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Conserved domains on  [gi|528953954|ref|XP_005208350|]
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transforming acidic coiled-coil-containing protein 3 isoform X2 [Bos taurus]

Protein Classification

transforming acidic coiled-coil-containing protein( domain architecture ID 12059788)

transforming acidic coiled-coil (TACC)-containing protein similar to human TACC1 that is involved in transcription regulation induced by nuclear receptors, including in T3 thyroid hormone and all-trans retinoic acid pathways

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 611-797 3.38e-100

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


:

Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 308.53  E-value: 3.38e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  611 YSQKDLDSAVEATQKENEV-------LRGKCAALQERLLEMGKIMDSFEGTVYQVMEESQKQKELTKAEMQKVLKEKAQL 683
Cdd:pfam05010   1 YSQKDMDAALEKARNEIEEkeleineLKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  684 TADLHSMEKSFSDLFKRFEKQKE-------NEESLKKCVEDYIERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSKAQT 756
Cdd:pfam05010  81 LADLNSVEKSFSDLFKRYEKQKEvisgykkNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 528953954  757 DALALQAVLRKEQMRVHSLEKVVEQKTKENDELTRICDDLI 797
Cdd:pfam05010 161 ETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 127-417 1.10e-07

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 55.95  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  127 EPPSEDMRPVSEDQPPGGPPSAPLVSLGPSSSsqipesvenpeasrgPAPGSPECAREEHVHPWPSEESMPLGPMAPEQ- 205
Cdd:PHA03307   98 ASPAREGSPTPPGPSSPDPPPPTPPPASPPPS---------------PAPDLSEMLRPVGSPGPPPAASPPAAGASPAAv 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  206 PSGVVSQDTAEDPLSGTGGDSEGV--PGPPARPASPCGAPPGEKPLVDLPGAAPVGSMDATSREDTALTGPGEAAGATHP 283
Cdd:PHA03307  163 ASDAASSRQAALPLSSPEETARAPssPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSS 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  284 GAQG------EETCGQAASSLRSGPVRLEFDFSDATGKRSPPLRKRGKalglkPPSRRPEARPGKatleagkgceltlrg 357
Cdd:PHA03307  243 ESSGcgwgpeNECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSS-----PRERSPSPSPSS--------------- 302

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  358 sdgpswdkPDDPDCNPAADSGEARPLEHPQSGQATEALSLSRQACSDDTPGTRAPARTPG 417
Cdd:PHA03307  303 --------PGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPS 354
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 611-797 3.38e-100

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 308.53  E-value: 3.38e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  611 YSQKDLDSAVEATQKENEV-------LRGKCAALQERLLEMGKIMDSFEGTVYQVMEESQKQKELTKAEMQKVLKEKAQL 683
Cdd:pfam05010   1 YSQKDMDAALEKARNEIEEkeleineLKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  684 TADLHSMEKSFSDLFKRFEKQKE-------NEESLKKCVEDYIERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSKAQT 756
Cdd:pfam05010  81 LADLNSVEKSFSDLFKRYEKQKEvisgykkNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 528953954  757 DALALQAVLRKEQMRVHSLEKVVEQKTKENDELTRICDDLI 797
Cdd:pfam05010 161 ETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 127-417 1.10e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 55.95  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  127 EPPSEDMRPVSEDQPPGGPPSAPLVSLGPSSSsqipesvenpeasrgPAPGSPECAREEHVHPWPSEESMPLGPMAPEQ- 205
Cdd:PHA03307   98 ASPAREGSPTPPGPSSPDPPPPTPPPASPPPS---------------PAPDLSEMLRPVGSPGPPPAASPPAAGASPAAv 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  206 PSGVVSQDTAEDPLSGTGGDSEGV--PGPPARPASPCGAPPGEKPLVDLPGAAPVGSMDATSREDTALTGPGEAAGATHP 283
Cdd:PHA03307  163 ASDAASSRQAALPLSSPEETARAPssPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSS 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  284 GAQG------EETCGQAASSLRSGPVRLEFDFSDATGKRSPPLRKRGKalglkPPSRRPEARPGKatleagkgceltlrg 357
Cdd:PHA03307  243 ESSGcgwgpeNECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSS-----PRERSPSPSPSS--------------- 302

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  358 sdgpswdkPDDPDCNPAADSGEARPLEHPQSGQATEALSLSRQACSDDTPGTRAPARTPG 417
Cdd:PHA03307  303 --------PGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPS 354
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 606-803 1.12e-07

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 55.41  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  606 VDVLQYSQKDLDSAVEATQKEnevlrgkcaaLQERLLEMGKIMDsfegtvyQVMEESQKQKELTKAemQKVLKEKAQ-LT 684
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKE----------LKSKEKELKKLNE-------EKKELEEKVKDLTKK--ISSLKEKIEkLE 530

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  685 ADLHSMEKSFSDLFKRFEKQKEN--EESLKKCVEDYIERVEKEAQKYQALKA---QAEEKLRQASEEIAQVRSKaqtdal 759
Cdd:TIGR04523 531 SEKKEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKSLKKkqeEKQELIDQKEKEKKDLIKE------ 604

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 528953954  760 alqavLRKEQMRVHSLEKVVEQKTKENDELTRICDDLISKMKRI 803
Cdd:TIGR04523 605 -----IEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 657-768 3.36e-07

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 50.27  E-value: 3.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954   657 QVMEESqkqkELTKAEMQKVLKEKAQLTADLHSMEKSFSDLFKRFEKQKE--NEESLKKCVEDYiervEKEAQKYQALKA 734
Cdd:smart00935   8 KILQES----PAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAAtlSEAAREKKEKEL----QKKVQEFQRKQQ 79

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 528953954   735 QAEEKLRQAS-EEIAQVRSKAQTdalALQAVLRKE 768
Cdd:smart00935  80 KLQQDLQKRQqEELQKILDKINK---AIKEVAKKK 111
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 657-768 1.92e-06

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 48.68  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 657 QVMEESQKqkelTKAEMQKVLKEKAQLTADLHSMEKSFSDLFKRFEKQKE--NEESLKKCVEDYIERvEKEAQKYQAlKA 734
Cdd:COG2825   33 RILQESPE----GKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEAAtlSEEERQKKERELQKK-QQELQRKQQ-EA 106

                         90       100       110
                 ....*....|....*....|....*....|....
gi 528953954 735 QAEEKLRQAsEEIAQVRSKAQTdalALQAVLRKE 768
Cdd:COG2825  107 QQDLQKRQQ-ELLQPILEKIQK---AIKEVAKEE 136
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
621-792 1.94e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.60  E-value: 1.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 621 EATQKENEV---------LRGKCAALQERLLEMGKIMDSFEgtvyqvmeESQKQKEltkaemqKVLKEKAQLTADLHSME 691
Cdd:PRK03918 201 ELEEVLREIneisselpeLREELEKLEKEVKELEELKEEIE--------ELEKELE-------SLEGSKRKLEEKIRELE 265

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 692 KSFSDLFKRFEKQKENEESLKKcvedyIERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSKAQtdalALQAVLRKEQMR 771
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKE-----LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN----GIEERIKELEEK 336

                        170       180
                 ....*....|....*....|.
gi 528953954 772 VHSLEKVVEQKTKENDELTRI 792
Cdd:PRK03918 337 EERLEELKKKLKELEKRLEEL 357
iSH2_PIK3R2 cd12926
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ...
 649-788 4.74e-06

Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 2, PIK3R2, also called p85beta; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. p85beta, also called PIK3R2, contains N-terminal SH3 and GAP domains. It is expressed ubiquitously but at lower levels than p85alpha. Its expression is increased in breast and colon cancer, correlates with tumor progression, and enhanced invasion. During viral infection, the viral nonstructural (NS1) protein binds p85beta specifically, which leads to PI3K activation and the promotion of viral replication. Mice deficient with PIK3R2 develop normally and exhibit moderate metabolic and immunological defects.


Pssm-ID: 214019 [Multi-domain]  Cd Length: 161  Bit Score: 47.38  E-value: 4.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 649 DSFEGTVYQVMEESQKQKEltKAEMQKVLKEKAQLTADLHSMEKS----FSDLFKRFEKQKENEEslkKCVEDYIERVEK 724
Cdd:cd12926    1 DSVEAVGAQLKVYHQQYQD--KSREYDQLYEEYTRTSQELQMKRTaieaFNETIKIFEEQGQTQE---KCSKEYLERFRR 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528953954 725 EAQKYQALKAQA-EEKLRQASEEIAQVRSKAQTDaLALQAVLRKE-QMRVHSLEKVVEQKTKENDE 788
Cdd:cd12926   76 EGNEKEMQRILLnSERLKSRIAEIHESRTKLEQD-LRAQASDNREiDKRMNSLKPDLMQLRKIRDQ 140
DUF4813 pfam16072
Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. ...
 144-244 3.46e-04

Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. This family of proteins is found in eukaryotes. Proteins in this family are typically between 345 and 672 amino acids in length.


