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Conserved domains on  [gi|57157855|dbj|BAD83881|]
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hypothetical protein 4-B-3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
48-336 4.76e-28

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 117.32  E-value: 4.76e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  48 VAFDGSGDSFIAGDHQGNIYVFDLH-GNRFNLVQRTAQACTALAFNlrRKSEFLV-ALADYSIKCFDTVTKELVSWMRGH 125
Cdd:COG2319 126 VAFSPDGKTLASGSADGTVRLWDLAtGKLLRTLTGHSGAVTSVAFS--PDGKLLAsGSDDGTVRLWDLATGKLLRTLTGH 203
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 126 ESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLFCKY 204
Cdd:COG2319 204 TGAVRSVAFSPDGKLLASGSADgTVRLWDLATGKLLRTLTGHSG-SVRSVAFSPDGRLLASGSADGTVRLWDLATGELLR 282
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 205 QLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQmpAKVRAVRHLEFLPDsfdagsNQVLGVLSQ 284
Cdd:COG2319 283 TLTGHSGGVNSV----AFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT--GHTGAVRSVAFSPD------GKTLASGSD 350
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 57157855 285 DGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQ 336
Cdd:COG2319 351 DGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
DUF5401 super family cl38662
Family of unknown function (DUF5401); This is a family of unknown function found in ...
688-832 5.14e-11

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


The actual alignment was detected with superfamily member pfam17380:

Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 66.30  E-value: 5.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   688 QTREWERIRNDELDflrERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEE----KMAQQRQRLAAVKR 763
Cdd:pfam17380 444 RAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEerkqAMIEEERKRKLLEK 520
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57157855   764 ELEIKEIHLQDAARRRLLKLQQ-DQREMELRRLEDEIERKVQMRDQEIAATAKDLE-IRQL-ELEAQKRLYE 832
Cdd:pfam17380 521 EMEERQKAIYEEERRREAEEERrKQQEMEERRRIQEQMRKATEERSRLEAMEREREmMRQIvESEKARAEYE 592
RabGAP-TBC super family cl46302
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
461-605 2.84e-09

Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are GTPase activator proteins of yeast Ypt6 and Ypt7, implies that these domains are GTPase activator proteins of Rab-like small GTPases.


The actual alignment was detected with superfamily member pfam00566:

Pssm-ID: 480642  Cd Length: 178  Bit Score: 57.26  E-value: 2.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   461 SLQKKYPIKSRKLLRVLQRTLSALAHWsaiFSDTPY---LPLLAFPFVkLFQNNQLICFEVVATLIINwcQHWFEYFPN- 536
Cdd:pfam00566  19 TFPHSFFFDNGPGQNSLRRILKAYSIY---NPDVGYcqgMNFIAAPLL-LVYLDEEDAFWCFVSLLEN--YLLRDFYTPd 92
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57157855   537 -PPINILSMI-ENVLAFHDKELLQHFIDRDITSQVYAWPLLETLFSEVLTREEWLRLFDNIFSNHPSFLLM 605
Cdd:pfam00566  93 fPGLKRDLYVfEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVLF 163
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
48-336 4.76e-28

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 117.32  E-value: 4.76e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  48 VAFDGSGDSFIAGDHQGNIYVFDLH-GNRFNLVQRTAQACTALAFNlrRKSEFLV-ALADYSIKCFDTVTKELVSWMRGH 125
Cdd:COG2319 126 VAFSPDGKTLASGSADGTVRLWDLAtGKLLRTLTGHSGAVTSVAFS--PDGKLLAsGSDDGTVRLWDLATGKLLRTLTGH 203
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 126 ESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLFCKY 204
Cdd:COG2319 204 TGAVRSVAFSPDGKLLASGSADgTVRLWDLATGKLLRTLTGHSG-SVRSVAFSPDGRLLASGSADGTVRLWDLATGELLR 282
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 205 QLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQmpAKVRAVRHLEFLPDsfdagsNQVLGVLSQ 284
Cdd:COG2319 283 TLTGHSGGVNSV----AFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT--GHTGAVRSVAFSPD------GKTLASGSD 350
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 57157855 285 DGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQ 336
Cdd:COG2319 351 DGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
39-334 7.45e-25

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 105.49  E-value: 7.45e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  39 HPKVLRFlnVAFDGSGDSFIAGDHQGNIYVFDLHGNRFNLVQR----TAQACTALAFNLRrkseFLVALADYSIKCFDTV 114
Cdd:cd00200   8 HTGGVTC--VAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKghtgPVRDVAASADGTY----LASGSSDKTIRLWDLE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 115 TKELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 193
Cdd:cd00200  82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDkTIKVWDVETGKCLTTLRGHTD-WVNSVAFSPDGTFVASSSQDGTIK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 194 AWECDTLFCKYQLPGpPEGSnilykVFAVT--RDGRILAAGGKSNHLHLWclEATGLFRIIQMPAKVRAVRHLEFLPDsf 271
Cdd:cd00200 161 LWDLRTGKCVATLTG-HTGE-----VNSVAfsPDGEKLLSSSSDGTIKLW--DLSTGKCLGTLRGHENGVNSVAFSPD-- 230
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57157855 272 dagsNQVLGVLSQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYS 334
Cdd:cd00200 231 ----GYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
688-832 5.14e-11

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 66.30  E-value: 5.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   688 QTREWERIRNDELDflrERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEE----KMAQQRQRLAAVKR 763
Cdd:pfam17380 444 RAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEerkqAMIEEERKRKLLEK 520
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57157855   764 ELEIKEIHLQDAARRRLLKLQQ-DQREMELRRLEDEIERKVQMRDQEIAATAKDLE-IRQL-ELEAQKRLYE 832
Cdd:pfam17380 521 EMEERQKAIYEEERRREAEEERrKQQEMEERRRIQEQMRKATEERSRLEAMEREREmMRQIvESEKARAEYE 592
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
688-830 8.99e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.65  E-value: 8.99e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 688 QTREWE-RIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELL---RRAEETRREILLQEEEKMAQQRQRLAAVKR 763
Cdd:COG1196 261 ELAELEaELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLeerRRELEERLEELEEELAELEEELEELEEELE 340
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57157855 764 ELEIKEIHLQDAARRRLLKLQQ--DQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRL 830
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEaeEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
461-605 2.84e-09

Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are GTPase activator proteins of yeast Ypt6 and Ypt7, implies that these domains are GTPase activator proteins of Rab-like small GTPases.


Pssm-ID: 459855  Cd Length: 178  Bit Score: 57.26  E-value: 2.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   461 SLQKKYPIKSRKLLRVLQRTLSALAHWsaiFSDTPY---LPLLAFPFVkLFQNNQLICFEVVATLIINwcQHWFEYFPN- 536
Cdd:pfam00566  19 TFPHSFFFDNGPGQNSLRRILKAYSIY---NPDVGYcqgMNFIAAPLL-LVYLDEEDAFWCFVSLLEN--YLLRDFYTPd 92
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57157855   537 -PPINILSMI-ENVLAFHDKELLQHFIDRDITSQVYAWPLLETLFSEVLTREEWLRLFDNIFSNHPSFLLM 605
Cdd:pfam00566  93 fPGLKRDLYVfEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVLF 163
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
693-836 1.44e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 55.46  E-value: 1.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855    693 ERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWyqkQELLRRAEETRREIL--LQEEEKMAQQ-RQRLAAVKRELE--I 767
Cdd:TIGR02169  322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKL---TEEYAELKEELEDLRaeLEEVDKEFAEtRDELKDYREKLEklK 398
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855    768 KEIHLQDAARRRLLKLQQdQREMELRRLEDEIER-----------------KVQMRDQEIAATAKDLEIRQLELEAQKRL 830
Cdd:TIGR02169  399 REINELKRELDRLQEELQ-RLSEELADLNAAIAGieakineleeekedkalEIKKQEWKLEQLAADLSKYEQELYDLKEE 477

                   ....*.
gi 57157855    831 YEKVES 836
Cdd:TIGR02169  478 YDRVEK 483
PRK12704 PRK12704
phosphodiesterase; Provisional
682-832 1.63e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 54.78  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  682 KFIVDYQTREWERIRNDEL-----DFLRERQTVENmqaEVDEQRAKdeawYQKQEL-LRRAEET---RREILLQEEEKMA 752
Cdd:PRK12704  41 KRILEEAKKEAEAIKKEALleakeEIHKLRNEFEK---ELRERRNE----LQKLEKrLLQKEENldrKLELLEKREEELE 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  753 QQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQ-------DQREMELRRLEDEIErkvqmrdQEIAATAKDLEiRQLELE 825
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEELEELIEEQLQELERisgltaeEAKEILLEKVEEEAR-------HEAAVLIKEIE-EEAKEE 185

                 ....*..
gi 57157855  826 AQKRLYE 832
Cdd:PRK12704 186 ADKKAKE 192
COG5210 COG5210
GTPase-activating protein [General function prediction only];
542-658 2.99e-05

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 47.49  E-value: 2.99e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 542 LSMIENVLAFHDKELLQHFIDRDITSQVYAWPLLETLFSEVLTREEWLRLFDNIFSNHPSFLLMTVVAYSTCSRAPLLNC 621
Cdd:COG5210 350 LKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKL 429
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 57157855 622 TLKNDFEYFFHHRNNLDINVVIREVYHLMETTPADIH 658
Cdd:COG5210 430 DSDELLDLLLKQLFLHSGKEAWSSILKFRHGTDRDIL 466
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
115-153 5.62e-05

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 41.14  E-value: 5.62e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 57157855    115 TKELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWD 153
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDgTIKLWD 40
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
501-609 1.30e-04

Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.


Pssm-ID: 214540 [Multi-domain]  Cd Length: 216  Bit Score: 44.22  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855    501 AFP-FVKLFQNNQLIcFEVVATLIINWCQHWFEYFpnppinilsmienvLAFHDKELLQHFIDRDITSQVYAWPLLETLF 579
Cdd:smart00164 112 AFWcLVKLMERYGPN-FYLPDMSGLQLDLLQLDRL--------------VKEYDPDLYKHLKDLGITPSLYALRWFLTLF 176
                           90       100       110
                   ....*....|....*....|....*....|
gi 57157855    580 SEVLTREEWLRLFDNIFSNHPSFLLMTVVA 609
Cdd:smart00164 177 ARELPLEIVLRIWDVLFAEGSDFLFRVALA 206
WD40 pfam00400
WD domain, G-beta repeat;
116-153 8.19e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 37.71  E-value: 8.19e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 57157855   116 KELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWD 153
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDgTVKVWD 39
ClassIIa_HDAC5_Gln-rich-N cd10164
Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase; This ...
703-799 5.99e-03

Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase; This family consists of the glutamine-rich domain of histone deacetylase 5 (HDAC5). It belongs to a superfamily that consists of the glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDCA9; it is missing from HDAC7. This domain confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors, and it is able to repress transcription independently of the HDAC C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues.


