19220 127 LaaeteqnrALEEENKALREEAQAAEKA 154
Kelch_3 pfam13415
Galactose oxidase, central domain;
305-355 6.31e-08

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 49.21  E-value: 6.31e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 42572263   305 GKTLVIFGGQDAKRS-LLNDLHILDLDTMTWDEIdavGVSPSPRSDHAAAVH 355
Cdd:pfam13415   1 GDKLYIFGGLGFDGQtRLNDLYVYDLDTNTWTQI---GDLPPPRSGHSATYI 49
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
485-648 5.11e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.85  E-value: 5.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 485 SHKSTLQtKTLEAPLPGSLSAvnnattrdiESEVEVSQEGRVREIVMDNVNPGS---KVEGNSERIIATIKSEKEELEAS 561
Cdd:COG4717  34 AGKSTLL-AFIRAMLLERLEK---------EADELFKPQGRKPELNLKELKELEeelKEAEEKEEEYAELQEELEELEEE 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 562 LN--KERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLETLQKELELLQRQKAASE 639
Cdd:COG4717 104 LEelEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELL 183


                ....*....
gi 42572263 640 QAAMNAKRQ 648
Cdd:COG4717 184 EQLSLATEE 192
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
392-481 2.22e-05

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 46.69  E-value: 2.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 392 GDAPTPRAGHAGVTIGENWFIVGGGDNKSGASESVVLNMSTLAWSVVASvqgrVPLASEGLSLVVsSYNGEdVLVaFGGY 471
Cdd:COG3055   7 PDLPTPRSEAAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTWSELAP----LPGPPRHHAAAV-AQDGK-LYV-FGGF 79

                        90
                ....*....|
gi 42572263 472 NGRYNNEINL 481
Cdd:COG3055  80 TGANPSSTPL 89
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
539-632 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 42572263  539 KVEGNSERIIATIKSEKEELEASLNKERMQTLQLRQELGEA--------ELRN--TDLYKELQSVRGQLAAEQSRCFKLE 608
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLekevkeleELKEeiEELEKELESLEGSKRKLEEKIRELE 265

                         90       100
                 ....*....|....*....|....
gi 42572263  609 VDVAELRQKLQTLETLQKELELLQ 632
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELK 289
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 545-650 2.09e-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: 2.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263    545 ERIIATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSvrgqLAAEQSRcfkLEVDVAELRQKLQTLETL 624
Cdd:TIGR02168  245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA----LANEISR---LEQQKQILRERLANLERQ 317

                           90       100       110
                   ....*....|....*....|....*....|.
gi 42572263    625 QKELE-----LLQRQKAASEQAAMNAKRQGS 650
Cdd:TIGR02168  318 LEELEaqleeLESKLDELAEELAELEEKLEE 348
 
Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
182-426 1.29e-28

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 115.64  E-value: 1.29e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 182 PKARYEHGAAVIQDKMYIYGGNHNGRYLGDLHVLDLKSWTWSRVetkvatesqeTSTPTllAPCAGHSLIAWDNKLLSIG 261
Cdd:COG3055  10 PTPRSEAAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTWSEL----------APLPG--PPRHHAAAVAQDGKLYVFG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 262 GHTKDPSESMQVK---VFDPHTITWSMLktyGKPPVSRGGQSVTMVGKTLVIFGGQDAKRSLlNDLHILDLDTMTWDEID 338
Cdd:COG3055  78 GFTGANPSSTPLNdvyVYDPATNTWTKL---APMPTPRGGATALLLDGKIYVVGGWDDGGNV-AWVEVYDPATGTWTQLA 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 339 AVgvsPSPRSDHAAAVHAERFLLIFGG------------------------------------GSHATcFDDLHVLDLQT 382
Cdd:COG3055 154 PL---PTPRDHLAAAVLPDGKILVIGGrngsgfsntwttlaplptaraghaaavlggkilvfgGESGF-SDEVEAYDPAT 229

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 42572263 383 MEWSrpaQQGDAPTPRAGHAGVTIGENWFIVGGGDNKSGASESV 426
Cdd:COG3055 230 NTWT---ALGELPTPRHGHAAVLTDGKVYVIGGETKPGVRTPLV 270
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
236-477 7.70e-26

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 107.55  E-value: 7.70e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 236 TSTPTLLAPCAGHSLIAWDNKLLSIGGHTKDpSESMQVKVFDPHTITWSMLKTYgkpPVSRGGQSVTMV--GKTLVI--F 311
Cdd:COG3055   4 SSLPDLPTPRSEAAAALLDGKVYVAGGLSGG-SASNSFEVYDPATNTWSELAPL---PGPPRHHAAAVAqdGKLYVFggF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 312 GGQDAKRSLLNDLHILDLDTMTWDEIdavGVSPSPRSDHAAAVHAERfLLIFGGGSHATCFDDLHVLDLQTMEWSrpaQQ 391
Cdd:COG3055  80 TGANPSSTPLNDVYVYDPATNTWTKL---APMPTPRGGATALLLDGK-IYVVGGWDDGGNVAWVEVYDPATGTWT---QL 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 392 GDAPTPRAGHAGVTIGENWFIVGGGDNKSGASEsvvlnmstlAWSVVAsvqgrvPLASEGLSLVVSSYNGEdvLVAFGGY 471
Cdd:COG3055 153 APLPTPRDHLAAAVLPDGKILVIGGRNGSGFSN---------TWTTLA------PLPTARAGHAAAVLGGK--ILVFGGE 215


                ....*.
gi 42572263 472 NGRYNN 477
Cdd:COG3055 216 SGFSDE 221
ACBP pfam00887
Acyl CoA binding protein;
14-97 6.35e-23

Acyl CoA binding protein;


Pssm-ID: 459982  Cd Length: 76  Bit Score: 92.66  E-value: 6.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263    14 ERFYAAASYVgldgsdssaKNVISKFPDDTALLLYALYQQATVGPCNTPKPSAWRPVEQSKWKSWQGLGTMPSIEAMRLF 93
Cdd:pfam00887   2 EKFEAAAEFV---------KKLKSKPSNEEKLELYGLYKQATVGDCNTPRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKY 72


