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Conserved domains on  [gi|264681545|ref|NP_001161151|]
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TBC1 domain family member 31 isoform 2 [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 4.82e-28

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 117.32  E-value: 4.82e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  48 VAFDGSGDSFIAGDHQGNIYVFDLH-GNRFNLVQRTAQACTALAFNlrRKSEFLV-ALADYSIKCFDTVTKELVSWMRGH 125
Cdd:COG2319  126 VAFSPDGKTLASGSADGTVRLWDLAtGKLLRTLTGHSGAVTSVAFS--PDGKLLAsGSDDGTVRLWDLATGKLLRTLTGH 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 126 ESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLFCKY 204
Cdd:COG2319  204 TGAVRSVAFSPDGKLLASGSADgTVRLWDLATGKLLRTLTGHSG-SVRSVAFSPDGRLLASGSADGTVRLWDLATGELLR 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 205 QLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQmpAKVRAVRHLEFLPDsfdagsNQVLGVLSQ 284
Cdd:COG2319  283 TLTGHSGGVNSV----AFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT--GHTGAVRSVAFSPD------GKTLASGSD 350
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 264681545 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 4.19e-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: 66.69  E-value: 4.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  688 QTREWERIRNDELDflrERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEE----KMAQQRQRLAAVKR 763
Cdd:pfam17380 444 RAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEerkqAMIEEERKRKLLEK 520
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 264681545  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 3.99e-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: 56.88  E-value: 3.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  461 SLQKKYPIKSRKLLRVLQRTLSALAHWsaiFSDTPY---LPLLAFPFVkLFQNNQLICFEVVATLIINwcQHWFEYFPN- 536
Cdd:pfam00566  19 TFPHSFFFDNGPGQNSLRRILKAYSIY---NPDVGYcqgMNFIAAPLL-LVYLDEEDAFWCFVSLLEN--YLLRDFYTPd 92
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 264681545  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 4.82e-28

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 117.32  E-value: 4.82e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  48 VAFDGSGDSFIAGDHQGNIYVFDLH-GNRFNLVQRTAQACTALAFNlrRKSEFLV-ALADYSIKCFDTVTKELVSWMRGH 125
Cdd:COG2319  126 VAFSPDGKTLASGSADGTVRLWDLAtGKLLRTLTGHSGAVTSVAFS--PDGKLLAsGSDDGTVRLWDLATGKLLRTLTGH 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 126 ESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLFCKY 204
Cdd:COG2319  204 TGAVRSVAFSPDGKLLASGSADgTVRLWDLATGKLLRTLTGHSG-SVRSVAFSPDGRLLASGSADGTVRLWDLATGELLR 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 205 QLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQmpAKVRAVRHLEFLPDsfdagsNQVLGVLSQ 284
Cdd:COG2319  283 TLTGHSGGVNSV----AFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT--GHTGAVRSVAFSPD------GKTLASGSD 350
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 264681545 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 7.52e-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: 7.52e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  39 HPKVLRFlnVAFDGSGDSFIAGDHQGNIYVFDLHGNRFNLVQR----TAQACTALAFNLRrkseFLVALADYSIKCFDTV 114
Cdd:cd00200    8 HTGGVTC--VAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKghtgPVRDVAASADGTY----LASGSSDKTIRLWDLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 115 TKELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 193
Cdd:cd00200   82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDkTIKVWDVETGKCLTTLRGHTD-WVNSVAFSPDGTFVASSSQDGTIK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 194 AWECDTLFCKYQLPGpPEGSnilykVFAVT--RDGRILAAGGKSNHLHLWclEATGLFRIIQMPAKVRAVRHLEFLPDsf 271
Cdd:cd00200  161 LWDLRTGKCVATLTG-HTGE-----VNSVAfsPDGEKLLSSSSDGTIKLW--DLSTGKCLGTLRGHENGVNSVAFSPD-- 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 264681545 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 4.19e-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: 66.69  E-value: 4.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  688 QTREWERIRNDELDflrERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEE----KMAQQRQRLAAVKR 763
Cdd:pfam17380 444 RAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEerkqAMIEEERKRKLLEK 520
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 264681545  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 7.40e-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: 7.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 688 QTREWE-RIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELL---RRAEETRREILLQEEEKMAQQRQRLAAVKR 763
Cdd:COG1196  261 ELAELEaELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLeerRRELEERLEELEEELAELEEELEELEEELE 340
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 264681545 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 3.99e-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: 56.88  E-value: 3.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  461 SLQKKYPIKSRKLLRVLQRTLSALAHWsaiFSDTPY---LPLLAFPFVkLFQNNQLICFEVVATLIINwcQHWFEYFPN- 536
Cdd:pfam00566  19 TFPHSFFFDNGPGQNSLRRILKAYSIY---NPDVGYcqgMNFIAAPLL-LVYLDEEDAFWCFVSLLEN--YLLRDFYTPd 92
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 264681545  537 -PPINILSMI-ENVLAFHDKELLQHFIDRDITSQVYAWPLLETLFSEVLTREEWLRLFDNIFSNHPSFLLM 605
Cdd:pfam00566  93 fPGLKRDLYVfEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVLF 163
PRK12704 PRK12704
phosphodiesterase; Provisional
682-832 1.39e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 55.17  E-value: 1.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 682 KFIVDYQTREWERIRNDEL-----DFLRERQTVENmqaEVDEQRAKdeawYQKQEL-LRRAEET---RREILLQEEEKMA 752
Cdd:PRK12704  41 KRILEEAKKEAEAIKKEALleakeEIHKLRNEFEK---ELRERRNE----LQKLEKrLLQKEENldrKLELLEKREEELE 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 753 QQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQ-------DQREMELRRLEDEIErkvqmrdQEIAATAKDLEiRQLELE 825
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEELEELIEEQLQELERisgltaeEAKEILLEKVEEEAR-------HEAAVLIKEIE-EEAKEE 185

                 ....*..
gi 264681545 826 AQKRLYE 832
Cdd:PRK12704 186 ADKKAKE 192
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
685-843 6.16e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 6.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545   685 VDYQTREWERIRNDELDFLRERQTVENM-QAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKR 763
Cdd:TIGR02168  321 LEAQLEELESKLDELAEELAELEEKLEElKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545   764 ELEIKEIHLQDAARRRLlKLQQDQREMELRRLE---DEIERKVQMRDQEIAATAKDLE---------------IRQLELE 825
Cdd:TIGR02168  401 EIERLEARLERLEDRRE-RLQQEIEELLKKLEEaelKELQAELEELEEELEELQEELErleealeelreeleeAEQALDA 479
                          170       180
                   ....*....|....*....|
gi 264681545   826 AQKRLYEKYS--FSLSFMQN 843
Cdd:TIGR02168  480 AERELAQLQArlDSLERLQE 499
COG5210 COG5210
GTPase-activating protein [General function prediction only];
542-658 3.18e-05

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 47.49  E-value: 3.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 542 LSMIENVLAFHDKELLQHFIDRDITSQVYAWPLLETLFSEVLTREEWLRLFDNIFSNHPSFLLMTVVAYSTCSRAPLLNC 621
Cdd:COG5210  350 LKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKL 429
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 264681545 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 5.66e-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: 5.66e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 264681545   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 1.43e-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: 43.83  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545   501 AFP-FVKLFQNNQLIcFEVVATLIINWCQHWFEYFpnppinilsmienvLAFHDKELLQHFIDRDITSQVYAWPLLETLF 579
Cdd:smart00164 112 AFWcLVKLMERYGPN-FYLPDMSGLQLDLLQLDRL--------------VKEYDPDLYKHLKDLGITPSLYALRWFLTLF 176
                           90       100       110
                   ....*....|....*....|....*....|
gi 264681545   580 SEVLTREEWLRLFDNIFSNHPSFLLMTVVA 609
Cdd:smart00164 177 ARELPLEIVLRIWDVLFAEGSDFLFRVALA 206
WD40 pfam00400
WD domain, G-beta repeat;
116-153 8.25e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 37.71  E-value: 8.25e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 264681545  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 4.83e-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: 4.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 703 LRERQTVENMQAEVDEQRAKDE---AWYQKQ-ELLRRAEETR--REILLQEEEKMAQQRQRLAAVKRELEIKEihlqdaA 776
Cdd:cd10164    4 LREQQLQQELLLLKQQQQLQKQllfAEFQKQhEHLTRQHEVQlqKHLKVRAELFSEQQQQEILAAKRQQELEQ------Q 77
                         90       100
                 ....*....|....*....|...
gi 264681545 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 4.82e-28

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 117.32  E-value: 4.82e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  48 VAFDGSGDSFIAGDHQGNIYVFDLH-GNRFNLVQRTAQACTALAFNlrRKSEFLV-ALADYSIKCFDTVTKELVSWMRGH 125
Cdd:COG2319  126 VAFSPDGKTLASGSADGTVRLWDLAtGKLLRTLTGHSGAVTSVAFS--PDGKLLAsGSDDGTVRLWDLATGKLLRTLTGH 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 126 ESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLFCKY 204
Cdd:COG2319  204 TGAVRSVAFSPDGKLLASGSADgTVRLWDLATGKLLRTLTGHSG-SVRSVAFSPDGRLLASGSADGTVRLWDLATGELLR 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 205 QLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQmpAKVRAVRHLEFLPDsfdagsNQVLGVLSQ 284
Cdd:COG2319  283 TLTGHSGGVNSV----AFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT--GHTGAVRSVAFSPD------GKTLASGSD 350
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 264681545 285 DGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQ 336
Cdd:COG2319  351 DGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
44-340 1.25e-26