Pssm-ID: 197400 [Multi-domain]  Cd Length: 97  Bit Score: 37.11  E-value: 5.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 703 LRERQTVENMQAEVDEQRAKDE---AWYQKQ-ELLRRAEETR--REILLQEEEKMAQQRQRLAAVKRELEIKEihlqdaA 776
Cdd:cd10164   4 LREQQLQQELLLLKQQQQLQKQllfAEFQKQhEHLTRQHEVQlqKHLKVRAELFSEQQQQEILAAKRQQELEQ------Q 77
                        90       100
                ....*....|....*....|...
gi 57157855 777 RRRLlklQQDQREMELRRLEDEI 799
Cdd:cd10164  78 RKRE---QQRQEELEKQRLEQQL 97
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
48-336 4.76e-28

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 117.32  E-value: 4.76e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  48 VAFDGSGDSFIAGDHQGNIYVFDLH-GNRFNLVQRTAQACTALAFNlrRKSEFLV-ALADYSIKCFDTVTKELVSWMRGH 125
Cdd:COG2319 126 VAFSPDGKTLASGSADGTVRLWDLAtGKLLRTLTGHSGAVTSVAFS--PDGKLLAsGSDDGTVRLWDLATGKLLRTLTGH 203
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 126 ESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLFCKY 204
Cdd:COG2319 204 TGAVRSVAFSPDGKLLASGSADgTVRLWDLATGKLLRTLTGHSG-SVRSVAFSPDGRLLASGSADGTVRLWDLATGELLR 282
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 205 QLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQmpAKVRAVRHLEFLPDsfdagsNQVLGVLSQ 284
Cdd:COG2319 283 TLTGHSGGVNSV----AFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT--GHTGAVRSVAFSPD------GKTLASGSD 350
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 57157855 285 DGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQ 336
Cdd:COG2319 351 DGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
44-340 1.24e-26

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 113.47  E-value: 1.24e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  44 RFLNVAFDGSGDSFIAGDHQGNIYVFDL-HGNRFNLVQRTAQACTALAFNLRRKSeFLVALADYSIKCFDTVTKELVSWM 122
Cdd:COG2319  80 AVLSVAFSPDGRLLASASADGTVRLWDLaTGLLLRTLTGHTGAVRSVAFSPDGKT-LASGSADGTVRLWDLATGKLLRTL 158
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 123 RGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLF 201
Cdd:COG2319 159 TGHSGAVTSVAFSPDGKLLASGSDDgTVRLWDLATGKLLRTLTGHTG-AVRSVAFSPDGKLLASGSADGTVRLWDLATGK 237
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 202 CKYQLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQMPAkvRAVRHLEFLPDSfdagsnQVLGV 281
Cdd:COG2319 238 LLRTLTGHSGSVRSV----AFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHS--GGVNSVAFSPDG------KLLAS 305
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 57157855 282 LSQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQALTQ 340
Cdd:COG2319 306 GSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
39-334 7.45e-25

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 105.49  E-value: 7.45e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  39 HPKVLRFlnVAFDGSGDSFIAGDHQGNIYVFDLHGNRFNLVQR----TAQACTALAFNLRrkseFLVALADYSIKCFDTV 114
Cdd:cd00200   8 HTGGVTC--VAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKghtgPVRDVAASADGTY----LASGSSDKTIRLWDLE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 115 TKELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 193
Cdd:cd00200  82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDkTIKVWDVETGKCLTTLRGHTD-WVNSVAFSPDGTFVASSSQDGTIK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 194 AWECDTLFCKYQLPGpPEGSnilykVFAVT--RDGRILAAGGKSNHLHLWclEATGLFRIIQMPAKVRAVRHLEFLPDsf 271
Cdd:cd00200 161 LWDLRTGKCVATLTG-HTGE-----VNSVAfsPDGEKLLSSSSDGTIKLW--DLSTGKCLGTLRGHENGVNSVAFSPD-- 230
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57157855 272 dagsNQVLGVLSQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYS 334
Cdd:cd00200 231 ----GYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
39-336 1.53e-24

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 106.92  E-value: 1.53e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  39 HPKVLRFLNVAFDGSGDSFIAGDHQGNIYVFDLHGNRFNLVQRTAQAcTALAFNLRRKSeFLVALADYSIKCFDTVTKEL 118
Cdd:COG2319  35 LAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAV-LSVAFSPDGRL-LASASADGTVRLWDLATGLL 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 119 VSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNiRQSVGIQKVFFLPLSNTILSCFKDNSIFAWEC 197
Cdd:COG2319 113 LRTLTGHTGAVRSVAFSPDGKTLASGSADgTVRLWDLATGKLLRTLT-GHSGAVTSVAFSPDGKLLASGSDDGTVRLWDL 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 198 DTLFCKYQLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQMPAkvRAVRHLEFLPDSfdagsnQ 277
Cdd:COG2319 192 ATGKLLRTLTGHTGAVRSV----AFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHS--GSVRSVAFSPDG------R 259
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 57157855 278 VLGVLSQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQ 336
Cdd:COG2319 260 LLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLA 318
WD40 COG2319
WD40 repeat [General function prediction only];
49-336 7.03e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 96.13  E-value: 7.03e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  49 AFDGSGDSFIAGDHQGNIYVFDLHGNRFNLVQRTAQACTALAFNLRRKSEFLVALADYSIKCFDTVTKELVSWMRGHESS 128
Cdd:COG2319   1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 129 VCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLFCKYQLP 207
Cdd:COG2319  81 VLSVAFSPDGRLLASASADgTVRLWDLATGLLLRTLTGHTG-AVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 208 GPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQmpAKVRAVRHLEFLPDSfdagsnQVLGVLSQDGI 287
Cdd:COG2319 160 GHSGAVTSV----AFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT--GHTGAVRSVAFSPDG------KLLASGSADGT 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 57157855 288 MRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQ 336
Cdd:COG2319 228 VRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA 276
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
123-337 2.38e-16

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 80.46  E-value: 2.38e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 123 RGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIrQSVGIQKVFFLPLSNTILSCFKDNSIFAWECDTLF 201
Cdd:cd00200   6 KGHTGGVTCVAFSPDGKLLATGSGDgTIKVWDLETGELLRTLKG-HTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 202 CKYQLPGPPEGsnilykVFAV--TRDGRILAAGGKSNHLHLWCLEATGLfrIIQMPAKVRAVRHLEFLPDsfdagsNQVL 279
Cdd:cd00200  85 CVRTLTGHTSY------VSSVafSPDGRILSSSSRDKTIKVWDVETGKC--LTTLRGHTDWVNSVAFSPD------GTFV 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 57157855 280 GVLSQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQA 337
Cdd:cd00200 151 ASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLST 208
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
688-832 5.14e-11

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 66.30  E-value: 5.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   688 QTREWERIRNDELDflrERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEE----KMAQQRQRLAAVKR 763
Cdd:pfam17380 444 RAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEerkqAMIEEERKRKLLEK 520
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57157855   764 ELEIKEIHLQDAARRRLLKLQQ-DQREMELRRLEDEIERKVQMRDQEIAATAKDLE-IRQL-ELEAQKRLYE 832
Cdd:pfam17380 521 EMEERQKAIYEEERRREAEEERrKQQEMEERRRIQEQMRKATEERSRLEAMEREREmMRQIvESEKARAEYE 592
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
688-830 8.99e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.65  E-value: 8.99e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 688 QTREWE-RIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELL---RRAEETRREILLQEEEKMAQQRQRLAAVKR 763
Cdd:COG1196 261 ELAELEaELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLeerRRELEERLEELEEELAELEEELEELEEELE 340
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57157855 764 ELEIKEIHLQDAARRRLLKLQQ--DQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRL 830
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEaeEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
WD40 COG2319
WD40 repeat [General function prediction only];
48-156 1.67e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 60.70  E-value: 1.67e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  48 VAFDGSGDSFIAGDHQGNIYVFDLH-GNRFNLVQRTAQACTALAFNlrRKSEFLV-ALADYSIKCFDTVTKELVSWMRGH 125
Cdd:COG2319 294 VAFSPDGKLLASGSDDGTVRLWDLAtGKLLRTLTGHTGAVRSVAFS--PDGKTLAsGSDDGTVRLWDLATGELLRTLTGH 371
                        90       100       110
                ....*....|....*....|....*....|..
gi 57157855 126 ESSVCSISVHASGRYAITTSSD-TAQLWDLDT 156
Cdd:COG2319 372 TGAVTSVAFSPDGRTLASGSADgTVRLWDLAT 403
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
701-839 1.76e-09

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 61.12  E-value: 1.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   701 DFLRERQT------VENMQAEVDEQRAkdeawyQKQELLRRAEETRREILLQ-----EEEKMAQQRQRLAAVKRELEIKE 769
Cdd:pfam15709 336 DRLRAERAemrrleVERKRREQEEQRR------LQQEQLERAEKMREELELEqqrrfEEIRLRKQRLEEERQRQEEEERK 409
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57157855   770 IHLQDAARRRLLKLQQDqremELRRLEDEIERKVQmrdQEIAATAKDLEIRQLELEAQ-----KRLYEKVESSSL 839
Cdd:pfam15709 410 QRLQLQAAQERARQQQE----EFRRKLQELQRKKQ---QEEAERAEAEKQRQKELEMQlaeeqKRLMEMAEEERL 477
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
461-605 2.84e-09

Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are GTPase activator proteins of yeast Ypt6 and Ypt7, implies that these domains are GTPase activator proteins of Rab-like small GTPases.


Pssm-ID: 459855  Cd Length: 178  Bit Score: 57.26  E-value: 2.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   461 SLQKKYPIKSRKLLRVLQRTLSALAHWsaiFSDTPY---LPLLAFPFVkLFQNNQLICFEVVATLIINwcQHWFEYFPN- 536
Cdd:pfam00566  19 TFPHSFFFDNGPGQNSLRRILKAYSIY---NPDVGYcqgMNFIAAPLL-LVYLDEEDAFWCFVSLLEN--YLLRDFYTPd 92
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57157855   537 -PPINILSMI-ENVLAFHDKELLQHFIDRDITSQVYAWPLLETLFSEVLTREEWLRLFDNIFSNHPSFLLM 605
Cdd:pfam00566  93 fPGLKRDLYVfEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVLF 163
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
684-834 4.98e-09

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 60.14  E-value: 4.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   684 IVDYQTREWERIRNDELDFL---RERQTVENMQAEVDEQRAKDEAwyqkqELLRRAEETRREILLQEEEKMAQQRQR--- 757
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMeqeRLRQEKEEKAREVERRRKLEEA-----EKARQAEMDRQAAIYAEQERMAMERERele 351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   758 ---LAAVKRELE---IKEIHLQDAARRRLLKLQQD-QREMELRRLEDEIERKVQMRDQEiaatakdleiRQLELEAQKRL 830
Cdd:pfam17380 352 rirQEERKRELErirQEEIAMEISRMRELERLQMErQQKNERVRQELEAARKVKILEEE----------RQRKIQQQKVE 421

                  ....
gi 57157855   831 YEKV 834
Cdd:pfam17380 422 MEQI 425
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
689-835 8.53e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 8.53e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 689 TREWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAwyQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIK 768
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEE--ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57157855 769 E-----IHLQDAARRRLLKLQQDQREME------LRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKVE 835
Cdd:COG1196 372 AelaeaEEELEELAEELLEALRAAAELAaqleelEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
690-830 2.42e-08

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 56.85  E-value: 2.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   690 REWERIRNDELDflrERqtVENMQAEVDEQRAKDEAwyqKQELLRRAEETRREILLQEEEKMAQQRQRL---------AA 760
Cdd:pfam13868 143 KELEKEEEREED---ER--ILEYLKEKAEREEEREA---EREEIEEEKEREIARLRAQQEKAQDEKAERdelraklyqEE 214
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57157855   761 VKRELEIKEIhlQDAARRR-----LLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRL 830
Cdd:pfam13868 215 QERKERQKER--EEAEKKArqrqeLQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMK 287
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
693-833 2.45e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 2.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 693 ERIRNDELDFLRERQTVENMQAEVDEQRAK--------DEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRE 764
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLEleelelelEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57157855 765 LEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLE----IRQLELEAQKRLYEK 833
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEeleeLAEELLEALRAAAEL 398
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
693-836 7.05e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 7.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 693 ERIRNDELDFLRERQTVENMQAEVDEQRAKDEAwyQKQELLRRAEETRREILLQEEEKmAQQRQRLAAVKRELEIKEIHL 772
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEE--RLEELEEELAELEEELEELEEEL-EELEEELEEAEEELEEAEAEL 360
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57157855 773 QDAARRRllkLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKVES 836
Cdd:COG1196 361 AEAEEAL---LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
688-828 7.15e-08

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 56.11  E-value: 7.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   688 QTREWE--RIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKREL 765
Cdd:pfam15709 382 QQRRFEeiRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQL 461
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57157855   766 EIKEIHLQD-AARRRLLKLQQDQREMELRRLEDEiERKvqMRDQEIAATAKDLEIRQLELEAQK 828
Cdd:pfam15709 462 AEEQKRLMEmAEEERLEYQRQKQEAEEKARLEAE-ERR--QKEEEAARLALEEAMKQAQEQARQ 522
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
693-836 1.44e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 55.46  E-value: 1.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855    693 ERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWyqkQELLRRAEETRREIL--LQEEEKMAQQ-RQRLAAVKRELE--I 767
Cdd:TIGR02169  322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKL---TEEYAELKEELEDLRaeLEEVDKEFAEtRDELKDYREKLEklK 398
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855    768 KEIHLQDAARRRLLKLQQdQREMELRRLEDEIER-----------------KVQMRDQEIAATAKDLEIRQLELEAQKRL 830
Cdd:TIGR02169  399 REINELKRELDRLQEELQ-RLSEELADLNAAIAGieakineleeekedkalEIKKQEWKLEQLAADLSKYEQELYDLKEE 477