                  ....
gi 42572263    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 2.65e-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: 2.65e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  14 ERFYAAASYVgldgsdssaKNVISKFPDDTALLLYALYQQATVGPCNTPKPSAWRPVEQSKWKSWQGLGTMPSIEAMRLF 93
Cdd:cd00435   3 EEFEAAAEKV---------KKLKTKPSNEEKLQLYSLYKQATVGDCNTERPGMFDLKGRAKWDAWNSLKGMSKEDAMKAY 73


                ....*.
gi 42572263  94 VKILEE 99
Cdd:cd00435  74 IAKVEE 79
PLN02153 PLN02153
epithiospecifier protein
 171-416 6.86e-13

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 70.40  E-value: 6.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  171 QW-TAPQTSGQRPKARYEHGAAVIQDKMYIYGGN--HNGRYLGDLHVLDLKSWTWS-------------------RVETK 228
Cdd:PLN02153   8 GWiKVEQKGGKGPGPRCSHGIAVVGDKLYSFGGElkPNEHIDKDLYVFDFNTHTWSiapangdvprisclgvrmvAVGTK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  229 VA------------------TESQETSTPTLLAPCAG------HSLIAWDNKL-----LSIGGHTKDPSESMQVKVFDPH 279
Cdd:PLN02153  88 LYifggrdekrefsdfysydTVKNEWTFLTKLDEEGGpeartfHSMASDENHVyvfggVSKGGLMKTPERFRTIEAYNIA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  280 TITWSMLKTYGKPPVSRGGQSVTMV-GKTLVIFG--------GQDAKRSllNDLHILDLDTMTWDEIDAVGVSPSPRSDH 350
Cdd:PLN02153 168 DGKWVQLPDPGENFEKRGGAGFAVVqGKIWVVYGfatsilpgGKSDYES--NAVQFFDPASGKWTEVETTGAKPSARSVF 245

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42572263  351 AAAVhAERFLLIFGG------GSH---ATCFDDLHVLDLQTMEWSRPAQQGDAPTPRAGHAGVTI---GENWFIVGGG 416
Cdd:PLN02153 246 AHAV-VGKYIIIFGGevwpdlKGHlgpGTLSNEGYALDTETLVWEKLGECGEPAMPRGWTAYTTAtvyGKNGLLMHGG 322
PLN02193 PLN02193
nitrile-specifier protein
 163-416 1.55e-12

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 70.37  E-value: 1.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  163 SNTVSVYNQWTAPQTSGQRPKARYEHGAAVIQDKMYIYGGNHNGRYLGD--LHVLDLKSWTWS----------------- 223
Cdd:PLN02193 144 PSTPKLLGKWIKVEQKGEGPGLRCSHGIAQVGNKIYSFGGEFTPNQPIDkhLYVFDLETRTWSispatgdvphlsclgvr 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  224 -----------------------------RVETKVATESQETSTPTllapcAGHSLIAWDNKLLSIGGhtkdPSESMQVK 274
Cdd:PLN02193 224 mvsigstlyvfggrdasrqyngfysfdttTNEWKLLTPVEEGPTPR-----SFHSMAADEENVYVFGG----VSATARLK 294

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  275 VFDPHTI---TWSMLKTYGKPPVSRGGQSVTMV-GKTLVIFGGQDAKrslLNDLHILDLDTMTWDEIDAVGVSPSPRSDH 350
Cdd:PLN02193 295 TLDSYNIvdkKWFHCSTPGDSFSIRGGAGLEVVqGKVWVVYGFNGCE---VDDVHYYDPVQDKWTQVETFGVRPSERSVF 371

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  351 AAAVHAeRFLLIFGGG------SH---ATCFDDLHVLDLQTMEWSRPAQQG---DAPTPR---AGHAGVTIGENWFIVGG 415
Cdd:PLN02193 372 ASAAVG-KHIVIFGGEiamdplAHvgpGQLTDGTFALDTETLQWERLDKFGeeeETPSSRgwtASTTGTIDGKKGLVMHG 450


                 .
gi 42572263  416 G 416
Cdd:PLN02193 451 G 451
PHA03098 PHA03098
kelch-like protein; Provisional
 185-438 4.27e-11

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 65.94  E-value: 4.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  185 RYEHGAAVIQDKMYIYGG-NHNGRYLGDLHVLDLKSwtwsrvetkvateSQETSTPTLLAPCAGHSLIAWDNKLLSIGGH 263
Cdd:PHA03098 285 VYCFGSVVLNNVIYFIGGmNKNNLSVNSVVSYDTKT-------------KSWNKVPELIYPRKNPGVTVFNNRIYVIGGI 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  264 TKDPSESmQVKVFDPHTITWSMLKTYGKPpvsRGGQSVTMVGKTLVIFGGQDAKRSLLNDLHILDLDTMTWDEIDAvgvS 343
Cdd:PHA03098 352 YNSISLN-TVESWKPGESKWREEPPLIFP---RYNPCVVNVNNLIYVIGGISKNDELLKTVECFSLNTNKWSKGSP---L 424

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  344 PSPRSDHAAAVHAErFLLIFGGGSHAT---CFDDLHVLDLQTMEWSRPAQQGdapTPRaGHAGVTIGENWFIVGGGD-NK 419
Cdd:PHA03098 425 PISHYGGCAIYHDG-KIYVIGGISYIDnikVYNIVESYNPVTNKWTELSSLN---FPR-INASLCIFNNKIYVVGGDkYE 499

                        250
                 ....*....|....*....
gi 42572263  420 SGASESVVLNMSTLAWSVV 438
Cdd:PHA03098 500 YYINEIEVYDDKTNTWTLF 518
ACB COG4281
Acyl-CoA-binding protein [Lipid transport and metabolism];
14-99 7.56e-11