Pssm-ID: 435117 [Multi-domain]  Cd Length: 288  Bit Score: 43.21  E-value: 3.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  144 GPPSAPLVSLGPSSSSQIPESVENPEASRGPA-----PGSPECAREEHVHPWPSEESMPLGPMAPEQPSGVVSQDTAEDP 218
Cdd:pfam16072 144 GPPGSVTTTSAGSGTTVINAGGQQPAAPAAPAypvapAAYPAQAPAAAPAPAPGAPQTPLAPLNPVAAAPAAAAGAAAAP 223

                          90       100
                  ....*....|....*....|....*.
gi 528953954  219 LSGTGGDSEGVPGPPARPASPCGAPP 244
Cdd:pfam16072 224 VVAAAAPAAAAPPPPAPAAPPADAAP 249
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 611-797 3.38e-100

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 308.53  E-value: 3.38e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  611 YSQKDLDSAVEATQKENEV-------LRGKCAALQERLLEMGKIMDSFEGTVYQVMEESQKQKELTKAEMQKVLKEKAQL 683
Cdd:pfam05010   1 YSQKDMDAALEKARNEIEEkeleineLKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  684 TADLHSMEKSFSDLFKRFEKQKE-------NEESLKKCVEDYIERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSKAQT 756
Cdd:pfam05010  81 LADLNSVEKSFSDLFKRYEKQKEvisgykkNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 528953954  757 DALALQAVLRKEQMRVHSLEKVVEQKTKENDELTRICDDLI 797
Cdd:pfam05010 161 ETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 127-417 1.10e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 55.95  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  127 EPPSEDMRPVSEDQPPGGPPSAPLVSLGPSSSsqipesvenpeasrgPAPGSPECAREEHVHPWPSEESMPLGPMAPEQ- 205
Cdd:PHA03307   98 ASPAREGSPTPPGPSSPDPPPPTPPPASPPPS---------------PAPDLSEMLRPVGSPGPPPAASPPAAGASPAAv 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  206 PSGVVSQDTAEDPLSGTGGDSEGV--PGPPARPASPCGAPPGEKPLVDLPGAAPVGSMDATSREDTALTGPGEAAGATHP 283
Cdd:PHA03307  163 ASDAASSRQAALPLSSPEETARAPssPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSS 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  284 GAQG------EETCGQAASSLRSGPVRLEFDFSDATGKRSPPLRKRGKalglkPPSRRPEARPGKatleagkgceltlrg 357
Cdd:PHA03307  243 ESSGcgwgpeNECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSS-----PRERSPSPSPSS--------------- 302

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  358 sdgpswdkPDDPDCNPAADSGEARPLEHPQSGQATEALSLSRQACSDDTPGTRAPARTPG 417
Cdd:PHA03307  303 --------PGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPS 354
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 606-803 1.12e-07

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 55.41  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  606 VDVLQYSQKDLDSAVEATQKEnevlrgkcaaLQERLLEMGKIMDsfegtvyQVMEESQKQKELTKAemQKVLKEKAQ-LT 684
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKE----------LKSKEKELKKLNE-------EKKELEEKVKDLTKK--ISSLKEKIEkLE 530

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  685 ADLHSMEKSFSDLFKRFEKQKEN--EESLKKCVEDYIERVEKEAQKYQALKA---QAEEKLRQASEEIAQVRSKaqtdal 759
Cdd:TIGR04523 531 SEKKEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKSLKKkqeEKQELIDQKEKEKKDLIKE------ 604

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 528953954  760 alqavLRKEQMRVHSLEKVVEQKTKENDELTRICDDLISKMKRI 803
Cdd:TIGR04523 605 -----IEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 601-791 2.63e-07

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: 54.26  E-value: 2.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  601 PVGPIVDVLQYSQKDLDsavEATQKENEVLRGKCAALQERLLEMGKIMDSFEGTVYQVMEESQkQKELTKAEMQKVLKEK 680
Cdd:pfam05667 314 AATSSPPTKVETEEELQ---QQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELE-ELKEQNEELEKQYKVK 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  681 AQlTADLhsmeksfsdlfkrFEKQKENEESLKKCVEDYIERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSKAQtdala 760
Cdd:pfam05667 390 KK-TLDL-------------LPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDESQ----- 450

                         170       180       190
                  ....*....|....*....|....*....|..
gi 528953954  761 lqavLRKEQMRV-HSLEKVVEQKTKENDELTR 791
Cdd:pfam05667 451 ----RKLEEIKElREKIKEVAEEAKQKEELYK 478
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 606-803 3.30e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 54.30  E-value: 3.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954   606 VDVLQYSQKDLDSAVEATQKENEVLRGKCAALQERLlemgkimdsfegtvYQVMEE-SQKQKELT--KAEMQKVLKEKAQ 682
Cdd:TIGR02169  704 LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL--------------EELEEDlSSLEQEIEnvKSELKELEARIEE 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954   683 LTADLHSMEKSFSDLFKRF--EKQKENEESLKKcVEDYIER-------VEKEAQKYQALKAQAEEKLRQASEEI----AQ 749
Cdd:TIGR02169  770 LEEDLHKLEEALNDLEARLshSRIPEIQAELSK-LEEEVSRiearlreIEQKLNRLTLEKEYLEKEIQELQEQRidlkEQ 848

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 528953954   750 VRSKAQTDALaLQAVLRKEQMRVHSLEKVVEQKTKENDELTRICDDLISKMKRI 803
Cdd:TIGR02169  849 IKSIEKEIEN-LNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 657-768 3.36e-07

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 50.27  E-value: 3.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954   657 QVMEESqkqkELTKAEMQKVLKEKAQLTADLHSMEKSFSDLFKRFEKQKE--NEESLKKCVEDYiervEKEAQKYQALKA 734
Cdd:smart00935   8 KILQES----PAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAAtlSEAAREKKEKEL----QKKVQEFQRKQQ 79

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 528953954   735 QAEEKLRQAS-EEIAQVRSKAQTdalALQAVLRKE 768
Cdd:smart00935  80 KLQQDLQKRQqEELQKILDKINK---AIKEVAKKK 111
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 657-768 1.92e-06

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 48.68  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 657 QVMEESQKqkelTKAEMQKVLKEKAQLTADLHSMEKSFSDLFKRFEKQKE--NEESLKKCVEDYIERvEKEAQKYQAlKA 734
Cdd:COG2825   33 RILQESPE----GKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEAAtlSEEERQKKERELQKK-QQELQRKQQ-EA 106

                         90       100       110
                 ....*....|....*....|....*....|....
gi 528953954 735 QAEEKLRQAsEEIAQVRSKAQTdalALQAVLRKE 768
Cdd:COG2825  107 QQDLQKRQQ-ELLQPILEKIQK---AIKEVAKEE 136
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
621-792 1.94e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.60  E-value: 1.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 621 EATQKENEV---------LRGKCAALQERLLEMGKIMDSFEgtvyqvmeESQKQKEltkaemqKVLKEKAQLTADLHSME 691
Cdd:PRK03918 201 ELEEVLREIneisselpeLREELEKLEKEVKELEELKEEIE--------ELEKELE-------SLEGSKRKLEEKIRELE 265

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 692 KSFSDLFKRFEKQKENEESLKKcvedyIERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSKAQtdalALQAVLRKEQMR 771
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKE-----LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN----GIEERIKELEEK 336

                        170       180
                 ....*....|....*....|.
gi 528953954 772 VHSLEKVVEQKTKENDELTRI 792
Cdd:PRK03918 337 EERLEELKKKLKELEKRLEEL 357
PTZ00121 PTZ00121
MAEBL; Provisional
 620-791 2.00e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  620 VEATQKENEvlrGKCAALQeRLLEMGKIMDSFEGTVYQVMEESQKQK--ELTKAEMQKVlkeKAQLTADLHSMEKSFSDL 697
Cdd:PTZ00121 1566 AEEAKKAEE---DKNMALR-KAEEAKKAEEARIEEVMKLYEEEKKMKaeEAKKAEEAKI---KAEELKKAEEEKKKVEQL 1638

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  698 FKRFEKQKENEESLKKCVEDYIERVEKEAQKYQALKAQAEEkLRQASEEiaqvrSKAQTDALALQAvlrKEQMRVHSLEK 777
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE-AKKAEED-----EKKAAEALKKEA---EEAKKAEELKK 1709

                         170
                  ....*....|....
gi 528953954  778 VVEQKTKENDELTR 791
Cdd:PTZ00121 1710 KEAEEKKKAEELKK 1723
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
662-803 3.80e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.90  E-value: 3.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 662 SQKQKELTKAEMQKVLKEKAQLTADLHSMEKSFSDLFKRFEKQKENEESLkkcvEDYIERVEKEAQKYQALKAQAEEKLR 741
Cdd:COG4372   29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQL----EEELEELNEQLQAAQAELAQAQEELE 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528953954 742 QASEEIAQVRS---KAQTDALALQAVLRKEQMRVHSLEKVVEQKTKENDELTRICDDLISKMKRI 803
Cdd:COG4372  105 SLQEEAEELQEeleELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 660-801 3.91e-06

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 50.40  E-value: 3.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  660 EESQKQKELTK--AEMQKVLKEKAQLTADLHSMEKSFSDLFKRFEKQKEN----EESLKKCVEDYiERVEKEAQKYQALK 733
Cdd:TIGR04523 357 ENSEKQRELEEkqNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLnqqkDEQIKKLQQEK-ELLEKEIERLKETI 435

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528953954  734 AQAEEKLRQASEEIA----------QVRSKAQTDALALQAVLRKEQMRVHSLEKVVEQKTKENDELTRICDDLISKMK 801
Cdd:TIGR04523 436 IKNNSEIKDLTNQDSvkeliiknldNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK 513
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
614-789 4.28e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.45  E-value: 4.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 614 KDLDSAVEATQKENEVLRGKCAALQERLLEmgkIMDSFEGTVYQVMEESQKQKEL-------------------TKAEMQ 674
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRE---LEERIEELKKEIEELEEKVKELkelkekaeeyiklsefyeeYLDELR 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 675 KVLKEKAQLTADLHSMEKSFSDLFKRFEKQKENEESLKKcVEDYIERVEKEAQKYQ---ALKAQAEE-KLRQASEEIAQV 750
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE-LEKRLEELEERHELYEeakAKKEELERlKKRLTGLTPEKL 389