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 113.47  E-value: 1.25e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  44 RFLNVAFDGSGDSFIAGDHQGNIYVFDL-HGNRFNLVQRTAQACTALAFNLRRKSeFLVALADYSIKCFDTVTKELVSWM 122
Cdd:COG2319   80 AVLSVAFSPDGRLLASASADGTVRLWDLaTGLLLRTLTGHTGAVRSVAFSPDGKT-LASGSADGTVRLWDLATGKLLRTL 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 123 RGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLF 201
Cdd:COG2319  159 TGHSGAVTSVAFSPDGKLLASGSDDgTVRLWDLATGKLLRTLTGHTG-AVRSVAFSPDGKLLASGSADGTVRLWDLATGK 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 202 CKYQLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQMPAkvRAVRHLEFLPDSfdagsnQVLGV 281
Cdd:COG2319  238 LLRTLTGHSGSVRSV----AFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHS--GGVNSVAFSPDG------KLLAS 305
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 264681545 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 7.52e-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: 7.52e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  39 HPKVLRFlnVAFDGSGDSFIAGDHQGNIYVFDLHGNRFNLVQR----TAQACTALAFNLRrkseFLVALADYSIKCFDTV 114
Cdd:cd00200    8 HTGGVTC--VAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKghtgPVRDVAASADGTY----LASGSSDKTIRLWDLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 115 TKELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 193
Cdd:cd00200   82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDkTIKVWDVETGKCLTTLRGHTD-WVNSVAFSPDGTFVASSSQDGTIK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 194 AWECDTLFCKYQLPGpPEGSnilykVFAVT--RDGRILAAGGKSNHLHLWclEATGLFRIIQMPAKVRAVRHLEFLPDsf 271
Cdd:cd00200  161 LWDLRTGKCVATLTG-HTGE-----VNSVAfsPDGEKLLSSSSDGTIKLW--DLSTGKCLGTLRGHENGVNSVAFSPD-- 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 264681545 272 dagsNQVLGVLSQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYS 334
Cdd:cd00200  231 ----GYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
39-336 1.54e-24

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 106.92  E-value: 1.54e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  39 HPKVLRFLNVAFDGSGDSFIAGDHQGNIYVFDLHGNRFNLVQRTAQAcTALAFNLRRKSeFLVALADYSIKCFDTVTKEL 118
Cdd:COG2319   35 LAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAV-LSVAFSPDGRL-LASASADGTVRLWDLATGLL 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 119 VSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNiRQSVGIQKVFFLPLSNTILSCFKDNSIFAWEC 197
Cdd:COG2319  113 LRTLTGHTGAVRSVAFSPDGKTLASGSADgTVRLWDLATGKLLRTLT-GHSGAVTSVAFSPDGKLLASGSDDGTVRLWDL 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 198 DTLFCKYQLPGPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQMPAkvRAVRHLEFLPDSfdagsnQ 277
Cdd:COG2319  192 ATGKLLRTLTGHTGAVRSV----AFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHS--GSVRSVAFSPDG------R 259
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 264681545 278 VLGVLSQDGIMRFVNIQTCKLLFEIGTVEEGISSSVISPHGRYIASIMENGSLNVYSVQ 336
Cdd:COG2319  260 LLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLA 318
WD40 COG2319
WD40 repeat [General function prediction only];
49-336 7.10e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 96.13  E-value: 7.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  49 AFDGSGDSFIAGDHQGNIYVFDLHGNRFNLVQRTAQACTALAFNLRRKSEFLVALADYSIKCFDTVTKELVSWMRGHESS 128
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 129 VCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLFCKYQLP 207
Cdd:COG2319   81 VLSVAFSPDGRLLASASADgTVRLWDLATGLLLRTLTGHTG-AVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 208 GPPEGSNILykvfAVTRDGRILAAGGKSNHLHLWCLEATGLFRIIQmpAKVRAVRHLEFLPDSfdagsnQVLGVLSQDGI 287
Cdd:COG2319  160 GHSGAVTSV----AFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT--GHTGAVRSVAFSPDG------KLLASGSADGT 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 264681545 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 2.40e-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: 2.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 123 RGHESSVCSISVHASGRYAITTSSD-TAQLWDLDTFQRKRKLNIrQSVGIQKVFFLPLSNTILSCFKDNSIFAWECDTLF 201
Cdd:cd00200    6 KGHTGGVTCVAFSPDGKLLATGSGDgTIKVWDLETGELLRTLKG-HTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 202 CKYQLPGPPEGsnilykVFAV--TRDGRILAAGGKSNHLHLWCLEATGLfrIIQMPAKVRAVRHLEFLPDsfdagsNQVL 279
Cdd:cd00200   85 CVRTLTGHTSY------VSSVafSPDGRILSSSSRDKTIKVWDVETGKC--LTTLRGHTDWVNSVAFSPD------GTFV 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 264681545 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 4.19e-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: 66.69  E-value: 4.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  688 QTREWERIRNDELDflrERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEE----KMAQQRQRLAAVKR 763
Cdd:pfam17380 444 RAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEerkqAMIEEERKRKLLEK 520
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 264681545  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 7.40e-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: 7.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 688 QTREWE-RIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELL---RRAEETRREILLQEEEKMAQQRQRLAAVKR 763
Cdd:COG1196  261 ELAELEaELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLeerRRELEERLEELEEELAELEEELEELEEELE 340
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 264681545 764 ELEIKEIHLQDAARRRLLKLQQ--DQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRL 830
Cdd:COG1196  341 ELEEELEEAEEELEEAEAELAEaeEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
WD40 COG2319
WD40 repeat [General function prediction only];
48-156 1.68e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 60.70  E-value: 1.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  48 VAFDGSGDSFIAGDHQGNIYVFDLH-GNRFNLVQRTAQACTALAFNlrRKSEFLV-ALADYSIKCFDTVTKELVSWMRGH 125
Cdd:COG2319  294 VAFSPDGKLLASGSDDGTVRLWDLAtGKLLRTLTGHTGAVRSVAFS--PDGKTLAsGSDDGTVRLWDLATGELLRTLTGH 371
                         90       100       110
                 ....*....|....*....|....*....|..
gi 264681545 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 ...
701-832 3.46e-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: 60.35  E-value: 3.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  701 DFLRERQT------VENMQAEVDEQRAkdeawyQKQELLRRAEETRREILLQ-----EEEKMAQQRQRLAAVKRELEIKE 769
Cdd:pfam15709 336 DRLRAERAemrrleVERKRREQEEQRR------LQQEQLERAEKMREELELEqqrrfEEIRLRKQRLEEERQRQEEEERK 409
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 264681545  770 IHLQDAARRRLLKLQQDqremELRRLEDEIERKVQmrdQEIAATAKDLEIRQLELEAQ-----KRLYE 832
Cdd:pfam15709 410 QRLQLQAAQERARQQQE----EFRRKLQELQRKKQ---QEEAERAEAEKQRQKELEMQlaeeqKRLME 470
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
461-605 3.99e-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: 56.88  E-value: 3.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  461 SLQKKYPIKSRKLLRVLQRTLSALAHWsaiFSDTPY---LPLLAFPFVkLFQNNQLICFEVVATLIINwcQHWFEYFPN- 536
Cdd:pfam00566  19 TFPHSFFFDNGPGQNSLRRILKAYSIY---NPDVGYcqgMNFIAAPLL-LVYLDEEDAFWCFVSLLEN--YLLRDFYTPd 92
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 264681545  537 -PPINILSMI-ENVLAFHDKELLQHFIDRDITSQVYAWPLLETLFSEVLTREEWLRLFDNIFSNHPSFLLM 605
Cdd:pfam00566  93 fPGLKRDLYVfEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVLF 163
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
690-834 9.18e-09

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: 58.01  E-value: 9.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  690 REWERIRNDELDflrERqtVENMQAEVDEQRAKDEAwyqKQELLRRAEETRREILLQEEEKMAQQRQRL---------AA 760
Cdd:pfam13868 143 KELEKEEEREED---ER--ILEYLKEKAEREEEREA---EREEIEEEKEREIARLRAQQEKAQDEKAERdelraklyqEE 214
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 264681545  761 VKRELEIKEIhlQDAARRR-----LLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKY 834
Cdd:pfam13868 215 QERKERQKER--EEAEKKArqrqeLQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEH 291
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
684-829 9.73e-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: 58.98  E-value: 9.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  684 IVDYQTREWERIRNDELDFL---RERQTVENMQAEVDEQRAKDEAwyqkqELLRRAEETRREILLQEEEKMAQQRQRlaa 760
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMeqeRLRQEKEEKAREVERRRKLEEA-----EKARQAEMDRQAAIYAEQERMAMERER--- 348
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 264681545  761 vkrelEIKEIHLQDaARRRLLKLQQDQREMELRRLEdEIERkVQMRDQEiaataKDLEIRQlELEAQKR 829
Cdd:pfam17380 349 -----ELERIRQEE-RKRELERIRQEEIAMEISRMR-ELER-LQMERQQ-----KNERVRQ-ELEAARK 403
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
689-833 1.01e-08

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: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 689 TREWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAwyQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIK 768
Cdd:COG1196  294 LAELARLEQDIARLEERRRELEERLEELEEELAELEE--ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 264681545 769 E-----IHLQDAARRRLLKLQQDQREME------LRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEK 833
Cdd:COG1196  372 AelaeaEEELEELAEELLEALRAAAELAaqleelEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
693-833 2.00e-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: 2.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 693 ERIRNDELDFLRERQTVENMQAEVDEQRAK--------DEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRE 764
Cdd:COG1196  246 AELEELEAELEELEAELAELEAELEELRLEleelelelEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 264681545 765 LEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLE----IRQLELEAQKRLYEK 833
Cdd:COG1196  326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEeleeLAEELLEALRAAAEL 398
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
688-828 4.90e-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: 56.50  E-value: 4.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  688 QTREWE--RIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKREL 765
Cdd:pfam15709 382 QQRRFEeiRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQL 461
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 264681545  766 EIKEIHLQD-AARRRLLKLQQDQREMELRRLEDEiERKvqMRDQEIAATAKDLEIRQLELEAQK 828
Cdd:pfam15709 462 AEEQKRLMEmAEEERLEYQRQKQEAEEKARLEAE-ERR--QKEEEAARLALEEAMKQAQEQARQ 522
PRK12704 PRK12704
phosphodiesterase; Provisional
682-832 1.39e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 55.17  E-value: 1.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 682 KFIVDYQTREWERIRNDEL-----DFLRERQTVENmqaEVDEQRAKdeawYQKQEL-LRRAEET---RREILLQEEEKMA 752
Cdd:PRK12704  41 KRILEEAKKEAEAIKKEALleakeEIHKLRNEFEK---ELRERRNE----LQKLEKrLLQKEENldrKLELLEKREEELE 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 753 QQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQ-------DQREMELRRLEDEIErkvqmrdQEIAATAKDLEiRQLELE 825
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEELEELIEEQLQELERisgltaeEAKEILLEKVEEEAR-------HEAAVLIKEIE-EEAKEE 185