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


Pssm-ID: 443422  Cd Length: 87  Bit Score: 58.71  E-value: 7.56e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  14 ERFYAAASYVgldgsdssaKNVISKFPDDTALLLYALYQQATVGPCNTPKPSAWRPVEQSKWKSWQGLGTMPSIEAMRLF 93
Cdd:COG4281   6 AAFEAAVARV---------KTLTERPDNDTLLKLYALYKQATEGDVTGKRPGMTDFVGRAKYDAWAQLKGMSKDEAMQQY 76


                ....*.
gi 42572263  94 VKILEE 99
Cdd:COG4281  77 IDLVNS 82
PLN02153 PLN02153
epithiospecifier protein
 148-365 4.37e-10

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 61.93  E-value: 4.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  148 GRLAETQDKDVVSEDSntvsVYNQWTAPQTSGQR--PKARYEHGAAVIQDKMYIYGGNHNG---------RYLGDLHVLD 216
Cdd:PLN02153  93 GRDEKREFSDFYSYDT----VKNEWTFLTKLDEEggPEARTFHSMASDENHVYVFGGVSKGglmktperfRTIEAYNIAD 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  217 LKswtWsrVETKVATESQETSTPTLLAPCAGHSLIAWDNKLLSIGGhTKDPSESMQVKVFDPHTITWSMLKTYGKPPVSR 296
Cdd:PLN02153 169 GK---W--VQLPDPGENFEKRGGAGFAVVQGKIWVVYGFATSILPG-GKSDYESNAVQFFDPASGKWTEVETTGAKPSAR 242

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  297 GGQSVTMVGKTLVIFGGQ---DAKR-----SLLNDLHILDLDTMTWDEIDAVGVSPSPR---SDHAAAVHAERFLLIFGG 365
Cdd:PLN02153 243 SVFAHAVVGKYIIIFGGEvwpDLKGhlgpgTLSNEGYALDTETLVWEKLGECGEPAMPRgwtAYTTATVYGKNGLLMHGG 322
PLN02193 PLN02193
nitrile-specifier protein
 231-415 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 42572263  231 TESQETSTPTLLAPcaGHSLIAWDNKLLSIGGHTKDPSESMQVKVFDPHTI----TWSMLKTYGKPPVSRGGQSVTMVGK 306
Cdd:PLN02193  99 TYKGKTSHPIEKRP--GVKFVLQGGKIVGFHGRSTDVLHSLGAYISLPSTPkllgKWIKVEQKGEGPGLRCSHGIAQVGN 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  307 TLVIFGGQ-DAKRSLLNDLHILDLDTMTWDEIDAVGVSPSPRSDHAAAVHAERFLLIFGGGSHATCFDDLHVLDLQTMEW 385
Cdd:PLN02193 177 KIYSFGGEfTPNQPIDKHLYVFDLETRTWSISPATGDVPHLSCLGVRMVSIGSTLYVFGGRDASRQYNGFYSFDTTTNEW 256

                        170       180       190
                 ....*....|....*....|....*....|..
gi 42572263  386 S--RPAQQGdaPTPRAGHAGVTIGENWFIVGG 415
Cdd:PLN02193 257 KllTPVEEG--PTPRSFHSMAADEENVYVFGG 286
PTZ00458 PTZ00458
acyl CoA binding protein; Provisional
 40-104 5.85e-09

acyl CoA binding protein; Provisional


Pssm-ID: 185637  Cd Length: 90  Bit Score: 53.67  E-value: 5.85e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42572263   40 PDDTALLLYALYQQATVGPCNTPKPSAWRPVEQSKWKSWQGLGTMPSIEAMRLFVKILEEDDPGW 104
Cdd:PTZ00458  22 SVEIKLDLYKYYKQSTVGNCNIKEPSMFKYQDRKKYEAWKSIENLNREDAKKRYVEIVTELFPNW 86
PLN02193 PLN02193
nitrile-specifier protein
 142-375 9.16e-09

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 58.43  E-value: 9.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  142 TISTENGRLAETQDKDVVSEDSNTvsvyNQWTAPQTSGQRPKARYEHGAAVIQDKMYIYGGNHNGRYLGDLHVLDLKSWT 221
Cdd:PLN02193 230 TLYVFGGRDASRQYNGFYSFDTTT----NEWKLLTPVEEGPTPRSFHSMAADEENVYVFGGVSATARLKTLDSYNIVDKK 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  222 WSrvetkvatesqETSTP-TLLAPCAGHSLIAWDNKLLSIGGHtkDPSESMQVKVFDPHTITWSMLKTYGKPPVSRGGQS 300
Cdd:PLN02193 306 WF-----------HCSTPgDSFSIRGGAGLEVVQGKVWVVYGF--NGCEVDDVHYYDPVQDKWTQVETFGVRPSERSVFA 372

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  301 VTMVGKTLVIFGGQDAKR--------SLLNDLHILDLDTMTWDEIDAVGV---SPSPR---SDHAAAVHAERFLLIFGGG 366
Cdd:PLN02193 373 SAAVGKHIVIFGGEIAMDplahvgpgQLTDGTFALDTETLQWERLDKFGEeeeTPSSRgwtASTTGTIDGKKGLVMHGGK 452

                        250
                 ....*....|
gi 42572263  367 SHAT-CFDDL 375
Cdd:PLN02193 453 APTNdRFDDL 462
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 552-647 2.07e-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: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263   552 KSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELR----QKLQTLETLQKE 627
Cdd:pfam19220  47 KSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRielrDKTAQAEALERQ 126

                          90       100
                  ....*....|....*....|....*...
gi 42572263   628 L--------ELLQRQKAASEQAAMNAKR 647
Cdd:pfam19220 127 LaaeteqnrALEEENKALREEAQAAEKA 154
Kelch_3 pfam13415
Galactose oxidase, central domain;
305-355 6.31e-08