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 528953954 751 RSK---AQTDALALQAVLRKEQMRVHSLEKVVEQKTKENDEL 789
Cdd:PRK03918 390 EKEleeLEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL 431
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 135-603 4.41e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.55  E-value: 4.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  135 PVSEDQPPGGPPSAPLVSLGPSSSSQI---PESVENPEASRGPAPGSPECAREEHVHPWPSEESMPLGPMAPEQPsgvvs 211
Cdd:PHA03307   35 LLSGSQGQLVSDSAELAAVTVVAGAAAcdrFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPP----- 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  212 qdtaedplsgtGGDSEGVPGPPARPASPcGAPPGEKPLVDLPGAAPVGSMDATSREDTALTGPGEAAGATHPgaqgeetc 291
Cdd:PHA03307  110 -----------GPSSPDPPPPTPPPASP-PPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASS-------- 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  292 GQAASSLRSGPvrlefdfsDATGKRSPPLRKRGKALGLKPPSRRPEARPGKATLEAGKGCELTLRGSDGPSWDKPDDPDC 371
Cdd:PHA03307  170 RQAALPLSSPE--------ETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSS 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  372 NPAADSGEARPLEHPQSGQATEAL-SLSRQACSDDTPGTRAPARTPGAAgegwtTGSLGGSAPLSSPSSEPPTAPTNPTP 450
Cdd:PHA03307  242 SESSGCGWGPENECPLPRPAPITLpTRIWEASGWNGPSSRPGPASSSSS-----PRERSPSPSPSSPGSGPAPSSPRASS 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  451 PTERGPEPTLDLNGEQ-FRDPAEVLGAGAELDYLEQFGAPSfkesalrkqslylnfdpllqDSPQGLTPSSSGRPRGLPV 529
Cdd:PHA03307  317 SSSSSRESSSSSTSSSsESSRGAAVSPGPSPSRSPSPSRPP--------------------PPADPSSPRKRPRPSRAPS 376

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528953954  530 PSAGPLASEESPglmqtAGGFSLGLRARSVDKPSS---GSPPEAQLLDLDFPGAPGIPIPGLAPC-DLGPGAPLLPVG 603
Cdd:PHA03307  377 SPAASAGRPTRR-----RARAAVAGRARRRDATGRfpaGRPRPSPLDAGAASGAFYARYPLLTPSgEPWPGSPPPPPG 449
iSH2_PIK3R2 cd12926
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ...
 649-788 4.74e-06

Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 2, PIK3R2, also called p85beta; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. p85beta, also called PIK3R2, contains N-terminal SH3 and GAP domains. It is expressed ubiquitously but at lower levels than p85alpha. Its expression is increased in breast and colon cancer, correlates with tumor progression, and enhanced invasion. During viral infection, the viral nonstructural (NS1) protein binds p85beta specifically, which leads to PI3K activation and the promotion of viral replication. Mice deficient with PIK3R2 develop normally and exhibit moderate metabolic and immunological defects.


Pssm-ID: 214019 [Multi-domain]  Cd Length: 161  Bit Score: 47.38  E-value: 4.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 649 DSFEGTVYQVMEESQKQKEltKAEMQKVLKEKAQLTADLHSMEKS----FSDLFKRFEKQKENEEslkKCVEDYIERVEK 724
Cdd:cd12926    1 DSVEAVGAQLKVYHQQYQD--KSREYDQLYEEYTRTSQELQMKRTaieaFNETIKIFEEQGQTQE---KCSKEYLERFRR 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528953954 725 EAQKYQALKAQA-EEKLRQASEEIAQVRSKAQTDaLALQAVLRKE-QMRVHSLEKVVEQKTKENDE 788
Cdd:cd12926   76 EGNEKEMQRILLnSERLKSRIAEIHESRTKLEQD-LRAQASDNREiDKRMNSLKPDLMQLRKIRDQ 140
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 657-768 5.75e-06

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 46.80  E-value: 5.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  657 QVMEESQKqkelTKAEMQKVLKEKAQLTADLHSMEKSFSDLFKRFEKQKENEESLKKCVEDYIERVEKEAQKYQALKAQA 736
Cdd:pfam03938   9 KILEESPE----GKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQE 84

                          90       100       110
                  ....*....|....*....|....*....|..
gi 528953954  737 EEKLRQasEEIAQVRSKAQTdalALQAVLRKE 768
Cdd:pfam03938  85 LQKKQQ--ELLQPIQDKINK---AIKEVAKEK 111
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 614-761 6.19e-06

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: 48.38  E-value: 6.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 614 KDLDSAVEATQKENEVLRGKCAALQERLLEMGKIMDSFEGTVYQVMEE----SQKQKELTKA-EMQKVLKEKAQLTADLH 688
Cdd:COG1579   27 KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyEEQLGNVRNNkEYEALQKEIESLKRRIS 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528953954 689 SMEKSFSDLFKRFEKQKENEESLKKCVEDYIERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSKAQTDALAL 761
Cdd:COG1579  107 DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPELLAL 179
PTZ00121 PTZ00121
MAEBL; Provisional
 611-799 6.55e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 6.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  611 YSQKDLDSAVEATQKENEVLRGkcaalqERLLEMGKIMDSFEGTVYQVMEESQKQKELTKAEMQKVL------------K 678
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKA------EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIkaaeeakkaeedK 1674

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  679 EKAQLTADLHSMEKSFSDLFKRFEKQKENEESLKKCVEDYI---ERVEKEAQ----KYQALKAQAEEKLRQASEEIAQVR 751
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKkkaEELKKAEEenkiKAEEAKKEAEEDKKKAEEAKKDEE 1754

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 528953954  752 SKAQTDALALQAVLRKEQMRVHSlEKVVEQKTKENDELTRICDDLISK 799
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEK-EAVIEEELDEEDEKRRMEVDKKIK 1801
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
614-791 8.54e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 8.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 614 KDLDSAVEATQKENEVLRGKCAALQE------RLLEMGKIMDSFEGTVYQVMEESQKQKELTKaEMQKVLKEKAQLTADL 687
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKElkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEIN-GIEERIKELEEKEERL 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 688 HSMEKSFSDLFKRFE------------KQKENE-ESLKKCVEDY-IERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSK 753
Cdd:PRK03918 341 EELKKKLKELEKRLEeleerhelyeeaKAKKEElERLKKRLTGLtPEKLEKELEELEKAKEEIEEEISKITARIGELKKE 420

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 528953954 754 AQTDALALQAVL-----------------RKEQMRVHSLE-KVVEQKTKENDELTR 791
Cdd:PRK03918 421 IKELKKAIEELKkakgkcpvcgrelteehRKELLEEYTAElKRIEKELKEIEEKER 476
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 613-803 1.03e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 49.25  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  613 QKDLDSAVEATQKENEVLRGKCAALQERLLEMGKIMDSFEGTVYQVMEE--------SQKQKELTKAEmqKVLKEkaqLT 684
Cdd:TIGR04523 213 NKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEqnkikkqlSEKQKELEQNN--KKIKE---LE 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  685 ADLHSMEKSFSDLfkrfEKQKENEesLKKCVEDYIERVEKEAQKYQALKAQAEEKLRQASEEIAQV---RSKAQTDALAL 761
Cdd:TIGR04523 288 KQLNQLKSEISDL----NNQKEQD--WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLkkeLTNSESENSEK 361

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 528953954  762 QAVLRKEQMRVHSLEKVVEQKTKENDELTRICDDLISKMKRI 803
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQ 403
PTZ00121 PTZ00121
MAEBL; Provisional
 660-791 1.28e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  660 EESQKQKELTKAEMQ------KVLKEKAQLTADLHSMEKSFSDLFKRFEKQKENEESLKKCVE------DYIERVEKEAQ 727
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEaaadeaEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEedkkkaDELKKAAAAKK 1418

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528953954  728 KYQALKAQAEEKlRQASEEIAQVRSKAQTDALALQAvlrKEQMRVHSLEKVVEQKTKEnDELTR 791
Cdd:PTZ00121 1419 KADEAKKKAEEK-KKADEAKKKAEEAKKADEAKKKA---EEAKKAEEAKKKAEEAKKA-DEAKK 1477
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 715-768 1.98e-05

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 44.74  E-value: 1.98e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 528953954 715 VEDYIERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSKAQTDALALQAVLRKE 768
Cdd:cd06503   35 IAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEILAE 88
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 625-788 2.42e-05

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 47.11  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  625 KENEVLRGKCAA---------LQERLLEMGKIMDSFEGTVYQVMEESQKQKELTKAEMQKVLKEKAQLTADLHSMEKsfs 695
Cdd:pfam15905 136 RVNELLKAKFSEdgtqkkmssLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEK--- 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  696 dlfkrfEKQKENEESLKkcVEDYIER---VEKEAQKYQALKAQAEEKLRQASEEIAQVRSKAQTDALALQAVLRKEQMRV 772
Cdd:pfam15905 213 ------EKIEEKSETEK--LLEYITElscVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKC 284

                         170
                  ....*....|....*.
gi 528953954  773 HSLEKVVEQKTKENDE 788
Cdd:pfam15905 285 KLLESEKEELLREYEE 300
PTZ00121 PTZ00121
MAEBL; Provisional
 619-791 2.70e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 2.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  619 AVEATQKENEVLRgkcaALQERLLEMGKIMDSFEGTVYQVMEESQKQKELTKAEMQKVLKEKAQLTADLHSMEKSFSDLF 698
Cdd:PTZ00121 1232 AEEAKKDAEEAKK----AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEA 1307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  699 KRFEKQKENEESLKKcvedyieRVEKEAQKYQALKAQAEEKLRQAseEIAQVRSKAQTDAlalqavLRKEQMRVHSLEKV 778
Cdd:PTZ00121 1308 KKKAEEAKKADEAKK-------KAEEAKKKADAAKKKAEEAKKAA--EAAKAEAEAAADE------AEAAEEKAEAAEKK 1372

                         170
                  ....*....|...
gi 528953954  779 VEQKTKENDELTR 791
Cdd:PTZ00121 1373 KEEAKKKADAAKK 1385
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 625-791 3.03e-05