                 ....*..
gi 264681545 826 AQKRLYE 832
Cdd:PRK12704 186 ADKKAKE 192
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
693-833 1.52e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 1.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 693 ERIRNDELDFLRERQTVENmQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEkmAQQRQRLAAVKRELEIKEIHL 772
Cdd:COG1196  284 EEAQAEEYELLAELARLEQ-DIARLEERRRELEERLEELEEELAELEEELEELEEEL--EELEEELEEAEEELEEAEAEL 360
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 264681545 773 QDAARRRllkLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEK 833
Cdd:COG1196  361 AEAEEAL---LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
704-832 2.50e-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: 50.81  E-value: 2.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  704 RERQTVENMQAEVDEQRAKDEAWYQ-KQELLRRAEETRREillQEEE--KMAQQRQRLAAVKRELEIKEIHLQDAARRRL 780
Cdd:pfam05672  19 KRRQAREQREREEQERLEKEEEERLrKEELRRRAEEERAR---REEEarRLEEERRREEEERQRKAEEEAEEREQREQEE 95
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 264681545  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 2.81e-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: 50.81  E-value: 2.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  691 EWERIRNDELdflRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMA-QQRQRLAAVKRELEike 769
Cdd:pfam05672  39 EEERLRKEEL---RRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQErLQKQKEEAEAKARE--- 112
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 264681545  770 ihlqDAARRRLLKLQQDQREMELR-----RLEdEIERKVQMRDQ 808
Cdd:pfam05672 113 ----EAERQRQEREKIMQQEEQERlerkkRIE-EIMKRTRKSDQ 151
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
693-834 3.47e-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: 3.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 693 ERIRNDELDFLRERQTVENMQAEVDEQRAkdeawyQKQELLRRAEETRREILLQEEekmaqQRQRLAAvkRELEIKEIHL 772
Cdd:COG1196  260 AELAELEAELEELRLELEELELELEEAQA------EEYELLAELARLEQDIARLEE-----RRRELEE--RLEELEEELA 326
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 264681545 773 QDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKY 834
Cdd:COG1196  327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
684-829 5.17e-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: 52.61  E-value: 5.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  684 IVDYQTREWERIRNDEldflRERQTVENMQAEVDEQRAKDEawYQKQELLRRAE------------ETRREILLQEEEKM 751
Cdd:pfam13868  23 ERDAQIAEKKRIKAEE----KEEERRLDEMMEEERERALEE--EEEKEEERKEErkryrqeleeqiEEREQKRQEEYEEK 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  752 AQQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMR--DQEIAATAKDLEIRQLELEAQKR 829
Cdd:pfam13868  97 LQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEReeDERILEYLKEKAEREEEREAERE 176
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
688-840 5.94e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.23  E-value: 5.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 688 QTREWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREI---------LLQEEEKMAQQRQRL 758
Cdd:COG4717   86 KEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELaelperleeLEERLEELRELEEEL 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 759 AAVKRELEIKEIHLQDAARRRLLKLQQDQREM--ELRRLEDEIER------KVQMRDQEIAATAKDLEIRQLELEAQKRL 830
Cdd:COG4717  166 EELEAELAELQEELEELLEQLSLATEEELQDLaeELEELQQRLAEleeeleEAQEELEELEEELEQLENELEAAALEERL 245
                        170
                 ....*....|
gi 264681545 831 YEKYSFSLSF 840
Cdd:COG4717  246 KEARLLLLIA 255
PRK12704 PRK12704
phosphodiesterase; Provisional
721-833 6.38e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 52.86  E-value: 6.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 721 AKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLaavKRELEIKEIHLQDAARRRLlklqqdQREMELRRLEDEIE 800
Cdd:PRK12704  36 AEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEF---EKELRERRNELQKLEKRLL------QKEENLDRKLELLE 106
                         90       100       110
                 ....*....|....*....|....*....|...
gi 264681545 801 RkvqmRDQEIAATAKDLEIRQLELEAQKRLYEK 833
Cdd:PRK12704 107 K----REEELEKKEKELEQKQQELEKKEEELEE 135
PTZ00121 PTZ00121
MAEBL; Provisional
690-832 7.62e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 7.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  690 REWERIRNDELDFLRERQtvENMQAEvdeQRAKDEAWYQKQELLRRAEETRREILlQEEEKMAQQRQRLAAVKRELEIKE 769
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEE--KKMKAE---EAKKAEEAKIKAEELKKAEEEKKKVE-QLKKKEAEEKKKAEELKKAEEENK 1660
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 264681545  770 IHLQDAARrrllKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLE-IRQLELEAQKRLYE 832
Cdd:PTZ00121 1661 IKAAEEAK----KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEeLKKKEAEEKKKAEE 1720
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
690-833 8.26e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 8.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 690 REWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKE 769
Cdd:COG1196  232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 264681545 770 IHLQdaarRRLLKLQQDQREMElRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEK 833
Cdd:COG1196  312 RELE----ERLEELEEELAELE-EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
690-830 1.28e-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: 51.46  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  690 REWERIRN---------DELDFLRERQTVENMQAEvDEQRAKDEAwYQKQELLRRAEETRREILLQEEEKMAQQRQR--- 757
Cdd:pfam13868 184 REIARLRAqqekaqdekAERDELRAKLYQEEQERK-ERQKEREEA-EKKARQRQELQQAREEQIELKERRLAEEAEReee 261
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 264681545  758 --LAAVKRELEIKEIHLQDAARRRLLKLQQdQREmelrrLEDEIERKVQMRDQEIAATAKDLE-IRQLELEAQKRL 830
Cdd:pfam13868 262 efERMLRKQAEDEEIEQEEAEKRRMKRLEH-RRE-----LEKQIEEREEQRAAEREEELEEGErLREEEAERRERI 331
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
696-830 1.72e-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: 51.19  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  696 RNDELDFLRERQTVENMQAEvdEQRAKDEawyQKQELLRRaeETRREILLQEEEKMAQQRQRLAAVKRELE------IKE 769
Cdd:pfam15558  16 RHKEEQRMRELQQQAALAWE--ELRRRDQ---KRQETLER--ERRLLLQQSQEQWQAEKEQRKARLGREERrradrrEKQ 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 264681545  770 IHLQDAARRRLLKLQQDQRE--MELRRLEDEIERKVQMRD-QEIAATAKDLEIRQlELEAQKRL 830
Cdd:pfam15558  89 VIEKESRWREQAEDQENQRQekLERARQEAEQRKQCQEQRlKEKEEELQALREQN-SLQLQERL 151
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
690-833 2.80e-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: 2.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  690 REWERIRNdELDFLR-------ERQ-TVENMQAEVDEQRAKDEAwyQKQELLRRAEETR-REILLQEEEKMAQQRQrlaa 760
Cdd:pfam17380 389 QKNERVRQ-ELEAARkvkileeERQrKIQQQKVEMEQIRAEQEE--ARQREVRRLEEERaREMERVRLEEQERQQQ---- 461
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 264681545  761 vkreleiKEIHLQDAARRRLLKLQQDQREMELRRLEDE----IERKVQMRDQEIAATAKDLEIRQLELEA-QKRLYEK 833
Cdd:pfam17380 462 -------VERLRQQEEERKRKKLELEKEKRDRKRAEEQrrkiLEKELEERKQAMIEEERKRKLLEKEMEErQKAIYEE 532
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
740-845 3.95e-06

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: 46.79  E-value: 3.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  740 RREI-LLQEE-----EKMAQQRQRLAAVKRELEIKEIHLQDAARR--RLLKLQQDQREMELRRLEDEIERKVQmRDQEIA 811
Cdd:pfam13863   5 KREMfLVQLAldakrEEIERLEELLKQREEELEKKEQELKEDLIKfdKFLKENDAKRRRALKKAEEETKLKKE-KEKEIK 83
                          90       100       110
                  ....*....|....*....|....*....|....
gi 264681545  812 ATAKDLEIRQLELEAQKRLYEKYSFSLSFMQNIV 845
Cdd:pfam13863  84 KLTAQIEELKSEISKLEEKLEEYKPYEDFLEKVV 117
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
713-833 4.91e-06

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 50.04  E-value: 4.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 713 QAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELE--IKEIHLQDAARRRLLKLQQDQREM 790
Cdd:COG3064    1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEeeAREAKAEAEQRAAELAAEAAKKLA 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 264681545 791 ELRRLEDEIERKVQMRDQEIAATA-KDLEIRQLELEAQKRLYEK 833
Cdd:COG3064   81 EAEKAAAEAEKKAAAEKAKAAKEAeAAAAAEKAAAAAEKEKAEE 124
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
685-843 6.16e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 6.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545   685 VDYQTREWERIRNDELDFLRERQTVENM-QAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKR 763
Cdd:TIGR02168  321 LEAQLEELESKLDELAEELAELEEKLEElKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545   764 ELEIKEIHLQDAARRRLlKLQQDQREMELRRLE---DEIERKVQMRDQEIAATAKDLE---------------IRQLELE 825
Cdd:TIGR02168  401 EIERLEARLERLEDRRE-RLQQEIEELLKKLEEaelKELQAELEELEEELEELQEELErleealeelreeleeAEQALDA 479
                          170       180
                   ....*....|....*....|
gi 264681545   826 AQKRLYEKYS--FSLSFMQN 843
Cdd:TIGR02168  480 AERELAQLQArlDSLERLQE 499
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
686-828 9.46e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.53  E-value: 9.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  686 DYQTREWERIRNDELDFLRERQTVENMQaevdeqrakdeawyQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKREL 765
Cdd:COG4913   260 LAERYAAARERLAELEYLRAALRLWFAQ--------------RRLELLEAELEELRAELARLEAELERLEARLDALREEL 325
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 264681545  766 EIKEIHLQDAARRRLLKLQQdqremELRRLEDEIERKVQMRDQ----------EIAATAKDLEIRQLELEAQK 828
Cdd:COG4913   326 DELEAQIRGNGGDRLEQLER-----EIERLERELEERERRRARleallaalglPLPASAEEFAALRAEAAALL 393
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
703-830 9.50e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 9.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 703 LRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLK 782
Cdd:COG1196  680 ELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP 759
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 783 LQQDQREMELRRLEDEI------------------ERKVQMRDQ--EIAATAKDLE--IRQLELEAQKRL 830
Cdd:COG1196  760 PDLEELERELERLEREIealgpvnllaieeyeeleERYDFLSEQreDLEEARETLEeaIEEIDRETRERF 829
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
699-833 1.29e-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: 1.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545   699 ELDFLRER-QTVENMQAEVDEQRAKDEawyQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQD--- 774
Cdd:TIGR02168  303 QKQILRERlANLERQLEELEAQLEELE---SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEElee 379
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 264681545   775 -----AARRRLLKLQQDQREMELRRLEDEIER---KVQMRDQEIAATAKDLEIRQLElEAQKRLYEK 833
Cdd:TIGR02168  380 qletlRSKVAQLELQIASLNNEIERLEARLERledRRERLQQEIEELLKKLEEAELK-ELQAELEEL 445
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
733-832 2.01e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 2.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 733 LRRAEE--TRREILLQEeekMAQQRQRLA----------AVKRELEIKEIHLQdAARRRLLKLQQDQREMELRRLEDEIE 800
Cdd:COG1196  181 LEATEEnlERLEDILGE---LERQLEPLErqaekaeryrELKEELKELEAELL-LLKLRELEAELEELEAELEELEAELE 256
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 264681545 801 R-KVQMRDQEIAATAKDLEIRQLELE---AQKRLYE 832
Cdd:COG1196  257 ElEAELAELEAELEELRLELEELELEleeAQAEEYE 292
RNase_Y_N pfam12072
RNase Y N-terminal region;
713-832 2.45e-05

