NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767969882|ref|XP_011541016|]
View 

pleckstrin homology-like domain family B member 1 isoform X42 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
FHA_PHLB1 cd22713
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 ...
70-188 2.03e-77

forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 (PHLDB1) and similar proteins; PHLDB1, also called protein LL5-alpha (LL5A), acts as an insulin-responsive protein that enhances Akt activation. PHLDB1 contains a pleckstrin homology domain, which binds phosphatidylinositol PI(3,4)P(2), PI(3,5)P(2), and PI(3,4,5)P(3), as well as a Forkhead-associated (FHA) domain and coiled coil regions. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


:

Pssm-ID: 438765  Cd Length: 120  Bit Score: 246.08  E-value: 2.03e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  70 LDLIETGKGLKVQTDKPHLVSLGSGRLSTAITLLPLEEGRTVIGSAARD-ISLQGPGLAPEHCYIENLRGTLTLYPCGNA 148
Cdd:cd22713    1 LELTETGKALKVQTEKPHLVSLGSGRLSTAVTLLPLPEGKTTIGTAASDiISLQGPGVEPEHCYIENINGTVTLYPCGNL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767969882 149 CTIDGLPVRQPTRLTQGCMLCLGQSTFLRFNHPAEAKWMK 188
Cdd:cd22713   81 CSVDGLPITEPTRLTQGCMICLGRSNYFRFNHPAEAKRMK 120
PspA_IM30 super family cl37531
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
741-839 4.23e-08

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.


The actual alignment was detected with superfamily member pfam04012:

Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 54.69  E-value: 4.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  741 ESTQQEHEDApSTKLQGEVLALEEERAQVLGHVEQLKVRVKE-LEQQLQESAREAEMERALLQGEREAERALLQKEQKAV 819
Cdd:pfam04012  35 QSELVKARQA-LAQTIARQKQLERRLEQQTEQAKKLEEKAQAaLTKGNEELAREALAEKKSLEKQAEALETQLAQQRSAV 113
                          90       100
                  ....*....|....*....|
gi 767969882  820 DQLQEKLVALETGIQKERDK 839
Cdd:pfam04012 114 EQLRKQLAALETKIQQLKAK 133
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
198-592 2.78e-07

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 54.41  E-value: 2.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  198 PGPPYSPVPAESESLVNGNHTPQTATRGPSACashsslvssiEKDLQEIMDSLVLEEPGAAGKKPAATSPLSPMANGGRy 277
Cdd:PHA03307   47 SAELAAVTVVAGAAACDRFEPPTGPPPGPGTE----------APANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPD- 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  278 llSPPTSPGAMSVGSSYENTSPAFSPLSSPASSGSCASHSPSGQEPGPSVPPLVPARSSSYHLALQPPQSRPSGARSESP 357
Cdd:PHA03307  116 --PPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEP 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  358 RLSRKGGHERPPSPGLR-------GLLTDSPAATVLAEARRATESPRLGGQLPVVAISLSEYP----ASGALSQPTSIPG 426
Cdd:PHA03307  194 PPSTPPAAASPRPPRRSspisasaSSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPlprpAPITLPTRIWEAS 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  427 SPKFQPPVPAPRNKIGTLQDRPPSPFREPPGSERVLTTSPSRQLVGRTFSDGL-ATRTLQPPESPRLGRRGLDSMRELPP 505
Cdd:PHA03307  274 GWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSsSTSSSSESSRGAAVSPGPSPSRSPSP 353
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  506 LSPSLSRRAlSPLPTRTTPDPKLNREVAESPRPRRWAAhGASPEDFSLTLGARGRRTRSPSPTLGESLAPHKGSFSGRLS 585
Cdd:PHA03307  354 SRPPPPADP-SSPRKRPRPSRAPSSPAASAGRPTRRRA-RAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYARYP 431

                  ....*..
gi 767969882  586 PAYSLGS 592
Cdd:PHA03307  432 LLTPSGE 438
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
625-838 7.18e-06

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


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.91  E-value: 7.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  625 ITEISDNEDDLLEYHRRqrqerlreqeMERLERQR--LETILNLCAEYSRADGgpEAGELPSIGEATAALALAGRRpsRG 702
Cdd:COG4913   227 ADALVEHFDDLERAHEA----------LEDAREQIelLEPIRELAERYAAARE--RLAELEYLRAALRLWFAQRRL--EL 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  703 LAGASGRSSEEPGVATQRLWESmeRSDEENLKEECSSTESTQQEHEDAPSTKLQGEVLALEEERAQVLGHVEQLKVRVKE 782
Cdd:COG4913   293 LEAELEELRAELARLEAELERL--EARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAA 370
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767969882  783 LEQQLQESAREAEMERALLQGEREAERALLQKEQKAVDQLQEKLVALE---TGIQKERD 838
Cdd:COG4913   371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRrelRELEAEIA 429
 
Name Accession Description Interval E-value
FHA_PHLB1 cd22713
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 ...
70-188 2.03e-77

forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 (PHLDB1) and similar proteins; PHLDB1, also called protein LL5-alpha (LL5A), acts as an insulin-responsive protein that enhances Akt activation. PHLDB1 contains a pleckstrin homology domain, which binds phosphatidylinositol PI(3,4)P(2), PI(3,5)P(2), and PI(3,4,5)P(3), as well as a Forkhead-associated (FHA) domain and coiled coil regions. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438765  Cd Length: 120  Bit Score: 246.08  E-value: 2.03e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  70 LDLIETGKGLKVQTDKPHLVSLGSGRLSTAITLLPLEEGRTVIGSAARD-ISLQGPGLAPEHCYIENLRGTLTLYPCGNA 148
Cdd:cd22713    1 LELTETGKALKVQTEKPHLVSLGSGRLSTAVTLLPLPEGKTTIGTAASDiISLQGPGVEPEHCYIENINGTVTLYPCGNL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767969882 149 CTIDGLPVRQPTRLTQGCMLCLGQSTFLRFNHPAEAKWMK 188
Cdd:cd22713   81 CSVDGLPITEPTRLTQGCMICLGRSNYFRFNHPAEAKRMK 120
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
741-839 4.23e-08

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: 54.69  E-value: 4.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  741 ESTQQEHEDApSTKLQGEVLALEEERAQVLGHVEQLKVRVKE-LEQQLQESAREAEMERALLQGEREAERALLQKEQKAV 819
Cdd:pfam04012  35 QSELVKARQA-LAQTIARQKQLERRLEQQTEQAKKLEEKAQAaLTKGNEELAREALAEKKSLEKQAEALETQLAQQRSAV 113
                          90       100
                  ....*....|....*....|
gi 767969882  820 DQLQEKLVALETGIQKERDK 839
Cdd:pfam04012 114 EQLRKQLAALETKIQQLKAK 133
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
198-592 2.78e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 54.41  E-value: 2.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  198 PGPPYSPVPAESESLVNGNHTPQTATRGPSACashsslvssiEKDLQEIMDSLVLEEPGAAGKKPAATSPLSPMANGGRy 277
Cdd:PHA03307   47 SAELAAVTVVAGAAACDRFEPPTGPPPGPGTE----------APANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPD- 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  278 llSPPTSPGAMSVGSSYENTSPAFSPLSSPASSGSCASHSPSGQEPGPSVPPLVPARSSSYHLALQPPQSRPSGARSESP 357
Cdd:PHA03307  116 --PPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEP 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  358 RLSRKGGHERPPSPGLR-------GLLTDSPAATVLAEARRATESPRLGGQLPVVAISLSEYP----ASGALSQPTSIPG 426
Cdd:PHA03307  194 PPSTPPAAASPRPPRRSspisasaSSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPlprpAPITLPTRIWEAS 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  427 SPKFQPPVPAPRNKIGTLQDRPPSPFREPPGSERVLTTSPSRQLVGRTFSDGL-ATRTLQPPESPRLGRRGLDSMRELPP 505
Cdd:PHA03307  274 GWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSsSTSSSSESSRGAAVSPGPSPSRSPSP 353
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  506 LSPSLSRRAlSPLPTRTTPDPKLNREVAESPRPRRWAAhGASPEDFSLTLGARGRRTRSPSPTLGESLAPHKGSFSGRLS 585
Cdd:PHA03307  354 SRPPPPADP-SSPRKRPRPSRAPSSPAASAGRPTRRRA-RAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYARYP 431

                  ....*..
gi 767969882  586 PAYSLGS 592
Cdd:PHA03307  432 LLTPSGE 438
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
103-176 9.44e-07

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 47.65  E-value: 9.44e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767969882 103 LPLEEGRTVIGSAAR-DISLQGPGLAPEHCYIENLRGTLTLYPCG--NACTIDGLPVRQPTRLTQGCMLCLGQSTFL 176
Cdd:COG1716   16 FPLDGGPLTIGRAPDnDIVLDDPTVSRRHARIRRDGGGWVLEDLGstNGTFVNGQRVTEPAPLRDGDVIRLGKTELR 92
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
280-619 6.55e-06

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: 49.91  E-value: 6.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  280 SPPTSPGAMSVGSSYENTSPAF-------SPLSSPASSG------SCASHSPSGQEPGPSvpPLVPArsssyhlalqpPQ 346
Cdd:pfam05109 427 STTTSPTLNTTGFAAPNTTTGLpssthvpTNLTAPASTGptvstaDVTSPTPAGTTSGAS--PVTPS-----------PS 493
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  347 SRPSGARSESPRLSRKGGHERPPSPGlrgllTDSPAATVLAEARRATeSPRLGGQLPvvaislseypaSGALSQPTSIPG 426
Cdd:pfam05109 494 PRDNGTESKAPDMTSPTSAVTTPTPN-----ATSPTPAVTTPTPNAT-SPTLGKTSP-----------TSAVTTPTPNAT 556
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  427 SPKFQPPVPAPRNKIGTLQDRPPSPFREPP----GSERVLTTSPSRQLVGRTFSDGLATRTL-QPPESP---------RL 492
Cdd:pfam05109 557 SPTPAVTTPTPNATIPTLGKTSPTSAVTTPtpnaTSPTVGETSPQANTTNHTLGGTSSTPVVtSPPKNAtsavttgqhNI 636
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  493 GRRGLDSMRELPP-----LSPSLSRRALSPLPTRTTPDPKLNREVAE--------------SPRPRRWAAHGAS------ 547
Cdd:pfam05109 637 TSSSTSSMSLRPSsisetLSPSTSDNSTSHMPLLTSAHPTGGENITQvtpaststhhvstsSPAPRPGTTSQASgpgnss 716
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767969882  548 ----PEDFSLTLGARGRRTRSPSPTLGESLAPHKGSFSGRLSPAYSLGSLTGASPCQSPCVQRKLSSGDLRVPVTR 619
Cdd:pfam05109 717 tstkPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPRTR 792
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
625-838 7.18e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.91  E-value: 7.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  625 ITEISDNEDDLLEYHRRqrqerlreqeMERLERQR--LETILNLCAEYSRADGgpEAGELPSIGEATAALALAGRRpsRG 702
Cdd:COG4913   227 ADALVEHFDDLERAHEA----------LEDAREQIelLEPIRELAERYAAARE--RLAELEYLRAALRLWFAQRRL--EL 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  703 LAGASGRSSEEPGVATQRLWESmeRSDEENLKEECSSTESTQQEHEDAPSTKLQGEVLALEEERAQVLGHVEQLKVRVKE 782
Cdd:COG4913   293 LEAELEELRAELARLEAELERL--EARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAA 370
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767969882  783 LEQQLQESAREAEMERALLQGEREAERALLQKEQKAVDQLQEKLVALE---TGIQKERD 838
Cdd:COG4913   371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRrelRELEAEIA 429
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
731-846 9.02e-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: 48.00  E-value: 9.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 731 ENLKEECSSTESTQQEHEDApSTKLQGEVLALEEERAQVLGHVEQLKVRVKELEQQLQE--SAREAE------------- 795
Cdd:COG1579   27 KELPAELAELEDELAALEAR-LEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrNNKEYEalqkeieslkrri 105
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767969882 796 ----------MER--------ALLQGEREAERALLQKEQKAVDQLQEKLVALETGIQKERD---KEVPKPLL 846
Cdd:COG1579  106 sdledeilelMERieeleeelAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREelaAKIPPELL 177
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
731-843 6.12e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 6.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 731 ENLKEECSSTESTQQ---EHEDAPSTKLQgEVLALEEERAQVLGHVEQLKVRVKELEqQLQESAREAEMERALLQGEREA 807
Cdd:PRK03918 179 ERLEKFIKRTENIEElikEKEKELEEVLR-EINEISSELPELREELEKLEKEVKELE-ELKEEIEELEKELESLEGSKRK 256
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767969882 808 ERALLQKEQKAVDQLQEKLVALEtgiqkERDKEVPK 843
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELE-----EKVKELKE 287
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
110-170 1.23e-04