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 49.21  E-value: 6.31e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 42572263   305 GKTLVIFGGQDAKRS-LLNDLHILDLDTMTWDEIdavGVSPSPRSDHAAAVH 355
Cdd:pfam13415   1 GDKLYIFGGLGFDGQtRLNDLYVYDLDTNTWTQI---GDLPPPRSGHSATYI 49
Kelch_3 pfam13415
Galactose oxidase, central domain;
357-406 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 42572263   357 ERFLLIFGG--GSHATCFDDLHVLDLQTMEWSRPaqqGDAPTPRAGHAGVTI 406
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 ...
 184-225 3.91e-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: 3.91e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 42572263   184 ARYEHGAAVIQDKMYIYGGNHNGRYLGDLHVLDLKSWTWSRV 225
Cdd:pfam01344   1 RRSGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSKL 42
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
485-648 5.11e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.85  E-value: 5.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 485 SHKSTLQtKTLEAPLPGSLSAvnnattrdiESEVEVSQEGRVREIVMDNVNPGS---KVEGNSERIIATIKSEKEELEAS 561
Cdd:COG4717  34 AGKSTLL-AFIRAMLLERLEK---------EADELFKPQGRKPELNLKELKELEeelKEAEEKEEEYAELQEELEELEEE 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 562 LN--KERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLETLQKELELLQRQKAASE 639
Cdd:COG4717 104 LEelEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELL 183


                ....*....
gi 42572263 640 QAAMNAKRQ 648
Cdd:COG4717 184 EQLSLATEE 192
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 512-642 8.12e-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: 8.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263   512 RDIESEVEVSQEGRVREIVMDNVNPGSKV---EGNSERIIATIK---SEKEELEAslnkERMQtLQLRQELGEAELRNtd 585
Cdd:pfam07888 117 KDALLAQRAAHEARIRELEEDIKTLTQRVlerETELERMKERAKkagAQRKEEEA----ERKQ-LQAKLQQTEEELRS-- 189

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42572263   586 LYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQT-------LETLQKELELLQRQKAASEQAA 642
Cdd:pfam07888 190 LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTahrkeaeNEALLEELRSLQERLNASERKV 253
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
548-648 1.29e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.06  E-value: 1.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 548 IATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLETLQKE 627
Cdd:COG4372  54 LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ 133

                        90       100
                ....*....|....*....|....*
gi 42572263 628 LE----LLQRQKAASEQAAMNAKRQ 648
Cdd:COG4372 134 LEaqiaELQSEIAEREEELKELEEQ 158
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
548-648 3.30e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.90  E-value: 3.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 548 IATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTL----ET 623
Cdd:COG4372  40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELqeelEE 119

                        90       100
                ....*....|....*....|....*
gi 42572263 624 LQKELELLQRQKAASEQAAMNAKRQ 648
Cdd:COG4372 120 LQKERQDLEQQRKQLEAQIAELQSE 144
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 182-220 5.85e-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: 5.85e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 42572263   182 PKARYEHGAAVIQDKMYIYGGNH--NGRYLGDLHVLDLKSW 220
Cdd:pfam13854   1 PVPRYGHCAVTVGDYIYLYGGYTggEGQPSDDVYVLSLPTF 41
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 545-648 1.22e-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: 1.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 545 ERIIATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRcfkLEVDVAELRQKLQTLETL 624
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD---IARLEERRRELEERLEEL 321

                        90       100
                ....*....|....*....|....
gi 42572263 625 QKELELLQRQKAASEQAAMNAKRQ 648
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEE 345
PHA03098 PHA03098
kelch-like protein; Provisional
 155-386 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 42572263  155 DKDVVSEDSNTvsvyNQW-TAPQTSgqrpKARYEHGAAVIQDKMYIYGGNHNGRYLgdlhvldlkswtwSRVETKVATES 233
Cdd:PHA03098 310 VNSVVSYDTKT----KSWnKVPELI----YPRKNPGVTVFNNRIYVIGGIYNSISL-------------NTVESWKPGES 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  234 QETSTPTLLAPCAGHSLIAWDNKLLSIGGHTKDPSESMQVKVFDPHTITWSMLKTYgkpPVSRGGQSVTMVGKTLVIFGG 313
Cdd:PHA03098 369 KWREEPPLIFPRYNPCVVNVNNLIYVIGGISKNDELLKTVECFSLNTNKWSKGSPL---PISHYGGCAIYHDGKIYVIGG 445

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42572263  314 ----QDAKRslLNDLHILDLDTMTWDEIDAVGVspsPRSDhAAAVHAERFLLIFGGGSHATCFDDLHVLDLQTMEWS 386
Cdd:PHA03098 446 isyiDNIKV--YNIVESYNPVTNKWTELSSLNF---PRIN-ASLCIFNNKIYVVGGDKYEYYINEIEVYDDKTNTWT 516
Kelch_6 pfam13964
Kelch motif;
298-337 1.77e-05

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 42.32  E-value: 1.77e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 42572263   298 GQSVTMVGKTLVIFGGQDAKRSLLNDLHILDLDTMTWDEI 337
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 ...
 544-641 2.02e-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: 47.86  E-value: 2.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263    544 SERIiATIKSEK------EELEAslnkermqtlqLRQELgEAELRNTDLYKELQSVRGQLAAEQSRCFK-----LEVDVA 612
Cdd:pfam01576  282 SERA-ARNKAEKqrrdlgEELEA-----------LKTEL-EDTLDTTAAQQELRSKREQEVTELKKALEeetrsHEAQLQ 348

                           90       100       110
                   ....*....|....*....|....*....|
gi 42572263    613 ELRQK-LQTLETLQKELELLQRQKAASEQA 641
Cdd:pfam01576  349 EMRQKhTQALEELTEQLEQAKRNKANLEKA 378
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
392-481 2.22e-05

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 46.69  E-value: 2.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 392 GDAPTPRAGHAGVTIGENWFIVGGGDNKSGASESVVLNMSTLAWSVVASvqgrVPLASEGLSLVVsSYNGEdVLVaFGGY 471
Cdd:COG3055   7 PDLPTPRSEAAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTWSELAP----LPGPPRHHAAAV-AQDGK-LYV-FGGF 79