                   ....*.
gi 57157855    831 YEKVES 836
Cdd:TIGR02169  478 YDRVEK 483
PRK12704 PRK12704
phosphodiesterase; Provisional
682-832 1.63e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 54.78  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  682 KFIVDYQTREWERIRNDEL-----DFLRERQTVENmqaEVDEQRAKdeawYQKQEL-LRRAEET---RREILLQEEEKMA 752
Cdd:PRK12704  41 KRILEEAKKEAEAIKKEALleakeEIHKLRNEFEK---ELRERRNE----LQKLEKrLLQKEENldrKLELLEKREEELE 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  753 QQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQ-------DQREMELRRLEDEIErkvqmrdQEIAATAKDLEiRQLELE 825
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEELEELIEEQLQELERisgltaeEAKEILLEKVEEEAR-------HEAAVLIKEIE-EEAKEE 185

                 ....*..
gi 57157855  826 AQKRLYE 832
Cdd:PRK12704 186 ADKKAKE 192
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
690-836 3.58e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 3.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 690 REWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKE 769
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57157855 770 IHLQDAARRrlLKLQQDQREMELRRLEDEIERKvqmrDQEIAATAKDLEIRQLELEAQKRLYEKVES 836
Cdd:COG1196 312 RELEERLEE--LEEELAELEEELEELEEELEEL----EEELEEAEEELEEAEAELAEAEEALLEAEA 372
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
704-832 4.00e-07

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 50.42  E-value: 4.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   704 RERQTVENMQAEVDEQRAKDEAWYQ-KQELLRRAEETRREillQEEE--KMAQQRQRLAAVKRELEIKEIHLQDAARRRL 780
Cdd:pfam05672  19 KRRQAREQREREEQERLEKEEEERLrKEELRRRAEEERAR---REEEarRLEEERRREEEERQRKAEEEAEEREQREQEE 95
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 57157855   781 LKLQQDQREMELRRLEDEIERKVQMRDQEIaatakdLEIRQLELEAQKRLYE 832
Cdd:pfam05672  96 QERLQKQKEEAEAKAREEAERQRQEREKIM------QQEEQERLERKKRIEE 141
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
691-808 4.71e-07

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 50.04  E-value: 4.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   691 EWERIRNDELdflRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMA-QQRQRLAAVKRELEike 769
Cdd:pfam05672  39 EEERLRKEEL---RRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQErLQKQKEEAEAKARE--- 112
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 57157855   770 ihlqDAARRRLLKLQQDQREMELR-----RLEdEIERKVQMRDQ 808
Cdd:pfam05672 113 ----EAERQRQEREKIMQQEEQERlerkkRIE-EIMKRTRKSDQ 151
PRK12704 PRK12704
phosphodiesterase; Provisional
721-839 5.41e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 53.24  E-value: 5.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  721 AKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLaavKRELEIKEIHLQDAARRRLlklqqdQREMELRRLEDEIE 800
Cdd:PRK12704  36 AEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEF---EKELRERRNELQKLEKRLL------QKEENLDRKLELLE 106
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 57157855  801 RkvqmRDQEIAATAKDLEIRQLELEAQKRLYEKVESSSL 839
Cdd:PRK12704 107 K----REEELEKKEKELEQKQQELEKKEEELEELIEEQL 141
PTZ00121 PTZ00121
MAEBL; Provisional
690-835 5.81e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 5.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   690 REWERIRNDELDFLRERQtvENMQAEvdeQRAKDEAWYQKQELLRRAEETRREILlQEEEKMAQQRQRLAAVKRELEIKE 769
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEE--KKMKAE---EAKKAEEAKIKAEELKKAEEEKKKVE-QLKKKEAEEKKKAEELKKAEEENK 1660
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57157855   770 IHLQDAARrrllKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKVE 835
Cdd:PTZ00121 1661 IKAAEEAK----KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELK 1722
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
684-829 7.16e-07

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 52.23  E-value: 7.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   684 IVDYQTREWERIRNDEldflRERQTVENMQAEVDEQRAKDEawYQKQELLRRAE------------ETRREILLQEEEKM 751
Cdd:pfam13868  23 ERDAQIAEKKRIKAEE----KEEERRLDEMMEEERERALEE--EEEKEEERKEErkryrqeleeqiEEREQKRQEEYEEK 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   752 AQQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMR--DQEIAATAKDLEIRQLELEAQKR 829
Cdd:pfam13868  97 LQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEReeDERILEYLKEKAEREEEREAERE 176
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
690-830 1.78e-06

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 51.07  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   690 REWERIRN---------DELDFLRERQTVENMQAEvDEQRAKDEAwYQKQELLRRAEETRREILLQEEEKMAQQRQR--- 757
Cdd:pfam13868 184 REIARLRAqqekaqdekAERDELRAKLYQEEQERK-ERQKEREEA-EKKARQRQELQQAREEQIELKERRLAEEAEReee 261
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57157855   758 --LAAVKRELEIKEIHLQDAARRRLLKLQQdQREmelrrLEDEIERKVQMRDQEIAATAKDLE-IRQLELEAQKRL 830
Cdd:pfam13868 262 efERMLRKQAEDEEIEQEEAEKRRMKRLEH-RRE-----LEKQIEEREEQRAAEREEELEEGErLREEEAERRERI 331
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
688-832 2.26e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.31  E-value: 2.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 688 QTREWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREI---------LLQEEEKMAQQRQRL 758
Cdd:COG4717  86 KEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELaelperleeLEERLEELRELEEEL 165
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 759 AAVKRELEIKEIHLQDAARRRLLKLQQDQREM--ELRRLEDEIER------KVQMRDQEIAATAKDLEIRQLELEAQKRL 830
Cdd:COG4717 166 EELEAELAELQEELEELLEQLSLATEEELQDLaeELEELQQRLAEleeeleEAQEELEELEEELEQLENELEAAALEERL 245

                ..
gi 57157855 831 YE 832
Cdd:COG4717 246 KE 247
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
696-830 2.33e-06

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 50.81  E-value: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   696 RNDELDFLRERQTVENMQAEvdEQRAKDEawyQKQELLRRaeETRREILLQEEEKMAQQRQRLAAVKRELE------IKE 769
Cdd:pfam15558  16 RHKEEQRMRELQQQAALAWE--ELRRRDQ---KRQETLER--ERRLLLQQSQEQWQAEKEQRKARLGREERrradrrEKQ 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57157855   770 IHLQDAARRRLLKLQQDQRE--MELRRLEDEIERKVQMRD-QEIAATAKDLEIRQlELEAQKRL 830
Cdd:pfam15558  89 VIEKESRWREQAEDQENQRQekLERARQEAEQRKQCQEQRlKEKEEELQALREQN-SLQLQERL 151
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
713-835 2.68e-06

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 50.81  E-value: 2.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 713 QAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELE--IKEIHLQDAARRRLLKLQQDQREM 790
Cdd:COG3064   1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEeeAREAKAEAEQRAAELAAEAAKKLA 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 57157855 791 ELRRLEDEIERKVQMRDQEIAATA-KDLEIRQLELEAQKRLYEKVE 835
Cdd:COG3064  81 EAEKAAAEAEKKAAAEKAKAAKEAeAAAAAEKAAAAAEKEKAEEAK 126
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
690-835 2.79e-06

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 50.89  E-value: 2.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   690 REWERIRNdELDFLR-------ERQ-TVENMQAEVDEQRAKDEAwyQKQELLRRAEETR-REILLQEEEKMAQQRQrlaa 760
Cdd:pfam17380 389 QKNERVRQ-ELEAARkvkileeERQrKIQQQKVEMEQIRAEQEE--ARQREVRRLEEERaREMERVRLEEQERQQQ---- 461
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   761 vkreleiKEIHLQDAARRRLLKLQQDQREMELRRLEDE----IERKVQMRDQEIAATAKDLEIRQLELEA-QKRLYEKVE 835
Cdd:pfam17380 462 -------VERLRQQEEERKRKKLELEKEKRDRKRAEEQrrkiLEKELEERKQAMIEEERKRKLLEKEMEErQKAIYEEER 534
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
703-834 3.69e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 3.69e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 703 LRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLK 782
Cdd:COG1196 680 ELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP 759
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57157855 783 LQQDQREMELRRLEDEI------------------ERKVQMRDQ--EIAATAKDLE--IRQLELEAQKRL---YEKV 834
Cdd:COG1196 760 PDLEELERELERLEREIealgpvnllaieeyeeleERYDFLSEQreDLEEARETLEeaIEEIDRETRERFletFDAV 836
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
706-838 5.99e-06

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 49.65  E-value: 5.99e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 706 RQTVENMQAEVDEQRAKDEAwyqKQELLRRAEETRREILLQEEEKMAQQRQRLAA------VKRELEIKEIHLQDAARRR 779
Cdd:COG3064   2 QEALEEKAAEAAAQERLEQA---EAEKRAAAEAEQKAKEEAEEERLAELEAKRQAeeeareAKAEAEQRAAELAAEAAKK 78
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57157855 780 LLKLQQDQREMElRRLEDEIERKVQ-----MRDQEIAATAKDLEIRQLELEAQKRLYEKVESSS 838
Cdd:COG3064  79 LAEAEKAAAEAE-KKAAAEKAKAAKeaeaaAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEER 141
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
690-835 9.93e-06

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 48.38  E-value: 9.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   690 REWERIRNDELDFLRERQT-VENMQAEVDEQRAK-DEAWYQKQELLRRAEETRREIllQEEEKMAQQRQRLAAVKRELEI 767
Cdd:pfam13868 176 EEIEEEKEREIARLRAQQEkAQDEKAERDELRAKlYQEEQERKERQKEREEAEKKA--RQRQELQQAREEQIELKERRLA 253
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57157855   768 KEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKV--------QMRDQE---IAATAKDLEIRQLELEAQKRLYEKVE 835
Cdd:pfam13868 254 EEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLehrrelekQIEEREeqrAAEREEELEEGERLREEEAERRERIE 332
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
707-833 1.02e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 1.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 707 QTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREI------LLQEEEKMAQQRQ------RLAAVKRELEIKEIHLqD 774
Cdd:COG4717  71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELeaeleeLREELEKLEKLLQllplyqELEALEAELAELPERL-E 149
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57157855 775 AARRRLLKLQQDQREM-----ELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEK 833
Cdd:COG4717 150 ELEERLEELRELEEELeeleaELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEE 213
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
686-828 1.02e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.53  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  686 DYQTREWERIRNDELDFLRERQTVENMQaevdeqrakdeawyQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKREL 765
Cdd:COG4913  260 LAERYAAARERLAELEYLRAALRLWFAQ--------------RRLELLEAELEELRAELARLEAELERLEARLDALREEL 325
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57157855  766 EIKEIHLQDAARRRLLKLQQdqremELRRLEDEIERKVQMRDQ----------EIAATAKDLEIRQLELEAQK 828
Cdd:COG4913  326 DELEAQIRGNGGDRLEQLER-----EIERLERELEERERRRARleallaalglPLPASAEEFAALRAEAAALL 393
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
685-833 1.16e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 1.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855    685 VDYQTREWERIRNDELDFLRERQTVENM-QAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKR 763
Cdd:TIGR02168  321 LEAQLEELESKLDELAEELAELEEKLEElKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855    764 ELEIKEIHLQDAARRRLlKLQQDQREMELRRLE---DEIERKVQMRDQEIAATAKDLE---------------IRQLELE 825
Cdd:TIGR02168  401 EIERLEARLERLEDRRE-RLQQEIEELLKKLEEaelKELQAELEELEEELEELQEELErleealeelreeleeAEQALDA 479