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 40.64  E-value: 1.23e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767969882  110 TVIGSAAR-DISLQGPGLAPEHCYIENLRG-TLTLYPCG--NACTIDGLPVR-QPTRLTQGCMLCL 170
Cdd:pfam00498   1 VTIGRSPDcDIVLDDPSVSRRHAEIRYDGGgRFYLEDLGstNGTFVNGQRLGpEPVRLKDGDVIRL 66
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
718-848 3.29e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.57  E-value: 3.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882   718 TQRL--WESMERSDEENLKEECSST-----ESTQQEHEDAPSTKLQGEVLALEEEraqvlghvEQLKVRVKELEQQ-LQE 789
Cdd:TIGR00618  378 TQHIhtLQQQKTTLTQKLQSLCKELdilqrEQATIDTRTSAFRDLQGQLAHAKKQ--------QELQQRYAELCAAaITC 449
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882   790 SAREAEMERALLQGEREAERALLQKEQ-KAVDQLQEKLVALETGIQKERDKEVPKPLLGQ 848
Cdd:TIGR00618  450 TAQCEKLEKIHLQESAQSLKEREQQLQtKEQIHLQETRKKAVVLARLLELQEEPCPLCGS 509
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
605-826 9.03e-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: 43.12  E-value: 9.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882   605 QRKLSSGDLRVPVTRERKNSITEISDNEDDLLEYHRRQRQERLREQEMERLERQRLET-ILNLCAEYSRAdggpeAGELP 683
Cdd:TIGR02168  725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAeIEELEAQIEQL-----KEELK 799
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882   684 SIGEATAALALAGRRPSRGLAGASGR--SSEEPGVATQRLWESMERSDEENLKEECSSTEStqQEHEDAPSTKLQGEVLA 761
Cdd:TIGR02168  800 ALREALDELRAELTLLNEEAANLRERleSLERRIAATERRLEDLEEQIEELSEDIESLAAE--IEELEELIEELESELEA 877
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767969882   762 LEEERAQVLGHVEQLKVRVKELEQQLQES---AREAEMERALLQGEREAERALLQKEQKAVDQLQEKL 826
Cdd:TIGR02168  878 LLNERASLEEALALLRSELEELSEELRELeskRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
761-839 1.14e-03

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 41.90  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 761 ALEEERAQVLghveqlkvrVKELEQQLQEsaREAEMER--ALLQGEREAERALLQKEQKAVDQLQEKLVA-LETGIQKER 837
Cdd:cd03406  170 AMEAEKTKLL---------IAEQHQKVVE--KEAETERkrAVIEAEKDAEVAKIQMQQKIMEKEAEKKISeIEDEMHLAR 238

                 ..
gi 767969882 838 DK 839
Cdd:cd03406  239 EK 240
 
Name Accession Description Interval E-value
FHA_PHLB1 cd22713
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 ...
70-188 2.03e-77

forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 (PHLDB1) and similar proteins; PHLDB1, also called protein LL5-alpha (LL5A), acts as an insulin-responsive protein that enhances Akt activation. PHLDB1 contains a pleckstrin homology domain, which binds phosphatidylinositol PI(3,4)P(2), PI(3,5)P(2), and PI(3,4,5)P(3), as well as a Forkhead-associated (FHA) domain and coiled coil regions. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438765  Cd Length: 120  Bit Score: 246.08  E-value: 2.03e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  70 LDLIETGKGLKVQTDKPHLVSLGSGRLSTAITLLPLEEGRTVIGSAARD-ISLQGPGLAPEHCYIENLRGTLTLYPCGNA 148
Cdd:cd22713    1 LELTETGKALKVQTEKPHLVSLGSGRLSTAVTLLPLPEGKTTIGTAASDiISLQGPGVEPEHCYIENINGTVTLYPCGNL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767969882 149 CTIDGLPVRQPTRLTQGCMLCLGQSTFLRFNHPAEAKWMK 188
Cdd:cd22713   81 CSVDGLPITEPTRLTQGCMICLGRSNYFRFNHPAEAKRMK 120
FHA_KIF16 cd22708
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 ...
78-181 1.32e-30

forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 family includes StARD9/KIF16A and KIF16B. StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438760 [Multi-domain]  Cd Length: 109  Bit Score: 116.22  E-value: 1.32e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  78 GLKVQTDKPHLVSLGSGRLSTAITLLPLEEGRTVIGSA----ARDISLQGPGLAPEHCYIENLRGTLTLYPCGNA-CTID 152
Cdd:cd22708    1 GVVLDSELPHLIGIDDDLLSTGVVLYHLKEGKTRIGREdapqEQDIVLDGEDIEAEHCIIENVGGVVTLHPLPGAlCAVN 80
                         90       100
                 ....*....|....*....|....*....
gi 767969882 153 GLPVRQPTRLTQGCMLCLGQSTFLRFNHP 181
Cdd:cd22708   81 GQVITQPTRLTQGDVILLGKTNMFRFNHP 109
FHA_KIF16B cd22732
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ...
78-184 9.22e-26

forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438784 [Multi-domain]  Cd Length: 117  Bit Score: 102.70  E-value: 9.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  78 GLKVQTDKPHLVSLGSGRLSTAITLLPLEEGRTVIG----SAARDISLQGPGLAPEHCYIENLRGTLTLYPCGNA-CTID 152
Cdd:cd22732    1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGrddaTTEQDIVLHGLDLESEHCIFENLNGTVTLIPLNGAqCSVN 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 767969882 153 GLPVRQPTRLTQGCMLCLGQSTFLRFNHPAEA 184
Cdd:cd22732   81 GVQITEATQLNQGAVILLGRTNMFRFNHPKEA 112
FHA_KIF16A_STARD9 cd22731
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ...
78-184 6.21e-25

forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438783 [Multi-domain]  Cd Length: 119  Bit Score: 100.23  E-value: 6.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  78 GLKVQTDKPHLVSLGSGRLSTAITLLPLEEGRTVIGSAA----RDISLQGPGLAPEHCYIENLRGTLTLYPCGNA-CTID 152
Cdd:cd22731    1 GVTIDSNLPHLIAMDDDILSTGVVLYHLREGTTKIGRSDseqeQDIVLQGPWIERDHCMIHNECGVVTLRPAQGAqCTVN 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 767969882 153 GLPVRQPTRLTQGCMLCLGQSTFLRFNHPAEA 184
Cdd:cd22731   81 GREVTESCRLSQGAVIVLGKTHKFRFNHPAEA 112
FHA_KIF14 cd22707
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ...
79-181 3.15e-17

forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; KIF14 is a microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity. It plays a role in many processes like cell division, cytokinesis and in cell proliferation and apoptosis. KIF14 is a potential oncogene and is involved in the metastasis of various cancers. Mutations of KIF14 cause primary microcephaly by impairing cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438759 [Multi-domain]  Cd Length: 108  Bit Score: 78.08  E-value: 3.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  79 LKVQTDKPHLVSLGSGRLSTAITLLPLEEGRTVIG----SAARDISLQGPGLAPEHCYIENLRGTLTLYPCGNACT-IDG 153
Cdd:cd22707    1 FKVDNKLPNLVNLNEDPQLSEMLLYMLKEGQTRVGrskaSSSHDIQLSGALIADDHCTIENNGGKVTIIPVGDAETyVNG 80
                         90       100
                 ....*....|....*....|....*...
gi 767969882 154 LPVRQPTRLTQGCMLCLGQSTFLRFNHP 181
Cdd:cd22707   81 ELISEPTVLHHGDRVILGGDHYFRFNHP 108
FHA_KIF1 cd22705
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ...
86-180 2.41e-16

forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 family includes KIF1A, KIF1B, and KIF1C. KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438757 [Multi-domain]  Cd Length: 101  Bit Score: 75.35  E-value: 2.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  86 PHLVSLGSGRLSTAITLLPLEEGRTVIGSA----ARDISLQGPGLAPEHCYIENLRGTLTLYPCGNA-CTIDGLPVRQPT 160
Cdd:cd22705    2 PHLVNLNEDPLMSECLLYYIKPGITRVGRAdadvPQDIQLSGTHILEEHCTFENEDGVVTLEPCEGAlTYVNGKRVTEPT 81
                         90       100
                 ....*....|....*....|
gi 767969882 161 RLTQGCMLCLGQSTFLRFNH 180
Cdd:cd22705   82 RLKTGSRVILGKNHVFRFNH 101
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
87-175 6.34e-11

forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.