                        90
                ....*....|
gi 42572263 472 NGRYNNEINL 481
Cdd:COG3055  80 TGANPSSTPL 89
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 539-651 4.56e-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: 4.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263   539 KVEGNSERIIATIKSEKEELEAslNKERMQTLQLRQEL----GEAELRNTDLYkELQSVRGQLAAEQSRCFKLEVDVAEL 614
Cdd:pfam04012  40 KARQALAQTIARQKQLERRLEQ--QTEQAKKLEEKAQAaltkGNEELAREALA-EKKSLEKQAEALETQLAQQRSAVEQL 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 42572263   615 RQKLQTLETLQKELE-----LLQRQKAASEQAAMNAKRQGSG 651
Cdd:pfam04012 117 RKQLAALETKIQQLKakknlLKARLKAAKAQEAVQTSLGSLS 158
Kelch_4 pfam13418
Galactose oxidase, central domain;
184-228 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 42572263   184 ARYEHGAAVIQDKM-YIYGG-NHNGRYLGDLHVLDLKSWTWSRVETK 228
Cdd:pfam13418   1 PRAYHTSTSIPDDTiYLFGGeGEDGTLLSDLWVFDLSTNEWTRLGSL 47
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
539-632 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 42572263  539 KVEGNSERIIATIKSEKEELEASLNKERMQTLQLRQELGEA--------ELRN--TDLYKELQSVRGQLAAEQSRCFKLE 608
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLekevkeleELKEeiEELEKELESLEGSKRKLEEKIRELE 265

                         90       100
                 ....*....|....*....|....
gi 42572263  609 VDVAELRQKLQTLETLQKELELLQ 632
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELK 289
Kelch_4 pfam13418
Galactose oxidase, central domain;
346-387 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 42572263   346 PRSDHAAAVHAERFLLIFGG-GSHATCFDDLHVLDLQTMEWSR 387
Cdd:pfam13418   1 PRAYHTSTSIPDDTIYLFGGeGEDGTLLSDLWVFDLSTNEWTR 43
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
514-640 1.41e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  514 IESEVEvSQEGR---VREIVmdNVNPGSKVEGNSERIIATIKSEKEELEaslnKERMQTLQLRQELGEAELRNTDLYKEL 590
Cdd:PRK03918 137 IDAILE-SDESRekvVRQIL--GLDDYENAYKNLGEVIKEIKRRIERLE----KFIKRTENIEELIKEKEKELEEVLREI 209

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 42572263  591 QSVRGQLAaeqsrcfKLEVDVAELRQKLQTLETLQKELELLQRQKAASEQ 640
Cdd:PRK03918 210 NEISSELP-------ELREELEKLEKEVKELEELKEEIEELEKELESLEG 252
Kelch_3 pfam13415
Galactose oxidase, central domain;
195-252 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 42572263   195 DKMYIYGGNH--NGRYLGDLHVLDLKSWTWsrvetkvatesqeTSTPTLLAPCAGHSLIA 252
Cdd:pfam13415   2 DKLYIFGGLGfdGQTRLNDLYVYDLDTNTW-------------TQIGDLPPPRSGHSATY 48
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
548-646 1.85e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 1.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 548 IATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSV----------RGQLAAEQSrcfKLEVDVAELRQK 617
Cdd:COG4372  75 LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELqkerqdleqqRKQLEAQIA---ELQSEIAEREEE 151

                        90       100       110
                ....*....|....*....|....*....|...
gi 42572263 618 LQTLET----LQKELELLQRQKAASEQAAMNAK 646
Cdd:COG4372 152 LKELEEqlesLQEELAALEQELQALSEAEAEQA 184
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 545-650 2.09e-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: 2.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263    545 ERIIATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSvrgqLAAEQSRcfkLEVDVAELRQKLQTLETL 624
Cdd:TIGR02168  245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA----LANEISR---LEQQKQILRERLANLERQ 317

                           90       100       110
                   ....*....|....*....|....*....|.
gi 42572263    625 QKELE-----LLQRQKAASEQAAMNAKRQGS 650
Cdd:TIGR02168  318 LEELEaqleeLESKLDELAEELAELEEKLEE 348
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 548-648 2.99e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 2.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 548 IATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKL----QTLET 623
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELeeleEELEE 341

                        90       100
                ....*....|....*....|....*
gi 42572263 624 LQKELELLQRQKAASEQAAMNAKRQ 648
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEA 366
Kelch_6 pfam13964
Kelch motif;
244-296 3.09e-04

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 38.86  E-value: 3.09e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 42572263   244 PCAGHSLIAWDNKLLSIGGHTKDPSESMQVKVFDPHTITWsmlKTYGKPPVSR 296
Cdd:pfam13964   1 PRTFHSVVSVGGYIYVFGGYTNASPALNKLEVYNPLTKSW---EELPPLPTPR 50
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 548-645 3.26e-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: 42.60  E-value: 3.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 548 IATIKSEKEELEASLNKermqtlqLRQELGEAElrntdlyKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLET---- 623
Cdd:COG1579  19 LDRLEHRLKELPAELAE-------LEDELAALE-------ARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgn 84

                        90       100       110
                ....*....|....*....|....*....|.
gi 42572263 624 ---------LQKELELLQRQKAASEQAAMNA 645
Cdd:COG1579  85 vrnnkeyeaLQKEIESLKRRISDLEDEILEL 115
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 550-648 3.37e-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: 3.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 550 TIKSEKEELEASLNKERMQTLQ-----LRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKL----QT 620
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEaeleeLEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellAE 296

                        90       100
                ....*....|....*....|....*...
gi 42572263 621 LETLQKELELLQRQKAASEQAAMNAKRQ 648
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEE 324
Kelch_4 pfam13418
Galactose oxidase, central domain;
296-337 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 42572263   296 RGGQSVTMVGK-TLVIFGGQDAKRSLLNDLHILDLDTMTWDEI 337
Cdd:pfam13418   2 RAYHTSTSIPDdTIYLFGGEGEDGTLLSDLWVFDLSTNEWTRL 44
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
551-647 4.41e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 4.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 551 IKSEKEELEASLNKERMQTLQLRQELGEAELRntdlyKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLETLQKELEL 630
Cdd:COG4717 400 LKEELEELEEQLEELLGELEELLEALDEEELE-----EELEELEEELEELEEELEELREELAELEAELEQLEEDGELAEL 474