                   ....*...
gi 57157855    826 AQKRLYEK 833
Cdd:TIGR02168  480 AERELAQL 487
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
699-833 1.63e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.90  E-value: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855    699 ELDFLRER-QTVENMQAEVDEQRAKDEawyQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQD--- 774
Cdd:TIGR02168  303 QKQILRERlANLERQLEELEAQLEELE---SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEElee 379
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57157855    775 -----AARRRLLKLQQDQREMELRRLEDEIER---KVQMRDQEIAATAKDLEIRQLElEAQKRLYEK 833
Cdd:TIGR02168  380 qletlRSKVAQLELQIASLNNEIERLEARLERledRRERLQQEIEELLKKLEEAELK-ELQAELEEL 445
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
733-836 1.64e-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: 1.64e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 733 LRRAEE--TRREILLQEeekMAQQRQRLA----------AVKRELEIKEIHLQdAARRRLLKLQQDQREMELRRLEDEIE 800
Cdd:COG1196 181 LEATEEnlERLEDILGE---LERQLEPLErqaekaeryrELKEELKELEAELL-LLKLRELEAELEELEAELEELEAELE 256
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 57157855 801 R-KVQMRDQEIAATAKDLEIRQLELE---AQKRLYEKVES 836
Cdd:COG1196 257 ElEAELAELEAELEELRLELEELELEleeAQAEEYELLAE 296
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
687-838 2.36e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 2.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 687 YQT-REWERIRNDELdFLRERQTVENMQAEVDEQRAkdeawyQKQELLRRAEETRREIllqeEEKMAQQRQRLAAVKREL 765
Cdd:COG1196 215 YRElKEELKELEAEL-LLLKLRELEAELEELEAELE------ELEAELEELEAELAEL----EAELEELRLELEELELEL 283
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57157855 766 EIKEIHLQdAARRRLLKLQQDQR--EMELRRLEDEIERKvQMRDQEIAATAKDLEIRQLELEAQKRLYEKVESSS 838
Cdd:COG1196 284 EEAQAEEY-ELLAELARLEQDIArlEERRRELEERLEEL-EEELAELEEELEELEEELEELEEELEEAEEELEEA 356
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
690-829 2.61e-05

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 47.22  E-value: 2.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   690 REWERIRNDELdFLRERQTVENMQAEVDEQRAKdeawyQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELE--- 766
Cdd:pfam13868  85 REQKRQEEYEE-KLQEREQMDEIVERIQEEDQA-----EAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDEril 158
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57157855   767 --IKEIHLQDAARRRLLKLQQDQREMELRRL----------EDEIERKVQMRDQEiaatAKDLEIRQLELEAQKR 829
Cdd:pfam13868 159 eyLKEKAEREEEREAEREEIEEEKEREIARLraqqekaqdeKAERDELRAKLYQE----EQERKERQKEREEAEK 229
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
712-835 2.90e-05

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 47.22  E-value: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   712 MQAEVDEQRA-----KDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELeikEIHLQDAARRRLLKLQQD 786
Cdd:pfam13868  20 CNKERDAQIAekkriKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQEL---EEQIEEREQKRQEEYEEK 96
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57157855   787 QREMEL-----RRLEDEIERKVQMRDQEIAATAKDL--------EIRQLELEAQKRLYEKVE 835
Cdd:pfam13868  97 LQEREQmdeivERIQEEDQAEAEEKLEKQRQLREEIdefneeqaEWKELEKEEEREEDERIL 158
COG5210 COG5210
GTPase-activating protein [General function prediction only];
542-658 2.99e-05

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 47.49  E-value: 2.99e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 542 LSMIENVLAFHDKELLQHFIDRDITSQVYAWPLLETLFSEVLTREEWLRLFDNIFSNHPSFLLMTVVAYSTCSRAPLLNC 621
Cdd:COG5210 350 LKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKL 429
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 57157855 622 TLKNDFEYFFHHRNNLDINVVIREVYHLMETTPADIH 658
Cdd:COG5210 430 DSDELLDLLLKQLFLHSGKEAWSSILKFRHGTDRDIL 466
RNase_Y_N pfam12072
RNase Y N-terminal region;
713-838 3.18e-05

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 45.65  E-value: 3.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   713 QAEVDEQRAKDEAwyqKQEllrrAEETRREILLQEEEKMAQQRQRLaavkrELEIKEihlqdaaRRRLLKLQQD---QRE 789
Cdd:pfam12072  31 SAEELAKRIIEEA---KKE----AETKKKEALLEAKEEIHKLRAEA-----ERELKE-------RRNELQRQERrllQKE 91
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 57157855   790 MEL-RRLE--DEIERKVQMRDQEIAATAKDLEIRQLELEA--QKRLyEKVESSS 838
Cdd:pfam12072  92 ETLdRKDEslEKKEESLEKKEKELEAQQQQLEEKEEELEEliEEQR-QELERIS 144
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
707-830 4.01e-05

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 47.64  E-value: 4.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  707 QTVENMQAEVDeqraKDEAWYQKQELLRRAEETRreillqeeeKMAQQRQRLAAVKRELEiKEIHLQDAARRRL------ 780
Cdd:COG3096  479 ELVCKIAGEVE----RSQAWQTARELLRRYRSQQ---------ALAQRLQQLRAQLAELE-QRLRQQQNAERLLeefcqr 544
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57157855  781 ----------LKLQQDQREMELRRLEDE----IERKVQMRDQEIAATAKDLEIRQLE---LEAQKRL 830
Cdd:COG3096  545 igqqldaaeeLEELLAELEAQLEELEEQaaeaVEQRSELRQQLEQLRARIKELAARApawLAAQDAL 611
Pinin_SDK_memA pfam04696
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ...
719-809 4.02e-05

pinin/SDK/memA/ protein conserved region; Members of this family have very varied localizations within the eukaryotic cell. pinin is known to localize at the desmosomes and is implicated in anchoring intermediate filaments to the desmosomal plaque. SDK2/3 is a dynamically localized nuclear protein thought to be involved in modulation of alternative pre-mRNA splicing. memA is a tumour marker preferentially expressed in human melanoma cell lines. A common feature of the members of this family is that they may all participate in regulating protein-protein interactions.


Pssm-ID: 461396 [Multi-domain]  Cd Length: 130  Bit Score: 43.82  E-value: 4.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   719 QRAKDEAWYQKQELLRRAEETRREillqeEEKMAQQRQRLAAVKREleikeihlqdaaRRRLLKLQQDQREMELRRLEDE 798
Cdd:pfam04696  19 QKFKKEESKQKEKEERRAEIEKRL-----EEKAKQEKEELEERKRE------------EREELFEERRAEQIELRALEEK 81
                          90
                  ....*....|.
gi 57157855   799 IERKVQMRDQE 809
Cdd:pfam04696  82 LELKELMETWH 92
PTZ00121 PTZ00121
MAEBL; Provisional
690-835 4.21e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 4.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   690 REWERIRNDELDFLRERQTVENMQaEVDEQRAKDEAwyQKQELLRRAEETRReillQEEEKMAQQRQRLAAVKRELEIKE 769
Cdd:PTZ00121 1505 AAEAKKKADEAKKAEEAKKADEAK-KAEEAKKADEA--KKAEEKKKADELKK----AEELKKAEEKKKAEEAKKAEEDKN 1577
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57157855   770 IHLQDAARRR---------LLKLQQDQREM---ELRRLEDEIERKVQMRDQEiaATAKDLEIRQLELEAQKRLYEKVE 835
Cdd:PTZ00121 1578 MALRKAEEAKkaeearieeVMKLYEEEKKMkaeEAKKAEEAKIKAEELKKAE--EEKKKVEQLKKKEAEEKKKAEELK 1653
Caldesmon pfam02029
Caldesmon;
697-839 4.36e-05

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 46.78  E-value: 4.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   697 NDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAavKRELEIKEIHLQDAA 776
Cdd:pfam02029 211 NGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQ--EAELELEELKKKREE 288
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57157855   777 RRRLLKLQQDQREME--LRRLEDEIERKvQMRDqeiaatakDLEIRQLElEAQKRLyeKVESSSL 839
Cdd:pfam02029 289 RRKLLEEEEQRRKQEeaERKLREEEEKR-RMKE--------EIERRRAE-AAEKRQ--KLPEDSS 341
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
688-836 4.92e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 4.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855    688 QTREWERIRND---ELDFLR-ERQTVENMQAEVDEQRAK-----DEAWYQKQELLRRAEETRREI--LLQEEEKMAQQRQ 756
Cdd:TIGR02169  813 RLREIEQKLNRltlEKEYLEkEIQELQEQRIDLKEQIKSiekeiENLNGKKEELEEELEELEAALrdLESRLGDLKKERD 892
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855    757 RLAAVKRELEIK--EIHLQDAARRRLLKLQQDQREMELRRLeDEIERKVQmRDQEIAATAKDLEIRQLELEAQKRLYEKV 834
Cdd:TIGR02169  893 ELEAQLRELERKieELEAQIEKKRKRLSELKAKLEALEEEL-SEIEDPKG-EDEEIPEEELSLEDVQAELQRVEEEIRAL 970

                   ..
gi 57157855    835 ES 836
Cdd:TIGR02169  971 EP 972
PTZ00121 PTZ00121
MAEBL; Provisional
693-830 5.12e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 5.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   693 ERIRNDELdflreRQTVENMQAEVDEQRAKDEAwYQKQELLRRAEETRR--EILLQEEEKMAQQRQRLAAVKRELEIKEI 770
Cdd:PTZ00121 1481 EAKKADEA-----KKKAEEAKKKADEAKKAAEA-KKKADEAKKAEEAKKadEAKKAEEAKKADEAKKAEEKKKADELKKA 1554
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57157855   771 -HLQDAARRRLL---KLQQDQREMELRRLED--EIERKVQMRDQEIAATAKDLEIRQLELEAQKRL 830
Cdd:PTZ00121 1555 eELKKAEEKKKAeeaKKAEEDKNMALRKAEEakKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI 1620
PTZ00121 PTZ00121
MAEBL; Provisional
691-832 5.21e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 5.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   691 EWERIRNDELDFLRE-RQTVENMQAEVDEQ--------RAKDEAWYQKQELLRRAEETRR--EILLQEEE---KMAQQRQ 756
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEeKKKVEQLKKKEAEEkkkaeelkKAEEENKIKAAEEAKKAEEDKKkaEEAKKAEEdekKAAEALK 1695
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   757 RLAAVKRELEikEIHLQDAARRRllKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLE-----IRQLELEAQKRLY 831
Cdd:PTZ00121 1696 KEAEEAKKAE--ELKKKEAEEKK--KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEeekkkIAHLKKEEEKKAE 1771

                  .
gi 57157855   832 E 832
Cdd:PTZ00121 1772 E 1772
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
735-835 5.62e-05

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 46.48  E-value: 5.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   735 RAEETRREILLQEEEKMAQQRQRL---AAVKRELEIKEIHLQDAARRRLlklQQDQREMElRRLEDEIERKVQMRDQEIA 811
Cdd:pfam15709 315 RSEEDPSKALLEKREQEKASRDRLraeRAEMRRLEVERKRREQEEQRRL---QQEQLERA-EKMREELELEQQRRFEEIR 390
                          90       100
                  ....*....|....*....|....*..
gi 57157855   812 ATAKDLE---IRQLELEAQKRLYEKVE 835
Cdd:pfam15709 391 LRKQRLEeerQRQEEEERKQRLQLQAA 417
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
115-153 5.62e-05

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 41.14  E-value: 5.62e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 57157855    115 TKELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWD 153
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDgTIKLWD 40
PRK12705 PRK12705
hypothetical protein; Provisional
713-828 6.12e-05

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 46.63  E-value: 6.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  713 QAEVDEQRAKDEAWYQKQELLRRAEET-------RREILLQEEEKMAQQRQRLAAVKRELEIKEIHLqdAARRRLLKLQQ 785
Cdd:PRK12705  41 EAQKEAEEKLEAALLEAKELLLRERNQqrqearrEREELQREEERLVQKEEQLDARAEKLDNLENQL--EEREKALSARE 118
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 57157855  786 DQREMELRRLEDEIERKVQMRDQEiaatAKDLEIRQLELEAQK 828
Cdd:PRK12705 119 LELEELEKQLDNELYRVAGLTPEQ----ARKLLLKLLDAELEE 157
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
690-826 6.35e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 6.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855    690 REWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEE-----EKMAQQRQRLAAVKRE 764
Cdd:TIGR02169  230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqlrvkEKIGELEAEIASLERS 309
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57157855    765 LEIKEIHLQDAA-RRRLLKLQQDQREMELRRLEDEIERKVQMRDQ---EIAATAKDLEIRQLELEA 826
Cdd:TIGR02169  310 IAEKERELEDAEeRLAKLEAEIDKLLAEIEELEREIEEERKRRDKlteEYAELKEELEDLRAELEE 375
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
702-810 6.41e-05