Pssm-ID: 438714 [Multi-domain]  Cd Length: 92  Bit Score: 59.60  E-value: 6.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  87 HLVSLGSGRLSTAItllPLEEGRTVIGSAAR-DISLQGPGLAPEHCYIENLRGTLTLYPCG--NACTIDGLPVRQPTRLT 163
Cdd:cd00060    1 RLIVLDGDGGGREF---PLTKGVVTIGRSPDcDIVLDDPSVSRRHARIEVDGGGVYLEDLGstNGTFVNGKRITPPVPLQ 77
                         90
                 ....*....|..
gi 767969882 164 QGCMLCLGQSTF 175
Cdd:cd00060   78 DGDVIRLGDTTF 89
FHA_KIF1B cd22727
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ...
86-183 1.23e-10

forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438779 [Multi-domain]  Cd Length: 110  Bit Score: 59.28  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  86 PHLVSLGSGRLSTAITLLPLEEGRTVIGSA----ARDISLQGPGLAPEHCY-----IENLRGTLTLYPCGNACT-IDGLP 155
Cdd:cd22727    3 PHLVNLNEDPLMSECLLYYIKDGITRVGQAdaerRQDIVLSGAHIKEEHCIfrserNNNGEVIVTLEPCERSETyVNGKR 82
                         90       100
                 ....*....|....*....|....*...
gi 767969882 156 VRQPTRLTQGCMLCLGQSTFLRFNHPAE 183
Cdd:cd22727   83 VVQPVQLRSGNRIIMGKNHVFRFNHPEQ 110
FHA_KIF1A cd22726
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ...
86-185 3.83e-10

forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438778 [Multi-domain]  Cd Length: 115  Bit Score: 58.02  E-value: 3.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  86 PHLVSLGSGRLSTAITLLPLEEGRTVIG----SAARDISLQGPGLAPEHC-YIENLRGTL----TLYPCGNACT-IDGLP 155
Cdd:cd22726    2 PHLVNLNEDPLMSECLLYYIKDGITRVGredaERRQDIVLSGHFIKEEHCiFRSDTRSGGeavvTLEPCEGADTyVNGKK 81
                         90       100       110
                 ....*....|....*....|....*....|
gi 767969882 156 VRQPTRLTQGCMLCLGQSTFLRFNHPAEAK 185
Cdd:cd22726   82 VTEPSILRSGNRIIMGKSHVFRFNHPEQAR 111
FHA_KIF28P cd22709
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ...
86-181 4.55e-10

forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; KIF28P, also called kinesin-like protein 6 (KLP6), is a microtubule-dependent motor protein required for mitochondrion morphology and transport of mitochondria in neuronal cells. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438761 [Multi-domain]  Cd Length: 102  Bit Score: 57.23  E-value: 4.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  86 PHLVSLGSGRLSTAITLLPLEEGRTVIGSAAR----DISLQGPGLAPEHCYIENLRGTLTLYPCGNACTI--DGLPVRQP 159
Cdd:cd22709    1 PHLLNLNEDPQLSGVIVHFLQEGETTIGRADAepepDIVLSGLSIQKQHAVITNTDGKVTIEPVSPGAKVivNGVPVTGE 80
                         90       100
                 ....*....|....*....|..
gi 767969882 160 TRLTQGCMLCLGQSTFLRFNHP 181
Cdd:cd22709   81 TELHHLDRVILGSNHLYVFVGP 102
FHA_AFDN cd22711
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ...
86-181 6.10e-10

forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ALL1-fused gene from chromosome 6 protein, protein AF-6, Afadin adherens junction formation factor, or MLLT4, is a nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton. It is essential for the organization of adherens junctions. It may play a key role in the organization of epithelial structures of the embryonic ectoderm. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438763 [Multi-domain]  Cd Length: 106  Bit Score: 56.95  E-value: 6.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  86 PHLVSLG-SGRLSTAITLLPLEEGRTVIGS------AARDISLQGPGLAPEHCYIENLRGTLTLYPCGNA--CTIDGLPV 156
Cdd:cd22711    2 PYLLELSpDGSDRDKPRRHRLQPNVTEVGSerspanSGQFIQLFGPDILPRHCVITHMEGVVTVTPASQDaeTYVNGQRI 81
                         90       100
                 ....*....|....*....|....*
gi 767969882 157 RQPTRLTQGCMLCLGQSTFLRFNHP 181
Cdd:cd22711   82 YETTMLQHGMVVQFGRSHTFRFCDP 106
FHA_KIF13 cd22706
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 ...
108-181 6.64e-10

forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 family includes KIF13A and KIF13B. KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438758 [Multi-domain]  Cd Length: 101  Bit Score: 56.92  E-value: 6.64e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767969882 108 GRTVIGSA----ARDISLQGPGLAPEHCYIENLRGTLTLYPCGNA-CTIDGLPVRQPTRLTQGCMLCLGQSTFLRFNHP 181
Cdd:cd22706   23 EHTLIGRSdaptQQDIQLSGLGIQPEHCIITIENEDVYLTPLEGArTCVNGSIVTEKTQLRHGDRILWGNNHFFRLNCP 101
FHA_KIF1C cd22728
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ...
86-180 4.16e-09

forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438780 [Multi-domain]  Cd Length: 102  Bit Score: 54.49  E-value: 4.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  86 PHLVSLGSGRLSTAITLLPLEEGRTVIGSAARDISLQGPGLAPEHCYI-----ENLRGTLTLYPCGNACT-IDGLPVRQP 159
Cdd:cd22728    2 PHLVNLNEDPLMSECLLYHIKDGVTRVGQVDVDIKLSGQFIREQHCLFrsipnPSGEVVVTLEPCEGAETyVNGKQVTEP 81
                         90       100
                 ....*....|....*....|.
gi 767969882 160 TRLTQGCMLCLGQSTFLRFNH 180
Cdd:cd22728   82 LVLKSGNRIVMGKNHVFRFNH 102
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
741-839 4.23e-08

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: 54.69  E-value: 4.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  741 ESTQQEHEDApSTKLQGEVLALEEERAQVLGHVEQLKVRVKE-LEQQLQESAREAEMERALLQGEREAERALLQKEQKAV 819
Cdd:pfam04012  35 QSELVKARQA-LAQTIARQKQLERRLEQQTEQAKKLEEKAQAaLTKGNEELAREALAEKKSLEKQAEALETQLAQQRSAV 113
                          90       100
                  ....*....|....*....|
gi 767969882  820 DQLQEKLVALETGIQKERDK 839
Cdd:pfam04012 114 EQLRKQLAALETKIQQLKAK 133
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
110-181 1.61e-07

forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438782 [Multi-domain]  Cd Length: 99  Bit Score: 49.91  E-value: 1.61e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767969882 110 TVIGSA-ARDISLQGPGLAPEHCYIE-NLRGTLTLYPCGNACT-IDGLPVRQPTRLTQGCMLCLGQSTFLRFNHP 181
Cdd:cd22730   25 TLIGSAdSQDIQLCGMGILPEHCIIDiTPEGQVMLTPQKNTRTfVNGSAVTSPIQLHHGDRILWGNNHFFRINLP 99
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
198-592 2.78e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 54.41  E-value: 2.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  198 PGPPYSPVPAESESLVNGNHTPQTATRGPSACashsslvssiEKDLQEIMDSLVLEEPGAAGKKPAATSPLSPMANGGRy 277
Cdd:PHA03307   47 SAELAAVTVVAGAAACDRFEPPTGPPPGPGTE----------APANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPD- 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  278 llSPPTSPGAMSVGSSYENTSPAFSPLSSPASSGSCASHSPSGQEPGPSVPPLVPARSSSYHLALQPPQSRPSGARSESP 357
Cdd:PHA03307  116 --PPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEP 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  358 RLSRKGGHERPPSPGLR-------GLLTDSPAATVLAEARRATESPRLGGQLPVVAISLSEYP----ASGALSQPTSIPG 426
Cdd:PHA03307  194 PPSTPPAAASPRPPRRSspisasaSSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPlprpAPITLPTRIWEAS 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  427 SPKFQPPVPAPRNKIGTLQDRPPSPFREPPGSERVLTTSPSRQLVGRTFSDGL-ATRTLQPPESPRLGRRGLDSMRELPP 505
Cdd:PHA03307  274 GWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSsSTSSSSESSRGAAVSPGPSPSRSPSP 353
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  506 LSPSLSRRAlSPLPTRTTPDPKLNREVAESPRPRRWAAhGASPEDFSLTLGARGRRTRSPSPTLGESLAPHKGSFSGRLS 585
Cdd:PHA03307  354 SRPPPPADP-SSPRKRPRPSRAPSSPAASAGRPTRRRA-RAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYARYP 431

                  ....*..
gi 767969882  586 PAYSLGS 592
Cdd:PHA03307  432 LLTPSGE 438
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
103-176 9.44e-07

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 47.65  E-value: 9.44e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767969882 103 LPLEEGRTVIGSAAR-DISLQGPGLAPEHCYIENLRGTLTLYPCG--NACTIDGLPVRQPTRLTQGCMLCLGQSTFL 176
Cdd:COG1716   16 FPLDGGPLTIGRAPDnDIVLDDPTVSRRHARIRRDGGGWVLEDLGstNGTFVNGQRVTEPAPLRDGDVIRLGKTELR 92
PHA03247 PHA03247
large tegument protein UL36; Provisional
192-602 1.03e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.02  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  192 PAGGRAPGPPY--SPVPAESESLVNGNHTPQTATRGPSACASHSSLVSSIEKDLQEIMDSLV----LEEPGAAGKKPAAT 265
Cdd:PHA03247 2595 SARPRAPVDDRgdPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPapgrVSRPRRARRLGRAA 2674
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  266 SPLSPMANGGRYLLSPPTSPGAMSVGSSYENTSPAFSPlsSPASSGSCASHSPSGQEPGPSVPPLVPARSSSYHLALQPP 345
Cdd:PHA03247 2675 QASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAP--HALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPG 2752
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  346 QSRPSGARSESPRLSRKGGHERPPSPGLRGLltDSPAATVLAEARRATESPRLGGQLPVV------AISLSEYPASGALS 419
Cdd:PHA03247 2753 GPARPARPPTTAGPPAPAPPAAPAAGPPRRL--TRPAVASLSESRESLPSPWDPADPPAAvlapaaALPPAASPAGPLPP 2830
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  420 QPTSIPGSPKFQP-PVPAPRNKIGTLQDRPPSPFREPPGSERVLTTSPSRqlvgrtfsdglatrtlqpPESPRLGRrgld 498
Cdd:PHA03247 2831 PTSAQPTAPPPPPgPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPAR------------------PPVRRLAR---- 2888
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  499 smrelPPLSPSLSRRALSP----------LPTRTTPDPKLNREVAESPRPRRWAAHGASPEDFSLTLGARGRRTRSPSPT 568
Cdd:PHA03247 2889 -----PAVSRSTESFALPPdqperppqpqAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPW 2963
                         410       420       430
                  ....*....|....*....|....*....|....
gi 767969882  569 LGeSLAPHKGSFSGRLSPAYSLGSLTGASPCQSP 602
Cdd:PHA03247 2964 LG-ALVPGRVAVPRFRVPQPAPSREAPASSTPPL 2996
FHA_KIF13A cd22729
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ...
107-188 2.05e-06

forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438781 [Multi-domain]  Cd Length: 109  Bit Score: 47.19  E-value: 2.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 107 EGRTVIGS-AARDISLQGPGLAPEHCYIE-NLRGTLTLYPCGNACT-IDGLPVRQPTRLTQGCMLCLGQSTFLRFNHPAE 183
Cdd:cd22729   22 KDHTRVGAdTSQDIQLFGIGIQPEHCVIDiAADGDVTLTPKENARTcVNGTLVCSVTQLWHGDRILWGNNHFFRINLPKR 101