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 46.84  E-value: 3.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  625 KENEVLRgkCAALQERLLEmGKIMDSFegtVYQVMEESQKQKELTKAEMQKVLKEKAQLTADLhsmeksfsDLFKRFEKQ 704
Cdd:pfam13868  83 EEREQKR--QEEYEEKLQE-REQMDEI---VERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQ--------AEWKELEKE 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  705 KENEESLKkcVEDYIERVEKEAQKYQALKAQAEEKLRQASEEIAQV-----RSKAQTDALALQAVL--RKEQMRVHSLEK 777
Cdd:pfam13868 149 EEREEDER--ILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQqekaqDEKAERDELRAKLYQeeQERKERQKEREE 226

                         170
                  ....*....|....
gi 528953954  778 vVEQKTKENDELTR 791
Cdd:pfam13868 227 -AEKKARQRQELQQ 239
PRK12704 PRK12704
phosphodiesterase; Provisional
 657-761 3.19e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.47  E-value: 3.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 657 QVMEESQKQKELTKAEM-----QKVLKEKAQLTADLHSMEKSFSDLFKRFEKQKEN-----------EESLKKCVEDYIE 720
Cdd:PRK12704  42 RILEEAKKEAEAIKKEAlleakEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENldrklellekrEEELEKKEKELEQ 121

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 528953954 721 R---VEKEAQKYQALKAQAEEKLRQAS----EE-----IAQVRSKAQTDALAL 761
Cdd:PRK12704 122 KqqeLEKKEEELEELIEEQLQELERISgltaEEakeilLEKVEEEARHEAAVL 174
PTZ00121 PTZ00121
MAEBL; Provisional
 615-791 3.36e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 3.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  615 DLDSAVEATQKENEVLRGKcAALQERLLEMGKIMDSFEGTVYQVMEESQKQKELTKAEMQK---VLKEKAQLTADLHSME 691
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKK-AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKkadAAKKKAEEKKKADEAK 1397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  692 KSFSDLFKRFEKQKENEESLKKCVE-----------DYIERVEKEAQKYQALKAQAEEKlRQASEEIAQVRSKAQTDALA 760
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADEakkkaeekkkaDEAKKKAEEAKKADEAKKKAEEA-KKAEEAKKKAEEAKKADEAK 1476

                         170       180       190
                  ....*....|....*....|....*....|.
gi 528953954  761 LQAvlrKEQMRVHSLEKVVEQKTKENDELTR 791
Cdd:PTZ00121 1477 KKA---EEAKKADEAKKKAEEAKKKADEAKK 1504
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 622-747 4.16e-05

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


Pssm-ID: 463102 [Multi-domain]  Cd Length: 140  Bit Score: 44.21  E-value: 4.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  622 ATQKENEVLRGKCAALqERLLEMgkIMDSFEGTVYQvMEESQKQKELTKAEMQKVLKEKAQLTADLHSMEKSFSDLFKRF 701
Cdd:pfam10473  14 ESERKADSLKDKVENL-ERELEM--SEENQELAILE-AENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSEKENLTKEL 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 528953954  702 EKQKENEESLKKCVEDYIERVEKEAQKyqalKAQAEEKLRQASEEI 747
Cdd:pfam10473  90 QKKQERVSELESLNSSLENLLEEKEQE----KVQMKEESKTAVEML 131
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 622-803 4.35e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 4.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954   622 ATQKENEVLRGKCAALQERLLEMGKimdsfegtvyQVMEESQKQKELTKaEMQKVLKEKAQLTADLHSMEKSFSDLFKRF 701
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEK----------ALAELRKELEELEE-ELEQLRKELEELSRQISALRKDLARLEAEV 742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954   702 EKQKENEESLKKCVEDYIERVEKEAQ---KYQALKAQAEEKLRQASEEIAQVRS--KAQTDAL-ALQAVLRKEQMRVHSL 775
Cdd:TIGR02168  743 EQLEERIAQLSKELTELEAEIEELEErleEAEEELAEAEAEIEELEAQIEQLKEelKALREALdELRAELTLLNEEAANL 822

                          170       180
                   ....*....|....*....|....*...
gi 528953954   776 EKVVEQKTKENDELTRICDDLISKMKRI 803
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQIEEL 850
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 614-792 5.18e-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: 5.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 614 KDLDSAVEATQKENEVLRGKCAALQERLLEMGKIMDSFEGTVYQV---MEESQKQKELTKAEMQKVLKEKAQLTADLHSM 690
Cdd:COG1196  249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELlaeLARLEQDIARLEERRRELEERLEELEEELAEL 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 691 EksfsdlfkrfEKQKENEESLKKCVEDyIERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSKAQTDALALQAVLRKEQM 770
Cdd:COG1196  329 E----------EELEELEEELEELEEE-LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397

                        170       180
                 ....*....|....*....|..
gi 528953954 771 RVHSLEKVVEQKTKENDELTRI 792
Cdd:COG1196  398 LAAQLEELEEAEEALLERLERL 419
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 610-802 5.25e-05

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: 46.89  E-value: 5.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954   610 QYSQKDLDSAVEATQKENEVLRGKCA--ALQERLLEMGKIMDSFEGTVyQVMEESQKQKELTKAEMQKVLKEKAQLTADL 687
Cdd:pfam02463  287 ELKLLAKEEEELKSELLKLERRKVDDeeKLKESEKEKKKAEKELKKEK-EEIEELEKELKELEIKREAEEEEEEELEKLQ 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954   688 HSMEKSFSDLFKRFEKQKENEESLKKCVEDYIERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSKAQTDALALQAVLRK 767
Cdd:pfam02463  366 EKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGK 445

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 528953954   768 EQMRVHSLEKVVEQKTKENDELTRICDDLISKMKR 802
Cdd:pfam02463  446 LTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 613-789 5.53e-05

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 45.96  E-value: 5.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  613 QKDLDSAVEATQKENEVLRGKCAALQERLLEMgkimdsfegtvyqvmeesQKQKELTKAEMQKVLKEKAQLTADLHSMEK 692
Cdd:pfam15905 179 QEGMEGKLQVTQKNLEHSKGKVAQLEEKLVST------------------EKEKIEEKSETEKLLEYITELSCVSEQVEK 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  693 SFSDLFKRFE--KQKENE-ESLKKCVEdyiervekeaQKYQALKAQAE---EKLRQASEEIAQVRSKAQTDALALQAVLR 766
Cdd:pfam15905 241 YKLDIAQLEEllKEKNDEiESLKQSLE----------EKEQELSKQIKdlnEKCKLLESEKEELLREYEEKEQTLNAELE 310

                         170       180
                  ....*....|....*....|...
gi 528953954  767 keqmrvhSLEKVVEQKTKENDEL 789
Cdd:pfam15905 311 -------ELKEKLTLEEQEHQKL 326
PTZ00121 PTZ00121
MAEBL; Provisional
 621-791 7.71e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 7.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  621 EATQKENEVLRGKCAALQERLLEMGKImdsfEGTVYQVMEESQKQKELTKAEMQKVLKEKAQLTADlhsmEKSFSDLFKR 700
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKA----DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE----EKKKADEAKK 1438

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  701 FEKQKENEESLKKCVEdyiervekEAQKYQALKAQAEEKlRQASEEIAQVRSKAQTDALALQAvlRKEQMRVHSLEKVVE 780
Cdd:PTZ00121 1439 KAEEAKKADEAKKKAE--------EAKKAEEAKKKAEEA-KKADEAKKKAEEAKKADEAKKKA--EEAKKKADEAKKAAE 1507

                         170
                  ....*....|.
gi 528953954  781 QKtKENDELTR 791
Cdd:PTZ00121 1508 AK-KKADEAKK 1517
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
606-753 1.02e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  606 VDVLQYSQKDLDSAVEATQKENEVLRGKCAALQERLLEMGKIMDSFEGTVYQVMEESQKQKELTKAEMQKVLKEKAQLTA 685
Cdd:COG4913   290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLA 369

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528953954  686 DLH----SMEKSFSDLFKRFEKQKENEESLKkcvedyiERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSK 753
Cdd:COG4913   370 ALGlplpASAEEFAALRAEAAALLEALEEEL-------EALEEALAEAEAALRDLRRELRELEAEIASLERR 434
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 121-289 1.23e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.75  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 121 PVPVNTEPPSEDMRPVSEDQP-------PGGPPSAPLVSLGPSSSSQIPESVENPEASRGPAPGSPECAREEHVHPWPSE 193
Cdd:PRK07764 601 PAPASSGPPEEAARPAAPAAPaapaapaPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAA 680

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 194 ESMPLGPMAPEQPSGVVSQDTAED----PLSGTGGDSEGV-PGPPARPASPCGAPPGEKPLVDLPGAAPVGSMDATSRED 268
Cdd:PRK07764 681 PPPAPAPAAPAAPAGAAPAQPAPApaatPPAGQADDPAAQpPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPP 760

                        170       180
                 ....*....|....*....|.
gi 528953954 269 TALTGPGEAAGATHPGAQGEE 289
Cdd:PRK07764 761 PPAPAPAAAPAAAPPPSPPSE 781
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 609-760 1.24e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 45.18  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 609 LQYSQKDLDSAVEATQKENEV----LRGKCAALQERLLEMGKIMDSFEGTVYQVMEESQKQKELTK--AEMQKVLKEKAQ 682
Cdd:PRK09510  67 QQQQQKSAKRAEEQRKKKEQQqaeeLQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKqaEEAAAKAAAAAK 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 683 LTADlhSMEKSFSDLFKRFE---KQKENEESLKKCVEDYIERVEKEAQkyQALKAQAEEKLRQASEEIAQVRSKAQTDAL 759
Cdd:PRK09510 147 AKAE--AEAKRAAAAAKKAAaeaKKKAEAEAAKKAAAEAKKKAEAEAA--AKAAAEAKKKAEAEAKKKAAAEAKKKAAAE 222