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 45.74  E-value: 6.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   702 FLRERQTVENM-----QAEVDEQRAKdEAWYQKQELLRRAEETRREILLQEEEKMAQQRQR----LAAVKRELEIKEIHL 772
Cdd:pfam02841 181 FLQSKEAVEEAilqtdQALTAKEKAI-EAERAKAEAAEAEQELLREKQKEEEQMMEAQERSyqehVKQLIEKMEAEREQL 259
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 57157855   773 QDAARRRLLKLQQDQREMelrrLEDEIERKVQMRDQEI 810
Cdd:pfam02841 260 LAEQERMLEHKLQEQEEL----LKEGFKTEAESLQKEI 293
mukB PRK04863
chromosome partition protein MukB;
707-827 6.88e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.87  E-value: 6.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   707 QTVENMQAEVDEQRAKDEAwyqkQELLRRAEETR--------REILLQEEEKMAQQRQRLAAVKRELEIK-EIHLQDAAr 777
Cdd:PRK04863  480 QLVRKIAGEVSRSEAWDVA----RELLRRLREQRhlaeqlqqLRMRLSELEQRLRQQQRAERLLAEFCKRlGKNLDDED- 554
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 57157855   778 rrLLKLQQDQREMELRRLEDE----IERKVQMRDQEiaataKDLEIRQLELEAQ 827
Cdd:PRK04863  555 --ELEQLQEELEARLESLSESvseaRERRMALRQQL-----EQLQARIQRLAAR 601
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
740-833 7.21e-05

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


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 42.94  E-value: 7.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   740 RREI-LLQEE-----EKMAQQRQRLAAVKRELEIKEIHLQDAARR--RLLKLQQDQREMELRRLEDEIERKVQmRDQEIA 811
Cdd:pfam13863   5 KREMfLVQLAldakrEEIERLEELLKQREEELEKKEQELKEDLIKfdKFLKENDAKRRRALKKAEEETKLKKE-KEKEIK 83
                          90       100
                  ....*....|....*....|..
gi 57157855   812 ATAKDLEIRQLELEAQKRLYEK 833
Cdd:pfam13863  84 KLTAQIEELKSEISKLEEKLEE 105
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
706-828 7.28e-05

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 42.98  E-value: 7.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   706 RQTVENMQAEVdEQRAKdeawyQKQELLRRAEE-----TRREILLQEEEKMAQ-QRQRLAAVKRELE-----IKEIHLQD 774
Cdd:pfam20492   1 REEAEREKQEL-EERLK-----QYEEETKKAQEeleesEETAEELEEERRQAEeEAERLEQKRQEAEeekerLEESAEME 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 57157855   775 AARRRLLKLQQDQREMELRRLEDEIERkvqmrdqeiaataKDLEIRQLELEAQK 828
Cdd:pfam20492  75 AEEKEQLEAELAEAQEEIARLEEEVER-------------KEEEARRLQEELEE 115
PTZ00121 PTZ00121
MAEBL; Provisional
698-828 7.56e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 7.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   698 DELDFLRERQTVENMQAEvdEQRAKDEAwYQKQELLRRAEETRR--EILLQEEEKMAQQRQRLAAVKReleikeihLQDA 775
Cdd:PTZ00121 1095 EAFGKAEEAKKTETGKAE--EARKAEEA-KKKAEDARKAEEARKaeDARKAEEARKAEDAKRVEIARK--------AEDA 1163
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 57157855   776 ARRRLLKLQQDQREMELRRLEDEIERKVQMRDQE----IAATAKDLEIRQLElEAQK 828
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEdarkAEAARKAEEERKAE-EARK 1219
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
714-835 8.69e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 46.02  E-value: 8.69e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 714 AEVDEQRAKDEAwyqkqELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQDQREMELR 793
Cdd:COG2268 195 AEIIRDARIAEA-----EAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYE 269
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 57157855 794 RLEDEIERKVQM------RDQEIAATAKDLEIRQLELEAQKRLYEKVE 835
Cdd:COG2268 270 IAEANAEREVQRqleiaeREREIELQEKEAEREEAELEADVRKPAEAE 317
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
693-805 1.28e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.91  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   693 ERIRNDELDFLRERQT-VENMQAEVDEQRAKDEAWYQKqeLLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIH 771
Cdd:pfam13868 228 EKKARQRQELQQAREEqIELKERRLAEEAEREEEEFER--MLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQ 305
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 57157855   772 LQDAARRRLLKLQQDQREMELR--RLEDEIERKVQM 805
Cdd:pfam13868 306 RAAEREEELEEGERLREEEAERreRIEEERQKKLKE 341
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
501-609 1.30e-04

Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.


Pssm-ID: 214540 [Multi-domain]  Cd Length: 216  Bit Score: 44.22  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855    501 AFP-FVKLFQNNQLIcFEVVATLIINWCQHWFEYFpnppinilsmienvLAFHDKELLQHFIDRDITSQVYAWPLLETLF 579
Cdd:smart00164 112 AFWcLVKLMERYGPN-FYLPDMSGLQLDLLQLDRL--------------VKEYDPDLYKHLKDLGITPSLYALRWFLTLF 176
                           90       100       110
                   ....*....|....*....|....*....|
gi 57157855    580 SEVLTREEWLRLFDNIFSNHPSFLLMTVVA 609
Cdd:smart00164 177 ARELPLEIVLRIWDVLFAEGSDFLFRVALA 206
PTZ00121 PTZ00121
MAEBL; Provisional
693-835 1.34e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   693 ERIRNDEldflRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRRE-----ILLQEEEKMAQQRQRLAAVKRELEI 767
Cdd:PTZ00121 1610 EEAKKAE----EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAeeenkIKAAEEAKKAEEDKKKAEEAKKAEE 1685
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   768 KEIHLQDAARRrllKLQQDQREMELRRLEDEIERKV-QMRDQEIAATAKDLEIRQLELEAQKRLYE-KVE 835
Cdd:PTZ00121 1686 DEKKAAEALKK---EAEEAKKAEELKKKEAEEKKKAeELKKAEEENKIKAEEAKKEAEEDKKKAEEaKKD 1752
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
696-829 2.09e-04

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 45.02  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   696 RNDELDFLRER-----QTVENMQAEVDE-----QRAKDEAWYQKQELLRRAEETRR-----EILLQEEEKMAQ-QR---- 755
Cdd:pfam05667 333 REEELEELQEQledleSSIQELEKEIKKlessiKQVEEELEELKEQNEELEKQYKVkkktlDLLPDAEENIAKlQAlvda 412
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57157855   756 --QRLAAVKRELEIKEIHLQDAARRrlLKLQQDQREMELRRLEDEIER-KVQMRDQEIAATAKDLEIRQLELEAQKR 829
Cdd:pfam05667 413 saQRLVELAGQWEKHRVPLIEEYRA--LKEAKSNKEDESQRKLEEIKElREKIKEVAEEAKQKEELYKQLVAEYERL 487
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
684-829 2.49e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 2.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 684 IVDYQTREWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKmAQQRQRLAAVKR 763
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA-EEELELEEALLA 701
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57157855 764 ELEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKR 829
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
691-829 2.62e-04

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 44.07  E-value: 2.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   691 EWERIRNDELDFLR-ERQT---VENMQAEVDEQRAKDEAwyQKQELLRRAEEtrreillQEEEKMAQQRQRLAAVKR--E 764
Cdd:TIGR02794  51 QANRIQQQKKPAAKkEQERqkkLEQQAEEAEKQRAAEQA--RQKELEQRAAA-------EKAAKQAEQAAKQAEEKQkqA 121
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57157855   765 LEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKdleiRQLELEAQKR 829
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAK----KKAEAEAKAK 182
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
686-834 2.89e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 2.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 686 DYQTREWERIRnDELDFLRErqtvenmqAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKREL 765
Cdd:COG4717 315 ELEEEELEELL-AALGLPPD--------LSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE 385
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57157855 766 EIKEIHLQDAARRRLLKlQQDQREMELRRLEDEIERKVQMRDQE-IAATAKDLEIRQLELEAQ-KRLYEKV 834
Cdd:COG4717 386 ELRAALEQAEEYQELKE-ELEELEEQLEELLGELEELLEALDEEeLEEELEELEEELEELEEElEELREEL 455
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
744-834 3.17e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.98  E-value: 3.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 744 LLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARRR---LLKLQQDQREM-ELRRLEDEIERKVQMRDQEIAATAKDLEI 819
Cdd:COG4942  15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEkalLKQLAALERRIaALARRIRALEQELAALEAELAELEKEIAE 94
                        90
                ....*....|....*
gi 57157855 820 RQLELEAQKRLYEKV 834
Cdd:COG4942  95 LRAELEAQKEELAEL 109
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
697-831 3.19e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 3.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 697 NDELDFLRE-----RQTVENMQAEVDEQRAK-DEAWYQKQELLRRAEETRREILL---------QEEEKMAQQRQRLAAV 761
Cdd:COG4372  44 QEELEQLREeleqaREELEQLEEELEQARSElEQLEEELEELNEQLQAAQAELAQaqeeleslqEEAEELQEELEELQKE 123
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57157855 762 KRELEIKEIHLQdaARRRLLKLQQDQREMELRRLEDEIER------KVQMRDQEIAATAKDLEIRQLELEAQKRLY 831
Cdd:COG4372 124 RQDLEQQRKQLE--AQIAELQSEIAEREEELKELEEQLESlqeelaALEQELQALSEAEAEQALDELLKEANRNAE 197
Nop53 pfam07767
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ...
714-833 3.22e-04

Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.


Pssm-ID: 462259 [Multi-domain]  Cd Length: 353  Bit Score: 43.82  E-value: 3.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   714 AEVDEQRAKDEAwyQKQELLRRAEETRREILLQEEEKMAQQrQRLAAVKRELEIKEihlqdAARRRLLKLQQDQremeLR 793
Cdd:pfam07767 205 VEAEKKRLKEEE--KLERVLEKIAESAATAEAREEKRKTKA-QRNKEKRRKEEERE-----AKEEKALKKKLAQ----LE 272
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 57157855   794 RLEdEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEK 833
Cdd:pfam07767 273 RLK-EIAKEIAEKEKEREEKAEARKREKRKKKKEEKKLRP 311
DegS pfam05384
Sensor protein DegS; This is small family of Bacillus DegS proteins. The DegS-DegU ...
708-803 3.36e-04

Sensor protein DegS; This is small family of Bacillus DegS proteins. The DegS-DegU two-component regulatory system of Bacillus subtilis controls various processes that characterize the transition from the exponential to the stationary growth phase, including the induction of extracellular degradative enzymes, expression of late competence genes and down-regulation of the sigma D regulon. The family also contains one sequence Swiss:Q8R9D3 from Thermoanaerobacter tengcongensis which are described as sensory transduction histidine kinases.


Pssm-ID: 428449 [Multi-domain]  Cd Length: 159  Bit Score: 42.08  E-value: 3.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   708 TVENMQAEVDE--QRAKDEAWYQKQELlrraEETRREIL--------LQEEEKMAqqRQRLAAVKR------ELEIKEIH 771
Cdd:pfam05384  10 TIENSKEEIFEiaENARQEYERLKQEL----EELKEEVSetikevdkLEKKERRA--RQRLMEVSRdfnrysEEDIKEAY 83
                          90       100       110
                  ....*....|....*....|....*....|...
gi 57157855   772 LQ-DAARRRLLKLQQdqREMELRRLEDEIERKV 803
Cdd:pfam05384  84 EEaKDLQVELALLRE--REKQLRERRDELERRL 114
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
689-829 3.40e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 44.03  E-value: 3.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  689 TREWERIRNDELDFLR---ERQTVENMQAEvdEQRAKDEAWYQK-----------QELLRRAEETRREILLQEEEKMAQQ 754
Cdd:PRK09510  61 VEQYNRQQQQQKSAKRaeeQRKKKEQQQAE--ELQQKQAAEQERlkqlekerlaaQEQKKQAEEAAKQAALKQKQAEEAA 138
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57157855  755 RQRLAAVKRELEIKEIHLQDAARRrlLKLQQDQREMELRRLEDEIERKVQMrDQEIAATAKDLEIRQLELEAQKR 829
Cdd:PRK09510 139 AKAAAAAKAKAEAEAKRAAAAAKK--AAAEAKKKAEAEAAKKAAAEAKKKA-EAEAAAKAAAEAKKKAEAEAKKK 210
EVC2_like pfam12297
Ellis van Creveld protein 2 like protein; This family of proteins is found in eukaryotes. ...
689-801 3.57e-04

Ellis van Creveld protein 2 like protein; This family of proteins is found in eukaryotes. Proteins in this family are typically between 571 and 1310 amino acids in length. There are two conserved sequence motifs: LPA and ELH. EVC2 is implicated in Ellis van Creveld chondrodysplastic dwarfism in humans. Mutations in this protein can give rise to this congenital condition. LIMBIN is a protein which shares around 80% sequence homology with EVC2 and it is implicated in a similar condition in bovine chondrodysplastic dwarfism.