                 ....*..
gi 767969882 184 A--KWMK 188
Cdd:cd22729  102 KrrDWLK 108
PHA03247 PHA03247
large tegument protein UL36; Provisional
196-538 3.33e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 3.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  196 RAPGPPYSPVPAESESLVNGNHTPQTATRGPSACASHSSLVSSIEKDlqeimDSLVLEEPGAAGKKPAATSPLSPMANGG 275
Cdd:PHA03247 2700 DPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPA-----GPATPGGPARPARPPTTAGPPAPAPPAA 2774
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  276 RYLLSPP--TSPGAMSVGSSYENTSPAFSPLSSPASSGSCASHSPSGQEPGPSVPPLVPARSSSYHLALQPPQSR--PSG 351
Cdd:PHA03247 2775 PAAGPPRrlTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSlpLGG 2854
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  352 ARSESPRLSRKGGHERPPSpglrglltdSPAATVLAEARR--ATESPRLGGQLPVVAISLSEYPASGALSQPTSIPGSPk 429
Cdd:PHA03247 2855 SVAPGGDVRRRPPSRSPAA---------KPAAPARPPVRRlaRPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPP- 2924
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  430 fQPPVPAPRNKIGTLQDRPPSPFREPPGSERVLTTSPSRQLVGRTFSDGLATRTLQPPESPRlgrrgldsmRELPPLSPS 509
Cdd:PHA03247 2925 -PPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPS---------REAPASSTP 2994
                         330       340
                  ....*....|....*....|....*....
gi 767969882  510 LSRRalSPLPTRTTPDPKLNREVAESPRP 538
Cdd:PHA03247 2995 PLTG--HSLSRVSSWASSLALHEETDPPP 3021
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
280-619 6.55e-06

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: 49.91  E-value: 6.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  280 SPPTSPGAMSVGSSYENTSPAF-------SPLSSPASSG------SCASHSPSGQEPGPSvpPLVPArsssyhlalqpPQ 346
Cdd:pfam05109 427 STTTSPTLNTTGFAAPNTTTGLpssthvpTNLTAPASTGptvstaDVTSPTPAGTTSGAS--PVTPS-----------PS 493
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  347 SRPSGARSESPRLSRKGGHERPPSPGlrgllTDSPAATVLAEARRATeSPRLGGQLPvvaislseypaSGALSQPTSIPG 426
Cdd:pfam05109 494 PRDNGTESKAPDMTSPTSAVTTPTPN-----ATSPTPAVTTPTPNAT-SPTLGKTSP-----------TSAVTTPTPNAT 556
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  427 SPKFQPPVPAPRNKIGTLQDRPPSPFREPP----GSERVLTTSPSRQLVGRTFSDGLATRTL-QPPESP---------RL 492
Cdd:pfam05109 557 SPTPAVTTPTPNATIPTLGKTSPTSAVTTPtpnaTSPTVGETSPQANTTNHTLGGTSSTPVVtSPPKNAtsavttgqhNI 636
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  493 GRRGLDSMRELPP-----LSPSLSRRALSPLPTRTTPDPKLNREVAE--------------SPRPRRWAAHGAS------ 547
Cdd:pfam05109 637 TSSSTSSMSLRPSsisetLSPSTSDNSTSHMPLLTSAHPTGGENITQvtpaststhhvstsSPAPRPGTTSQASgpgnss 716
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767969882  548 ----PEDFSLTLGARGRRTRSPSPTLGESLAPHKGSFSGRLSPAYSLGSLTGASPCQSPCVQRKLSSGDLRVPVTR 619
Cdd:pfam05109 717 tstkPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPRTR 792
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
625-838 7.18e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.91  E-value: 7.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  625 ITEISDNEDDLLEYHRRqrqerlreqeMERLERQR--LETILNLCAEYSRADGgpEAGELPSIGEATAALALAGRRpsRG 702
Cdd:COG4913   227 ADALVEHFDDLERAHEA----------LEDAREQIelLEPIRELAERYAAARE--RLAELEYLRAALRLWFAQRRL--EL 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  703 LAGASGRSSEEPGVATQRLWESmeRSDEENLKEECSSTESTQQEHEDAPSTKLQGEVLALEEERAQVLGHVEQLKVRVKE 782
Cdd:COG4913   293 LEAELEELRAELARLEAELERL--EARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAA 370
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767969882  783 LEQQLQESAREAEMERALLQGEREAERALLQKEQKAVDQLQEKLVALE---TGIQKERD 838
Cdd:COG4913   371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRrelRELEAEIA 429
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
731-846 9.02e-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: 48.00  E-value: 9.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 731 ENLKEECSSTESTQQEHEDApSTKLQGEVLALEEERAQVLGHVEQLKVRVKELEQQLQE--SAREAE------------- 795
Cdd:COG1579   27 KELPAELAELEDELAALEAR-LEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrNNKEYEalqkeieslkrri 105
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767969882 796 ----------MER--------ALLQGEREAERALLQKEQKAVDQLQEKLVALETGIQKERD---KEVPKPLL 846
Cdd:COG1579  106 sdledeilelMERieeleeelAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREelaAKIPPELL 177
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
725-842 9.66e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 49.09  E-value: 9.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 725 MERSDEENLKEEcsSTESTQQEHEDAPSTKLQGEVLALEEERAQVLGHVEQLKVRVKELEQQLQESarEAEMERALLQGE 804
Cdd:COG2433  383 EELIEKELPEEE--PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERL--ERELSEARSEER 458
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767969882 805 REAE---------------RALLQKEQKAVDQLQEKLVALETGIQKE-RDKEVP 842
Cdd:COG2433  459 REIRkdreisrldreierlERELEEERERIEELKRKLERLKELWKLEhSGELVP 512
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
726-840 1.31e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 726 ERSDEENLKEECSSTESTQQEHEDAPSTKLQGEVLALEEERAQVLGHVEQLKVRVKELEQQLQESAREAEMERALLQGER 805
Cdd:COG1196  285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767969882 806 EAERALLQKEQKAVDQLQEKLVALETGIQKERDKE 840
Cdd:COG1196  365 EALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
FHA_RADIL-like cd22712
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ...
83-181 1.39e-05

forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing protein (Radil)-like family; The Radil-like family includes Radil and Ras-interacting protein 1 (Rain). Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility by linking Rap1 to beta2-integrin activation. Rain, also called Rasip1, is an endothelial-specific Ras-interacting protein required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. It acts as a critical and vascular-specific regulator of GTPase signaling, cell architecture, and adhesion, which is essential for endothelial cell morphogenesis and blood vessel tubulogenesis. Rain interacts with Ras in a GTP-dependent manner and may serve as an effector for endomembrane-associated Ras. Both Radil and Rain contain an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438764 [Multi-domain]  Cd Length: 120  Bit Score: 44.99  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  83 TDKPHLVSLGSGRLSTAITLLPLEEGRTVIGSAAR-----DISLQGPGLAPEHCYIEN---------------LRGTLTL 142
Cdd:cd22712    1 SDYPYLLTLRGFSPKQDLLVYPLLEQVILVGSRTEgarkvDISLRAPDILPQHCWIRRkpeplsddedsdkesADYRVVL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767969882 143 YPCGNA-CTIDGLPVRQPTRLTQGCMLCLGQSTFLRFNHP 181
Cdd:cd22712   81 SPLRGAhVTVNGVPVLSETELHPGDLLGIGEHYLFLFKDP 120
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
761-839 2.18e-05

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 46.36  E-value: 2.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 761 ALEEERAQVLGHVEQLKVRVKELEQQLQE---------------SAREAEMERALLQGEREAERALLQKEQKAVDQLQEK 825
Cdd:COG1842   41 EARQALAQVIANQKRLERQLEELEAEAEKweekarlalekgredLAREALERKAELEAQAEALEAQLAQLEEQVEKLKEA 120
                         90
                 ....*....|....
gi 767969882 826 LVALETGIQKERDK 839
Cdd:COG1842  121 LRQLESKLEELKAK 134
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
723-831 2.20e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 48.25  E-value: 2.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882   723 ESMERSDEENLKEEcsstESTQQEHE------DAPSTKLQGEV----LALEEERAQVLGHVEQLKVRVKELEQ------Q 786
Cdd:pfam01576  186 EAMISDLEERLKKE----EKGRQELEkakrklEGESTDLQEQIaelqAQIAELRAQLAKKEEELQAALARLEEetaqknN 261
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 767969882   787 LQESAREAEMERALLQGEREAERALLQKEQKAVDQLQEKLVALET 831
Cdd:pfam01576  262 ALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKT 306
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
723-841 3.13e-05

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.


Pssm-ID: 462861 [Multi-domain]  Cd Length: 302  Bit Score: 46.87  E-value: 3.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  723 ESMERSDEENLKEEcSSTE---------STQQEHEDAPSTKLQGEVLALEEeRAQVLG--------HVEQLkVRVKELEQ 785
Cdd:pfam09728  89 ESKKLAKEEEEKRK-ELSEkfqstlkdiQDKMEEKSEKNNKLREENEELRE-KLKSLIeqyelrelHFEKL-LKTKELEV 165
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  786 QLQEsAR--EAEMERALLQGEREAERALLQKEQkaVDQLQEKLVALETGIQ--KERDKEV 841
Cdd:pfam09728 166 QLAE-AKlqQATEEEEKKAQEKEVAKARELKAQ--VQTLSETEKELREQLNlyVEKFEEF 222
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
719-839 4.16e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.82  E-value: 4.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 719 QRLWESMERSDEEnLKEECSSTESTQQEhedapSTKLQGEVLALEEERAQVLGHVEQLKVRVKELEQQLQEsareAEMER 798
Cdd:COG4372   55 EQAREELEQLEEE-LEQARSELEQLEEE-----LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE----LQKER 124
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767969882 799 ALLQGEREAERALLQKEQKAVDQLQEKLVALETGIQKERDK 839
Cdd:COG4372  125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
180-462 5.84e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.09  E-value: 5.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  180 HPAEAKWMKSMIPAGGRAPGPPYSPVPAESESlvnGNHTPQTATRGPSACASHSSLVSSIEKDLqeimDSLVLEEPGAAG 259
Cdd:PHA03307  168 SSRQAALPLSSPEETARAPSSPPAEPPPSTPP---AAASPRPPRRSSPISASASSPAPAPGRSA----ADDAGASSSDSS 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  260 KKPAATSPLSPMANGGRYLLSPPTSPGAMSVGSSYENTSPAFSPLSSPASSGscaSHSPSGQEPGPSVPPLVPARSSSYH 339
Cdd:PHA03307  241 SSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPR---ERSPSPSPSSPGSGPAPSSPRASSS 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  340 LALQPPQS----RPSGARSESPRLSRKGGHERPPSPGlrgllTDSPAATVLAEARR--------------ATESPRLGGQ 401
Cdd:PHA03307  318 SSSSRESSssstSSSSESSRGAAVSPGPSPSRSPSPS-----RPPPPADPSSPRKRprpsrapsspaasaGRPTRRRARA 392
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767969882  402 LPVVAISLSEYPASGALSQPTSIPGSPKFQPPVPAPRNKIGTLqDRPPSPFREPPGSERVL 462
Cdd:PHA03307  393 AVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYARYPLLTP-SGEPWPGSPPPPPGRVR 452
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
731-843 6.12e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 6.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 731 ENLKEECSSTESTQQ---EHEDAPSTKLQgEVLALEEERAQVLGHVEQLKVRVKELEqQLQESAREAEMERALLQGEREA 807
Cdd:PRK03918 179 ERLEKFIKRTENIEElikEKEKELEEVLR-EINEISSELPELREELEKLEKEVKELE-ELKEEIEELEKELESLEGSKRK 256
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767969882 808 ERALLQKEQKAVDQLQEKLVALEtgiqkERDKEVPK 843
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELE-----EKVKELKE 287
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
726-840 6.81e-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: 6.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 726 ERSDEENLKEECSSTESTQQEHEDApSTKLQGEVLALEEERAQVLGHVEQLKVRVKELEQQLQESAREAEMERALLQGER 805
Cdd:COG1196  258 LEAELAELEAELEELRLELEELELE-LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767969882 806 EAERALLQKEQKAVDQLQEKLVALETGIQKERDKE 840
Cdd:COG1196  337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
723-840 6.87e-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: 6.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 723 ESMERSDEENLKEECSSTESTQQEHEdapstKLQGEVLALEEERAQVLGHVEQLKVRVKELEQQLQESAREAEMERALLQ 802
Cdd:COG1196  301 EQDIARLEERRRELEERLEELEEELA-----ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767969882 803 GEREAERALLQKEQKAVDQLQEKLVALETGIQKERDKE 840
Cdd:COG1196  376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
741-824 9.05e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 9.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 741 ESTQQEHEDAPST--KLQGEVLALEEERAQVLGHVEQLKVRVKELEQQLQE-SAREAEMERALLQGEREAERALLQKEQK 817
Cdd:COG4372  104 ESLQEEAEELQEEleELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKElEEQLESLQEELAALEQELQALSEAEAEQ 183