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 46.03  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  713 QAEVDEQRAKDEAwyqKQEllrrAEETRREILLQEEEKMAQQRQRLaavkrELEIKEihlqdaaRRRLLKLQQD---QRE 789
Cdd:pfam12072  31 SAEELAKRIIEEA---KKE----AETKKKEALLEAKEEIHKLRAEA-----ERELKE-------RRNELQRQERrllQKE 91
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 264681545  790 MEL-RRLE--DEIERKVQMRDQEIAATAKDLEIRQLELEA-----QKRLYE 832
Cdd:pfam12072  92 ETLdRKDEslEKKEESLEKKEKELEAQQQQLEEKEEELEElieeqRQELER 142
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
712-830 2.59e-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: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  712 MQAEVDEQRA-----KDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELeikEIHLQDAARRRLLKLQQD 786
Cdd:pfam13868  20 CNKERDAQIAekkriKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQEL---EEQIEEREQKRQEEYEEK 96
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 264681545  787 QREMEL-----RRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRL 830
Cdd:pfam13868  97 LQEREQmdeivERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKEL 145
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
707-830 2.59e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 2.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 707 QTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREIllqeEEKMAQQRQRLAAVKRELEIKEIHLQ-DAARRRLLKLQQ 785
Cdd:COG4717   71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEEL----EAELEELREELEKLEKLLQLLPLYQElEALEAELAELPE 146
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 264681545 786 -----DQREMELRRLEDEIERkvqmRDQEIAATAKDLE--IRQLELEAQKRL 830
Cdd:COG4717  147 rleelEERLEELRELEEELEE----LEAELAELQEELEelLEQLSLATEEEL 194
COG5210 COG5210
GTPase-activating protein [General function prediction only];
542-658 3.18e-05

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 47.49  E-value: 3.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 542 LSMIENVLAFHDKELLQHFIDRDITSQVYAWPLLETLFSEVLTREEWLRLFDNIFSNHPSFLLMTVVAYSTCSRAPLLNC 621
Cdd:COG5210  350 LKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKL 429
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 264681545 622 TLKNDFEYFFHHRNNLDINVVIREVYHLMETTPADIH 658
Cdd:COG5210  430 DSDELLDLLLKQLFLHSGKEAWSSILKFRHGTDRDIL 466
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
707-830 3.27e-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: 3.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  707 QTVENMQAEVDeqraKDEAWYQKQELLRRAEETRreillqeeeKMAQQRQRLAAVKRELEiKEIHLQDAARRRL------ 780
Cdd:COG3096   479 ELVCKIAGEVE----RSQAWQTARELLRRYRSQQ---------ALAQRLQQLRAQLAELE-QRLRQQQNAERLLeefcqr 544
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 264681545  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 3.50e-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: 44.21  E-value: 3.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  719 QRAKDEAWYQKQELLRRAEETRREillqeEEKMAQQRQRLAAVKREleikeihlqdaaRRRLLKLQQDQREMELRRLEDE 798
Cdd:pfam04696  19 QKFKKEESKQKEKEERRAEIEKRL-----EEKAKQEKEELEERKRE------------EREELFEERRAEQIELRALEEK 81
                          90
                  ....*....|.
gi 264681545  799 IERKVQMRDQE 809
Cdd:pfam04696  82 LELKELMETWH 92
PTZ00121 PTZ00121
MAEBL; Provisional
690-828 3.91e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 3.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  690 REWERIRNDELDFLRERQTVENMQaEVDEQRAKDEAwyQKQELLRRAEETRReillQEEEKMAQQRQRLAAVKRELEIKE 769
Cdd:PTZ00121 1505 AAEAKKKADEAKKAEEAKKADEAK-KAEEAKKADEA--KKAEEKKKADELKK----AEELKKAEEKKKAEEAKKAEEDKN 1577
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 264681545  770 IHLQDAARRRllKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQK 828
Cdd:PTZ00121 1578 MALRKAEEAK--KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK 1634
Caldesmon pfam02029
Caldesmon;
697-830 4.47e-05

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 46.78  E-value: 4.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  697 NDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAavKRELEIKEIHLQDAA 776
Cdd:pfam02029 211 NGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQ--EAELELEELKKKREE 288
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 264681545  777 RRRLLKLQQDQREME--LRRLEDEIERKvQMRDqeiaatakDLEIRQLElEAQKRL 830
Cdd:pfam02029 289 RRKLLEEEEQRRKQEeaERKLREEEEKR-RMKE--------EIERRRAE-AAEKRQ 334
PTZ00121 PTZ00121
MAEBL; Provisional
693-830 4.67e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 4.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  693 ERIRNDELdflreRQTVENMQAEVDEQRAKDEAwYQKQELLRRAEETRR--EILLQEEEKMAQQRQRLAAVKRELEIKEI 770
Cdd:PTZ00121 1481 EAKKADEA-----KKKAEEAKKKADEAKKAAEA-KKKADEAKKAEEAKKadEAKKAEEAKKADEAKKAEEKKKADELKKA 1554
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 264681545  771 -HLQDAARRRLL---KLQQDQREMELRRLED--EIERKVQMRDQEIAATAKDLEIRQLELEAQKRL 830
Cdd:PTZ00121 1555 eELKKAEEKKKAeeaKKAEEDKNMALRKAEEakKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI 1620
PTZ00121 PTZ00121
MAEBL; Provisional
691-832 4.67e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 4.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  691 EWERIRNDELDFLRE-RQTVENMQAEVDEQ--------RAKDEAWYQKQELLRRAEETRR--EILLQEEE---KMAQQRQ 756
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEeKKKVEQLKKKEAEEkkkaeelkKAEEENKIKAAEEAKKAEEDKKkaEEAKKAEEdekKAAEALK 1695
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  757 RLAAVKRELEikEIHLQDAARRRllKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLE-----IRQLELEAQKRLY 831
Cdd:PTZ00121 1696 KEAEEAKKAE--ELKKKEAEEKK--KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEeekkkIAHLKKEEEKKAE 1771

                  .
gi 264681545  832 E 832
Cdd:PTZ00121 1772 E 1772
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
706-828 4.75e-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: 43.37  E-value: 4.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  706 RQTVENMQAEVdEQRAKdeawyQKQELLRRAEE-----TRREILLQEEEKMAQ-QRQRLAAVKRELE-----IKEIHLQD 774
Cdd:pfam20492   1 REEAEREKQEL-EERLK-----QYEEETKKAQEeleesEETAEELEEERRQAEeEAERLEQKRQEAEeekerLEESAEME 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 264681545  775 AARRRLLKLQQDQREMELRRLEDEIERkvqmrdqeiaataKDLEIRQLELEAQK 828
Cdd:pfam20492  75 AEEKEQLEAELAEAQEEIARLEEEVER-------------KEEEARRLQEELEE 115
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
730-829 5.43e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 5.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 730 QELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQdaARRRLLKLQQDQREMELRRLEDEIERK---VQMR 806
Cdd:COG1196  216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELE--AELAELEAELEELRLELEELELELEEAqaeEYEL 293
                         90       100
                 ....*....|....*....|...
gi 264681545 807 DQEIAATAKDLEIRQLELEAQKR 829
Cdd:COG1196  294 LAELARLEQDIARLEERRRELEE 316
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
690-826 5.54e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 5.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545   690 REWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEE-----EKMAQQRQRLAAVKRE 764
Cdd:TIGR02169  230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqlrvkEKIGELEAEIASLERS 309
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 264681545   765 LEIKEIHLQDAA-RRRLLKLQQDQREMELRRLEDEIERKVQMRDQ---EIAATAKDLEIRQLELEA 826
Cdd:TIGR02169  310 IAEKERELEDAEeRLAKLEAEIDKLLAEIEELEREIEEERKRRDKlteEYAELKEELEDLRAELEE 375
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
115-153 5.66e-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: 5.66e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 264681545   115 TKELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWD 153
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDgTIKLWD 40
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
702-810 5.71e-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: 46.13  E-value: 5.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  702 FLRERQTVENM-----QAEVDEQRAKdEAWYQKQELLRRAEETRREILLQEEEKMAQQRQR----LAAVKRELEIKEIHL 772
Cdd:pfam02841 181 FLQSKEAVEEAilqtdQALTAKEKAI-EAERAKAEAAEAEQELLREKQKEEEQMMEAQERSyqehVKQLIEKMEAEREQL 259
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 264681545  773 QDAARRRLLKLQQDQREMelrrLEDEIERKVQMRDQEI 810
Cdd:pfam02841 260 LAEQERMLEHKLQEQEEL----LKEGFKTEAESLQKEI 293
mukB PRK04863
chromosome partition protein MukB;
707-827 5.91e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.87  E-value: 5.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  707 QTVENMQAEVDEQRAKDEAwyqkQELLRRAEETR--------REILLQEEEKMAQQRQRLAAVKRELEIK-EIHLQDAAr 777
Cdd:PRK04863  480 QLVRKIAGEVSRSEAWDVA----RELLRRLREQRhlaeqlqqLRMRLSELEQRLRQQQRAERLLAEFCKRlGKNLDDED- 554
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 264681545  778 rrLLKLQQDQREMELRRLEDE----IERKVQMRDQEiaataKDLEIRQLELEAQ 827
Cdd:PRK04863  555 --ELEQLQEELEARLESLSESvseaRERRMALRQQL-----EQLQARIQRLAAR 601
PRK12705 PRK12705
hypothetical protein; Provisional
713-828 5.96e-05