Pssm-ID: 463525 [Multi-domain]  Cd Length: 428  Bit Score: 43.92  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   689 TREWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRR-----AEETRREILLQEEEKMAQQRQRLaAVKR 763
Cdd:pfam12297 223 AAECNLETREKMEAQHQREMAEKEEAEELLKHADEQEALECSSLLDKlhkleQEHLQRSLLLRQEEDFAKAQRQL-AVFQ 301
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 57157855   764 ELEIKEI---HLQDAARRRLLKLQQDQREM-ELRRLEDEIER 801
Cdd:pfam12297 302 RVELHKIfftQLKEATRKGELKPEAAKRLLqDYSKIQEQIEE 343
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
707-835 3.60e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 3.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 707 QTVENMQAEVDEQRAK-DEAWYQKQELLRRAEETRREiLLQEEEKMAQQRQRLAAVKRELEIKEIHLQDA------ARRR 779
Cdd:COG4372  38 FELDKLQEELEQLREElEQAREELEQLEEELEQARSE-LEQLEEELEELNEQLQAAQAELAQAQEELESLqeeaeeLQEE 116
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57157855 780 LLKLQQDQREME-----LRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKVE 835
Cdd:COG4372 117 LEELQKERQDLEqqrkqLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
707-835 3.91e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.08  E-value: 3.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 707 QTVENMQAEVDEQRAKDEAwyQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEiKEIHLQDAARRRL---LKL 783
Cdd:COG2433 376 LSIEEALEELIEKELPEEE--PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE-AELEEKDERIERLereLSE 452
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 57157855 784 QQDQREMELRRledeiERKVQMRDQEIAATAKdlEIRQLElEAQKRLYEKVE 835
Cdd:COG2433 453 ARSEERREIRK-----DREISRLDREIERLER--ELEEER-ERIEELKRKLE 496
G_path_suppress pfam15991
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ...
704-790 4.09e-04

G-protein pathway suppressor; This family of proteins inhibits G-protein- and mitogen-activated protein kinase-mediated signal transduction.


Pssm-ID: 464961 [Multi-domain]  Cd Length: 272  Bit Score: 42.99  E-value: 4.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   704 RERQTVEnMQAEVDEQRAKDEAWYQKQELLRRAEETRREIlLQEEEKMAQQRQRlaavKREL--EIKEIHLQDAARRRLL 781
Cdd:pfam15991  22 RERKKQE-QEAKMEEERLRREREEREKEDRMTLEETKEQI-LKLEKKLADLKEE----KHQLflQLKKVLHEDETRKRQL 95

                  ....*....
gi 57157855   782 KLQQDQREM 790
Cdd:pfam15991  96 KEQSELFAL 104
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
735-830 4.64e-04

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 41.56  E-value: 4.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   735 RAEETRReiLLQEEEKMA-QQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQDQREmELRRLEDeiERKVQMRDQEIAAT 813
Cdd:pfam05672   8 DAEEAAR--ILAEKRRQArEQREREEQERLEKEEEERLRKEELRRRAEEERARREE-EARRLEE--ERRREEEERQRKAE 82
                          90
                  ....*....|....*..
gi 57157855   814 AKDLEIRQLELEAQKRL 830
Cdd:pfam05672  83 EEAEEREQREQEEQERL 99
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
696-838 4.81e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 43.49  E-value: 4.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 696 RNDELDFLRE-RQTVENMQAEVDEQRAKDEAwyQKQELLRRAEETRREI---LLQEEEKMAQQRQRLAAVKRELEIKEIH 771
Cdd:COG3064  43 RLAELEAKRQaEEEAREAKAEAEQRAAELAA--EAAKKLAEAEKAAAEAekkAAAEKAKAAKEAEAAAAAEKAAAAAEKE 120
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57157855 772 LQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKVESSS 838
Cdd:COG3064 121 KAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAA 187
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
705-835 4.93e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 43.37  E-value: 4.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   705 ERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQ------RLAAVKRELEIKEIHLQDAARR 778
Cdd:pfam13868  79 EEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREeidefnEEQAEWKELEKEEEREEDERIL 158
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 57157855   779 RLLKlQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEA--QKRLYEKVE 835
Cdd:pfam13868 159 EYLK-EKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDElrAKLYQEEQE 216
Caldesmon pfam02029
Caldesmon;
693-796 5.62e-04

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 43.32  E-value: 5.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   693 ERIRndeldflRERQTVENMQAEVDEQRaKDEAWYQKQELLRRAEEtRREILLQEEEKMAQQRQrLAAVKRELEikeihl 772
Cdd:pfam02029 251 EELR-------RRRQEKESEEFEKLRQK-QQEAELELEELKKKREE-RRKLLEEEEQRRKQEEA-ERKLREEEE------ 314
                          90       100
                  ....*....|....*....|....
gi 57157855   773 qdaaRRRLlklqqdQREMELRRLE 796
Cdd:pfam02029 315 ----KRRM------KEEIERRRAE 328
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
718-791 6.71e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 43.63  E-value: 6.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855    718 EQRAKDEAwyQKQELLRRAEETRREILLQ--EEEKMAQQRQ--------RLAAVKRELEIKEIHLQ--DAARRRLlklqq 785
Cdd:pfam01576  984 EQESRERQ--AANKLVRRTEKKLKEVLLQveDERRHADQYKdqaekgnsRMKQLKRQLEEAEEEASraNAARRKL----- 1056

                   ....*.
gi 57157855    786 dQREME 791
Cdd:pfam01576 1057 -QRELD 1061
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
702-835 6.77e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 43.63  E-value: 6.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855    702 FLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEE---TRREILLQEEEKmaqQRQRLAAVKREL--EIKEIHLQDA- 775
Cdd:pfam01576  150 LSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEamiSDLEERLKKEEK---GRQELEKAKRKLegESTDLQEQIAe 226
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57157855    776 --ARRRLLKLQQDQREMELR----RLEDEIERK--VQMRDQEIAATAKDLeirQLELEAQKRLYEKVE 835
Cdd:pfam01576  227 lqAQIAELRAQLAKKEEELQaalaRLEEETAQKnnALKKIRELEAQISEL---QEDLESERAARNKAE 291
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
697-833 6.94e-04

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 43.29  E-value: 6.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855    697 NDELDFlrerQTVENMQAEVDEQ-----------RAKDEAWYQKQELLRRAEETRREILL--QEEEKMAQQRQRLAAVKR 763
Cdd:pfam12128  190 SKEGKF----RDVKSMIVAILEDdgvvppksrlnRQQVEHWIRDIQAIAGIMKIRPEFTKlqQEFNTLESAELRLSHLHF 265
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57157855    764 EleIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEA---QKRLYEK 833
Cdd:pfam12128  266 G--YKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEAledQHGAFLD 336
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
693-829 7.46e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 43.10  E-value: 7.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 693 ERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQEllRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHL 772
Cdd:COG3064  16 ERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAE--EEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKA 93
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 57157855 773 QDAARRRLLKLQQDQREmelrrledeiERKVQMRDQEIAATAKdleiRQLELEAQKR 829
Cdd:COG3064  94 AAEKAKAAKEAEAAAAA----------EKAAAAAEKEKAEEAK----RKAEEEAKRK 136
WD40 pfam00400
WD domain, G-beta repeat;
116-153 8.19e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 37.71  E-value: 8.19e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 57157855   116 KELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWD 153
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDgTVKVWD 39
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
728-830 8.25e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 8.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 728 QKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRD 807
Cdd:COG1196 676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
                        90       100
                ....*....|....*....|....
gi 57157855 808 QEIAATAKDLEIRQLELEAQ-KRL 830
Cdd:COG1196 756 LPEPPDLEELERELERLEREiEAL 779
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
719-838 8.43e-04

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 41.61  E-value: 8.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   719 QRAKDEAWY--------QKQELLRRAEETRREillqeEEKMAQQRQRLAAVKRE--LEIKEihlQDAARRRLLKLQQDQR 788
Cdd:pfam13904  50 ERQPLEAYEnwlaakqrQRQKELQAQKEEREK-----EEQEAELRKRLAKEKYQewLQRKA---RQQTKKREESHKQKAA 121
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   789 EM--------ELRRLEDEIERKVQ--MRDQEIAATAKDLEIRQLELEAQKRLYEKVESSS 838
Cdd:pfam13904 122 ESaskslakpERKVSQEEAKEVLQewERKKLEQQQRKREEEQREQLKKEEEEQERKQLAE 181
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
705-838 9.75e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.85  E-value: 9.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855    705 ERQTVENMQAEVDEQRAKDEAwyQKQELLRRAEETRREILLQEEE--KMAQQRQRLAAVKRELEIKEI-----------H 771
Cdd:pfam01576  392 ELRTLQQAKQDSEHKRKKLEG--QLQELQARLSESERQRAELAEKlsKLQSELESVSSLLNEAEGKNIklskdvsslesQ 469
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855    772 LQDAAR------RRLLKLQQDQREME------LRRLEDE------IERKVQMRDQEIAATAKDLE-----IRQLElEAQK 828
Cdd:pfam01576  470 LQDTQEllqeetRQKLNLSTRLRQLEdernslQEQLEEEeeakrnVERQLSTLQAQLSDMKKKLEedagtLEALE-EGKK 548
                          170
                   ....*....|
gi 57157855    829 RLYEKVESSS 838
Cdd:pfam01576  549 RLQRELEALT 558
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
684-832 1.05e-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: 42.75  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855    684 IVDYQTREWERIRN--DELDFL-RERQTVENMQAEVD---EQRAKDEAWYQKQ--ELLRRAEETRREILLQEEEKMAQQR 755
Cdd:TIGR02169  728 LEQEEEKLKERLEEleEDLSSLeQEIENVKSELKELEariEELEEDLHKLEEAlnDLEARLSHSRIPEIQAELSKLEEEV 807
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57157855    756 QRLAAVKRELEIKEihlqdaaRRRLLKLQQDQREM-ELRRLEDEIERKVQMRDQEIAATAKDLEIRQLEL-EAQKRLYE 832
Cdd:TIGR02169  808 SRIEARLREIEQKL-------NRLTLEKEYLEKEIqELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELeELEAALRD 879
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
690-836 1.05e-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: 42.75  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855    690 REWERIRNdELDFLRERqtVENMQAEVDE--------QRAKDEAwYQKQELLRRAEETRREILLQEEEKMAQQRQrlaAV 761
Cdd:TIGR02169  170 RKKEKALE-ELEEVEEN--IERLDLIIDEkrqqlerlRREREKA-ERYQALLKEKREYEGYELLKEKEALERQKE---AI 242
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57157855    762 KRELEIKEIHLQdaarrrllklqqdQREMELRRLEDEIERKVQMRDQEiaatakDLEIRQLELEAQKRLYEKVES 836
Cdd:TIGR02169  243 ERQLASLEEELE-------------KLTEEISELEKRLEEIEQLLEEL------NKKIKDLGEEEQLRVKEKIGE 298
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
706-828 1.12e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 1.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 706 RQTVENMQAEVDE-QRAKDEAWYQKQELLRRAEETRREILlQEEEKMAQQR----QRLAAVKRE----------LEIKEI 770
Cdd:COG3883  36 QAELDALQAELEElNEEYNELQAELEALQAEIDKLQAEIA-EAEAEIEERReelgERARALYRSggsvsyldvlLGSESF 114
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57157855 771 -----------HLQDAARRRLLKLQQDQREMElrRLEDEIERKVqmrdQEIAATAKDLEIRQLELEAQK 828
Cdd:COG3883 115 sdfldrlsalsKIADADADLLEELKADKAELE--AKKAELEAKL----AELEALKAELEAAKAELEAQQ 177
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
696-837 1.14e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.85  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855    696 RNDELDFLRERQT-VENMQAEVDEQRA-KDEAWYQKQELLRRAEETRREIL-LQEEEKMAQQRQRLAAVKRElEIKEiHL 772
Cdd:pfam01576  793 REEAVKQLKKLQAqMKDLQRELEEARAsRDEILAQSKESEKKLKNLEAELLqLQEDLAASERARRQAQQERD-ELAD-EI 870
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855    773 QDAARRRLLkLQQDQREMELR--RLEDEIERK---VQMRDQEIAATAKDLEIRQLELEAQKRLYEKVESS 837
Cdd:pfam01576  871 ASGASGKSA-LQDEKRRLEARiaQLEEELEEEqsnTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESA 939
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
683-836 1.17e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 42.65  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855    683 FIVDYQTREWE-RIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRR-EILLQEEEKMAQQRQRLAA 760
Cdd:pfam02463  168 KRKKKEALKKLiEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLyLDYLKLNEERIDLLQELLR 247
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57157855    761 VKRELEIKEIHLQDAARRrllKLQQDQREMElrrledEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKVES 836
Cdd:pfam02463  248 DEQEEIESSKQEIEKEEE---KLAQVLKENK------EEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE 314
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
697-833 1.27e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.45  E-value: 1.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 697 NDELDFLRERQTV-----------ENMQAEVDEQRAKDEAWYQKQELLRRA-EETRREI------LLQEEEKMAQQRQRL 758
Cdd:COG1579   3 PEDLRALLDLQELdseldrlehrlKELPAELAELEDELAALEARLEAAKTElEDLEKEIkrleleIEEVEARIKKYEEQL 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57157855 759 AAVK--RELEI--KEIHlqdaarrrLLKLQQDQREMELRRLEDEIERKvqmrDQEIAATAKDLEIRQLELEAQKRLYEK 833
Cdd:COG1579  83 GNVRnnKEYEAlqKEIE--------SLKRRISDLEDEILELMERIEEL----EEELAELEAELAELEAELEEKKAELDE 149
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
731-829 1.30e-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: 42.06  E-value: 1.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 731 ELLRRAEETRREILlqeeEKMAQQRQRLAAVKRELEIKEIHLQD-----AARRRLLKLQQDQREMELRRLEDEIERKvQM 805
Cdd:COG4942 139 QYLKYLAPARREQA----EELRADLAELAALRAELEAERAELEAllaelEEERAALEALKAERQKLLARLEKELAEL-AA 213
                        90       100
                ....*....|....*....|....*.
gi 57157855 806 RDQEIAATAKDLE--IRQLELEAQKR 829
Cdd:COG4942 214 ELAELQQEAEELEalIARLEAEAAAA 239
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
693-839 1.36e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 1.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 693 ERIRNDELDFLRER-QTVENMQAEVDEQRAKDEAWYQKQELLRRAEEtRREILLQEEEKMAQQRQRLAAVKRELEIKEIH 771
Cdd:COG4717  49 ERLEKEADELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQE-ELEELEEELEELEAELEELREELEKLEKLLQL 127
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57157855 772 LQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQeiaatakdleIRQLELE---AQKRLYEKVESSSL 839
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEE----------LEELEAElaeLQEELEELLEQLSL 188
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
704-767 1.37e-03