                 ....*..
gi 767969882 818 AVDQLQE 824
Cdd:COG4372  184 ALDELLK 190
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
192-575 1.05e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.13  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 192 PAGGRAPGPPYSPVPAESESLVNGNHTPQTATRGPSACASHsslvssiekdlqeimdslvlEEPGAAGKKPAATSPLSPM 271
Cdd:PRK07764 398 APSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPA--------------------PAPPSPAGNAPAGGAPSPP 457
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 272 ANGgryllSPPTSPGAMSVGSSYENTSPAFSPLSSPASSGSCASHSPSGQEPG-----------PSVPPLVPARSSSYHL 340
Cdd:PRK07764 458 PAA-----APSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGaddaatlrerwPEILAAVPKRSRKTWA 532
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 341 ALQpPQSRPSGARSESPRLsrkgGHerpPSPGLRGLLTDSPAATVLAEARRATesprLGGQLPVVAISLSEYPASGALSQ 420
Cdd:PRK07764 533 ILL-PEATVLGVRGDTLVL----GF---STGGLARRFASPGNAEVLVTALAEE----LGGDWQVEAVVGPAPGAAGGEGP 600
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 421 PTSIPGSPKFQPPVPAPrnkigtlQDRPPSPFREPPGSErvlTTSPSRQLVGRTFSDGLATRTLQPPESPRLGRRGLDSM 500
Cdd:PRK07764 601 PAPASSGPPEEAARPAA-------PAAPAAPAAPAPAGA---AAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWP 670
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767969882 501 RELPPLSPSlsrrALSPLPTRTTPDPKlNREVAESPRPRRWAAHGASPEDFSLTLGARGRRTRSPSPTLGESLAP 575
Cdd:PRK07764 671 AKAGGAAPA----APPPAPAPAAPAAP-AGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVP 740
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
110-170 1.23e-04

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 40.64  E-value: 1.23e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767969882  110 TVIGSAAR-DISLQGPGLAPEHCYIENLRG-TLTLYPCG--NACTIDGLPVR-QPTRLTQGCMLCL 170
Cdd:pfam00498   1 VTIGRSPDcDIVLDDPSVSRRHAEIRYDGGgRFYLEDLGstNGTFVNGQRLGpEPVRLKDGDVIRL 66
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
760-839 1.58e-04

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


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 42.17  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  760 LALEEERAQVLGHVEQLKVRVKEL---EQQLQESARE-----AEMERALLQGEREAERALLQKEQKAVD--QLQEKLVAL 829
Cdd:pfam13863  13 LALDAKREEIERLEELLKQREEELekkEQELKEDLIKfdkflKENDAKRRRALKKAEEETKLKKEKEKEikKLTAQIEEL 92
                          90
                  ....*....|
gi 767969882  830 ETGIQKERDK 839
Cdd:pfam13863  93 KSEISKLEEK 102
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
730-845 2.05e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 2.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 730 EENLKEECSSTESTQQEHEDApstklQGEVLALEEERAQVLGHVEQLKVRVKELEQQLQE-SAREAEMERALLQGEREAE 808
Cdd:COG4372   79 EEELEELNEQLQAAQAELAQA-----QEELESLQEEAEELQEELEELQKERQDLEQQRKQlEAQIAELQSEIAEREEELK 153
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767969882 809 RAllqkeQKAVDQLQEKLVALETGIQKERDKEVPKPL 845
Cdd:COG4372  154 EL-----EEQLESLQEELAALEQELQALSEAEAEQAL 185
PHA03247 PHA03247
large tegument protein UL36; Provisional
193-567 2.25e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  193 AGGRAP-GPPYSPVPAESESLvngnHTPQTATRgPSACAshsslVSSIEKDLQEIMDSLVLEEPGAAGKKPAATSPLSPM 271
Cdd:PHA03247 2548 AGDPPPpLPPAAPPAAPDRSV----PPPRPAPR-PSEPA-----VTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPL 2617
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  272 ANGGRYLLSPPTSPGAMSVGSSYENTSPAFSP-LSSPASSGSCASH----SPSGQEPGPSVPP-------LVPARSSSYH 339
Cdd:PHA03247 2618 PPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPeRPRDDPAPGRVSRprraRRLGRAAQASSPPqrprrraARPTVGSLTS 2697
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  340 LALQPPQSR------------------PSGARSESPRLSRK-------------GGHERPPSPGLRG------------- 375
Cdd:PHA03247 2698 LADPPPPPPtpepaphalvsatplppgPAAARQASPALPAApappavpagpatpGGPARPARPPTTAgppapappaapaa 2777
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  376 ---LLTDSPAATVLAEARRATESPRLGGQLPVV------AISLSEYPASGALSQPTSIPGSPKFQP-PVPAPRNKIGTLQ 445
Cdd:PHA03247 2778 gppRRLTRPAVASLSESRESLPSPWDPADPPAAvlapaaALPPAASPAGPLPPPTSAQPTAPPPPPgPPPPSLPLGGSVA 2857
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  446 DRPPSPFREPPGSERVLTTSPSRQLVGRTFSDGLATRTL---QPPESPRLGRRGLDSMRELPPLSPSLSRRALSPLPTRT 522
Cdd:PHA03247 2858 PGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTEsfaLPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPP 2937
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767969882  523 TPDPKLnrevaeSPRPRRWAAHGASPEDFSLTLGA--RGR----RTRSPSP 567
Cdd:PHA03247 2938 RPQPPL------APTTDPAGAGEPSGAVPQPWLGAlvPGRvavpRFRVPQP 2982
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
774-846 2.30e-04

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: 42.52  E-value: 2.30e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767969882 774 EQLKVRVKELEQQLQESAREAEMERALLQGER----EAERALLQKE-QKAVDQLQEKLVALETGIQKERDKEVpKPLL 846
Cdd:COG2825   46 KKLEKEFKKRQAELQKLEKELQALQEKLQKEAatlsEEERQKKERElQKKQQELQRKQQEAQQDLQKRQQELL-QPIL 122
PTZ00121 PTZ00121
MAEBL; Provisional
723-825 2.59e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 2.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  723 ESMERSDEENLKEECSSTESTQQEHEDAPSTKLQGEVLALEEERAQVlghvEQLKVRVKELEQQLQESAREAEMERALLQ 802
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE----EENKIKAAEEAKKAEEDKKKAEEAKKAEE 1685
                          90       100
                  ....*....|....*....|....*
gi 767969882  803 GEREAERALLQKEQKA--VDQLQEK 825
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAkkAEELKKK 1710
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
287-548 3.21e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.48  E-value: 3.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 287 AMSVGSSYENTSPAfSPLSSPASSGSCASHSPSGQEPGPSVPPLVPArsssyhLALQPPQSRPSGARSESPRlsrkgghe 366
Cdd:PRK12323 362 AFRPGQSGGGAGPA-TAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPA------AAPAAAAAARAVAAAPARR-------- 426
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 367 rppspglrglltdSPAATVLAEARRAteSPRLGGQLPVVAISLSEYPASGALSQPTSIPGSPKFQPPVPAPRNKIGT--L 444
Cdd:PRK12323 427 -------------SPAPEALAAARQA--SARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAApaP 491
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 445 QDRPPSPFREPPGServlTTSPSRQLVGRTFSDGLATRTLQPPESPrlgrrgldsmrelpplsPSLSRRALSPLPTRT-T 523
Cdd:PRK12323 492 ADDDPPPWEELPPE----FASPAPAQPDAAPAGWVAESIPDPATAD-----------------PDDAFETLAPAPAAApA 550
                        250       260
                 ....*....|....*....|....*
gi 767969882 524 PDPKLNREVAESPRPRRWAAHGASP 548
Cdd:PRK12323 551 PRAAAATEPVVAPRPPRASASGLPD 575
Rab5-bind pfam09311
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ...
731-839 3.24e-04

Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow for binding to the GTPase Rab5. This interaction is necessary and sufficient for Rab5-dependent recruitment of Rabaptin5 to early endosomal membranes.


Pssm-ID: 462752 [Multi-domain]  Cd Length: 307  Bit Score: 43.80  E-value: 3.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  731 ENLKEECSSTESTQQEHEDAPSTKLQGEVLALEEERAqvlghVEQLKVRVKELEQQLQ-ESAREAEMERALLQGEREAER 809
Cdd:pfam09311 200 ENCKEEIASISSLKVELERIKAEKEQLENGLTEKIRQ-----LEDLQTTKGSLETQLKkETNEKAAVEQLVFEEKNKAQR 274
                          90       100       110
                  ....*....|....*....|....*....|
gi 767969882  810 alLQKEQKAVDQLQEKLVALETGIQKERDK 839
Cdd:pfam09311 275 --LQTELDVSEQVQRDFVKLSQTLQVQLER 302
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
718-848 3.29e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.57  E-value: 3.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882   718 TQRL--WESMERSDEENLKEECSST-----ESTQQEHEDAPSTKLQGEVLALEEEraqvlghvEQLKVRVKELEQQ-LQE 789
Cdd:TIGR00618  378 TQHIhtLQQQKTTLTQKLQSLCKELdilqrEQATIDTRTSAFRDLQGQLAHAKKQ--------QELQQRYAELCAAaITC 449
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882   790 SAREAEMERALLQGEREAERALLQKEQ-KAVDQLQEKLVALETGIQKERDKEVPKPLLGQ 848
Cdd:TIGR00618  450 TAQCEKLEKIHLQESAQSLKEREQQLQtKEQIHLQETRKKAVVLARLLELQEEPCPLCGS 509
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
728-841 4.37e-04

Family with sequence similarity 184, A and B; The function of FAM184 is not known.