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 46.63  E-value: 5.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 713 QAEVDEQRAKDEAWYQKQELLRRAEET-------RREILLQEEEKMAQQRQRLAAVKRELEIKEIHLqdAARRRLLKLQQ 785
Cdd:PRK12705  41 EAQKEAEEKLEAALLEAKELLLRERNQqrqearrEREELQREEERLVQKEEQLDARAEKLDNLENQL--EEREKALSARE 118
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 264681545 786 DQREMELRRLEDEIERKVQMRDQEiaatAKDLEIRQLELEAQK 828
Cdd:PRK12705 119 LELEELEKQLDNELYRVAGLTPEQ----ARKLLLKLLDAELEE 157
PTZ00121 PTZ00121
MAEBL; Provisional
698-828 6.71e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 6.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  698 DELDFLRERQTVENMQAEvdEQRAKDEAwYQKQELLRRAEETRR--EILLQEEEKMAQQRQRLAAVKReleikeihLQDA 775
Cdd:PTZ00121 1095 EAFGKAEEAKKTETGKAE--EARKAEEA-KKKAEDARKAEEARKaeDARKAEEARKAEDAKRVEIARK--------AEDA 1163
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 264681545  776 ARRRLLKLQQDQREMELRRLEDEIERKVQMRDQE----IAATAKDLEIRQLElEAQK 828
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEdarkAEAARKAEEERKAE-EARK 1219
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
688-826 7.72e-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: 46.60  E-value: 7.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545   688 QTREWERIRND---ELDFLR-ERQTVENMQAEVDEQRAK-----DEAWYQKQELLRRAEETRREI--LLQEEEKMAQQRQ 756
Cdd:TIGR02169  813 RLREIEQKLNRltlEKEYLEkEIQELQEQRIDLKEQIKSiekeiENLNGKKEELEEELEELEAALrdLESRLGDLKKERD 892
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 264681545   757 RLAAVKRELEIK--EIHLQDAARRRLLKLQQDQREMELRRLeDEIERKVQmRDQEIAATAKDLEIRQLELEA 826
Cdd:TIGR02169  893 ELEAQLRELERKieELEAQIEKKRKRLSELKAKLEALEEEL-SEIEDPKG-EDEEIPEEELSLEDVQAELQR 962
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
735-833 8.21e-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: 46.10  E-value: 8.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  735 RAEETRREILLQEEEKMAQQRQRL---AAVKRELEIKEIHLQDAARRRLlklQQDQREMElRRLEDEIERKVQMRDQEIA 811
Cdd:pfam15709 315 RSEEDPSKALLEKREQEKASRDRLraeRAEMRRLEVERKRREQEEQRRL---QQEQLERA-EKMREELELEQQRRFEEIR 390
                          90       100
                  ....*....|....*....|....*
gi 264681545  812 ATAKDLE---IRQLELEAQKRLYEK 833
Cdd:pfam15709 391 LRKQRLEeerQRQEEEERKQRLQLQ 415
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
693-805 1.00e-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: 45.29  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  693 ERIRNDELDFLRERQT-VENMQAEVDEQRAKDEAWYQKqeLLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIH 771
Cdd:pfam13868 228 EKKARQRQELQQAREEqIELKERRLAEEAEREEEEFER--MLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQ 305
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 264681545  772 LQDAARRRLLKLQQDQREMELR--RLEDEIERKVQM 805
Cdd:pfam13868 306 RAAEREEELEEGERLREEEAERreRIEEERQKKLKE 341
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
713-829 1.03e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 713 QAEV---------DEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQdAARRRLLKL 783
Cdd:COG1196  208 QAEKaeryrelkeELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE-ELELELEEA 286
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 264681545 784 QQDQRE--MELRRLEDEIERKVQMRdqeiaataKDLEIRQLELEAQKR 829
Cdd:COG1196  287 QAEEYEllAELARLEQDIARLEERR--------RELEERLEELEEELA 326
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
714-829 1.05e-04

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 45.63  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 714 AEVDEQRAKDEAwyqkqELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQDQREMELR 793
Cdd:COG2268  195 AEIIRDARIAEA-----EAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYE 269
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 264681545 794 RLEDEIERKVQM------RDQEIAATAKDLEIRQLELEAQKR 829
Cdd:COG2268  270 IAEANAEREVQRqleiaeREREIELQEKEAEREEAELEADVR 311
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
697-835 1.06e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 697 NDELDFLRE-----RQTVENMQAEVDEQRAkdeawyQKQELLRRAEETRREiLLQEEEKMAQQRQRLAAVKRELEIKEIH 771
Cdd:COG4372   44 QEELEQLREeleqaREELEQLEEELEQARS------ELEQLEEELEELNEQ-LQAAQAELAQAQEELESLQEEAEELQEE 116
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 264681545 772 LQDA-ARRRLLKLQQDQremeLRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKYS 835
Cdd:COG4372  117 LEELqKERQDLEQQRKQ----LEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
PTZ00121 PTZ00121
MAEBL; Provisional
693-832 1.31e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  693 ERIRNDEldflRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRRE-----ILLQEEEKMAQQRQRLAAVKRELEI 767
Cdd:PTZ00121 1610 EEAKKAE----EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAeeenkIKAAEEAKKAEEDKKKAEEAKKAEE 1685
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 264681545  768 KEIHLQDAARRrllKLQQDQREMELRRLEDEIERKV-QMRDQEIAATAKDLEIRQLELEAQKRLYE 832
Cdd:PTZ00121 1686 DEKKAAEALKK---EAEEAKKAEELKKKEAEEKKKAeELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
501-609 1.43e-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: 43.83  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545   501 AFP-FVKLFQNNQLIcFEVVATLIINWCQHWFEYFpnppinilsmienvLAFHDKELLQHFIDRDITSQVYAWPLLETLF 579
Cdd:smart00164 112 AFWcLVKLMERYGPN-FYLPDMSGLQLDLLQLDRL--------------VKEYDPDLYKHLKDLGITPSLYALRWFLTLF 176
                           90       100       110
                   ....*....|....*....|....*....|
gi 264681545   580 SEVLTREEWLRLFDNIFSNHPSFLLMTVVA 609
Cdd:smart00164 177 ARELPLEIVLRIWDVLFAEGSDFLFRVALA 206
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
696-829 1.84e-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: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  696 RNDELDFLRER-----QTVENMQAEVDE-----QRAKDEAWYQKQELLRRAEETRR-----EILLQEEEKMAQ-QR---- 755
Cdd:pfam05667 333 REEELEELQEQledleSSIQELEKEIKKlessiKQVEEELEELKEQNEELEKQYKVkkktlDLLPDAEENIAKlQAlvda 412
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 264681545  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 2.15e-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: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 684 IVDYQTREWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKmAQQRQRLAAVKR 763
Cdd:COG1196  623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA-EEELELEEALLA 701
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 264681545 764 ELEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKR 829
Cdd:COG1196  702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
Nop53 pfam07767
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ...
714-833 2.52e-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: 44.21  E-value: 2.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  714 AEVDEQRAKDEAwyQKQELLRRAEETRREILLQEEEKMAQQrQRLAAVKRELEIKEihlqdAARRRLLKLQQDQremeLR 793
Cdd:pfam07767 205 VEAEKKRLKEEE--KLERVLEKIAESAATAEAREEKRKTKA-QRNKEKRRKEEERE-----AKEEKALKKKLAQ----LE 272
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 264681545  794 RLEdEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEK 833
Cdd:pfam07767 273 RLK-EIAKEIAEKEKEREEKAEARKREKRKKKKEEKKLRP 311
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
691-829 2.64e-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: 2.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  691 EWERIRNDELDFLR-ERQT---VENMQAEVDEQRAKDEAwyQKQELLRRAEEtrreillQEEEKMAQQRQRLAAVKR--E 764
Cdd:TIGR02794  51 QANRIQQQKKPAAKkEQERqkkLEQQAEEAEKQRAAEQA--RQKELEQRAAA-------EKAAKQAEQAAKQAEEKQkqA 121
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 264681545  765 LEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKdleiRQLELEAQKR 829
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAK----KKAEAEAKAK 182
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
686-833 2.77e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 2.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 686 DYQTREWERIRnDELDFLRErqtvenmqAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKREL 765
Cdd:COG4717  315 ELEEEELEELL-AALGLPPD--------LSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE 385
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 766 EIKEIHLQDAARRRLLKlQQDQREMELRRLEDEIERKVQMRDQE-IAATAKDLEIRQLELEAQ-KRLYEK 833
Cdd:COG4717  386 ELRAALEQAEEYQELKE-ELEELEEQLEELLGELEELLEALDEEeLEEELEELEEELEELEEElEELREE 454
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
735-830 2.94e-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: 41.95  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  735 RAEETRReiLLQEEEKMA-QQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQDQREmELRRLEDeiERKVQMRDQEIAAT 813
Cdd:pfam05672   8 DAEEAAR--ILAEKRRQArEQREREEQERLEKEEEERLRKEELRRRAEEERARREE-EARRLEE--ERRREEEERQRKAE 82
                          90
                  ....*....|....*..
gi 264681545  814 AKDLEIRQLELEAQKRL 830
Cdd:pfam05672  83 EEAEEREQREQEEQERL 99
DegS pfam05384
Sensor protein DegS; This is small family of Bacillus DegS proteins. The DegS-DegU ...
708-803 2.97e-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: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  708 TVENMQAEVDE--QRAKDEAWYQKQELlrraEETRREIL--------LQEEEKMAqqRQRLAAVKR------ELEIKEIH 771
Cdd:pfam05384  10 TIENSKEEIFEiaENARQEYERLKQEL----EELKEEVSetikevdkLEKKERRA--RQRLMEVSRdfnrysEEDIKEAY 83
                          90       100       110
                  ....*....|....*....|....*....|...
gi 264681545  772 LQ-DAARRRLLKLQQdqREMELRRLEDEIERKV 803
Cdd:pfam05384  84 EEaKDLQVELALLRE--REKQLRERRDELERRL 114
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
683-845 3.12e-04

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: 44.58  E-value: 3.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545   683 FIVDYQTREWE-RIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRR-EILLQEEEKMAQQRQRLAA 760
Cdd:pfam02463  168 KRKKKEALKKLiEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLyLDYLKLNEERIDLLQELLR 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545   761 VKRELEIKEIHLQDAARRrllKLQQDQREMElrrledEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKYSFSLSF 840
Cdd:pfam02463  248 DEQEEIESSKQEIEKEEE---KLAQVLKENK------EEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318