                 .
gi 528953954 760 A 760
Cdd:PRK09510 223 A 223
PTZ00121 PTZ00121
MAEBL; Provisional
 660-791 1.28e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  660 EESQKQKELTKAEMqkvLKEKAQLTADLHSMEKSFSDLFKRFEKQKENEESLKKCVEDYIERVEKEAQKYQALKAQAEEK 739
Cdd:PTZ00121 1293 DEAKKAEEKKKADE---AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 528953954  740 LRQASEEiaqvrsKAQTDALALQAvlrKEQMRVHSLEKVVEQKTKENDELTR 791
Cdd:PTZ00121 1370 EKKKEEA------KKKADAAKKKA---EEKKKADEAKKKAEEDKKKADELKK 1412
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 143-338 1.29e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.75  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 143 GGPPSAPLVSLGPSSSSQIPESVENPEASrgPAPGSPECAREEHVHPWPSEESmplGPMAPEQPSGVVSQDTAEDPLSGT 222
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAP--AAPAAPAAPAPAGAAAAPAEAS---AAPAPGVAAPEHHPKHVAVPDASD 664

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 223 GGDSEGVPGPPARPASPCGAPPGEKPlvdlPGAAPVGSMDATSREDTALTGPGEAAGATHPGAQGEETCGQAASSLRSGP 302
Cdd:PRK07764 665 GGDGWPAKAGGAAPAAPPPAPAPAAP----AAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVP 740

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 528953954 303 VRLEFDFSDATGKRSPPLRKRGKALGLKPPSRRPEA 338
Cdd:PRK07764 741 LPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPP 776
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 615-799 1.74e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.44  E-value: 1.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954   615 DLDSAVEATQKENEVLRGKCAALQERLLEMGKIMDSFEGTVyqvmEESQKQKEltkaEMQKVLKEKAQLTADLhsmEKSF 694
Cdd:TIGR02169  816 EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI----ENLNGKKE----ELEEELEELEAALRDL---ESRL 884

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954   695 SDLfkrfEKQKENEESLKKCVEDYIERVEKEAQKYQALKAQAEEKLRQASEEIAQVR---------SKAQTDALALQAVL 765
Cdd:TIGR02169  885 GDL----KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEdpkgedeeiPEEELSLEDVQAEL 960

                          170       180       190
                   ....*....|....*....|....*....|....
gi 528953954   766 RKEQMRVHSLEKVVEQKTKENDELTRICDDLISK 799
Cdd:TIGR02169  961 QRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEK 994
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
636-786 2.10e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 2.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 636 ALQERLLEMGKIMDSFEgTVYQVMEESQKQKELTKAEMQKVLKEKAQLTADLHSMEKSFSDLFKRFEKQKENEESLKKCV 715
Cdd:COG4372   32 QLRKALFELDKLQEELE-QLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528953954 716 EDYIERVEKEAQKYQALKAQaEEKLRQASEEIAQVRSKAQTDALALQAVLRKEQMRVHSLEKVVEQKTKEN 786
Cdd:COG4372  111 EELQEELEELQKERQDLEQQ-RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
615-796 2.29e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.65  E-value: 2.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 615 DLDSAVEATQKENEVLRGKCAALQ-------------ERLLEMGK-------IMDSfegTVYQVMEESQKQKELTKAEMQ 674
Cdd:PRK02224 409 NAEDFLEELREERDELREREAELEatlrtarerveeaEALLEAGKcpecgqpVEGS---PHVETIEEDRERVEELEAELE 485

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 675 KVLKEKAQLTADLHSMEkSFSDLFKRFEKQKENEESLKKCVEDYIERVEKEAQKYQALKAQAEEkLRQASEEiaqVRSKA 754
Cdd:PRK02224 486 DLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE-LEAEAEE---KREAA 560

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 528953954 755 QTDALALQAVLRkeqmRVHSLEKVVEQKTKENDELTRICDDL 796
Cdd:PRK02224 561 AEAEEEAEEARE----EVAELNSKLAELKERIESLERIRTLL 598
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 606-792 2.30e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 2.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954   606 VDVLQYSQKDLDSAVEATQKENEVLRGKCAALQERLLEMGKIMDSFEgtvyQVMEESQKQKELTKAEMQKVLKEKAQLTA 685
Cdd:TIGR02168  791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE----RRLEDLEEQIEELSEDIESLAAEIEELEE 866

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954   686 DLHSMEKSFSDLFKRFEKQKENEESLKKCVEDY---IERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSKAQT--DALA 760
Cdd:TIGR02168  867 LIEELESELEALLNERASLEEALALLRSELEELseeLRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNlqERLS 946

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 528953954   761 ------LQAVLRKEQMRVHSLEKVVEQKTKENDELTRI 792
Cdd:TIGR02168  947 eeysltLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 657-803 2.42e-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: 2.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 657 QVMEESQKQKELTKAEMQKVLKEKAQLTADLHSMEKSFSDL----------FKRFEKQKENEESLKKCVEDYIERVEKEA 726
Cdd:COG1196  246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeyellaeLARLEQDIARLEERRRELEERLEELEEEL 325

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528953954 727 QKYQALKAQAEEKLRQASEEIAQVRSKAQTDALALQAVLRKEQMRVHSLEKVVEQKTKENDELTRICDDLISKMKRI 803
Cdd:COG1196  326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
121-283 3.16e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.48  E-value: 3.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 121 PVPVNTEPPSEDMRPVSEDQPPGGPPSAPLVSLGPSSSSQIPESVENPEASRGPAPGSPECAREEHVHPWpseESMPLGP 200
Cdd:PRK12323 430 PEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPW---EELPPEF 506

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 201 MAPEQPSGVVSQDTAEDPLSGTGGDSEGVPGPPARPASPCGAPPGEKPLVDLPGAAPVGSMDATSREDTALTGPGEAAGA 280
Cdd:PRK12323 507 ASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDGDWPALAA 586


                 ...
gi 528953954 281 THP 283
Cdd:PRK12323 587 RLP 589
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 659-770 3.16e-04

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


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 42.74  E-value: 3.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  659 MEESQKQKELTKAEMQKVLKEKAQLTADLHSMEKSF-------SDLFKRFEKQKE-----NEESL-------KKCVEDYI 719
Cdd:pfam04012  20 AEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLerrleqqTEQAKKLEEKAQaaltkGNEELarealaeKKSLEKQA 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528953954  720 ERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSKAQTDALALQAVLRKEQM 770
Cdd:pfam04012 100 EALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAV 150
DUF4813 pfam16072
Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. ...
 144-244 3.46e-04

Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. This family of proteins is found in eukaryotes. Proteins in this family are typically between 345 and 672 amino acids in length.


Pssm-ID: 435117 [Multi-domain]  Cd Length: 288  Bit Score: 43.21  E-value: 3.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  144 GPPSAPLVSLGPSSSSQIPESVENPEASRGPA-----PGSPECAREEHVHPWPSEESMPLGPMAPEQPSGVVSQDTAEDP 218
Cdd:pfam16072 144 GPPGSVTTTSAGSGTTVINAGGQQPAAPAAPAypvapAAYPAQAPAAAPAPAPGAPQTPLAPLNPVAAAPAAAAGAAAAP 223

                          90       100
                  ....*....|....*....|....*.
gi 528953954  219 LSGTGGDSEGVPGPPARPASPCGAPP 244
Cdd:pfam16072 224 VVAAAAPAAAAPPPPAPAAPPADAAP 249
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
606-792 3.56e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 3.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 606 VDVLQYSQKDLDSAVEATQKENEVLRGKCAALQERLLEMGKIMDSFEGTVYQV---MEESQKQKELTKAEMQKVLKEKAQ 682
Cdd:COG4372   33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELneqLQAAQAELAQAQEELESLQEEAEE 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 683 LTADLHSMEKSFSDLfkrfEKQKENEESLKKCVEDYIERVEKEAQKYQALKAQAEEKLrQASEEIAQVRSKAQTDAlALQ 762
Cdd:COG4372  113 LQEELEELQKERQDL----EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL-AALEQELQALSEAEAEQ-ALD 186

                        170       180       190
                 ....*....|....*....|....*....|
gi 528953954 763 AVLRKEQMRVHSLEKVVEQKTKENDELTRI 792
Cdd:COG4372  187 ELLKEANRNAEKEEELAEAEKLIESLPREL 216
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 614-803 4.07e-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: 4.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 614 KDLDSAVEATQKENEVLRGKCAALQERLLEMGKIMdsfegtvyqvmEESQKQKELTKAEMQKVLKeKAQLTADLHSME-- 691
Cdd:COG4942   58 AALERRIAALARRIRALEQELAALEAELAELEKEI-----------AELRAELEAQKEELAELLR-ALYRLGRQPPLAll 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 692 ---KSFSDLFKRFEkqkeneeSLKKCVEDYIERVEKEAQKYQALKAQAEEkLRQASEEIAQVRSKAQTDALALQAVLRKE 768
Cdd:COG4942  126 lspEDFLDAVRRLQ-------YLKYLAPARREQAEELRADLAELAALRAE-LEAERAELEALLAELEEERAALEALKAER 197

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 528953954 769 QMRVHSLEKVVEQKTKENDELTRICDDLISKMKRI 803
Cdd:COG4942  198 QKLLARLEKELAELAAELAELQQEAEELEALIARL 232
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 613-785 4.80e-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: 42.98  E-value: 4.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  613 QKDLDSAVEATQKENEVLRgkcaaLQERLLEMgKIMdsfegtvyQVMEESQKQKELTKAEMQKVLKEKAQLTADLhsmek 692
Cdd:pfam13868 129 REEIDEFNEEQAEWKELEK-----EEEREEDE-RIL--------EYLKEKAEREEEREAEREEIEEEKEREIARL----- 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  693 sFSDLFKRFEKQKENEE-SLKKCVEDYIERVEKEAQKYQALKAQAEEKLRQASEEiaQVRSKAQTDALALQavlRKEQMR 771
Cdd:pfam13868 190 -RAQQEKAQDEKAERDElRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREE--QIELKERRLAEEAE---REEEEF 263

