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Conserved domains on  [gi|767948853|ref|XP_011514920|]
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cortactin-binding protein 2 isoform X7 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CortBP2 pfam09727
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ...
 36-180 1.05e-49

Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.


:

Pssm-ID: 462860 [Multi-domain]  Cd Length: 187  Bit Score: 173.56  E-value: 1.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   36 LSKSELRMLLSVMEGELEARDLVIEALRARR-KEVFIQERYGRFNLNDPFLALQRDYEAGAG----DKEKKPVCTNPLSI 110
Cdd:pfam09727   2 LSKDDLLKLLSILEGELQARDIVIAVLKAEKvKQLLLEARYGFKYPSDPLLALQRDSELLRDqsqdEDVYEAMYEKPLAE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  111 LEAVMAHCKKMQERMSAQLAAAESRQKK------------------------------------LEMEKLQLQALEQEHK 154
Cdd:pfam09727  82 LEKLVEKQRETQRRMLEQLAAAEKRHRRvireleeekrkhardtaqgddftyllekererlkqeLEQEKAQQKRLEKELK 161

                         170       180
                  ....*....|....*....|....*.
gi 767948853  155 KLAARLEEERGKNKQVVLMLVKECKQ 180
Cdd:pfam09727 162 KLLEKLEEELSKQKQIALLLVKERKR 187
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
705-867 2.34e-44

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 162.43  E-value: 2.34e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 705 APLAGRPTLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAA 784
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 785 AAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMY 864
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240


                 ...
gi 767948853 865 HRI 867
Cdd:COG0666  241 AGA 243
DR0291 super family cl34310
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 123-264 2.02e-12

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


The actual alignment was detected with superfamily member COG1579:

Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 68.03  E-value: 2.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 123 ERMSAQLAAAESRQKKLEME----KLQLQALEQEHKKLAARLEEERGK------NKQVVLMLvKECKQLSGKVIEEAQKL 192
Cdd:COG1579   34 AELEDELAALEARLEAAKTEledlEKEIKRLELEIEEVEARIKKYEEQlgnvrnNKEYEALQ-KEIESLKRRISDLEDEI 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767948853 193 EDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKlnREEAHTT---DLKEEIDKMRK 264
Cdd:COG1579  113 LELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE--REELAAKippELLALYERIRK 185
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 351-718 7.58e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 7.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  351 MARPGIDRQASYGDLIGASVPAFP----PPsankiEENGPST-GSTPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAPPm 425
Cdd:PHA03247 2455 FARTILGAPFSLSLLLGELFPGAPvyrrPA-----EARFPFAaGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEP- 2528

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  426 hslhspcantsLHPGLNPRIQAARFRFQGNANDPDQNGNTTQSPPSRDVS-PTSRdnlVAKQLARNTVTQALSRFTSP-Q 503
Cdd:PHA03247 2529 -----------VHPRMLTWIRGLEELASDDAGDPPPPLPPAAPPAAPDRSvPPPR---PAPRPSEPAVTSRARRPDAPpQ 2594

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  504 AGAPSRPGVPPTGDVGTHPPV----GRTSLKTHGVARVDRGNpppippKKPGLSQTPSPPHPQLKVIIDSSRASNTgAKV 579
Cdd:PHA03247 2595 SARPRAPVDDRGDPRGPAPPSplppDTHAPDPPPPSPSPAAN------EPDPHPPPTVPPPERPRDDPAPGRVSRP-RRA 2667

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  580 DNKTVASTPSSLPQGNR-------VINEENL----PKSSSPQLPPKPSIDLTVAPAGCAVSALATSQVGAWPAATPGLNQ 648
Cdd:PHA03247 2668 RRLGRAAQASSPPQRPRrraarptVGSLTSLadppPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAG 2747

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  649 PAC--SDSSLVIPTTIAFCSSINPVSASSCRP----------GASDSLLVTASGWSPSLTPLLMSG---------GPAPL 707
Cdd:PHA03247 2748 PATpgGPARPARPPTTAGPPAPAPPAAPAAGPprrltrpavaSLSESRESLPSPWDPADPPAAVLApaaalppaaSPAGP 2827

                         410
                  ....*....|.
gi 767948853  708 AGRPTLLQQAA 718
Cdd:PHA03247 2828 LPPPTSAQPTA 2838
 
Name Accession Description Interval E-value
CortBP2 pfam09727
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ...
 36-180 1.05e-49

Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.