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 40.03  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   704 RERQTVENMQAEVDEQRAKDEAWYQKQELL--------RRAEETRR-----------EILLQEEEKMAQQRQRLAAVKRE 764
Cdd:pfam15346  54 VLEELEREREAELEEERRKEEEERKKREELerileennRKIEEAQRkeaeerlamleEQRRMKEERQRREKEEEEREKRE 133

                  ...
gi 57157855   765 LEI 767
Cdd:pfam15346 134 QQK 136
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
703-833 1.40e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 42.26  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855    703 LRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEE---TRREIL------------LQEEEKMAQQRQRLAAVKRELEI 767
Cdd:TIGR00618  327 LMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEvatSIREIScqqhtltqhihtLQQQKTTLTQKLQSLCKELDILQ 406
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57157855    768 KEIHLQDAARRRLLKLQQDqremeLRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEK 833
Cdd:TIGR00618  407 REQATIDTRTSAFRDLQGQ-----LAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQS 467
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
703-822 1.48e-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: 42.25  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  703 LRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQE-----EEKMA--QQRQRLAAVKRELEIKE---IHL 772
Cdd:COG3096  528 LRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQaaeavEQRSElrQQLEQLRARIKELAARApawLAA 607
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57157855  773 QDAARR-------RLLKLQQ--DQREMELRRledeiERKVQMRDQEIAATAKDLE--IRQL 822
Cdd:COG3096  608 QDALERlreqsgeALADSQEvtAAMQQLLER-----EREATVERDELAARKQALEsqIERL 663
PRK03963 PRK03963
V-type ATP synthase subunit E; Provisional
730-834 1.51e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 167649 [Multi-domain]  Cd Length: 198  Bit Score: 40.51  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  730 QELLRRAEETRREIlLQEEEKMAQQrqrlaavkreleIKEihlqdAARRRllklQQDQREMELRRLEDEIErkvqMRDQE 809
Cdd:PRK03963   9 QEINREAEQKIEYI-LEEAQKEAEK------------IKE-----EARKR----AESKAEWILRKAKTQAE----LEKQR 62
                         90       100
                 ....*....|....*....|....*
gi 57157855  810 IAATAKdLEIRQLELEAQKRLYEKV 834
Cdd:PRK03963  63 IIANAK-LEVRRKRLAVQEELISEV 86
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
694-835 1.52e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  694 RIRNDELDflRERQTVENMQAEVDEQ--RAKD--EAWYQKQELLRRAE------ETRREILLQEEEKMAQQRQRLAAVKR 763
Cdd:PRK02224 474 RERVEELE--AELEDLEEEVEEVEERleRAEDlvEAEDRIERLEERREdleeliAERRETIEEKRERAEELRERAAELEA 551
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  764 ELEIKEIHLQDA------ARRRLLKLQQDQREmelrrLEDEIER--KVQMRDQEIAATAKDLEIRQ--------LELEAQ 827
Cdd:PRK02224 552 EAEEKREAAAEAeeeaeeAREEVAELNSKLAE-----LKERIESleRIRTLLAAIADAEDEIERLRekrealaeLNDERR 626

                 ....*...
gi 57157855  828 KRLYEKVE 835
Cdd:PRK02224 627 ERLAEKRE 634
YscO-like pfam16789
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ...
727-835 1.61e-03

YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. The family includes Chlamydia trachomatis CT670 which is found in a type III secretion gene cluster. CT670 interacts with CT671, a putative YscP homolog and CT670 and CT671 may form a chaperone-effector pair.


Pssm-ID: 435583 [Multi-domain]  Cd Length: 160  Bit Score: 40.20  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   727 YQKQELL----RRAEETRReILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDaarrrllKLQQDQREME----------- 791
Cdd:pfam16789   3 YPLEQVLdikkKRVEEAEK-VVKDKKRALEKEKEKLAELEAERDKVRKHKKA-------KMQQLRDEMDrgttsdkilqm 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 57157855   792 ---LRRLEDEI---ERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKVE 835
Cdd:pfam16789  75 kryIKVVKERLkqeEKKVQDQKEQVRTAARNLEIAREELKKKRQEVEKLE 124
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
778-836 1.90e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.68  E-value: 1.90e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 778 RRLLKLQQ-DQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKVES 836
Cdd:COG1579   7 RALLDLQElDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLEL 66
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
697-832 2.02e-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: 2.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 697 NDELDFLRER-QTVENMQAEVDEQRAKDEAWYQK-QELLRRAEETRREI------------LLQEEEKMAQQRQRL---- 758
Cdd:COG3206 211 SEEAKLLLQQlSELESQLAEARAELAEAEARLAAlRAQLGSGPDALPELlqspviqqlraqLAELEAELAELSARYtpnh 290
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 759 ---AAVKRELEIKEIHLQDAARRRLLKLQQD-----QREMELRRLEDEIERKVQmrdqeiAATAKDLEIRQL--ELEAQK 828
Cdd:COG3206 291 pdvIALRAQIAALRAQLQQEAQRILASLEAElealqAREASLQAQLAQLEARLA------ELPELEAELRRLerEVEVAR 364

                ....
gi 57157855 829 RLYE 832
Cdd:COG3206 365 ELYE 368
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
706-814 2.11e-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: 2.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 706 RQTVENMQAEVDEQRAKdeawYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQ---DAARRRLLK 782
Cdd:COG4942 142 KYLAPARREQAEELRAD----LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEkelAELAAELAE 217
                        90       100       110
                ....*....|....*....|....*....|..
gi 57157855 783 LQQDQRemELRRLEDEIERKVQMRDQEIAATA 814
Cdd:COG4942 218 LQQEAE--ELEALIARLEAEAAAAAERTPAAG 247
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
727-835 2.14e-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: 41.97  E-value: 2.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855    727 YQKQELlrraEETRREILLQEEeKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQ-DQREMELRRLEDEIERKVQM 805
Cdd:TIGR02168  674 ERRREI----EELEEKIEELEE-KIAELEKALAELRKELEELEEELEQLRKELEELSRQiSALRKDLARLEAEVEQLEER 748
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 57157855    806 RDQ----------EIAATAKDLEIRQLELEAQKRLYEKVE 835
Cdd:TIGR02168  749 IAQlskelteleaEIEELEERLEEAEEELAEAEAEIEELE 788
PRK02292 PRK02292
V-type ATP synthase subunit E; Provisional
748-834 2.29e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 235026 [Multi-domain]  Cd Length: 188  Bit Score: 39.98  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  748 EEKMAQQRQRLAAVKRELEIKEIHLQDAARRRllklQQDQREMELRRLEDEIErkvQMRDQEIAaTAKdLEIRQLELEAQ 827
Cdd:PRK02292   8 EDIRDEARARASEIRAEADEEAEEIIAEAEAD----AEEILEDREAEAEREIE---QLREQELS-SAK-LEAKRERLNAR 78

                 ....*..
gi 57157855  828 KRLYEKV 834
Cdd:PRK02292  79 KEVLEDV 85
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
690-835 2.37e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 2.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  690 REWERIRNDELDFLRER--QTVEnmqaEVDEQRAKDEAWYQKQELLRRAE---ETRREILLQEEEKMAQQRQRLAAVKRE 764
Cdd:PRK03918 566 DELEEELAELLKELEELgfESVE----ELEERLKELEPFYNEYLELKDAEkelEREEKELKKLEEELDKAFEELAETEKR 641
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  765 LEIKEIHLQDA-----------ARRRLLKLqqdqrEMELRRLEDEIERKVQMRDqEIAATAKDLEIRQLELEAQKRLYEK 833
Cdd:PRK03918 642 LEELRKELEELekkyseeeyeeLREEYLEL-----SRELAGLRAELEELEKRRE-EIKKTLEKLKEELEEREKAKKELEK 715

                 ..
gi 57157855  834 VE 835
Cdd:PRK03918 716 LE 717
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
693-835 2.81e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 2.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  693 ERIRNDELDF---LRERQTVENMQAEVDEQRAKDEAWYQKQELLR-RAEETRREILLQE------EEKMAQQRQRLAAVK 762
Cdd:PRK03918 193 ELIKEKEKELeevLREINEISSELPELREELEKLEKEVKELEELKeEIEELEKELESLEgskrklEEKIRELEERIEELK 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  763 REL--------EIKEIHLQDAARRRLLKLQQDQREmELRRLEDEIERkVQMRDQEIAATAKDLEIRQLELEAQKRLYEKV 834
Cdd:PRK03918 273 KEIeeleekvkELKELKEKAEEYIKLSEFYEEYLD-ELREIEKRLSR-LEEEINGIEERIKELEEKEERLEELKKKLKEL 350

                 .
gi 57157855  835 E 835
Cdd:PRK03918 351 E 351
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
728-835 2.92e-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: 41.48  E-value: 2.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  728 QKQELLRRAEETRREiLLQEEEKMAQQRQRLAAVKRELEIK---EIHLQ---DAARRRLLKLQQDQREMElrrledeier 801
Cdd:COG3096  279 ERRELSERALELRRE-LFGARRQLAEEQYRLVEMARELEELsarESDLEqdyQAASDHLNLVQTALRQQE---------- 347
                         90       100       110
                 ....*....|....*....|....*....|....
gi 57157855  802 KVQMRDQEIAATAKDLEIRQLELEAQKRLYEKVE 835
Cdd:COG3096  348 KIERYQEDLEELTERLEEQEEVVEEAAEQLAEAE 381
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
719-833 2.99e-03

Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.