                         170
                  ....*....|....
gi 528953954  772 VHSLEKVVEQKTKE 785
Cdd:pfam13868 264 ERMLRKQAEDEEIE 277
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 609-761 6.08e-04

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 43.19  E-value: 6.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  609 LQYSQKDLDSAVEATQKENEVLRGKCAALQERLLEMGKIMDSFEGTVYQVMEESQKQKELTK--------AEMQKVLKEK 680
Cdd:pfam05557 116 LRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFeiqsqeqdSEIVKNSKSE 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  681 AQLTADLHSMEKSFSDLFKRFEKQKENEESLKKCVEDYIERVEKEaQKYQALKAQAEEKLRQASEEIAQVRSKAQTDALA 760
Cdd:pfam05557 196 LARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLERE-EKYREEAATLELEKEKLEQELQSWVKLAQDTGLN 274


                  .
gi 528953954  761 L 761
Cdd:pfam05557 275 L 275
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 639-792 6.42e-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: 43.52  E-value: 6.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954   639 ERLLEMGKIMDSFEGTVY-QVMEESQKQKELTKAEMQKVLKEKAQLTADL-------HSMEKSFSDLFKRFEKQKENEE- 709
Cdd:TIGR02169  211 ERYQALLKEKREYEGYELlKEKEALERQKEAIERQLASLEEELEKLTEEIselekrlEEIEQLLEELNKKIKDLGEEEQl 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954   710 SLKKCVEDY---IERVE-KEAQKYQALKaQAEEKLRQASEEIAQVRSKAQtdalALQAVLRKEQMRVHSL-EKVVEQKTK 784
Cdd:TIGR02169  291 RVKEKIGELeaeIASLErSIAEKERELE-DAEERLAKLEAEIDKLLAEIE----ELEREIEEERKRRDKLtEEYAELKEE 365


                   ....*...
gi 528953954   785 ENDELTRI 792
Cdd:TIGR02169  366 LEDLRAEL 373
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
135-340 7.02e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 43.30  E-value: 7.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 135 PVSEDQPPGGPPS-APLVSLGPSSSSQIPESVENPEASRGPAPGSPECAREEHVHPWPSEESMPlGPMAPEQPSGVVSQD 213
Cdd:PRK07003 391 VGASAVPAVTAVTgAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKAN-ARASADSRCDERDAQ 469

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 214 TAEDPLSGTGGDSEGVPGPPARPASPCGAPPGEKPLVDLPGAAPVgsmdATSREDtALTGPGEAAGATHPGAQGEetcgq 293
Cdd:PRK07003 470 PPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPA----AASRED-APAAAAPPAPEARPPTPAA----- 539

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 528953954 294 AASSLRSGPVRLEFDFSDATGKRSPPLRKRGKALGLKPPSRRPEARP 340
Cdd:PRK07003 540 AAPAARAGGAAAALDVLRNAGMRVSSDRGARAAAAAKPAAAPAAAPK 586
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
595-802 9.71e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 9.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 595 PGAPLLPVGPIVDVLQY---SQKDLDSAVEATQKENEVLRGKCAALQERLLEMG---KIMDSFEGTVYQVMEE-----SQ 663
Cdd:COG4717  276 AGVLFLVLGLLALLFLLlarEKASLGKEAEELQALPALEELEEEELEELLAALGlppDLSPEELLELLDRIEElqellRE 355

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 664 KQKELTKAEMQKVLKEKAQLTADLH-SMEKSFSDLFKRFEKQKENEESLKKcVEDYI----------------ERVEKEA 726
Cdd:COG4717  356 AEELEEELQLEELEQEIAALLAEAGvEDEEELRAALEQAEEYQELKEELEE-LEEQLeellgeleellealdeEELEEEL 434

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528953954 727 QKYQALKAQAEEKLRQASEEIAQVrsKAQTDALALQAVLRKEQMRVHSLEKVVEQKTKENDELtRICDDLISKMKR 802
Cdd:COG4717  435 EELEEELEELEEELEELREELAEL--EAELEQLEEDGELAELLQELEELKAELRELAEEWAAL-KLALELLEEARE 507
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 657-800 1.08e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 40.16  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 657 QVMEESQK--QKELTKAEmqkvlKEKAQLTADLHSMEksfsdlfkrfEKQKENEESLKKCVEDYIERVEKEAQKYQA-LK 733
Cdd:COG0711   27 KALDERQEkiADGLAEAE-----RAKEEAEAALAEYE----------EKLAEARAEAAEIIAEARKEAEAIAEEAKAeAE 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528953954 734 AQAEEKLRQASEEIAQVRSKAQTD------ALALQAVlrkeqmrvhslEKVVEQKTKENDElTRICDDLISKM 800
Cdd:COG0711   92 AEAERIIAQAEAEIEQERAKALAElraevaDLAVAIA-----------EKILGKELDAAAQ-AALVDRFIAEL 152
FCH_F-BAR cd07610
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a ...
 617-789 1.14e-03

The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a dimerization module that binds and bends membranes; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. F-BAR domain containing proteins, also known as Pombe Cdc15 homology (PCH) family proteins, include Fes and Fer tyrosine kinases, PACSINs/Syndapins, FCHO, PSTPIP, CIP4-like proteins and srGAPs. Many members also contain an SH3 domain and play roles in endocytosis. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. These tubules have diameters larger than those observed with N-BARs. The F-BAR domains of some members such as NOSTRIN and Rgd1 are important for the subcellular localization of the protein.


Pssm-ID: 153294 [Multi-domain]  Cd Length: 191  Bit Score: 40.79  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 617 DSAVEATQKENEVLRGkcaaLQERLLEMGKIMDSFEGTVYQVMEESQKQKELTKAEMQKVLKEKAQLT---ADLH----- 688
Cdd:cd07610    3 ELLEKRTELGLDLLKD----LREFLKKRAAIEEEYAKNLQKLAKKFSKKPESGKTSLGTSWNSLREETesaATVHeelse 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 689 SMEKSFSDLFKRFEKQKEneESLKKCVEDyIERVEKEAQK-YQALKAQAEEKLRQASEEIAQVRSKA-QTDALALQAVLR 766
Cdd:cd07610   79 KLSQLIREPLEKVKEDKE--QARKKELAE-GEKLKKKLQElWAKLAKKADEEYREQVEKLNPAQSEYeEEKLNKIQAEQE 155

                        170       180
                 ....*....|....*....|...
gi 528953954 767 KEQMRVHSLEKVVEQKTKENDEL 789
Cdd:cd07610  156 REEERLEILKDNLKNYINAIKEI 178
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 605-796 1.38e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 42.26  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954   605 IVDVLQYSQKDLDSAVEATQKENEVLRGKCAALQERLlemgKIMDSFEGTVYQvmeeSQKQKELTKAEMQKVLKEKAQLT 684
Cdd:TIGR00618  404 ILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYA----ELCAAAITCTAQ----CEKLEKIHLQESAQSLKEREQQL 475

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954   685 ADLHSMEKSFSDL----FKRFEKQKENEESLKK-CVEDYIERVEK-EAQKYQALKAQAEEKLRQASEEIAQVRskAQTDA 758
Cdd:TIGR00618  476 QTKEQIHLQETRKkavvLARLLELQEEPCPLCGsCIHPNPARQDIdNPGPLTRRMQRGEQTYAQLETSEEDVY--HQLTS 553

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 528953954   759 LALQAVLRKEQMR--VHSLEKVVEQKTK---ENDELTRICDDL 796
Cdd:TIGR00618  554 ERKQRASLKEQMQeiQQSFSILTQCDNRskeDIPNLQNITVRL 596
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
612-748 1.44e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 612 SQKDLDSAVEATQKENEVLRGKCAALQERLLEMGKImdsfegtvYQVMEESQKQKELTKAEmqkvlKEKAQLTADLHSME 691
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKK--------YSEEEYEELREEYLELS-----RELAGLRAELEELE 686

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528953954 692 KSFSDLFKRFEKQKENEESLKKC------VEDYIERVEKEAQKYQALKAQAEEKLRQASEEIA 748
Cdd:PRK03918 687 KRREEIKKTLEKLKEELEEREKAkkelekLEKALERVEELREKVKKYKALLKERALSKVGEIA 749
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
659-802 1.57e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.43  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 659 MEESQKQKELTKAEMQKVLKEKAQLTADLHSMEKsfsdLFKRFEKQKENE---ESLKKCVEDYIERVEKEAQKYQALKAQ 735
Cdd:COG1340  121 LEWRQQTEVLSPEEEKELVEKIKELEKELEKAKK----ALEKNEKLKELRaelKELRKEAEEIHKKIKELAEEAQELHEE 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 736 ------AEEKLRQASEEIAQ--VRSKAQTDAL-----ALQAVLRK--EQMRVHSLEKVVEQKTKENDELTRICDDLISKM 800
Cdd:COG1340  197 mielykEADELRKEADELHKeiVEAQEKADELheeiiELQKELRElrKELKKLRKKQRALKREKEKEELEEKAEEIFEKL 276