Pssm-ID: 462860 [Multi-domain]  Cd Length: 187  Bit Score: 173.56  E-value: 1.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   36 LSKSELRMLLSVMEGELEARDLVIEALRARR-KEVFIQERYGRFNLNDPFLALQRDYEAGAG----DKEKKPVCTNPLSI 110
Cdd:pfam09727   2 LSKDDLLKLLSILEGELQARDIVIAVLKAEKvKQLLLEARYGFKYPSDPLLALQRDSELLRDqsqdEDVYEAMYEKPLAE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  111 LEAVMAHCKKMQERMSAQLAAAESRQKK------------------------------------LEMEKLQLQALEQEHK 154
Cdd:pfam09727  82 LEKLVEKQRETQRRMLEQLAAAEKRHRRvireleeekrkhardtaqgddftyllekererlkqeLEQEKAQQKRLEKELK 161

                         170       180
                  ....*....|....*....|....*.
gi 767948853  155 KLAARLEEERGKNKQVVLMLVKECKQ 180
Cdd:pfam09727 162 KLLEKLEEELSKQKQIALLLVKERKR 187
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
705-867 2.34e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 162.43  E-value: 2.34e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 705 APLAGRPTLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAA 784
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 785 AAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMY 864
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240


                 ...
gi 767948853 865 HRI 867
Cdd:COG0666  241 AGA 243
Ank_2 pfam12796
Ankyrin repeats (3 copies);
748-835 7.09e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 99.42  E-value: 7.09e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  748 LYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYdANINhAADGGQTPLYLACKNGNKECIK 827
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78


                  ....*...
gi 767948853  828 LLLEAGTN 835
Cdd:pfam12796  79 LLLEKGAD 86
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 721-867 4.70e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.64  E-value: 4.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 721 GNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTD--CVRLLLSAEAQVNAADKngftplcaaaaqghfecVELLIS 798
Cdd:PHA03100 119 NSYSIVEYLLDN-GANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR-----------------VNYLLS 180

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767948853 799 YDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHRI 867
Cdd:PHA03100 181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 37-271 1.61e-12

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: 71.64  E-value: 1.61e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853    37 SKSELRMLLSVMEGELEARDLVIEALRAR--RKEVFIQERYGRFN--LNDPFLALQRDYEAGAGDKEKkpvctnplsiLE 112
Cdd:TIGR02169  238 QKEAIERQLASLEEELEKLTEEISELEKRleEIEQLLEELNKKIKdlGEEEQLRVKEKIGELEAEIAS----------LE 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   113 AVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKL 192
Cdd:TIGR02169  308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   193 EDVMAKLEEEKKKTNELEEELS---AEKRRSTEMEAQM-------EKQLSEFDTERE--------------QLRAKLNRE 248
Cdd:TIGR02169  388 KDYREKLEKLKREINELKRELDrlqEELQRLSEELADLnaaiagiEAKINELEEEKEdkaleikkqewkleQLAADLSKY 467

                          250       260
                   ....*....|....*....|...
gi 767948853   249 EAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:TIGR02169  468 EQELYDLKEEYDRVEKELSKLQR 490
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 123-264 2.02e-12

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: 68.03  E-value: 2.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 123 ERMSAQLAAAESRQKKLEME----KLQLQALEQEHKKLAARLEEERGK------NKQVVLMLvKECKQLSGKVIEEAQKL 192
Cdd:COG1579   34 AELEDELAALEARLEAAKTEledlEKEIKRLELEIEEVEARIKKYEEQlgnvrnNKEYEALQ-KEIESLKRRISDLEDEI 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767948853 193 EDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKlnREEAHTT---DLKEEIDKMRK 264
Cdd:COG1579  113 LELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE--REELAAKippELLALYERIRK 185
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 127-271 2.88e-12

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: 70.86  E-value: 2.88e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   127 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKT 206
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL 346