                   ....*
gi 264681545   841 MQNIV 845
Cdd:pfam02463  319 SEKEK 323
EVC2_like pfam12297
Ellis van Creveld protein 2 like protein; This family of proteins is found in eukaryotes. ...
689-801 3.27e-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: 3.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  689 TREWERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQELLRR-----AEETRREILLQEEEKMAQQRQRLaAVKR 763
Cdd:pfam12297 223 AAECNLETREKMEAQHQREMAEKEEAEELLKHADEQEALECSSLLDKlhkleQEHLQRSLLLRQEEDFAKAQRQL-AVFQ 301
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 264681545  764 ELEIKEI---HLQDAARRRLLKLQQDQREM-ELRRLEDEIER 801
Cdd:pfam12297 302 RVELHKIfftQLKEATRKGELKPEAAKRLLqDYSKIQEQIEE 343
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
689-829 3.43e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 44.03  E-value: 3.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 689 TREWERIRNDELDFLR---ERQTVENMQAEvdEQRAKDEAWYQK-----------QELLRRAEETRREILLQEEEKMAQQ 754
Cdd:PRK09510  61 VEQYNRQQQQQKSAKRaeeQRKKKEQQQAE--ELQQKQAAEQERlkqlekerlaaQEQKKQAEEAAKQAALKQKQAEEAA 138
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 264681545 755 RQRLAAVKRELEIKEIHLQDAARRrlLKLQQDQREMELRRLEDEIERKVQMrDQEIAATAKDLEIRQLELEAQKR 829
Cdd:PRK09510 139 AKAAAAAKAKAEAEAKRAAAAAKK--AAAEAKKKAEAEAAKKAAAEAKKKA-EAEAAAKAAAEAKKKAEAEAKKK 210
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
703-834 3.85e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.19  E-value: 3.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545   703 LRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEE---TRREIL------------LQEEEKMAQQRQRLAAVKRELEI 767
Cdd:TIGR00618  327 LMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEvatSIREIScqqhtltqhihtLQQQKTTLTQKLQSLCKELDILQ 406
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 264681545   768 KEIHLQDAARRRLLKLQQDqremeLRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEKY 834
Cdd:TIGR00618  407 REQATIDTRTSAFRDLQGQ-----LAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL 468
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
690-844 3.90e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 3.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 690 REWERIRNDELDFLRER--QTVEnmqaEVDEQRAKDEAWYQKQELLRRAE---ETRREILLQEEEKMAQQRQRLAAVKRE 764
Cdd:PRK03918 566 DELEEELAELLKELEELgfESVE----ELEERLKELEPFYNEYLELKDAEkelEREEKELKKLEEELDKAFEELAETEKR 641
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 765 LEIKEIHLQDA-----------ARRRLLKLqqdqrEMELRRLEDEIERKVQMRDqEIAATAKDLEIRQLELEAQKRLYEK 833
Cdd:PRK03918 642 LEELRKELEELekkyseeeyeeLREEYLEL-----SRELAGLRAELEELEKRRE-EIKKTLEKLKEELEEREKAKKELEK 715
                        170
                 ....*....|.
gi 264681545 834 YSFSLSFMQNI 844
Cdd:PRK03918 716 LEKALERVEEL 726
G_path_suppress pfam15991
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ...
704-790 3.91e-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: 43.37  E-value: 3.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  704 RERQTVEnMQAEVDEQRAKDEAWYQKQELLRRAEETRREIlLQEEEKMAQQRQRlaavKREL--EIKEIHLQDAARRRLL 781
Cdd:pfam15991  22 RERKKQE-QEAKMEEERLRREREEREKEDRMTLEETKEQI-LKLEKKLADLKEE----KHQLflQLKKVLHEDETRKRQL 95

                  ....*....
gi 264681545  782 KLQQDQREM 790
Cdd:pfam15991  96 KEQSELFAL 104
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
744-833 4.04e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.60  E-value: 4.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 744 LLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARRR---LLKLQQDQREM-ELRRLEDEIERKVQMRDQEIAATAKDLEI 819
Cdd:COG4942   15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEkalLKQLAALERRIaALARRIRALEQELAALEAELAELEKEIAE 94
                         90
                 ....*....|....
gi 264681545 820 RQLELEAQKRLYEK 833
Cdd:COG4942   95 LRAELEAQKEELAE 108
Caldesmon pfam02029
Caldesmon;
693-796 4.12e-04

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 43.70  E-value: 4.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  693 ERIRndeldflRERQTVENMQAEVDEQRaKDEAWYQKQELLRRAEEtRREILLQEEEKMAQQRQrLAAVKRELEikeihl 772
Cdd:pfam02029 251 EELR-------RRRQEKESEEFEKLRQK-QQEAELELEELKKKREE-RRKLLEEEEQRRKQEEA-ERKLREEEE------ 314
                          90       100
                  ....*....|....*....|....
gi 264681545  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 ...
714-843 4.24e-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: 44.01  E-value: 4.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545   714 AEVDEQRAKDEAwyQKQELLR---------RAEETRREILLQEEEKMAQQRQRLaavkrELEIKEihlQDAARRRlLKLQ 784
Cdd:pfam01576   57 AEAEEMRARLAA--RKQELEEilhelesrlEEEEERSQQLQNEKKKMQQHIQDL-----EEQLDE---EEAARQK-LQLE 125
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 264681545   785 QDQREMELRRLEDEIerkVQMRDQ--EIAATAKDLEIRQLELEAQKRLYEKYSFSLSFMQN 843
Cdd:pfam01576  126 KVTTEAKIKKLEEDI---LLLEDQnsKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKN 183
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
696-831 4.32e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 4.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 696 RNDELDFLRERqtVENMQAEVDEQRAKDEAwyQKQELLRRAEETRReiLLQEEEKMAQQRQRLAAVKRELE--IKEIHLQ 773
Cdd:COG4372   71 ARSELEQLEEE--LEELNEQLQAAQAELAQ--AQEELESLQEEAEE--LQEELEELQKERQDLEQQRKQLEaqIAELQSE 144
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 264681545 774 DAARRRLLKlqqdQREMELRRLEDEIERkVQMRDQEIAATAKDLEIRQLELEAQKRLY 831
Cdd:COG4372  145 IAEREEELK----ELEEQLESLQEELAA-LEQELQALSEAEAEQALDELLKEANRNAE 197
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
718-791 5.29e-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: 5.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545   718 EQRAKDEAwyQKQELLRRAEETRREILLQ--EEEKMAQQRQ--------RLAAVKRELEIKEIHLQ--DAARRRLlklqq 785
Cdd:pfam01576  984 EQESRERQ--AANKLVRRTEKKLKEVLLQveDERRHADQYKdqaekgnsRMKQLKRQLEEAEEEASraNAARRKL----- 1056

                   ....*.
gi 264681545   786 dQREME 791
Cdd:pfam01576 1057 -QRELD 1061
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
697-833 5.96e-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: 43.67  E-value: 5.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545   697 NDELDFlrerQTVENMQAEVDEQ-----------RAKDEAWYQKQELLRRAEETRREILL--QEEEKMAQQRQRLAAVKR 763
Cdd:pfam12128  190 SKEGKF----RDVKSMIVAILEDdgvvppksrlnRQQVEHWIRDIQAIAGIMKIRPEFTKlqQEFNTLESAELRLSHLHF 265
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 264681545   764 EleIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEA---QKRLYEK 833
Cdd:pfam12128  266 G--YKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEAledQHGAFLD 336
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
731-840 7.31e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 7.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 731 ELLRRAEETRREILlqeeEKMAQQRQRLAAVKRELEIKEIHLQD-----AARRRLLKLQQDQREMELRRLEDEIERKvQM 805
Cdd:COG4942  139 QYLKYLAPARREQA----EELRADLAELAALRAELEAERAELEAllaelEEERAALEALKAERQKLLARLEKELAEL-AA 213
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 264681545 806 RDQEIAATAKDLEIRQLELEAQKRLYEKYSFSLSF 840
Cdd:COG4942  214 ELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
693-829 7.52e-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: 7.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 693 ERIRNDELDFLRERQTVENMQAEVDEQRAKDEAWYQKQEllRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHL 772
Cdd:COG3064   16 ERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAE--EEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKA 93
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 264681545 773 QDAARRRLLKLQQDQREmelrrledeiERKVQMRDQEIAATAKdleiRQLELEAQKR 829
Cdd:COG3064   94 AAEKAKAAKEAEAAAAA----------EKAAAAAEKEKAEEAK----RKAEEEAKRK 136
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
728-830 7.65e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 7.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 728 QKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRD 807
Cdd:COG1196  676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
                         90       100
                 ....*....|....*....|....
gi 264681545 808 QEIAATAKDLEIRQLELEAQ-KRL 830
Cdd:COG1196  756 LPEPPDLEELERELERLEREiEAL 779
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
706-839 7.73e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 7.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 706 RQTVENMQAEVDE-QRAKDEAWYQKQELLRRAEETRREILlQEEEKMAQQR----QRLAAVKRE----------LEIKEI 770
Cdd:COG3883   36 QAELDALQAELEElNEEYNELQAELEALQAEIDKLQAEIA-EAEAEIEERReelgERARALYRSggsvsyldvlLGSESF 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 771 -----------HLQDAARRRLLKLQQDQREMElrRLEDEIERKVqmrdQEIAATAKDLEIRQLELEAQKRLYEKYSFSLS 839
Cdd:COG3883  115 sdfldrlsalsKIADADADLLEELKADKAELE--AKKAELEAKL----AELEALKAELEAAKAELEAQQAEQEALLAQLS 188
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
684-832 7.97e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 7.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545   684 IVDYQTREWERIRN--DELDFL-RERQTVENMQAEVD---EQRAKDEAWYQKQ--ELLRRAEETRREILLQEEEKMAQQR 755
Cdd:TIGR02169  728 LEQEEEKLKERLEEleEDLSSLeQEIENVKSELKELEariEELEEDLHKLEEAlnDLEARLSHSRIPEIQAELSKLEEEV 807
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 264681545   756 QRLAAVKRELEIKEihlqdaaRRRLLKLQQDQREM-ELRRLEDEIERKVQMRDQEIAATAKDLEIRQLEL-EAQKRLYE 832
Cdd:TIGR02169  808 SRIEARLREIEQKL-------NRLTLEKEYLEKEIqELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELeELEAALRD 879
WD40 pfam00400
WD domain, G-beta repeat;
116-153 8.25e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 37.71  E-value: 8.25e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 264681545  116 KELVSWMRGHESSVCSISVHASGRYAITTSSD-TAQLWD 153
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDgTVKVWD 39
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
693-812 8.91e-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: 8.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 693 ERIRNDELDFLRERQTVENMQAEVDEQRAKDEawyqkQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHL 772
Cdd:COG1196  664 GGSRRELLAALLEAEAELEELAERLAEEELEL-----EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 264681545 773 QDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEIAA 812
Cdd:COG1196  739 EELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
719-833 9.31e-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: 9.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  719 QRAKDEAWY--------QKQELLRRAEETRREillqeEEKMAQQRQRLAAVKRE--LEIKEihlQDAARRRLLKLQQDQR 788
Cdd:pfam13904  50 ERQPLEAYEnwlaakqrQRQKELQAQKEEREK-----EEQEAELRKRLAKEKYQewLQRKA---RQQTKKREESHKQKAA 121
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 264681545  789 EM--------ELRRLEDEIERKVQ--MRDQEIAATAKDLEIRQLELEAQKRLYEK 833
Cdd:pfam13904 122 ESaskslakpERKVSQEEAKEVLQewERKKLEQQQRKREEEQREQLKKEEEEQER 176
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
704-767 9.70e-04