                        90
                ....*....|....*..
gi 42572263 631 LQRQKAASEQAAMNAKR 647
Cdd:COG4717 475 LQELEELKAELRELAEE 491
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 538-648 5.25e-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: 5.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 538 SKVEGNSERIIATIKSEKEELEASLNKER---MQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAEL 614
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYellAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342

                        90       100       110
                ....*....|....*....|....*....|....
gi 42572263 615 RQKLQTLEtlqKELELLQRQKAASEQAAMNAKRQ 648
Cdd:COG1196 343 EEELEEAE---EELEEAEAELAEAEEALLEAEAE 373
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
548-644 5.30e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.08  E-value: 5.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 548 IATIKSEKEELEASLNKErmqtlqLRQELGEAELRNTDLYKELQSVRGQLAAEQSRcfklevdVAELRQKLQTLETLQKE 627
Cdd:COG3206 293 VIALRAQIAALRAQLQQE------AQRILASLEAELEALQAREASLQAQLAQLEAR-------LAELPELEAELRRLERE 359

                        90       100
                ....*....|....*....|....*
gi 42572263 628 LE--------LLQRQKAASEQAAMN 644
Cdd:COG3206 360 VEvarelyesLLQRLEEARLAEALT 384
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 551-648 5.34e-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: 5.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 551 IKSEKEELEASLN--KERMQTL-----QLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLET 623
Cdd:COG1196 293 LLAELARLEQDIArlEERRRELeerleELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                        90       100
                ....*....|....*....|....*
gi 42572263 624 LQKELELLQRQKAASEQAAMNAKRQ 648
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAE 397
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 553-642 5.46e-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: 5.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 553 SEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLETLQKELE--L 630
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRaeL 99

                        90
                ....*....|..
gi 42572263 631 LQRQKAASEQAA 642
Cdd:COG4942 100 EAQKEELAELLR 111
Kelch_6 pfam13964
Kelch motif;
184-225 6.21e-04

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 38.09  E-value: 6.21e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 42572263   184 ARYEHGAAVIQDKMYIYGGNHN-GRYLGDLHVLDLKSWTWSRV 225
Cdd:pfam13964   1 PRTFHSVVSVGGYIYVFGGYTNaSPALNKLEVYNPLTKSWEEL 43
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 548-648 8.61e-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: 8.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263    548 IATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQ-------- 619
Cdd:TIGR02168  360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaelkelq 439

                           90       100       110
                   ....*....|....*....|....*....|
gi 42572263    620 -TLETLQKELELLQRQKAASEQAAMNAKRQ 648
Cdd:TIGR02168  440 aELEELEEELEELQEELERLEEALEELREE 469
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 543-648 8.84e-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: 8.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 543 NSERIIATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRcfKLEVDVAELRQKLQTLE 622
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE--LAEAEEELEELAEELLE 390

                        90       100
                ....*....|....*....|....*.
gi 42572263 623 TLQKELELLQRQKAASEQAAMNAKRQ 648
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERL 416
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 548-648 8.91e-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: 8.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 548 IATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLETLQKE 627
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418

                        90       100
                ....*....|....*....|.
gi 42572263 628 LELLQRQKAASEQAAMNAKRQ 648
Cdd:COG1196 419 LEEELEELEEALAELEEEEEE 439
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 556-646 9.17e-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: 9.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263   556 EELEASLNKERMQTLQLRQELGEAElrntdlyKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLETLQKELELLQRQK 635
Cdd:pfam12795  81 EELEQRLLQTSAQLQELQNQLAQLN-------SQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWA 153

                          90
                  ....*....|.
gi 42572263   636 AASEQAAMNAK 646
Cdd:pfam12795 154 LQAELAALKAQ 164
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 548-648 1.34e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 1.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 548 IATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLE-TLQK 626
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEeAEEA 411

                        90       100
                ....*....|....*....|..
gi 42572263 627 ELELLQRQKAASEQAAMNAKRQ 648
Cdd:COG1196 412 LLERLERLEEELEELEEALAEL 433
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 545-656 1.45e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 1.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 545 ERIIATIKSEKEELEaslnkermqtlQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRC----FKLEVDVAELRQKLQT 620
Cdd:COG4942 149 REQAEELRADLAELA-----------ALRAELEAERAELEALLAELEEERAALEALKAERqkllARLEKELAELAAELAE 217

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 42572263 621 L----ETLQKELELLQRQKAASEQAAMNAKRQGSGGVWGW 656
Cdd:COG4942 218 LqqeaEELEALIARLEAEAAAAAERTPAAGFAALKGKLPW 257
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
548-648 1.52e-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: 1.52e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 548 IATIKSEKEELEASLNKERMQTLQLRQELGEAE-LRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLETLQK 626
Cdd:COG3206 272 LAELEAELAELSARYTPNHPDVIALRAQIAALRaQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEA 351

                        90       100
                ....*....|....*....|....
gi 42572263 627 ELELLQRQKAASEQA--AMNAKRQ 648
Cdd:COG3206 352 ELRRLEREVEVARELyeSLLQRLE 375
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 344-382 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 42572263   344 PSPRSDHAAAVHAERfLLIFGGGSHAT--CFDDLHVLDLQT 382
Cdd:pfam13854   1 PVPRYGHCAVTVGDY-IYLYGGYTGGEgqPSDDVYVLSLPT 40
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 551-648 1.72e-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: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263   551 IKSEKEELEASLNK--ERMQTLQLRqeLGEAELRNTDLYKELQSVR--GQLAAEQSRCFK------------LEVDVAEL 614
Cdd:pfam05911 693 LKSEKENLEVELASctENLESTKSQ--LQESEQLIAELRSELASLKesNSLAETQLKCMAesyedletrlteLEAELNEL 770