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767948853   207 NELEEELSAEKRRSTEMEAQ---MEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:TIGR02168  347 EELKEELESLEAELEELEAEleeLESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 119-271 1.04e-11

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: 67.25  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  119 KKMQERMSA-QLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEergknKQVVLMLVKECKQLSGKVIE---EAQKLED 194
Cdd:pfam13868  80 EQIEEREQKrQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEK-----QRQLREEIDEFNEEQAEWKElekEEEREED 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  195 V-----MAKLEEEKKKTNELEEELSAEK-RRSTEMEAQMEKQLSEFDtEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQ 268
Cdd:pfam13868 155 ErileyLKEKAEREEEREAEREEIEEEKeREIARLRAQQEKAQDEKA-ERDELRAKLYQEEQERKERQKEREEAEKKARQ 233


                  ...
gi 767948853  269 LKR 271
Cdd:pfam13868 234 RQE 236
PTZ00121 PTZ00121
MAEBL; Provisional
 119-289 2.21e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 68.24  E-value: 2.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  119 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKqvvLMLVKECKQLSGKVIEEAQKLEDVMAK 198
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE---AEAAEEKAEAAEKKKEEAKKKADAAKK 1385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  199 LEEEKKKTNELEEELSAEKRRSTEME--AQMEKQLSEFDTEREQLR----AKLNREEAHTTD-LKEEIDKMRKMIEQLKR 271
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKkadeAKKKAEEAKKADeAKKKAEEAKKAEEAKKK 1465

                         170
                  ....*....|....*...
gi 767948853  272 GSDSKPSLSLPRKTKDRR 289
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAK 1483
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 40-271 4.74e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.88  E-value: 4.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  40 ELRMLLSVMEGELEARDLVIEALRARRKEvfiqerygrfnlndpflALQRDYEAGAGdkekkpvctnpLSILEAVMAHCK 119
Cdd:COG1196  257 ELEAELAELEAELEELRLELEELELELEE-----------------AQAEEYELLAE-----------LARLEQDIARLE 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 120 KMQERMSAQLAAAESRQKKLEMEKLQLQA----LEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDV 195
Cdd:COG1196  309 ERRRELEERLEELEEELAELEEELEELEEeleeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 196 MAKL---EEEKKKTNELEEELSAEKRRSTEMEAQM---EKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQL 269
Cdd:COG1196  389 LEALraaAELAAQLEELEEAEEALLERLERLEEELeelEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468


                 ..
gi 767948853 270 KR 271
Cdd:COG1196  469 LE 470
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
28-271 2.07e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 61.62  E-value: 2.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  28 KKEFDvDTLSK-SELRMLLSVMEGELEArdlvieaLRARRKEVfiQERYGRFNlndpflALQRDYEAGAGDKEKkpvctn 106
Cdd:PRK03918 199 EKELE-EVLREiNEISSELPELREELEK-------LEKEVKEL--EELKEEIE------ELEKELESLEGSKRK------ 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 107 plsiLEAVMAHCKKMQERMSAQLAAAESRQKklEMEKLQLQALEQEhkklaaRLEEERGKNKQVVLMLVKECKQLSgkvi 186
Cdd:PRK03918 257 ----LEEKIRELEERIEELKKEIEELEEKVK--ELKELKEKAEEYI------KLSEFYEEYLDELREIEKRLSRLE---- 320

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 187 EEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEaqmekqlsEFDTEREQLRAKLNREEAHTTDLK-EEIDKMRKM 265
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELE--------ERHELYEEAKAKKEELERLKKRLTgLTPEKLEKE 392


                 ....*.
gi 767948853 266 IEQLKR 271
Cdd:PRK03918 393 LEELEK 398
PHA03247 PHA03247
large tegument protein UL36; Provisional
 351-718 7.58e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 7.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  351 MARPGIDRQASYGDLIGASVPAFP----PPsankiEENGPST-GSTPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAPPm 425
Cdd:PHA03247 2455 FARTILGAPFSLSLLLGELFPGAPvyrrPA-----EARFPFAaGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEP- 2528