Pssm-ID: 464788 [Multi-domain]  Cd Length: 211  Bit Score: 42.34  E-value: 4.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  728 SDEENLKEECSSTESTQQEHEdapstklqgevlaleEERAQVLGHVEQLKVRV--KELEQQLQESAREAEMERALLQGER 805
Cdd:pfam15665  46 GEELDLKRRIQTLEESLEQHE---------------RMKRQALTEFEQYKRRVeeRELKAEAEHRQRVVELSREVEEAKR 110
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767969882  806 EAERALLQKEQKAVDQLQEKLVALETgIQKERDKEV 841
Cdd:pfam15665 111 AFEEKLESFEQLQAQFEQEKRKALEE-LRAKHRQEI 145
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
696-826 4.65e-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: 43.90  E-value: 4.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882   696 GRRPSRGLAGASGRSSEEPGVATQRLwESMERsDEENLKEECSSTESTQQEHEDAPS------TKLQGEVLALEEERAQV 769
Cdd:TIGR02169  658 GSRAPRGGILFSRSEPAELQRLRERL-EGLKR-ELSSLQSELRRIENRLDELSQELSdasrkiGEIEKEIEQLEQEEEKL 735
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767969882   770 LGHVEQLKVRVKELEQQLQESarEAEMERalLQGEREAERALLQKEQKAVDQLQEKL 826
Cdd:TIGR02169  736 KERLEELEEDLSSLEQEIENV--KSELKE--LEARIEELEEDLHKLEEALNDLEARL 788
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
316-513 4.87e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 43.91  E-value: 4.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 316 HSPSGQEPGPS-VPPLVPARSSSYHLALQPPQSRPSGARSESPRLSRKGGHERPPSPGLRG------LLTDSPAATVLAE 388
Cdd:PTZ00449 507 HDEPPEGPEASgLPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKEHkpskipTLSKKPEFPKDPK 586
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 389 ARRATESPRlGGQLPVVAiSLSEYPASGALSQPTSIPGSPKFQPPVPAPRnkigtlqdRPPSPFRePPGSERVLTTSpsr 468
Cdd:PTZ00449 587 HPKDPEEPK-KPKRPRSA-QRPTRPKSPKLPELLDIPKSPKRPESPKSPK--------RPPPPQR-PSSPERPEGPK--- 652
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767969882 469 qlvgrtfsdglATRTLQPPESPRlgrrgldsmrelPPLSPSLSRR 513
Cdd:PTZ00449 653 -----------IIKSPKPPKSPK------------PPFDPKFKEK 674
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
727-839 5.91e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 5.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 727 RSDEENLKEECSSTESTQQEHEDAPST-KLQGEVLALEEERAQVLGHVEQLKVRVKELEQQLQE-SAREAEMERA----- 799
Cdd:COG4717  101 EEELEELEAELEELREELEKLEKLLQLlPLYQELEALEAELAELPERLEELEERLEELRELEEElEELEAELAELqeele 180
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767969882 800 -LLQGEREAERALLQKEQKAVDQLQEKLVALETGIQKERDK 839
Cdd:COG4717  181 eLLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
703-843 6.22e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 6.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 703 LAGASGRSSEEPGVATQRLWESMERSDEENLKEECSSTESTQQEHEDAPSTKLQGEVLALEEERAQVLGHVE---QLKVR 779
Cdd:COG4717  324 LLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEeyqELKEE 403
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 780 VKELEQQLQESAREAEMERALLQGER-EAERALLQKEQKA----VDQLQEKLVALETGIQK-ERDKEVPK 843
Cdd:COG4717  404 LEELEEQLEELLGELEELLEALDEEElEEELEELEEELEEleeeLEELREELAELEAELEQlEEDGELAE 473
PHA03247 PHA03247
large tegument protein UL36; Provisional
181-476 6.35e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 6.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  181 PAEAKWMKSMIPAGGRAPGPPYSPVPAESESLVNGNHTPQtatrgPSACASHSSLVssiekdlqeimdslvleePGAAGK 260
Cdd:PHA03247 2761 PTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPS-----PWDPADPPAAV------------------LAPAAA 2817
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  261 KPAATSPLSPmanggrylLSPPTSPGAMSVGSSYENTSPAFSPLSSPASSGSCASHSPSGQEPG-PSVPPLVPARSSSyh 339
Cdd:PHA03247 2818 LPPAASPAGP--------LPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAkPAAPARPPVRRLA-- 2887
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  340 lalQPPQSRPSGARSESPRlsrkgGHERPPSPGLRGLLTDSPAATVLAEARRATESPrlggqlPVVAISLSEYPASGALS 419
Cdd:PHA03247 2888 ---RPAVSRSTESFALPPD-----QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP------PRPQPPLAPTTDPAGAG 2953
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767969882  420 QPTSIPGSPKFQPPVPApRNKIGTLQDRPPSPFREPPGSErvlTTSPSRQLVGRTFS 476
Cdd:PHA03247 2954 EPSGAVPQPWLGALVPG-RVAVPRFRVPQPAPSREAPASS---TPPLTGHSLSRVSS 3006
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
286-468 6.77e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 6.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  286 GAMSVGSSYENTSPAFSPLSSPASSGSCASHSPSGQEPGPSVPPLVPARSSSYHLALQPP-------QSRPSGARSESPR 358
Cdd:PHA03307  743 RARARASAWDITDALFSNPSLVPAKLAEALALLEPAEPQRGAGSSPPVRAEAAFRRPGRLrrsgpaaDAASRTASKRKSR 822
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  359 LSRKGGHERPPSPGLrglltdSPAATVLAEARRATESPRLGGQLPVVAislseypASGALSQPTSIPGSPKFQPPVPAPR 438
Cdd:PHA03307  823 SHTPDGGSESSGPAR------PPGAAARPPPARSSESSKSKPAAAGGR-------ARGKNGRRRPRPPEPRARPGAAAPP 889
                         170       180       190
                  ....*....|....*....|....*....|
gi 767969882  439 NKIGTLQDRPPSPFREPPGSERVLTTSPSR 468
Cdd:PHA03307  890 KAAAAAPPAGAPAPRPRPAPRVKLGPMPPG 919
Yop-YscD_cpl pfam16697
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
103-181 7.43e-04

Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.


Pssm-ID: 465238 [Multi-domain]  Cd Length: 94  Bit Score: 39.55  E-value: 7.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  103 LPLEEGRTVIGSAAR-DISLQGPGLAPEHCYIE--NLRGTLTLYPCGNACTIDGLPVRQPTR-LTQGCMLCLGQsTFLRF 178
Cdd:pfam16697  12 FPLEGGRYRIGSDPDcDIVLSDKEVSRVHLKLEvdDEGWRLDDLGSGNGTLVNGQRVTELGIaLRPGDRIELGQ-TEFCL 90

                  ...
gi 767969882  179 NHP 181
Cdd:pfam16697  91 VPA 93
FHA_MDC1 cd22665
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ...
104-146 8.20e-04

forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also called nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438717 [Multi-domain]  Cd Length: 97  Bit Score: 39.52  E-value: 8.20e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 767969882 104 PLEEGRTVIG-SAARDISLQGPGLAPEHCYIENLRGTLTLYPCG 146
Cdd:cd22665   17 PLYEGENVIGrDPSCSVVLPDKSVSKQHACIEVDGGTHLIEDLG 60
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
720-835 8.51e-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: 43.12  E-value: 8.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882   720 RLWESMER--SDEENLKEECSSTESTQQEHEDAPSTKLQgevlALEEERAQVLGHVEQLKvRVKELEQQLQESAREAEME 797
Cdd:TIGR02168  681 ELEEKIEEleEKIAELEKALAELRKELEELEEELEQLRK----ELEELSRQISALRKDLA-RLEAEVEQLEERIAQLSKE 755
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 767969882   798 RALLQGEREAERALLQKEQKAVDQLQEKLVALETGIQK 835
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
605-826 9.03e-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: 43.12  E-value: 9.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882   605 QRKLSSGDLRVPVTRERKNSITEISDNEDDLLEYHRRQRQERLREQEMERLERQRLET-ILNLCAEYSRAdggpeAGELP 683
Cdd:TIGR02168  725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAeIEELEAQIEQL-----KEELK 799
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882   684 SIGEATAALALAGRRPSRGLAGASGR--SSEEPGVATQRLWESMERSDEENLKEECSSTEStqQEHEDAPSTKLQGEVLA 761
Cdd:TIGR02168  800 ALREALDELRAELTLLNEEAANLRERleSLERRIAATERRLEDLEEQIEELSEDIESLAAE--IEELEELIEELESELEA 877
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767969882   762 LEEERAQVLGHVEQLKVRVKELEQQLQES---AREAEMERALLQGEREAERALLQKEQKAVDQLQEKL 826
Cdd:TIGR02168  878 LLNERASLEEALALLRSELEELSEELRELeskRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
103-178 9.92e-04

forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438725 [Multi-domain]  Cd Length: 95  Bit Score: 39.12  E-value: 9.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 103 LPLEEGRTVIGSAAR-DISLQGPGLAPEHCYIENLR-GTLTLYPCG--NACTIDGLPVRQPTRLTQGCMLCLGQSTFlRF 178
Cdd:cd22673   16 FPLTKKSCTFGRDLScDIRIQLPGVSREHCRIEVDEnGKAYLENLSttNPTLVNGKAIEKSAELKDGDVITIGGRSF-RF 94
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
761-839 1.14e-03

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 41.90  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 761 ALEEERAQVLghveqlkvrVKELEQQLQEsaREAEMER--ALLQGEREAERALLQKEQKAVDQLQEKLVA-LETGIQKER 837
Cdd:cd03406  170 AMEAEKTKLL---------IAEQHQKVVE--KEAETERkrAVIEAEKDAEVAKIQMQQKIMEKEAEKKISeIEDEMHLAR 238

                 ..
gi 767969882 838 DK 839
Cdd:cd03406  239 EK 240
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
730-835 1.15e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 730 EENLKEECSSTESTQQEhedapSTKLQGEVLALEEERAQVLGHVEQLKVRVKELEQQLQESARE--------AEMERAL- 800
Cdd:COG4372   30 SEQLRKALFELDKLQEE-----LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQlqaaqaelAQAQEELe 104
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767969882 801 -LQGEREAERALLQKEQKAVDQLQEKLVALETGIQK 835
Cdd:COG4372  105 sLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE 140
PRK09039 PRK09039
peptidoglycan -binding protein;
738-840 1.24e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.88  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 738 SSTESTQQEHEDAPSTKLQ--GEVLALEEERAQVLGH-----------VEQLKVRVKELEQQLQESAREAEMERALLQGE 804
Cdd:PRK09039  45 SREISGKDSALDRLNSQIAelADLLSLERQGNQDLQDsvanlraslsaAEAERSRLQALLAELAGAGAAAEGRAGELAQE 124
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767969882 805 REAERALLQKEQKAVDQLQEKLVALETGIQ---------KERDKE 840
Cdd:PRK09039 125 LDSEKQVSARALAQVELLNQQIAALRRQLAaleaaldasEKRDRE 169
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
745-839 1.26e-03