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: 40.42  E-value: 9.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  704 RERQTVENMQAEVDEQRAKDEAWYQKQELL--------RRAEETRR-----------EILLQEEEKMAQQRQRLAAVKRE 764
Cdd:pfam15346  54 VLEELEREREAELEEERRKEEEERKKREELerileennRKIEEAQRkeaeerlamleEQRRMKEERQRREKEEEEREKRE 133

                  ...
gi 264681545  765 LEI 767
Cdd:pfam15346 134 QQK 136
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
705-834 1.04e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.21  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  705 ERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQ------RLAAVKRELEIKEIHLQDAARR 778
Cdd:pfam13868  79 EEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREeidefnEEQAEWKELEKEEEREEDERIL 158
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 264681545  779 RLLKlQQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEA--QKRLYEKY 834
Cdd:pfam13868 159 EYLK-EKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDElrAKLYQEEQ 215
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
690-832 1.25e-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: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545   690 REWERIRNdELDFLRERqtVENMQAEVDE--------QRAKDEAwYQKQELLRRAEETRREILLQEEEKMAQQRQR---- 757
Cdd:TIGR02169  170 RKKEKALE-ELEEVEEN--IERLDLIIDEkrqqlerlRREREKA-ERYQALLKEKREYEGYELLKEKEALERQKEAierq 245
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 264681545   758 LAAVKRELEIKEIHLQDAARRrllklqQDQREMELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYE 832
Cdd:TIGR02169  246 LASLEEELEKLTEEISELEKR------LEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKE 314
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
694-827 1.25e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 694 RIRNDELDflRERQTVENMQAEVDEQ--RAKD--EAWYQKQELLRRAE------ETRREILLQEEEKMAQQRQRLAAVKR 763
Cdd:PRK02224 474 RERVEELE--AELEDLEEEVEEVEERleRAEDlvEAEDRIERLEERREdleeliAERRETIEEKRERAEELRERAAELEA 551
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 264681545 764 ELEIKEIHLQDA------ARRRLLKLQQDQREmelrrLEDEIER--KVQMRDQEIAATAKDLEIRQLELEAQ 827
Cdd:PRK02224 552 EAEEKREAAAEAeeeaeeAREEVAELNSKLAE-----LKERIESleRIRTLLAAIADAEDEIERLREKREAL 618
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
703-822 1.26e-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: 42.63  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  703 LRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQE-----EEKMA--QQRQRLAAVKRELEIKE---IHL 772
Cdd:COG3096   528 LRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQaaeavEQRSElrQQLEQLRARIKELAARApawLAA 607
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 264681545  773 QDAARR-------RLLKLQQ--DQREMELRRledeiERKVQMRDQEIAATAKDLE--IRQL 822
Cdd:COG3096   608 QDALERlreqsgeALADSQEvtAAMQQLLER-----EREATVERDELAARKQALEsqIERL 663
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
702-829 1.29e-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: 42.47  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545   702 FLRERQTVENMQAEVDEQRAKDEAWYQKQELLRRAEE---TRREILLQEEEKmaqQRQRLAAVKREL--EIKEIHLQDA- 775
Cdd:pfam01576  150 LSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEamiSDLEERLKKEEK---GRQELEKAKRKLegESTDLQEQIAe 226
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 264681545   776 --ARRRLLKLQQDQREMELR----RLEDEIERK--VQMRDQEIAATAKDLEiRQLELEAQKR 829
Cdd:pfam01576  227 lqAQIAELRAQLAKKEEELQaalaRLEEETAQKnnALKKIRELEAQISELQ-EDLESERAAR 287
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
697-834 1.31e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.31  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 697 NDELDFLRER-QTVENMQAEVDEQRAKDEAWYQK-QELLRRAEETRREI------------LLQEEEKMAQQRQRL---- 758
Cdd:COG3206  211 SEEAKLLLQQlSELESQLAEARAELAEAEARLAAlRAQLGSGPDALPELlqspviqqlraqLAELEAELAELSARYtpnh 290
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 759 ---AAVKRELEIKEIHLQDAARRRLLKLQQD-----QREMELRRLEDEIERKVQmrdqeiAATAKDLEIRQL--ELEAQK 828
Cdd:COG3206  291 pdvIALRAQIAALRAQLQQEAQRILASLEAElealqAREASLQAQLAQLEARLA------ELPELEAELRRLerEVEVAR 364

                 ....*.
gi 264681545 829 RLYEKY 834
Cdd:COG3206  365 ELYESL 370
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
707-833 1.63e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.15  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 707 QTVENMQAEVDEQRAKDEAwyQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEiKEIHLQDAARRRL---LKL 783
Cdd:COG2433  376 LSIEEALEELIEKELPEEE--PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE-AELEEKDERIERLereLSE 452
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 264681545 784 QQDQREMELRRledeiERKVQMRDQEIAATAKdlEIRQLElEAQKRLYEK 833
Cdd:COG2433  453 ARSEERREIRK-----DREISRLDREIERLER--ELEEER-ERIEELKRK 494
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
719-842 1.82e-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: 40.52  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  719 QRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLaaVKRELEIKEIHLQDAARRRLLKLQQDQrEMELRRLEDE 798
Cdd:pfam14988  17 QKKIEKLWNQYVQECEEIERRRQELASRYTQQTAELQTQL--LQKEKEQASLKKELQALRPFAKLKESQ-EREIQDLEEE 93
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 264681545  799 IErKVQmrdQEIAATAKDLEIRQLEleaQKRLYEKYSFSLSFMQ 842
Cdd:pfam14988  94 KE-KVR---AETAEKDREAHLQFLK---EKALLEKQLQELRILE 130
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
706-814 1.95e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 706 RQTVENMQAEVDEQRAKdeawYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQ---DAARRRLLK 782
Cdd:COG4942  142 KYLAPARREQAEELRAD----LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEkelAELAAELAE 217
                         90       100       110
                 ....*....|....*....|....*....|..
gi 264681545 783 LQQDQRemELRRLEDEIERKVQMRDQEIAATA 814
Cdd:COG4942  218 LQQEAE--ELEALIARLEAEAAAAAERTPAAG 247
YscO-like pfam16789
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ...
688-804 2.37e-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: 39.43  E-value: 2.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  688 QTREWERIRNDELDFLRE--RQTVENMQAEVDEQRAKDeawyqKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKREL 765
Cdd:pfam16789  32 KEKEKLAELEAERDKVRKhkKAKMQQLRDEMDRGTTSD-----KILQMKRYIKVVKERLKQEEKKVQDQKEQVRTAARNL 106
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 264681545  766 EIKEIHLQDaARRRLLKLQQDQREM--ELRRLEDEIERKVQ 804
Cdd:pfam16789 107 EIAREELKK-KRQEVEKLEKHKKEWvkEMKKEEEDQEEREQ 146
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
728-833 2.66e-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: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  728 QKQELLRRAEETRREiLLQEEEKMAQQRQRLAAVKRELEIK---EIHLQ---DAARRRLLKLQQDQREME-LRRLEDEIE 800
Cdd:COG3096   279 ERRELSERALELRRE-LFGARRQLAEEQYRLVEMARELEELsarESDLEqdyQAASDHLNLVQTALRQQEkIERYQEDLE 357
                          90       100       110
                  ....*....|....*....|....*....|...
gi 264681545  801 rKVQMRDQEIAATAKDLEIRQLELEAQKRLYEK 833
Cdd:COG3096   358 -ELTERLEEQEEVVEEAAEQLAEAEARLEAAEE 389
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
642-769 2.96e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 2.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 642 VIREVYHLMETTPADI--HPNSMLDAFVALTKGQYpiFNQYPKFIVDYQTREWERIRNDELDFLRERQTVENMQAEVDEQ 719
Cdd:COG4942  109 LLRALYRLGRQPPLALllSPEDFLDAVRRLQYLKY--LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 264681545 720 RAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAAVKRELEIKE 769
Cdd:COG4942  187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
693-828 3.48e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 3.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 693 ERIRNDELDFLRER-QTVENMQAEVDEQRAKDEAWYQKQELLRRAEEtRREILLQEEEKMAQQRQRLAAVKRELEIKEIH 771
Cdd:COG4717   49 ERLEKEADELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQE-ELEELEEELEELEAELEELREELEKLEKLLQL 127
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 264681545 772 LQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQeiaatakdleIRQLELEAQK 828
Cdd:COG4717  128 LPLYQELEALEAELAELPERLEELEERLEELRELEEE----------LEELEAELAE 174
YscO-like pfam16789
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ...
727-830 3.49e-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: 3.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  727 YQKQELL----RRAEETRReILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDaarrrllKLQQDQREME----------- 791
Cdd:pfam16789   3 YPLEQVLdikkKRVEEAEK-VVKDKKRALEKEKEKLAELEAERDKVRKHKKA-------KMQQLRDEMDrgttsdkilqm 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 264681545  792 ---LRRLEDEI---ERKVQMRDQEIAATAKDLEIRQLEL-EAQKRL 830
Cdd:pfam16789  75 kryIKVVKERLkqeEKKVQDQKEQVRTAARNLEIAREELkKKRQEV 120
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
700-833 3.96e-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: 3.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 700 LDFLRERqtVENMQAEVDEQRAKDEAWYQKQELLRRAEETRREI---------LLQEEEKMAQQRQRLAAVKRELEIKEI 770
Cdd:COG3206  177 LEFLEEQ--LPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLqqlselesqLAEARAELAEAEARLAALRAQLGSGPD 254
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 771 HLQDAA--------RRRLLKLQQDQREM---------ELRRLEDEIERKVQMRDQEIAATAKDLEIRQLELEAQKRLYEK 833
Cdd:COG3206  255 ALPELLqspviqqlRAQLAELEAELAELsarytpnhpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQA 334
ClassIIa_HDAC5_Gln-rich-N cd10164
Glutamine-rich N-terminal helical domain of HDAC5, a Class IIa histone deacetylase; This ...
703-799 4.83e-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: 4.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 703 LRERQTVENMQAEVDEQRAKDE---AWYQKQ-ELLRRAEETR--REILLQEEEKMAQQRQRLAAVKRELEIKEihlqdaA 776
Cdd:cd10164    4 LREQQLQQELLLLKQQQQLQKQllfAEFQKQhEHLTRQHEVQlqKHLKVRAELFSEQQQQEILAAKRQQELEQ------Q 77
                         90       100
                 ....*....|....*....|...
gi 264681545 777 RRRLlklQQDQREMELRRLEDEI 799
Cdd:cd10164   78 RKRE---QQRQEELEKQRLEQQL 97
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
697-833 5.22e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.89  E-value: 5.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 697 NDELDFLRE-RQTVENMQAEVDEQRakDEAWYQKQELLRRAEETR--REILLQEEEKMAQQRQRLAAVKREL--EIKEIH 771
Cdd:COG1340   21 REEIEELKEkRDELNEELKELAEKR--DELNAQVKELREEAQELRekRDELNEKVKELKEERDELNEKLNELreELDELR 98
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 264681545 772 lQDAARRRLLKLQQDQREMELRRLEDEIERKVQMRDQEiaataKDL--EIRQLE--LEAQKRLYEK 833
Cdd:COG1340   99 -KELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEE-----KELveKIKELEkeLEKAKKALEK 158
PRK03963 PRK03963
V-type ATP synthase subunit E; Provisional
730-833 5.33e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 167649 [Multi-domain]  Cd Length: 198  Bit Score: 38.97  E-value: 5.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 730 QELLRRAEETRREIlLQEEEKMAQQrqrlaavkreleIKEihlqdAARRRllklQQDQREMELRRLEDEIErkvqMRDQE 809
Cdd:PRK03963   9 QEINREAEQKIEYI-LEEAQKEAEK------------IKE-----EARKR----AESKAEWILRKAKTQAE----LEKQR 62
                         90       100
                 ....*....|....*....|....
gi 264681545 810 IAATAKdLEIRQLELEAQKRLYEK 833
Cdd:PRK03963  63 IIANAK-LEVRRKRLAVQEELISE 85
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
705-830 5.52e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.54  E-value: 5.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545   705 ERQTVENMQAEVDEQRAKDEAwyQKQELLRRAEETRREILLQEEE--KMAQQRQRLAAVKRELEIKEI-----------H 771
Cdd:pfam01576  392 ELRTLQQAKQDSEHKRKKLEG--QLQELQARLSESERQRAELAEKlsKLQSELESVSSLLNEAEGKNIklskdvsslesQ 469
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545   772 LQDAAR------RRLLKLQQDQREME------LRRLEDE------IERKVQMRDQEIAATAKDLE-----IRQLElEAQK 828
Cdd:pfam01576  470 LQDTQEllqeetRQKLNLSTRLRQLEdernslQEQLEEEeeakrnVERQLSTLQAQLSDMKKKLEedagtLEALE-EGKK 548