                 ..
gi 528953954 801 KR 802
Cdd:COG1340  277 KK 278
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
609-776 2.10e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 609 LQYSQKDLDSAVEATQKENEVLRGKCAALqERLLEMGKIMDSFEGTVYQVMEESQKQKELTK--AEMQKVLKEKAQLTAD 686
Cdd:COG4717   93 LQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAELPERLEELEErlEELRELEEELEELEAE 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 687 LHSMEKSFSDLFKRFEKQKENEeslkkcVEDYIERVEKEAQKyqalKAQAEEKLRQASEEIAQVRskAQTDALALQAVLR 766
Cdd:COG4717  172 LAELQEELEELLEQLSLATEEE------LQDLAEELEELQQR----LAELEEELEEAQEELEELE--EELEQLENELEAA 239

                        170
                 ....*....|
gi 528953954 767 KEQMRVHSLE 776
Cdd:COG4717  240 ALEERLKEAR 249
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 617-789 2.17e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 617 DSAVEATQKENEVLRGKCAALQERLLEMGKIMDSfegtVYQVMEESQKQKELTKAEMQKVLKEKAQLTADLHSMEKSFSD 696
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEE----LNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 697 LFKRFEKQKENEESLK-----KCVEDYIERVE----------KEAQKYQALKAQAEEK---LRQASEEIAQVRSKAQTDA 758
Cdd:COG3883   91 RARALYRSGGSVSYLDvllgsESFSDFLDRLSalskiadadaDLLEELKADKAELEAKkaeLEAKLAELEALKAELEAAK 170

                        170       180       190
                 ....*....|....*....|....*....|.
gi 528953954 759 LALQAVLRKEQMRVHSLEKVVEQKTKENDEL 789
Cdd:COG3883  171 AELEAQQAEQEALLAQLSAEEAAAEAQLAEL 201
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 607-803 2.36e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.57  E-value: 2.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954   607 DVLQYSQKDLDSAVEATQKENEVLRGKCAALQERLLEMGKIMDSFEG-----TVYQVMEESQKQkeltkaeMQKVLKEKA 681
Cdd:TIGR00606  737 SIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESakvclTDVTIMERFQME-------LKDVERKIA 809

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954   682 QLTADLHSMEKSFSDLFKRFEKQKENE---------ESLKKCVEDYIERVE-----------------KEAQKYQALKAQ 735
Cdd:TIGR00606  810 QQAAKLQGSDLDRTVQQVNQEKQEKQHeldtvvskiELNRKLIQDQQEQIQhlksktnelkseklqigTNLQRRQQFEEQ 889

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528953954   736 AEEKLRQASE---EIAQVRSKAQTDALALQAVLRKEQMRVHSLEkvvEQKTKENDELTRI---CDDLISKMKRI 803
Cdd:TIGR00606  890 LVELSTEVQSlirEIKDAKEQDSPLETFLEKDQQEKEELISSKE---TSNKKAQDKVNDIkekVKNIHGYMKDI 960
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
628-802 2.44e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  628 EVLRGKCAALQERLLEMGKIMDSFEgtvyQVMEESQKQKEL---------TKAEMQKVLKEKAQLTADLHSMEKSFSDLf 698
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALE----AELDALQERREAlqrlaeyswDEIDVASAEREIAELEAELERLDASSDDL- 687

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  699 krfekqKENEESLKKCVEDyIERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSKAQ--------TDALALQAVLRKEQM 770
Cdd:COG4913   688 ------AALEEQLEELEAE-LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEaaedlarlELRALLEERFAAALG 760

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 528953954  771 RVHS---LEKVVEQKTKENDELTRICDDLISKMKR 802
Cdd:COG4913   761 DAVErelRENLEERIDALRARLNRAEEELERAMRA 795
DivIVA pfam05103
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ...
 611-737 2.50e-03

DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum during cell division, resulting in the formation of small, circular, anucleate mini-cells. Inactivation of divIVA produces a mini-cell phenotype, whereas overproduction of DivIVA results in a filamentation phenotype. These proteins appear to contain coiled-coils.


Pssm-ID: 428304 [Multi-domain]  Cd Length: 131  Bit Score: 38.70  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  611 YSQKDLDS-------AVEATQKENEVLRGKCAALQERLLEmgkimdsfegtvYQVMEESQKQKELTKAEMQKVLKEKAQL 683
Cdd:pfam05103  18 YDPDEVDEfldqvaeDYEALIRENAELKEKIEELEEKLAH------------YKNLEETLQNTLILAQETAEEVKANAQK 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 528953954  684 TADLhsmeksfsdlfkrfeKQKENEESLKKCVEDYIERVEKEAQKYQALKAQAE 737
Cdd:pfam05103  86 EAEL---------------IIKEAEAKAERIVDDANNEVKKINDEIEELKRQRR 124
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 662-770 2.64e-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: 2.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 662 SQKQKELTKAEMQKVLKEKAQLTADLHSMEKsfsdlfkrfeKQKENEESLKKcVEDYIERVEKEAQKYQALKAQAEEKLR 741
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAALKK----------EEKALLKQLAA-LERRIAALARRIRALEQELAALEAELA 86

                         90       100
                 ....*....|....*....|....*....
gi 528953954 742 QASEEIAQVRSKAQTDALALQAVLRKEQM 770
Cdd:COG4942   87 ELEKEIAELRAELEAQKEELAELLRALYR 115
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 154-427 3.45e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 41.06  E-value: 3.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  154 GPSSSSQIPESVENPEASRGPAPGSPECAREEHVHPWPSEESMPLGPMAPE-QPSGVVSQDTAEDPLSGTggdsEGVPGP 232
Cdd:pfam05109 441 APNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSpSPRDNGTESKAPDMTSPT----SAVTTP 516

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  233 PARPASPCGAPPGEKPLVDLPGAAPVGSMDATSREDTALTGPGEAAGATHPGAQGEETCGQAASSLRSGPVrlEFDFSDA 312
Cdd:pfam05109 517 TPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPT--PNATSPT 594

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  313 TGKRSPPLRKRGKALG--------LKPPSRRPEA-RPGKATLEAGKGCELTLRGSDGPSWDKPDDPDcnpaaDSGEARPL 383
Cdd:pfam05109 595 VGETSPQANTTNHTLGgtsstpvvTSPPKNATSAvTTGQHNITSSSTSSMSLRPSSISETLSPSTSD-----NSTSHMPL 669

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528953954  384 ---EHPQSG----QATEAlSLSRQACSDDTPGTRaPARTPGAAGEGWTTGS 427
Cdd:pfam05109 670 ltsAHPTGGenitQVTPA-STSTHHVSTSSPAPR-PGTTSQASGPGNSSTS 718
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 121-280 3.54e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.12  E-value: 3.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 121 PVPVNTEPPSEDMRPVSEDQPPGGPPSAPLVSLGPSSSSQIPESVENP--EASRGPAPGSPECAREEHVHPWPSEESMPL 198
Cdd:PRK07764 646 GVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPagAAPAQPAPAPAATPPAGQADDPAAQPPQAA 725

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 199 GPMAPEQPSGVVSQDTAEDPLSGTGGDSEGVPGPPARPASPCGAPPGEKPLVDLPGAAPVGSMDATSREDTALTGPGEAA 278
Cdd:PRK07764 726 QGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAEEVA 805


                 ..
gi 528953954 279 GA 280
Cdd:PRK07764 806 ME 807
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
652-803 3.61e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 3.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 652 EGTVYQVMEESQKQKELTKAEMQKVLKEKAQLTADLHSMEKsfsdLFKRFEKQKENEESLKKcvedYIERVEKEAQKYQA 731
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEK----EVKELEELKEEIEELEK----ELESLEGSKRKLEE 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 732 LKAQAEEKLRQASEEIAQVRSKAQ---------TDALALQAVLRKEQMRVHSLEKVVEQKTKENDELTRICDDLISKMKR 802
Cdd:PRK03918 260 KIRELEERIEELKKEIEELEEKVKelkelkekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER 339


                 .
gi 528953954 803 I 803
Cdd:PRK03918 340 L 340
Filament pfam00038
Intermediate filament protein;
620-796 4.11e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 40.29  E-value: 4.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  620 VEATQKENEVLRGKCAALQERL-LEMGKIMDSFEGTVyqvmEESQKQKELTKAEmqkvlkeKAQLTADLHSMEKSFSDLF 698
Cdd:pfam00038  20 VRFLEQQNKLLETKISELRQKKgAEPSRLYSLYEKEI----EDLRRQLDTLTVE-------RARLQLELDNLRLAAEDFR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  699 KRFEKqkenEESLKKCVEDYIERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSKAQTDALALQAVLRKEQMrvhslekV 778
Cdd:pfam00038  89 QKYED----ELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQV-------N 157

                         170
                  ....*....|....*...
gi 528953954  779 VEQKTKENDELTRICDDL 796
Cdd:pfam00038 158 VEMDAARKLDLTSALAEI 175
PHA01794 PHA01794
hypothetical protein
 646-754 4.69e-03

hypothetical protein


Pssm-ID: 222837 [Multi-domain]  Cd Length: 134  Bit Score: 38.01  E-value: 4.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 646 KIMDSFEGTVYQVMEESQKQKeLTKaemQKVLKEKAQLTADLHSMEKSFSDLFKRFEKQKENEESLKKCVEDYIERVEKE 725
Cdd:PHA01794  29 NILERDESAIVDLVRLSAKKA-LTE---DEILDAIADFVETFEDEEGTTEGLFAELEKEMVDSGFFRAKIKKYIENMEKS 104

                         90       100
                 ....*....|....*....|....*....
gi 528953954 726 AqKYQALKAQAEEKLRQASEEIAQVRSKA 754
Cdd:PHA01794 105 A-RYLKAKDDTEATQAKAIKDLIGRMKKA 132
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 615-763 4.70e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.52  E-value: 4.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 615 DLDSAVEATQKENEVLRGKCAALQERLLEMGKIMDSFEGTVyQVMEESQKQKELTKAEMQKVLKE-KAQLTA-----DLH 688
Cdd:COG1579   14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTEL-EDLEKEIKRLELEIEEVEARIKKyEEQLGNvrnnkEYE 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528953954 689 SMEKSFSDLFKRfekQKENEESLKKcVEDYIERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSKAQTDALALQA 763
Cdd:COG1579   93 ALQKEIESLKRR---ISDLEDEILE-LMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
PHA03169 PHA03169
hypothetical protein; Provisional
 137-290 5.41e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 39.95  E-value: 5.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 137 SEDQPPGGPPSAPLVSLGPSSSSQIPESVENPEASRGPAPGSPecAREEHVHPWPSEESMPLGPMAPEQPSGVVSQDTAE 216
Cdd:PHA03169  99 SVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPP--SHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPE 176