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


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 41.89  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  745 QEHEDAPSTKLQGEVLALEEERAQvlgHVEQLKVRVKELEQQLQESAREaEMERALLQGER-------------EAERAL 811
Cdd:pfam02841 183 QSKEAVEEAILQTDQALTAKEKAI---EAERAKAEAAEAEQELLREKQK-EEEQMMEAQERsyqehvkqliekmEAEREQ 258
                          90       100       110
                  ....*....|....*....|....*....|
gi 767969882  812 LQKEQKAV--DQLQEKLVALETGIQKERDK 839
Cdd:pfam02841 259 LLAEQERMleHKLQEQEELLKEGFKTEAES 288
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
720-830 1.32e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.42  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  720 RLWESMERSDEENLKEECSSTESTQQEHEDAPstklQGEVLALEEERAQvlghvEQLKVRVKELEQQLQ-ESAREAEMER 798
Cdd:pfam17380 402 RKVKILEEERQRKIQQQKVEMEQIRAEQEEAR----QREVRRLEEERAR-----EMERVRLEEQERQQQvERLRQQEEER 472
                          90       100       110
                  ....*....|....*....|....*....|..
gi 767969882  799 ALLQGEREAErallQKEQKAVDQLQEKLVALE 830
Cdd:pfam17380 473 KRKKLELEKE----KRDRKRAEEQRRKILEKE 500
racA PRK13182
chromosome-anchoring protein RacA;
731-844 1.36e-03

chromosome-anchoring protein RacA;


Pssm-ID: 237292 [Multi-domain]  Cd Length: 175  Bit Score: 40.42  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 731 ENLKEECSSTESTQQEHEDAPSTKLQGEVLALEEERAQVL-----GHVEQLKVRVKELEQQLQESAREAeMERALLQGER 805
Cdd:PRK13182  47 EYVKSQIEEGQNMQDTQKPSSNDVEETQVNTIVQNISSVDfeqleAQLNTITRRLDELERQLQQKADDV-VSYQLLQHRR 125
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767969882 806 EAE--RALLQKEQKAVDQLQEKLVALETGIQKERDKEVPKP 844
Cdd:PRK13182 126 EMEemLERLQKLEARLKKLEPIYITPDTEPTYEREKKPKRR 166
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
652-838 1.40e-03

LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.


Pssm-ID: 462869 [Multi-domain]  Cd Length: 303  Bit Score: 41.61  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  652 MERLERQRLETILNlcAEYSRADGGPEAGELPSIGEATAALALAGRRPSRGLAgaSGRSSEEPGVATQRlwESMERSDEE 731
Cdd:pfam09738  20 MRELERQQKEVEEN--ADRVFDMSSSSGADTASGSPTASTTSAGTLNSLGGTS--SRRSSEDSSISLED--EGSLRDIKH 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  732 NLKEecsstesTQQEHEDAPSTKLQgevlaLEEERAQVLGHVEQLKVRVKELEQQLQESAREAEmERAllqgeREAERal 811
Cdd:pfam09738  94 ELKE-------VEEKYRKAMISNAQ-----LDNEKSNLMYQVDLLKDKLEEMEESLAELQRELR-EKN-----KELER-- 153
                         170       180
                  ....*....|....*....|....*..
gi 767969882  812 lqkEQKAVDQLQEKLVALETGIqKERD 838
Cdd:pfam09738 154 ---LKRNLRRLQFQLAELKEQL-KQRD 176
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
723-824 1.46e-03

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


Pssm-ID: 463102 [Multi-domain]  Cd Length: 140  Bit Score: 39.59  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  723 ESMER-------------SDEENLKEECSSTEsTQQEHEDAPSTKLQGEVLALEEERAQVLGHVEQLKVRVKELEQ---Q 786
Cdd:pfam10473  27 ENLERelemseenqelaiLEAENSKAEVETLK-AEIEEMAQNLRDLELDLVTLRSEKENLTKELQKKQERVSELESlnsS 105
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767969882  787 LQESAREAEMERALLQGEREAERALLQKEQKavdQLQE 824
Cdd:pfam10473 106 LENLLEEKEQEKVQMKEESKTAVEMLQTQLK---ELNE 140
ZapB COG3074
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
762-831 1.63e-03

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442308 [Multi-domain]  Cd Length: 79  Bit Score: 38.03  E-value: 1.63e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767969882 762 LEEERAQVLGHVEQLKVRVKELEQ---QLQESAREAEMERALLQGEREAeralLQKEQkavDQLQEKLVALET 831
Cdd:COG3074    9 LEAKVQQAVDTIELLQMEVEELKEkneELEQENEELQSENEELQSENEQ----LKTEN---AEWQERIRSLLG 74
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
254-490 1.63e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 41.84  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 254 EPGAA-GKKPAATSPLSPMANGGRYLLSPP----TSPGAMSVGSSYENTSPAFSPLSSPASSGSCASHSPSGQEPGPSVP 328
Cdd:PLN03209 332 ESDAAdGPKPVPTKPVTPEAPSPPIEEEPPqpkaVVPRPLSPYTAYEDLKPPTSPIPTPPSSSPASSKSVDAVAKPAEPD 411
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 329 PLVPARSSSYHLALQPPQSRPSGARSESPrLSRKGGHERPPSPglrglltdSPAATVLAEARRATES--PRLGGQLPVVA 406
Cdd:PLN03209 412 VVPSPGSASNVPEVEPAQVEAKKTRPLSP-YARYEDLKPPTSP--------SPTAPTGVSPSVSSTSsvPAVPDTAPATA 482
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 407 ISLSEYPASGALSQPTSIPGSPKFQPPVPAPRNKIGTLQDRPPSPFREPPGSERVLTTSPSRQLVGRTFSDGLATRT--- 483
Cdd:PLN03209 483 ATDAAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGNSAPPTALADEQHHAQPKPRPLSPYTmye 562

                 ....*...
gi 767969882 484 -LQPPESP 490
Cdd:PLN03209 563 dLKPPTSP 570
PTZ00121 PTZ00121
MAEBL; Provisional
709-839 1.84e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  709 RSSEEpgvaTQRLWESMERSDEENLKEEcsstESTQQEHEDAPSTKLQGEVLALEEERAQVLGHVEQL-KVRVKELEQQL 787
Cdd:PTZ00121 1668 KKAEE----DKKKAEEAKKAEEDEKKAA----EALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnKIKAEEAKKEA 1739
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767969882  788 QESAREAEMERALLQGEREAERALLQKEQKAVDQLQEKLVALETGIQKERDK 839
Cdd:PTZ00121 1740 EEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEK 1791
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
722-829 1.87e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 722 WESMERSDEE--NLKEECSSTESTQQEHEDAPSTKLQGEVLALEEERAQVLGHVEQLKVRVKELEQQLQESarEAEMERA 799
Cdd:COG4717  148 LEELEERLEElrELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA--QEELEEL 225
                         90       100       110
                 ....*....|....*....|....*....|
gi 767969882 800 LLQGEREAERALLQKEQKAVDQLQEKLVAL 829
Cdd:COG4717  226 EEELEQLENELEAAALEERLKEARLLLLIA 255
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
731-835 2.07e-03

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: 41.93  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  731 ENLKEECSSTESTQQEHEDAPSTKLQgEVLALEEERAQVLGHVEQLKVRVKELE----------QQLQESAREAEMERAL 800
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQRELEEKQN-EIEKLKKENQSYKQEIKNLESQINDLEskiqnqeklnQQKDEQIKKLQQEKEL 423
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 767969882  801 LQGEREAERALLQKEQKAVDQLQEKLVALETGIQK 835
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKN 458
KAR9 pfam08580
Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal ...
345-586 2.12e-03

Yeast cortical protein KAR9; The KAR9 protein in Saccharomyces cerevisiae is a cytoskeletal protein required for karyogamy, correct positioning of the mitotic spindle and for orientation of cytoplasmic microtubules. KAR9 localizes at the shmoo tip in mating cells and at the tip of the growing bud in anaphase.


Pssm-ID: 430088 [Multi-domain]  Cd Length: 684  Bit Score: 41.74  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  345 PQSRPSGARSESPR--LSRKGGHERPPSPGLRGLLTDSPAATVLAEARratesprlggqLPVVAislseyPASGALSQPT 422
Cdd:pfam08580 430 PGSSPPSSVIMTPVnkGSKTPSSRRGSSFDFGSSSERVINSKLRRESK-----------LPQIA------STLKQTKRPS 492
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  423 SIPG-SPKFQPPVPAPRNKIGTL----QDRPPSPFREPPGSERV---LTTSPSRQLVGRTFSdglaTRTLQPPeSPRLGR 494
Cdd:pfam08580 493 KIPRaSPNHSGFLSTPSNTATSEtptpALRPPSRPQPPPPGNRPrwnASTNTNDLDVGHNFK----PLTLTTP-SPTPSR 567
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  495 RGLdSMRELPPLSP-----------------SLSRRALSPLPTRT------------TPDPKLN-REVAESPRPRRWAAH 544
Cdd:pfam08580 568 SSR-SSSTLPPVSPlsrdksrspaptcrsvsRASRRRASRKPTRIgspnsrtslldePPYPKLTlSKGLPRTPRNRQSYA 646
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767969882  545 GASPEDFSLTLGARGRRTRsPSPTLGeslapHKGSFSGRLSP 586
Cdd:pfam08580 647 GTSPSRSVSVSSGLGPQTR-PGTSLG-----SRFDESRLLSP 682
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
753-845 2.27e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 753 TKLQGEVLALEEERAQVLGHVEQLKVRVKELEQQLQE-SAREAEMERAL--LQGEREAERALLQKEQKAVDQLQEKLVAL 829
Cdd:COG4942  153 EELRADLAELAALRAELEAERAELEALLAELEEERAAlEALKAERQKLLarLEKELAELAAELAELQQEAEELEALIARL 232
                         90
                 ....*....|....*.
gi 767969882 830 ETGIQKERDKEVPKPL 845
Cdd:COG4942  233 EAEAAAAAERTPAAGF 248
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
736-839 2.44e-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: 2.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882   736 ECSSTESTQQEHEDAPSTKLQGEVLALEEERAQVLGHVEQLKVRVKELEQQLQESAREAEMERALLQGERE----AERAL 811
Cdd:TIGR00606  416 DLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERElskaEKNSL 495
                           90       100
                   ....*....|....*....|....*...
gi 767969882   812 LQKEQKAVDQLQEKLVALETGIQKERDK 839
Cdd:TIGR00606  496 TETLKKEVKSLQNEKADLDRKLRKLDQE 523
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
760-839 2.45e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 40.64  E-value: 2.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 760 LALEEERAQVLG-HVEQLKVRVKELEQQLQESAREAEMERALLQGEREAERALLQKEQKAV--DQLQEKLVALETGIQKE 836
Cdd:cd16269  200 IEAERAKAEAAEqERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERAleSKLKEQEALLEEGFKEQ 279

                 ...
gi 767969882 837 RDK 839
Cdd:cd16269  280 AEL 282
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
730-824 2.51e-03