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 42572263   615 RQKLQTLET-LQKE-----------LEL-LQRQKAASEQAAMNAKRQ 648
Cdd:pfam05911 771 RQKFEALEVeLEEEkncheeleakcLELqEQLERNEKKESSNCDADQ 817
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 543-634 1.96e-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: 1.96e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 543 NSERIIATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTL- 621
Cdd:COG4942  24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQk 103

                        90
                ....*....|...
gi 42572263 622 ETLQKELELLQRQ 634
Cdd:COG4942 104 EELAELLRALYRL 116
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 541-648 2.00e-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: 2.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263    541 EGNSERIIATIKSEKEELEASLNKERMQTLQLRQELGEAElrntdlyKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQT 620
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE-------AEIEELEAQIEQLKEELKALREALDELRAELTL 814

                           90       100       110
                   ....*....|....*....|....*....|..
gi 42572263    621 LE----TLQKELELLQRQKAASEQAAMNAKRQ 648
Cdd:TIGR02168  815 LNeeaaNLRERLESLERRIAATERRLEDLEEQ 846
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 508-646 2.05e-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: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263    508 NATTRDIES-EVEVSQEGRVREIVMDNVNPGSKVEGNSERIIATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDL 586
Cdd:TIGR02169  290 LRVKEKIGElEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDL 369

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42572263    587 YKELQSVrgqlaaeqsrcfklEVDVAELRQKL----QTLETLQKELELLQR---------QKAASEQAAMNAK 646
Cdd:TIGR02169  370 RAELEEV--------------DKEFAETRDELkdyrEKLEKLKREINELKReldrlqeelQRLSEELADLNAA 428
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 567-647 2.09e-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: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263   567 MQTLQLRQELGEAELRNT-------DLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQ-----------TLETLQKEL 628
Cdd:pfam08614  57 QLLAQLREELAELYRSRGelaqrlvDLNEELQELEKKLREDERRLAALEAERAQLEEKLKdreeelrekrkLNQDLQDEL 136

                          90
                  ....*....|....*....
gi 42572263   629 ELLQRQKAASEQAAMNAKR 647
Cdd:pfam08614 137 VALQLQLNMAEEKLRKLEK 155
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
548-641 2.14e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 2.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 548 IATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLETLQKE 627
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE 182

                        90
                ....*....|....
gi 42572263 628 LELLQRQKAASEQA 641
Cdd:COG4372 183 QALDELLKEANRNA 196
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 545-648 2.16e-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: 2.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263    545 ERIIATIKSEKEELEASLNK---------ERMQTLQLRQElgEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELR 615
Cdd:TIGR02169  804 EEEVSRIEARLREIEQKLNRltlekeyleKEIQELQEQRI--DLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLE 881

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 42572263    616 QKLQTLET----LQKELELLQR----QKAASEQAAMNAKRQ 648
Cdd:TIGR02169  882 SRLGDLKKerdeLEAQLRELERkieeLEAQIEKKRKRLSEL 922
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
545-635 2.20e-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: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  545 ERIIATIKSEKEELEASLNK--ERMQTLQLRQELGEAELrnTDLYKELQSVRGQLAAEQSRC----FKLEVDVAELRQKl 618
Cdd:COG4913  344 EREIERLERELEERERRRARleALLAALGLPLPASAEEF--AALRAEAAALLEALEEELEALeealAEAEAALRDLRRE- 420

                         90
                 ....*....|....*..
gi 42572263  619 qtLETLQKELELLQRQK 635
Cdd:COG4913  421 --LRELEAEIASLERRK 435
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 541-641 2.74e-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: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  541 EGNSERIIATIKSEKEELEASLNKERMQTLQLRQELGEAE---------------LRNTDLYKELQSVRGQL-AAEQSRC 604
Cdd:COG3096  831 APDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKeqlqllnkllpqanlLADETLADRLEELREELdAAQEAQA 910

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 42572263  605 F---------KLEVDVAELRQKLQTLETLQKE-LELLQRQKAASEQA 641
Cdd:COG3096  911 FiqqhgkalaQLEPLVAVLQSDPEQFEQLQADyLQAKEQQRRLKQQI 957
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 545-648 3.01e-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: 40.81  E-value: 3.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263    545 ERIIATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSrcfKLEVDVAELRQKLQTLETL 624
Cdd:TIGR02168  336 AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL---QIASLNNEIERLEARLERL 412

                           90       100
                   ....*....|....*....|....
gi 42572263    625 QKELELLQRQKAASEQAAMNAKRQ 648
Cdd:TIGR02168  413 EDRRERLQQEIEELLKKLEEAELK 436
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 555-650 3.21e-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: 40.44  E-value: 3.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263   555 KEE---LEASLNKERMQTLQLRQELGEAELRNTDLYKelqsvrgqlAAEQSRCFKLEVDVaeLRQ------KL-QTLETL 624
Cdd:pfam05622  72 QEEnfrLETARDDYRIKCEELEKEVLELQHRNEELTS---------LAEEAQALKDEMDI--LREssdkvkKLeATVETY 140

                          90       100       110
                  ....*....|....*....|....*....|
gi 42572263   625 QKELEL---LQRQ-KAASEQAAMNAKRQGS 650
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 ...
 538-635 3.36e-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: 3.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263    538 SKVEGNSERIIATIKSEKEELEASLNkermQTLQLRQELGEaelRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQK 617
Cdd:pfam01576  397 QQAKQDSEHKRKKLEGQLQELQARLS----ESERQRAELAE---KLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQ 469

                           90
                   ....*....|....*....
gi 42572263    618 LQ-TLETLQKElellQRQK 635
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 ...
 346-387 3.76e-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: 3.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 42572263   346 PRSDHAAAVHAERfLLIFGGGSHATCFDDLHVLDLQTMEWSR 387
Cdd:pfam01344   1 RRSGAGVVVVGGK-IYVIGGFDGNQSLNSVEVYDPETNTWSK 41
Kelch_2 pfam07646
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 185-225 3.94e-03