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  426 hslhspcantsLHPGLNPRIQAARFRFQGNANDPDQNGNTTQSPPSRDVS-PTSRdnlVAKQLARNTVTQALSRFTSP-Q 503
Cdd:PHA03247 2529 -----------VHPRMLTWIRGLEELASDDAGDPPPPLPPAAPPAAPDRSvPPPR---PAPRPSEPAVTSRARRPDAPpQ 2594

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  504 AGAPSRPGVPPTGDVGTHPPV----GRTSLKTHGVARVDRGNpppippKKPGLSQTPSPPHPQLKVIIDSSRASNTgAKV 579
Cdd:PHA03247 2595 SARPRAPVDDRGDPRGPAPPSplppDTHAPDPPPPSPSPAAN------EPDPHPPPTVPPPERPRDDPAPGRVSRP-RRA 2667

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  580 DNKTVASTPSSLPQGNR-------VINEENL----PKSSSPQLPPKPSIDLTVAPAGCAVSALATSQVGAWPAATPGLNQ 648
Cdd:PHA03247 2668 RRLGRAAQASSPPQRPRrraarptVGSLTSLadppPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAG 2747

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  649 PAC--SDSSLVIPTTIAFCSSINPVSASSCRP----------GASDSLLVTASGWSPSLTPLLMSG---------GPAPL 707
Cdd:PHA03247 2748 PATpgGPARPARPPTTAGPPAPAPPAAPAAGPprrltrpavaSLSESRESLPSPWDPADPPAAVLApaaalppaaSPAGP 2827

                         410
                  ....*....|.
gi 767948853  708 AGRPTLLQQAA 718
Cdd:PHA03247 2828 LPPPTSAQPTA 2838
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 712-848 7.69e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 53.09  E-value: 7.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 712 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQ-VNAADKN----GFTPLCAAAA 786
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSdlyqGETALHIAVV 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767948853 787 QGHFECVELLISYDANINHA-ADG-------------GQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVH 848
Cdd:cd22192   99 NQNLNLVRELIARGADVVSPrATGtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 367-736 5.11e-06

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 50.54  E-value: 5.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  367 GASVPAFPPPSankieenGPSTGSTPDPTSSTPPLPSNAAPPTAQTPgiAPQNSQAPPMHSLHSpcaNTSLHPglnPRIQ 446
Cdd:pfam03154 179 GAASPPSPPPP-------GTTQAATAGPTPSAPSVPPQGSPATSQPP--NQTQSTAAPHTLIQQ---TPTLHP---QRLP 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  447 AARFRFQGnandpdqngnTTQSPPSRDVSPTSRDNLVAK-QLARNTVTQALSRFTSPQAGAPSRPGVPPTGDVGTHPPVG 525
Cdd:pfam03154 244 SPHPPLQP----------MTQPPPPSQVSPQPLPQPSLHgQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGP 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  526 RTSLKTHGVARVDRGNPPPIPPKKPGLSQTPSPPHPQLKVIID-----------SSRASNTGAKVDNKTVASTPSSLPQG 594
Cdd:pfam03154 314 SPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKpppttpipqlpNPQSHKHPPHLSGPSPFQMNSNLPPP 393

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  595 NRVINEENLPKSSSPQLPPKPsidLTVAPAGcavsalatSQVGAWPAATPGLNQ-PACSDSSLVIPTTIAFCS--SINPV 671
Cdd:pfam03154 394 PALKPLSSLSTHHPPSAHPPP---LQLMPQS--------QQLPPPPAQPPVLTQsQSLPPPAASHPPTSGLHQvpSQSPF 462

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767948853  672 SASSCRPGASDSllVTASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLD 736
Cdd:pfam03154 463 PQHPFVPGGPPP--ITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALD 525
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 714-851 6.38e-06

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 50.08  E-value: 6.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  714 LQQAAAQGNVTLLSMLLNEEGLDInyscEDGHSALYSAAKNGH---TDCVRLLLSAEAQ------VNAADKNGF----TP 780
Cdd:TIGR00870  56 LFVAAIENENLELTELLLNLSCRG----AVGDTLLHAISLEYVdavEAILLHLLAAFRKsgplelANDQYTSEFtpgiTA 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  781 LCAAAAQGHFECVELLISYDANINHAADG--------------GQTPLYLACKNGNKECIKLLLEAGTNrsVKTTD--GW 844
Cdd:TIGR00870 132 LHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPAD--ILTADslGN 209