Pssm-ID: 405647 [Multi-domain]  Cd Length: 206  Bit Score: 39.75  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   719 QRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLaaVKRELEIKEIHLQDAARRRLLKLQQDQrEMELRRLEDE 798
Cdd:pfam14988  17 QKKIEKLWNQYVQECEEIERRRQELASRYTQQTAELQTQL--LQKEKEQASLKKELQALRPFAKLKESQ-EREIQDLEEE 93
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 57157855   799 IeRKVQmrdQEIAATAKDLEIRQLEleaQKRLYEK 833
Cdd:pfam14988  94 K-EKVR---AETAEKDREAHLQFLK---EKALLEK 121
YscO-like pfam16789
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ...
688-804 3.03e-03

YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. The family includes Chlamydia trachomatis CT670 which is found in a type III secretion gene cluster. CT670 interacts with CT671, a putative YscP homolog and CT670 and CT671 may form a chaperone-effector pair.


Pssm-ID: 435583 [Multi-domain]  Cd Length: 160  Bit Score: 39.05  E-value: 3.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   688 QTREWERIRNDELDFLRE--RQTVENMQAEVDEQRAKDeawyqKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKREL 765
Cdd:pfam16789  32 KEKEKLAELEAERDKVRKhkKAKMQQLRDEMDRGTTSD-----KILQMKRYIKVVKERLKQEEKKVQDQKEQVRTAARNL 106
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 57157855   766 EIKEIHLQDaARRRLLKLQQDQREM--ELRRLEDEIERKVQ 804
Cdd:pfam16789 107 EIAREELKK-KRQEVEKLEKHKKEWvkEMKKEEEDQEEREQ 146
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
642-769 3.26e-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: 40.52  E-value: 3.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 642 VIREVYHLMETTPADI--HPNSMLDAFVALTKGQYpiFNQYPKFIVDYQTREWERIRNDELDFLRERQTVENMQAEVDEQ 719
Cdd:COG4942 109 LLRALYRLGRQPPLALllSPEDFLDAVRRLQYLKY--LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 57157855 720 RAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKE 769
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
700-835 3.29e-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: 3.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  700 LDFLRERQT---VENMQAEVDEQRAKDEAWYQKqelLRRAEETR---REILLQEEEKMAQQRQRLAAVKRELEIKEIHLQ 773
Cdd:COG3096  960 LSEVVQRRPhfsYEDAVGLLGENSDLNEKLRAR---LEQAEEARreaREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQ 1036
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57157855  774 DAARR-RLLKLQQDQrEMELR-RLE-DEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKVE 835
Cdd:COG3096 1037 ELEQElEELGVQADA-EAEERaRIRrDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAE 1100
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
714-827 3.58e-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: 3.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855    714 AEVDEQRAKDEAwyQKQELLR---------RAEETRREILLQEEEKMAQQRQRLaavkrELEIKEihlQDAARRRlLKLQ 784
Cdd:pfam01576   57 AEAEEMRARLAA--RKQELEEilhelesrlEEEEERSQQLQNEKKKMQQHIQDL-----EEQLDE---EEAARQK-LQLE 125
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 57157855    785 QDQREMELRRLEDEIerkVQMRDQ--EIAATAKDLEIRQLELEAQ 827
Cdd:pfam01576  126 KVTTEAKIKKLEEDI---LLLEDQnsKLSKERKLLEERISEFTSN 167
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
690-814 3.83e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 3.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 690 REWERIRN------DELDFLRER-QTVENMQAEVDEQRAK-DEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAV 761
Cdd:COG4717 132 QELEALEAelaelpERLEELEERlEELRELEEELEELEAElAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 57157855 762 KRELEikeihlqdAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATA 814
Cdd:COG4717 212 EEELE--------EAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAA 256
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
700-833 4.24e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.77  E-value: 4.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 700 LDFLRERqtVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREI---------LLQEEEKMAQQRQRLAAVKRELEIKEI 770
Cdd:COG3206 177 LEFLEEQ--LPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLqqlselesqLAEARAELAEAEARLAALRAQLGSGPD 254
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 771 HLQDAA--------RRRLLKLQQDQREM---------ELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEK 833
Cdd:COG3206 255 ALPELLqspviqqlRAQLAELEAELAELsarytpnhpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQA 334
NtpE COG1390
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
729-834 5.18e-03

Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441000 [Multi-domain]  Cd Length: 196  Bit Score: 39.16  E-value: 5.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 729 KQELLRRAEETRREILLQEEEKmaqqrqrlaavkRELEIKEihlqdaARRRLLKlqqdQREMELRRLEDEIERKvqmRDQ 808
Cdd:COG1390   8 IEEILEEAEAEAEEILEEAEEE------------AEKILEE------AEEEAEE----IKEEILEKAEREAERE---KRR 62
                        90       100
                ....*....|....*....|....*.
gi 57157855 809 EIAATakDLEIRQLELEAQKRLYEKV 834
Cdd:COG1390  63 IISSA--ELEARKELLEAKEELIEEV 86
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
696-835 5.27e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 5.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  696 RNDELDFLRERQ-TVENMQAEVDEQRAKDEAWYQKQEllrraeetrreillQEEEKMAQQRQRlaavKRELE--IKEIHL 772
Cdd:PRK02224 587 RIESLERIRTLLaAIADAEDEIERLREKREALAELND--------------ERRERLAEKRER----KRELEaeFDEARI 648
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57157855  773 QDA-ARRRLLKLQQDQREMELRRLE---DEIERKVQMRDQEIAATA------KDLEIRQLELEAqkrLYEKVE 835
Cdd:PRK02224 649 EEArEDKERAEEYLEQVEEKLDELReerDDLQAEIGAVENELEELEelrerrEALENRVEALEA---LYDEAE 718
ClassIIa_HDAC5_Gln-rich-N cd10164
Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase; This ...
703-799 5.99e-03

Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase; This family consists of the glutamine-rich domain of histone deacetylase 5 (HDAC5). It belongs to a superfamily that consists of the glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDCA9; it is missing from HDAC7. This domain confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors, and it is able to repress transcription independently of the HDAC C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues.


Pssm-ID: 197400 [Multi-domain]  Cd Length: 97  Bit Score: 37.11  E-value: 5.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 703 LRERQTVENMQAEVDEQRAKDE---AWYQKQ-ELLRRAEETR--REILLQEEEKMAQQRQRLAAVKRELEIKEihlqdaA 776
Cdd:cd10164   4 LREQQLQQELLLLKQQQQLQKQllfAEFQKQhEHLTRQHEVQlqKHLKVRAELFSEQQQQEILAAKRQQELEQ------Q 77
                        90       100
                ....*....|....*....|...
gi 57157855 777 RRRLlklQQDQREMELRRLEDEI 799
Cdd:cd10164  78 RKRE---QQRQEELEKQRLEQQL 97
NtpE COG1390
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
711-800 6.29e-03

Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441000 [Multi-domain]  Cd Length: 196  Bit Score: 38.77  E-value: 6.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 711 NMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQR-QRLAAVKRELE-IKEIHLQDA---ARRRLLKLQQ 785
Cdd:COG1390   1 MMSLEKIIEEILEEAEAEAEEILEEAEEEAEKILEEAEEEAEEIKeEILEKAEREAErEKRRIISSAeleARKELLEAKE 80
                        90
                ....*....|....*
gi 57157855 786 DQREMELRRLEDEIE 800
Cdd:COG1390  81 ELIEEVFEEALEKLK 95
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
697-833 6.98e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.51  E-value: 6.98e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 697 NDELDFLRE-RQTVENMQAEVDEQRakDEAWYQKQELLRRAEETR--REILLQEEEKMAQQRQRLAAVKREL--EIKEIH 771
Cdd:COG1340  21 REEIEELKEkRDELNEELKELAEKR--DELNAQVKELREEAQELRekRDELNEKVKELKEERDELNEKLNELreELDELR 98
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57157855 772 lQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEiaataKDL--EIRQLE--LEAQKRLYEK 833
Cdd:COG1340  99 -KELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEE-----KELveKIKELEkeLEKAKKALEK 158
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
730-836 7.29e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 7.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 730 QEL---LRRAEETRREI---LLQEEEKMAQQRQRLAAVKREL-----EIKEIHLQ-DAARRRLLKLQQDQREM----ELR 793
Cdd:COG1579  13 QELdseLDRLEHRLKELpaeLAELEDELAALEARLEAAKTELedlekEIKRLELEiEEVEARIKKYEEQLGNVrnnkEYE 92
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 57157855 794 RLEDEIE---RKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKVES 836
Cdd:COG1579  93 ALQKEIEslkRRISDLEDEILELMERIEELEEELAELEAELAELEA 138
mukB PRK04863
chromosome partition protein MukB;
686-836 7.73e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 7.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   686 DYQTRE--WERIRN--DELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREI---LLQEEEKMAQQRQRL 758
Cdd:PRK04863  943 DYQQAQqtQRDAKQqaFALTEVVQRRAHFSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAreqLRQAQAQLAQYNQVL 1022
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   759 AAVKRELEIKEIHLQDAARR-RLLKLQQDQ-REMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKVES 836
Cdd:PRK04863 1023 ASLKSSYDAKRQMLQELKQElQDLGVPADSgAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLER 1102
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
697-835 8.67e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 8.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  697 NDELDFLRERQTVENMQAEVDEQrakDEAWYQKQELLRRAEETRREiLLQEEEKMAQQRQRLAAVKRELEikEIHLQDAA 776
Cdd:COG4913  637 EAELDALQERREALQRLAEYSWD---EIDVASAEREIAELEAELER-LDASSDDLAALEEQLEELEAELE--ELEEELDE 710
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57157855  777 ---RRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATA----KDLEIRQLELEAQKRLYEKVE 835
Cdd:COG4913  711 lkgEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLeerfAAALGDAVERELRENLEERID 776
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
693-834 9.29e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.75  E-value: 9.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 693 ERIRNDELDFLRERQTVENMQAEVDEQRAKDEAW------------YQKQ-ELLRRAEETRREILLQEEEKMAQQRQRLA 759
Cdd:COG1579  48 EAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeyeaLQKEiESLKRRISDLEDEILELMERIEELEEELA 127
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57157855 760 AVKRELEikeihlqdaARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLeirqleleaqKRLYEKV 834
Cdd:COG1579 128 ELEAELA---------ELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPEL----------LALYERI 183
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
689-815 9.45e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 39.63  E-value: 9.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855   689 TREWERIRN---DELDFLRERQTVENMQAE--VDEQRAKDEAWYQKQELLRRAEETRREiLLQEEEKMAQQRQRLAAVKR 763
Cdd:pfam05667 421 AGQWEKHRVpliEEYRALKEAKSNKEDESQrkLEEIKELREKIKEVAEEAKQKEELYKQ-LVAEYERLPKDVSRSAYTRR 499
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 57157855   764 ELEI-KEIHLQdaaRRRLLKLQQDQREM--ELRRLEDEIERKVQMRDQEIAATAK 815
Cdd:pfam05667 500 ILEIvKNIKKQ---KEEITKILSDTKSLqkEINSLTGKLDRTFTVTDELVFKDAK 551
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
690-839 9.79e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 9.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 690 REWERIRNdELDFLRERQTVENMQAEV-----DEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMA--------QQRQ 756
Cdd:COG4717 354 REAEELEE-ELQLEELEQEIAALLAEAgvedeEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllealdeeELEE 432
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855 757 RLAAVKRELEIKEIHLQDAaRRRLLKLQQDQREME----LRRLEDEIERKVqmrdQEIAATAKDLEIRQLELEAQKRLYE 832
Cdd:COG4717 433 ELEELEEELEELEEELEEL-REELAELEAELEQLEedgeLAELLQELEELK----AELRELAEEWAALKLALELLEEARE 507

                ....*..
gi 57157855 833 KVESSSL 839
Cdd:COG4717 508 EYREERL 514
PRK02292 PRK02292
V-type ATP synthase subunit E; Provisional
713-798 9.85e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 235026 [Multi-domain]  Cd Length: 188  Bit Score: 38.05  E-value: 9.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57157855  713 QAEVDEQRAKDEAwyQKQELLRRAEETRREIL---LQEEEKMAQQ--RQRLAAVKreLEIKEIHLqdAARRRLLKLQQDQ 787
Cdd:PRK02292  15 RARASEIRAEADE--EAEEIIAEAEADAEEILedrEAEAEREIEQlrEQELSSAK--LEAKRERL--NARKEVLEDVRNQ 88
                         90
                 ....*....|.
gi 57157855  788 REMELRRLEDE 798
Cdd:PRK02292  89 VEDEIASLDGD 99
 
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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