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528953954 217 DPLSGTGGDSEGVPGPPARPASPCGAPPGEKPLVDLPGAAPVGSMDATSREDTALTGPGEAAGATHPGAQGEET 290
Cdd:PHA03169 177 EPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPGH 250
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 621-791 6.11e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 40.34  E-value: 6.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954   621 EATQKENEVLRGKCAALQERLLEMGKIMDSFEGTVYQVMEESQKQKELTKAEMQKVLKEKAQLTADLHSMEKSFSDLFKR 700
Cdd:pfam02463  180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQE 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954   701 FEKQKE------NEESLKKCVEDYIERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSKAQTDALALQAVLRKEQmrvhs 774
Cdd:pfam02463  260 IEKEEEklaqvlKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEK----- 334

                          170
                   ....*....|....*..
gi 528953954   775 leKVVEQKTKENDELTR 791
Cdd:pfam02463  335 --EEIEELEKELKELEI 349
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 122-273 6.50e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 39.91  E-value: 6.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 122 VPVNTEPPSED---MRPVS-----ED-QPPGGP-PSAPlvSLGPSSSSQIPESVENPEASRGPAPGSPECAREEHVHPWP 191
Cdd:PLN03209 354 PPIEEEPPQPKavvPRPLSpytayEDlKPPTSPiPTPP--SSSPASSKSVDAVAKPAEPDVVPSPGSASNVPEVEPAQVE 431

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 192 SEESMPLGPMA------------PEQPSGVVSQDTAEDPLSGTG--------GDSEGVPGPPARPASPCGAPPGEKPLVD 251
Cdd:PLN03209 432 AKKTRPLSPYAryedlkpptspsPTAPTGVSPSVSSTSSVPAVPdtapataaTDAAAPPPANMRPLSPYAVYDDLKPPTS 511

                        170       180
                 ....*....|....*....|..
gi 528953954 252 LPGAAPVGSMDATSREDTALTG 273
Cdd:PLN03209 512 PSPAAPVGKVAPSSTNEVVKVG 533
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 657-780 7.05e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 37.42  E-value: 7.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 657 QVMEESQK--QKELTKAEMqkvLKEKAQltadlhsmeksfsdlfkrfEKQKENEESL---KKCVEDYIERVEKEAQK-YQ 730
Cdd:cd06503   26 KALDEREEkiAESLEEAEK---AKEEAE-------------------ELLAEYEEKLaeaRAEAQEIIEEARKEAEKiKE 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 731 ALKAQAEEK----LRQASEEIAQVRSKA------QTDALALQAVlrkeqmrvhslEKVVE 780
Cdd:cd06503   84 EILAEAKEEaeriLEQAKAEIEQEKEKAlaelrkEVADLAVEAA-----------EKILG 132
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 703-786 7.35e-03

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: 37.21  E-value: 7.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  703 KQKENEESLKKcVEDYIERVEKEAQKYQALKAQAEEKLRQASEEiAQVRSKAQTDALALQAVLRKEQMRvhslekvvEQK 782
Cdd:pfam20492   7 EKQELEERLKQ-YEEETKKAQEELEESEETAEELEEERRQAEEE-AERLEQKRQEAEEEKERLEESAEM--------EAE 76


                  ....
gi 528953954  783 TKEN 786
Cdd:pfam20492  77 EKEQ 80
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 609-757 7.70e-03

The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively.


Pssm-ID: 153271 [Multi-domain]  Cd Length: 194  Bit Score: 38.58  E-value: 7.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 609 LQYSQKDLDSAVEATQKENEVLRGKCAA---LQERLLEMGKIMDSFEGTVYQVMEESQK--QKELTKAEMQKVLKEKAQL 683
Cdd:cd07307    2 LDELEKLLKKLIKDTKKLLDSLKELPAAaekLSEALQELGKELPDLSNTDLGEALEKFGkiQKELEEFRDQLEQKLENKV 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528953954 684 TADLHSMEKSFsdlFKRFEKQKENEESLKKCVEDYIERVEKEAQKYQALK--AQAEEKLRQASEEIAQVRSKAQTD 757
Cdd:cd07307   82 IEPLKEYLKKD---LKEIKKRRKKLDKARLDYDAAREKLKKLRKKKKDSSklAEAEEELQEAKEKYEELREELIED 154
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 680-785 8.28e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.81  E-value: 8.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 680 KAQLTAD---LHSMEKSFSDLFKRFEKQKENEESLKKCVEDYIERVEKEAQKYQA----LKAQAEEK----LRQASEEIA 748
Cdd:PRK00409 508 KKLIGEDkekLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEeedkLLEEAEKEaqqaIKEAKKEAD 587

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 528953954 749 QV-RSKAQTDALALQAVLRKEQMRVH-----SLEKVVEQKTKE 785
Cdd:PRK00409 588 EIiKELRQLQKGGYASVKAHELIEARkrlnkANEKKEKKKKKQ 630
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 656-789 8.46e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 39.81  E-value: 8.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  656 YQVMEESQKQKELTKAEMQKVLKEKAQLTADLHS------------------MEKSFSDLFKRFEKQKENEESLKKCVED 717
Cdd:pfam10174  62 YRVTQEENQHLQLTIQALQDELRAQRDLNQLLQQdfttspvdgedkfstpelTEENFRRLQSEHERQAKELFLLRKTLEE 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528953954  718 YIERVEkeAQKyQALKAQaEEKLRQASEeiaQVRSKAQTDALALQAVLRKEQ-----MRVHSLEKVVEQKTKENDEL 789
Cdd:pfam10174 142 MELRIE--TQK-QTLGAR-DESIKKLLE---MLQSKGLPKKSGEEDWERTRRiaeaeMQLGHLEVLLDQKEKENIHL 211
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 606-799 8.56e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.67  E-value: 8.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954   606 VDVLQYSQKDLDSAVEATQKENEVLRGKCAALQERLLEMG--------KIMDSFEGTVYQV----------MEESQKQKE 667
Cdd:TIGR02169  246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGeeeqlrvkEKIGELEAEIASLersiaekereLEDAEERLA 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954   668 LTKAEMQKVLKEKAQLtadlhsmEKSFSDLFKRFEKQKENEESLKKCVEDYIERVEKEAQKYQALK---AQAEEKLRQAS 744
Cdd:TIGR02169  326 KLEAEIDKLLAEIEEL-------EREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRdelKDYREKLEKLK 398

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 528953954   745 EEIAQVrskaQTDALALQAVLRKEQMRVHSLE---KVVEQKTKENDELTRICDDLISK 799
Cdd:TIGR02169  399 REINEL----KRELDRLQEELQRLSEELADLNaaiAGIEAKINELEEEKEDKALEIKK 452
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 656-781 8.93e-03

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


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 36.78  E-value: 8.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  656 YQVMEESQKQKEltkaemqkvlkekaqltADLHSMEKSFSDLFKRFEK-QKENEESLKKCvedyiervEKEAQKYQALKA 734
Cdd:pfam13863  22 IERLEELLKQRE-----------------EELEKKEQELKEDLIKFDKfLKENDAKRRRA--------LKKAEEETKLKK 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 528953954  735 QAEEKLRQASEEIAQVRSKAQtdalALQAVLrkEQMRVHS--LEKVVEQ 781
Cdd:pfam13863  77 EKEKEIKKLTAQIEELKSEIS----KLEEKL--EEYKPYEdfLEKVVPK 119
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 621-785 8.96e-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: 39.13  E-value: 8.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  621 EATQKENEVLRGKCAALQERLLEMGKIMDSfegtvyQVMEESQ-KQKELTKAEMQKVLKEKAQLTADL--HSMEKSfsdL 697
Cdd:pfam13868 180 EEKEREIARLRAQQEKAQDEKAERDELRAK------LYQEEQErKERQKEREEAEKKARQRQELQQAReeQIELKE---R 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954  698 FKRFEKQKENEESL----KKCVEDYIERVEKEAQK------YQALKAQAEEKLRQASEEIAQVRSKAQtdalALQAVLRK 767
Cdd:pfam13868 251 RLAEEAEREEEEFErmlrKQAEDEEIEQEEAEKRRmkrlehRRELEKQIEEREEQRAAEREEELEEGE----RLREEEAE 326

                         170
                  ....*....|....*...
gi 528953954  768 EQMRvhsLEKVVEQKTKE 785
Cdd:pfam13868 327 RRER---IEEERQKKLKE 341
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
610-792 9.45e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.61  E-value: 9.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 610 QYSQKDLDSAVEATQKENEVLRGKCAALQERLLEMGKIMDSF------------EGTVYQVMEESQKQKELTKAEMQKVL 677
Cdd:COG3206  160 AYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFrqknglvdlseeAKLLLQQLSELESQLAEARAELAEAE 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528953954 678 KEKAQLTADLHSMEKSFSDLFK--RFEKQKENEESLKKCVEDYIERVEKEAQKYQALKAQAEEKLRQASEEIAQVRSKAQ 755
Cdd:COG3206  240 ARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLE 319

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 528953954 756 TDALALQAvlrkeqmRVHSLEKVVEQKTKENDELTRI 792
Cdd:COG3206  320 AELEALQA-------REASLQAQLAQLEARLAELPEL 349
 
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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