                  ....*..
gi 767948853  845 TPVHAAV 851
Cdd:TIGR00870 210 TLLHLLV 216
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 810-835 1.18e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.57  E-value: 1.18e-05
                           10        20
                   ....*....|....*....|....*.
gi 767948853   810 GQTPLYLACKNGNKECIKLLLEAGTN 835
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 129-276 1.87e-05

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 46.67  E-value: 1.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 129 LAAAESRQKKLEMEKLQLQALE---QEHKKLAARLEEERGKNKQVVLM----LVKECKQLSGKVIEEAQKLEDV------ 195
Cdd:cd00176   32 LESVEALLKKHEALEAELAAHEervEALNELGEQLIEEGHPDAEEIQErleeLNQRWEELRELAEERRQRLEEAldlqqf 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 196 MAKLEEEKKKTNELEEELSAEKRRS--TEMEAQMEKqLSEFDTEREQLRAKLNR------------EEAHTTDLKEEIDK 261
Cdd:cd00176  112 FRDADDLEQWLEEKEAALASEDLGKdlESVEELLKK-HKELEEELEAHEPRLKSlnelaeelleegHPDADEEIEEKLEE 190

                        170
                 ....*....|....*
gi 767948853 262 MRKMIEQLKRGSDSK 276
Cdd:cd00176  191 LNERWEELLELAEER 205
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 167-268 6.42e-05

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


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 43.73  E-value: 6.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   167 NKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEE-KKKTNELEEE---LSAEKRRstEMEAQMEKQLSEFDTEREQLR 242
Cdd:smart00935   5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKElQKLKEKLQKDaatLSEAARE--KKEKELQKKVQEFQRKQQKLQ 82

                           90       100
                   ....*....|....*....|....*.
gi 767948853   243 AKLNREEAhttdlkEEIDKMRKMIEQ 268
Cdd:smart00935  83 QDLQKRQQ------EELQKILDKINK 102
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
 119-168 8.71e-04

Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269834 [Multi-domain]  Cd Length: 52  Bit Score: 37.91  E-value: 8.71e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767948853 119 KKMQERMSAQlaaaESRQ-KKLEMEKL--QLQALEQEHKKLAARLEEERGKNK 168
Cdd:cd14686    4 RRERNREAAR----RSRErKKERIEELeeEVEELEEENEELKAELEELRAEVE 52
 
Name Accession Description Interval E-value
CortBP2 pfam09727
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ...
 36-180 1.05e-49

Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.


Pssm-ID: 462860 [Multi-domain]  Cd Length: 187  Bit Score: 173.56  E-value: 1.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   36 LSKSELRMLLSVMEGELEARDLVIEALRARR-KEVFIQERYGRFNLNDPFLALQRDYEAGAG----DKEKKPVCTNPLSI 110
Cdd:pfam09727   2 LSKDDLLKLLSILEGELQARDIVIAVLKAEKvKQLLLEARYGFKYPSDPLLALQRDSELLRDqsqdEDVYEAMYEKPLAE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  111 LEAVMAHCKKMQERMSAQLAAAESRQKK------------------------------------LEMEKLQLQALEQEHK 154
Cdd:pfam09727  82 LEKLVEKQRETQRRMLEQLAAAEKRHRRvireleeekrkhardtaqgddftyllekererlkqeLEQEKAQQKRLEKELK 161

                         170       180
                  ....*....|....*....|....*.
gi 767948853  155 KLAARLEEERGKNKQVVLMLVKECKQ 180
Cdd:pfam09727 162 KLLEKLEEELSKQKQIALLLVKERKR 187
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
705-867 2.34e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 162.43  E-value: 2.34e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 705 APLAGRPTLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAA 784
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 785 AAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMY 864
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240