                   ..
gi 264681545   829 RL 830
Cdd:pfam01576  549 RL 550
NtpE COG1390
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
711-800 5.52e-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: 5.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 711 NMQAEVDEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMAQQR-QRLAAVKRELE-IKEIHLQDA---ARRRLLKLQQ 785
Cdd:COG1390    1 MMSLEKIIEEILEEAEAEAEEILEEAEEEAEKILEEAEEEAEEIKeEILEKAEREAErEKRRIISSAeleARKELLEAKE 80
                         90
                 ....*....|....*
gi 264681545 786 DQREMELRRLEDEIE 800
Cdd:COG1390   81 ELIEEVFEEALEKLK 95
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
690-834 5.77e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 5.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 690 REWERIRNdELDFLRERQTVENMQAEV-----DEQRAKDEAWYQKQELLRRAEETRREILLQEEEKMA--------QQRQ 756
Cdd:COG4717  354 REAEELEE-ELQLEELEQEIAALLAEAgvedeEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllealdeeELEE 432
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 757 RLAAVKRELEIKEIHLQDAaRRRLLKLQQDQREME----LRRLEDEIERKV-QMRDQEIAATAKDLeIRQLELEAQKRLY 831
Cdd:COG4717  433 ELEELEEELEELEEELEEL-REELAELEAELEQLEedgeLAELLQELEELKaELRELAEEWAALKL-ALELLEEAREEYR 510

                 ...
gi 264681545 832 EKY 834
Cdd:COG4717  511 EER 513
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
693-832 7.67e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 7.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 693 ERIRNDELDF---LRERQTVENMQAEVDEQRAKDEAWYQKQELLR-RAEETRREILLQE------EEKMAQQRQRLAAVK 762
Cdd:PRK03918 193 ELIKEKEKELeevLREINEISSELPELREELEKLEKEVKELEELKeEIEELEKELESLEgskrklEEKIRELEERIEELK 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 763 REL--------EIKEIHLQDAARRRLLKLQQDQREmELRRLEDEIER------KVQMRDQEIAATAKDL-EIRQLELEAQ 827
Cdd:PRK03918 273 KEIeeleekvkELKELKEKAEEYIKLSEFYEEYLD-ELREIEKRLSRleeeinGIEERIKELEEKEERLeELKKKLKELE 351

                 ....*
gi 264681545 828 KRLYE 832
Cdd:PRK03918 352 KRLEE 356
PRK02292 PRK02292
V-type ATP synthase subunit E; Provisional
713-798 7.96e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 235026 [Multi-domain]  Cd Length: 188  Bit Score: 38.44  E-value: 7.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 713 QAEVDEQRAKDEAwyQKQELLRRAEETRREIL---LQEEEKMAQQ--RQRLAAVKreLEIKEIHLqdAARRRLLKLQQDQ 787
Cdd:PRK02292  15 RARASEIRAEADE--EAEEIIAEAEADAEEILedrEAEAEREIEQlrEQELSSAK--LEAKRERL--NARKEVLEDVRNQ 88
                         90
                 ....*....|.
gi 264681545 788 REMELRRLEDE 798
Cdd:PRK02292  89 VEDEIASLDGD 99
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
689-815 8.60e-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: 8.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545  689 TREWERIRN---DELDFLRERQTVENMQAE--VDEQRAKDEAWYQKQELLRRAEETRREiLLQEEEKMAQQRQRLAAVKR 763
Cdd:pfam05667 421 AGQWEKHRVpliEEYRALKEAKSNKEDESQrkLEEIKELREKIKEVAEEAKQKEELYKQ-LVAEYERLPKDVSRSAYTRR 499
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 264681545  764 ELEI-KEIHLQdaaRRRLLKLQQDQREM--ELRRLEDEIERKVQMRDQEIAATAK 815
Cdd:pfam05667 500 ILEIvKNIKKQ---KEEITKILSDTKSLqkEINSLTGKLDRTFTVTDELVFKDAK 551
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
727-832 8.81e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 8.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545   727 YQKQELlrraEETRREILLQEEeKMAQQRQRLAAVKRELEIKEIHLQDAARRRLLKLQQ-DQREMELRRLEDEIERKVQM 805
Cdd:TIGR02168  674 ERRREI----EELEEKIEELEE-KIAELEKALAELRKELEELEEELEQLRKELEELSRQiSALRKDLARLEAEVEQLEER 748
                           90       100
                   ....*....|....*....|....*..
gi 264681545   806 RDQeiaatakdLEIRQLELEAQKRLYE 832
Cdd:TIGR02168  749 IAQ--------LSKELTELEAEIEELE 767
PRK03963 PRK03963
V-type ATP synthase subunit E; Provisional
721-809 9.77e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 167649 [Multi-domain]  Cd Length: 198  Bit Score: 38.20  E-value: 9.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 721 AKDEAWYQKQELLRRAEETRREILLQEEEKMAQQRQRLAA-----VKRE-LEIKEIHLQ---DAARRRLLKLQQDQREME 791
Cdd:PRK03963  26 AQKEAEKIKEEARKRAESKAEWILRKAKTQAELEKQRIIAnakleVRRKrLAVQEELISevlEAVRERLAELPEDEYFET 105
                         90       100
                 ....*....|....*....|...
gi 264681545 792 LRRLEDEI-----ERKVQMRDQE 809
Cdd:PRK03963 106 LKALTKEAveelgEDKVVVRSNE 128
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
693-834 9.89e-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: 9.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545 693 ERIRNDELDFLRERQTVENMQAEVDEQRAKDEAW------------YQKQ-ELLRRAEETRREILLQEEEKMAQQRQRLA 759
Cdd:COG1579   48 EAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeyeaLQKEiESLKRRISDLEDEILELMERIEELEEELA 127
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 264681545 760 AVKRELEikeihlqdaARRRLLKLQQDQREMELRRLEDEIERkvqmRDQEIAATAKDLEirqleleaqKRLYEKY 834
Cdd:COG1579  128 ELEAELA---------ELEAELEEKKAELDEELAELEAELEE----LEAEREELAAKIP---------PELLALY 180
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
717-829 9.97e-03

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: 39.82  E-value: 9.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 264681545   717 DEQRAKDEAWYQKQELLRR-------AEETRREILLQEEEKMAQQRQRLAAVKRELEIKEIHLQDaARRRLLKLqQDQRE 789
Cdd:pfam12128  586 DLKRIDVPEWAASEEELRErldkaeeALQSAREKQAAAEEQLVQANGELEKASREETFARTALKN-ARLDLRRL-FDEKQ 663
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 264681545   790 MELRRLEDEIE---RKVQMRDQEIAATAKDLEIR-QLELEAQKR 829
Cdd:pfam12128  664 SEKDKKNKALAerkDSANERLNSLEAQLKQLDKKhQAWLEEQKE 707
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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