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


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 40.73  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  730 EENLKEECSSTESTQQEHEdapstklqgevlALEEERAQVLGHVEQLKVRVKELEQQLQEsarEAEMERALLQgeREAER 809
Cdd:pfam02841 203 EKAIEAERAKAEAAEAEQE------------LLREKQKEEEQMMEAQERSYQEHVKQLIE---KMEAEREQLL--AEQER 265
                          90
                  ....*....|....*
gi 767969882  810 ALLQKEQKAVDQLQE 824
Cdd:pfam02841 266 MLEHKLQEQEELLKE 280
PHA03247 PHA03247
large tegument protein UL36; Provisional
323-620 2.67e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  323 PGPSVPPLVPARSSSYHLALQPPQSRPSGARSESpRLSRKGGHERPPSPGLRGLLTDSPAATvlaearratesprlggql 402
Cdd:PHA03247 2551 PPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTS-RARRPDAPPQSARPRAPVDDRGDPRGP------------------ 2611
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  403 pvvaislseypasgalSQPTSIP-GSPKFQPPVPAPRNKIGTLQDRPPSPFREPPGSERvlTTSPSR-QLVGRTFSDGLA 480
Cdd:PHA03247 2612 ----------------APPSPLPpDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRD--DPAPGRvSRPRRARRLGRA 2673
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  481 TRTLQPPESPRlgrrgldsMRELPPLSPSLSRRALSPLPTRtTPDPKLNREVAESPRPRRWAAHGASPEDFSLTLGARGR 560
Cdd:PHA03247 2674 AQASSPPQRPR--------RRAARPTVGSLTSLADPPPPPP-TPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAV 2744
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  561 RTRSPSPTlGESLAPHKGSFSGRLSPAYSLGSLTGASPCQSPCVQRKLSSGDLRVPVTRE 620
Cdd:PHA03247 2745 PAGPATPG-GPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWD 2803
FHA_YscD-like cd22710
forkhead associated (FHA) domain found in Yersinia enterocolitica Yop proteins translocation ...
103-178 4.06e-03

forkhead associated (FHA) domain found in Yersinia enterocolitica Yop proteins translocation protein D (YscD) and similar proteins; YscD protein is a single-pass inner membrane protein required for the export process of the Yop proteins. It is an essential component of the type III secretion system. YscD protein contains an N-terminal cytoplasmic domain, a transmembrane linker and a large periplasmic domain. The cytoplasmic domain consists of a forkhead-associated (FHA) fold. The FHA domain is a small phosphopeptide recognition module. Due to the lack of the conserved residues that are required for binding phosphothreonine, the cytoplasmic domain of YscD protein is therefore unlikely to function as a true FHA domain.


Pssm-ID: 438762 [Multi-domain]  Cd Length: 94  Bit Score: 37.38  E-value: 4.06e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767969882 103 LPLEEGRTVIGS--AARDISLQGPGLAPEHCYIENLRGTLTLYPCGNACTIDGLPVRQPTRLTQGCMLCLGqstFLRF 178
Cdd:cd22710   14 VPLPPGRYVLGSdpLQCDLVLTDSGISPVHLVLEVDDGGVRLLDSAEPLYQNGEPVVLGVLLNAFSIISVG---FLFW 88
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
727-840 4.50e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 4.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 727 RSDEENLKEECSSTESTQQEHEdapstKLQGEVLALEEERAQVLGHVEQLKVRVKELEQQLQES-AREAEMERAL----- 800
Cdd:PRK03918 213 SSELPELREELEKLEKEVKELE-----ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELkKEIEELEEKVkelke 287
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767969882 801 LQGEREAERAL----------LQKEQKAVDQLQEKLVALETGIQKERDKE 840
Cdd:PRK03918 288 LKEKAEEYIKLsefyeeyldeLREIEKRLSRLEEEINGIEERIKELEEKE 337
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
762-843 5.08e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 39.74  E-value: 5.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  762 LEEERAQVLGHVEQLKVRVKELEQQLQESAREAEMERALLQGEREAERAL----------LQKEQKAVDQLQEKLVALET 831
Cdd:pfam09787  59 LREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSArreaeaelerLQEELRYLEEELRRSKATLQ 138
                          90
                  ....*....|..
gi 767969882  832 GIQKERDKEVPK 843
Cdd:pfam09787 139 SRIKDREAEIEK 150
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
762-830 5.14e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.87  E-value: 5.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767969882 762 LEEERAQVLGHVEQLKVRVKELEQQLQEsareaEMERALLQGEREAERALLQKEQKAVDQLQEKLVALE 830
Cdd:cd16269  228 LEDQERSYEEHLRQLKEKMEEERENLLK-----EQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
727-835 6.25e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 6.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882   727 RSDEENLKEECSSTESTQQEHE-DAPSTKLQGEVLA-----LEEERAQVLGHVEQLKVRVKELEQQLQE-----SAREAE 795
Cdd:TIGR02168  809 RAELTLLNEEAANLRERLESLErRIAATERRLEDLEeqieeLSEDIESLAAEIEELEELIEELESELEAllnerASLEEA 888
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 767969882   796 MERALLQGE------REAERALLQKEQKAvDQLQEKLVALETGIQK 835
Cdd:TIGR02168  889 LALLRSELEelseelRELESKRSELRREL-EELREKLAQLELRLEG 933
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
727-839 6.41e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 6.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882   727 RSDEENLKEECSSTESTQQEhEDAPSTKLQGEVLALEEERAQVLGHVEQLKVRVKELEQQLQE-SAREAEMERALLQGER 805
Cdd:TIGR02168  245 QEELKEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIlRERLANLERQLEELEA 323
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 767969882   806 EAERALLQKE---------QKAVDQLQEKLVALETGIQKERDK 839
Cdd:TIGR02168  324 QLEELESKLDelaeelaelEEKLEELKEELESLEAELEELEAE 366
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
754-839 6.53e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 6.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 754 KLQGEVLALEEERAQVLGHVEQLKVRVKELEQQLQESAREAEMERALLQGEREAERA-LLQKEQKAVDQLQEKLVALETG 832
Cdd:COG4717   92 ELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLeELEERLEELRELEEELEELEAE 171

                 ....*..
gi 767969882 833 IQKERDK 839
Cdd:COG4717  172 LAELQEE 178
KASH_CCD pfam14662
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ...
718-839 6.67e-03

Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.


Pssm-ID: 405365 [Multi-domain]  Cd Length: 191  Bit Score: 38.62  E-value: 6.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  718 TQRLWESMERSDEENLKEECSSTESTQQ--------------EHEDApstKLQGEVLALEEERAQVLGHVEQLKvRVKEL 783
Cdd:pfam14662  24 NSKLKATVETREETNAKLLEENLNLRKQaksqqqavqkekllEEELE---DLKLIVNSLEEARRSLLAQNKQLE-KENQS 99
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767969882  784 EQQLQESAREAEMEralLQGEREAERALLQKEQKAVDQLQEKLVALETGIQKERDK 839
Cdd:pfam14662 100 LLQEIESLQEENKK---NQAERDKLQKKKKELLKSKACLKEQLHSCEDLACNRETI 152
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
754-838 7.11e-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: 39.52  E-value: 7.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  754 KLQGEVLALEEERAQvlgHVEQLKVRVKELEQQLQESAREaemerallQGEREAERALLQKEQKAV-DQLQEKLVALETG 832
Cdd:pfam13868 127 QLREEIDEFNEEQAE---WKELEKEEEREEDERILEYLKE--------KAEREEEREAEREEIEEEkEREIARLRAQQEK 195

                  ....*.
gi 767969882  833 IQKERD 838
Cdd:pfam13868 196 AQDEKA 201
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
719-838 8.56e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 8.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882   719 QRLWESMERSDE--ENLKEECSSTESTQQEHEDApstKLQGEVLALEEERAQVLGHVEQLKVRVKELEQQLqesareaem 796
Cdd:TIGR02168  403 ERLEARLERLEDrrERLQQEIEELLKKLEEAELK---ELQAELEELEEELEELQEELERLEEALEELREEL--------- 470
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 767969882   797 erallqgeREAERALLQKEQKaVDQLQEKLVALETGIQKERD 838
Cdd:TIGR02168  471 --------EEAEQALDAAERE-LAQLQARLDSLERLQENLEG 503
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
686-830 8.66e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 8.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882 686 GEATAALALAGRRPSRGLAGASGRSSEEPGVATQRLwesmERSDEENLKEEcsstESTQQEHEDAPSTKLQGEVLALEEE 765
Cdd:COG1196  647 REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE----ELAERLAEEEL----ELEEALLAEEEEERELAEAEEERLE 718
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767969882 766 RAQVLGHVEQLKVRVKELEQQLQESAREAEMERALLQGEREAERALLQKEqkaVDQLQEKLVALE 830
Cdd:COG1196  719 EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE---LERLEREIEALG 780
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
755-839 8.86e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 8.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  755 LQGEVLALEEERAQVLGHVEQLKVRVKELEQQLQESAREAEMERALLQ--------GEREAERALLQKEQKAVDQLQEKL 826
Cdd:COG4913   615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasaereiAELEAELERLDASSDDLAALEEQL 694
                          90
                  ....*....|...
gi 767969882  827 VALETGIQKERDK 839
Cdd:COG4913   695 EELEAELEELEEE 707
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
752-826 9.45e-03

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: 37.56  E-value: 9.45e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767969882  752 STKLQGEVLALEEErAQVLghVEQLKVRVKELEQQLQESARE-AEMERALLQGEREAERALLQKEQKAVDQLQEKL 826
Cdd:pfam03938  28 FKKRQAELEAKQKE-LQKL--YEELQKDGALLEEEREEKEQElQKKEQELQQLQQKAQQELQKKQQELLQPIQDKI 100
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
657-833 9.62e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.94  E-value: 9.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  657 RQRLETILNLCAEYSRADGGPEAGELpsIGEATAALALAGRRPS--RGLAGASGRSSEEPGVatQRLWE------SMERS 728
Cdd:COG3096   475 EKAYELVCKIAGEVERSQAWQTAREL--LRRYRSQQALAQRLQQlrAQLAELEQRLRQQQNA--ERLLEefcqriGQQLD 550
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882  729 DEENLKEECSSTESTQQEHEDapstklqgEVLALEEERAQVLGHVEQLKVRVKELEQQ------LQESA-REAEMERALL 801
Cdd:COG3096   551 AAEELEELLAELEAQLEELEE--------QAAEAVEQRSELRQQLEQLRARIKELAARapawlaAQDALeRLREQSGEAL 622
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767969882  802 ---QGEREAERALLQKEQKAV---DQLQEKLVALETGI 833
Cdd:COG3096   623 adsQEVTAAMQQLLEREREATverDELAARKQALESQI 660
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
604-830 9.87e-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: 9.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882   604 VQRKLSSgdlrvpVTRERKNSITEISDNEDDLLEYHRRQRQERLREQEME-RLERQRLETILN----LCAEYSRADGgpe 678
Cdd:TIGR02169  742 LEEDLSS------LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEaRLSHSRIPEIQAelskLEEEVSRIEA--- 812
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882   679 agelpSIGEATAALAlagrrpSRGLAGASGRSSEEPGVATQRLWE---SMERSDEENLKEECSSTESTQQEHEDAPSTkL 755
Cdd:TIGR02169  813 -----RLREIEQKLN------RLTLEKEYLEKEIQELQEQRIDLKeqiKSIEKEIENLNGKKEELEEELEELEAALRD-L 880
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969882   756 QGEVLALEEERAQVLGHVEQLKVRVKELEQQLQE---------------SAREAEMERALLQGERE-AERALLQKEQKAV 819
Cdd:TIGR02169  881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKkrkrlselkaklealEEELSEIEDPKGEDEEIpEEELSLEDVQAEL 960
                          250
                   ....*....|.
gi 767969882   820 DQLQEKLVALE 830
Cdd:TIGR02169  961 QRVEEEIRALE 971
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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