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


Pssm-ID: 462220 [Multi-domain]  Cd Length: 47  Bit Score: 35.77  E-value: 3.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 42572263   185 RYEHGAAVIQDKMYIYGG--NHNGRYLGDLHVLDLKSWTWSRV 225
Cdd:pfam07646   2 RYPHASSVPGGKLYVVGGsdGLGDLSSSDVLVYDPETNVWTEV 44
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 505-652 4.16e-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: 4.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263    505 AVNNATTRDIESEVEVSQEGRVREIvmdnvnpgskveGNSERIIATIKSEKEELEASLNKERMQTLQLRQELGEAELRNT 584
Cdd:TIGR02169  377 DKEFAETRDELKDYREKLEKLKREI------------NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE 444

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42572263    585 DLYKELQSVRGQLAAEQSRCFKLEvdvAELRQKLQTLETLQKELELLQRQKAASEqAAMNAKRQGSGG 652
Cdd:TIGR02169  445 DKALEIKKQEWKLEQLAADLSKYE---QELYDLKEEYDRVEKELSKLQRELAEAE-AQARASEERVRG 508
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 523-640 4.20e-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: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263   523 EGRVREIVMdnvnpgskVEGNSERII---ATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQsvrgqlaA 599
Cdd:pfam10473  27 ENLERELEM--------SEENQELAIleaENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSEKENLTKELQ-------K 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 42572263   600 EQSRCFKLEVDVAELRQKLQTLEtlQKELELLQRQKAASEQ 640
Cdd:pfam10473  92 KQERVSELESLNSSLENLLEEKE--QEKVQMKEESKTAVEM 130
Kelch_2 pfam07646
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 244-284 4.44e-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: 4.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 42572263   244 PCAGHSLIAWDNKLLSIGGHTKDPSE-SMQVKVFDPHTITWS 284
Cdd:pfam07646   1 PRYPHASSVPGGKLYVVGGSDGLGDLsSSDVLVYDPETNVWT 42
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 538-649 4.45e-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: 4.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263    538 SKVEGNSERIIATIKsEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQK 617
Cdd:TIGR02168  824 ERLESLERRIAATER-RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902

                           90       100       110
                   ....*....|....*....|....*....|..
gi 42572263    618 LQTLETLQKELElLQRQKAASEQAAMNAKRQG 649
Cdd:TIGR02168  903 LRELESKRSELR-RELEELREKLAQLELRLEG 933
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
545-648 5.20e-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: 5.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  545 ERIIATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRG----QLAAEQSRcfkLEVDVAELRQKLQT 620
Cdd:COG4913  287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGdrleQLEREIER---LERELEERERRRAR 363

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 42572263  621 LETLQKELEL--------LQRQKAASEQAAMNAKRQ 648
Cdd:COG4913  364 LEALLAALGLplpasaeeFAALRAEAAALLEALEEE 399
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 551-640 6.21e-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: 6.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263    551 IKSEKEELEASLNKERMQTL-----QLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTL---- 621
Cdd:TIGR02168  218 LKAELRELELALLVLRLEELreeleELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALanei 297

                           90
                   ....*....|....*....
gi 42572263    622 ETLQKELELLQRQKAASEQ 640
Cdd:TIGR02168  298 SRLEQQKQILRERLANLER 316
mukB PRK04863
chromosome partition protein MukB;
541-648 6.34e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 6.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263   541 EGNSERIIATIKSEKEELEASLNKERMQTLQLRQELGEAE---------------LRNTDLYKELQSVRGQLA-AEQSRC 604
Cdd:PRK04863  832 EADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKeglsalnrllprlnlLADETLADRVEEIREQLDeAEEAKR 911

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 42572263   605 F--KLEVDVAELRQKLQTLETLQKELELLQRQKAASEQAAMNAKRQ 648
Cdd:PRK04863  912 FvqQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQ 957
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 511-648 7.17e-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: 39.67  E-value: 7.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263    511 TRDIESEVEV--SQEGRVREIVMDnvnpgSKVEGNS-ERIIATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTD-- 585
Cdd:TIGR02169  718 IGEIEKEIEQleQEEEKLKERLEE-----LEEDLSSlEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHsr 792

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42572263    586 ---LYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLETLQKELEllQRQKAASEQAAMNAKRQ 648
Cdd:TIGR02169  793 ipeIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ--EQRIDLKEQIKSIEKEI 856
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
551-646 7.34e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 7.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  551 IKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQ-----SRCFKLEVDVAELRQKLQTLE--- 622
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelrEEYLELSRELAGLRAELEELEkrr 689

                         90       100
                 ....*....|....*....|....*
gi 42572263  623 -TLQKELELLQRQKAASEQAAMNAK 646
Cdd:PRK03918 690 eEIKKTLEKLKEELEEREKAKKELE 714
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 556-635 7.41e-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: 39.34  E-value: 7.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263   556 EELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDvaELRQKLQTLETlqkELELLQRQK 635
Cdd:pfam05557 390 QKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVD--SLRRKLETLEL---ERQRLREQK 464
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 545-648 7.50e-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: 38.98  E-value: 7.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263 545 ERIIATIKSEKEELEASLNK------ERMQTLQLRQELGEAEL-----------RNTDLYKELQSVRGQLAAEqsrcfkL 607
Cdd:COG4942  82 EAELAELEKEIAELRAELEAqkeelaELLRALYRLGRQPPLALllspedfldavRRLQYLKYLAPARREQAEE------L 155

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 42572263 608 EVDVAELRQKLQTLETLQKELELLQRQKAAsEQAAMNAKRQ 648
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEE-ERAALEALKA 195
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
563-648 9.35e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 9.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572263  563 NKERMQTLQlrQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKL---------EVDV-------AELRQKLQTLETLQK 626
Cdd:COG4913  608 NRAKLAALE--AELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdEIDVasaereiAELEAELERLDASSD 685

                         90       100
                 ....*....|....*....|..
gi 42572263  627 ELELLQRQKAASEQAAMNAKRQ 648
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.
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