                 ...
gi 767948853 865 HRI 867
Cdd:COG0666  241 AGA 243
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
698-931 7.90e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.81  E-value: 7.90e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 698 LLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNG 777
Cdd:COG0666   41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 778 FTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVD 857
Cdd:COG0666  121 ETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767948853 858 SLKLLMyhripAHGnsfneeesessvfdldggeespegiskpvvpADlINHANREGWTAAHIAASKGFKMLLKY 931
Cdd:COG0666  201 IVKLLL-----EAG-------------------------------AD-VNAKDNDGKTALDLAAENGNLEIVKL 237
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
712-867 7.07e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.86  E-value: 7.07e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 712 TLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFE 791
Cdd:COG0666  122 TPLHLAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767948853 792 CVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHRI 867
Cdd:COG0666  201 IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
712-931 1.28e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.53  E-value: 1.28e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 712 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFE 791
Cdd:COG0666   22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 792 CVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMyhripAHG 871
Cdd:COG0666  102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL-----EAG 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767948853 872 nsfneeesessvfdldggeespegiskpvvpADlINHANREGWTAAHIAASKG----FKMLLKY 931
Cdd:COG0666  177 -------------------------------AD-VNARDNDGETPLHLAAENGhleiVKLLLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
748-835 7.09e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 99.42  E-value: 7.09e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  748 LYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYdANINhAADGGQTPLYLACKNGNKECIK 827
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78


                  ....*...
gi 767948853  828 LLLEAGTN 835
Cdd:pfam12796  79 LLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
714-804 5.98e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 5.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  714 LQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSaEAQVNAADkNGFTPLCAAAAQGHFECV 793
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIV 77

                          90
                  ....*....|.
gi 767948853  794 ELLISYDANIN 804
Cdd:pfam12796  78 KLLLEKGADIN 88
Ank_2 pfam12796
Ankyrin repeats (3 copies);
781-867 6.18e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.25  E-value: 6.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  781 LCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSvkTTDGWTPVHAAVDTGNVDSLK 860
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78


                  ....*..
gi 767948853  861 LLMYHRI 867
Cdd:pfam12796  79 LLLEKGA 85
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
725-931 1.14e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 90.40  E-value: 1.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 725 LLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANIN 804
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 805 HAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMyhripAHGnsfneeesessvf 884
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL-----EAG------------- 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767948853 885 dldggeespegiskpvvpADlINHANREGWTAAHIAASKGF----KMLLKY 931
Cdd:COG0666  144 ------------------AD-VNAQDNDGNTPLHLAAANGNleivKLLLEA 175
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 721-867 4.70e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.64  E-value: 4.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 721 GNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTD--CVRLLLSAEAQVNAADKngftplcaaaaqghfecVELLIS 798
Cdd:PHA03100 119 NSYSIVEYLLDN-GANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR-----------------VNYLLS 180

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767948853 799 YDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHRI 867
Cdd:PHA03100 181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 732-851 6.59e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 81.16  E-value: 6.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 732 EEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQ 811
Cdd:PHA02874 112 DCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGE 191

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767948853 812 TPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAV 851
Cdd:PHA02874 192 SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 712-866 2.81e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 79.24  E-value: 2.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 712 TLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFE 791
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYA 204

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767948853 792 CVELLISYDANINHAADGGQTPLYLACKNgNKECIKLLLeagTNRSVKTTD--GWTPVHAAVDTG-NVDSLKLLMYHR 866
Cdd:PHA02874 205 CIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLI---NNASINDQDidGSTPLHHAINPPcDIDIIDILLYHK 278
PHA03095 PHA03095
ankyrin-like protein; Provisional
 713-862 3.19e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 79.30  E-value: 3.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 713 LLQQAAAQGNVTLLSM-LLNEEGLDINYSCEDGHSALYSAAKNGHTDC---VRLLLSAEAQVNAADKNGFTPL-CAAAAQ 787
Cdd:PHA03095  15 LYDYLLNASNVTVEEVrRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLhLYLYNA 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767948853 788 GHFECVELLISYDANINHAADGGQTPL--YLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVD--SLKLL 862
Cdd:PHA03095  95 TTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLL 173
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 717-866 9.54e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 77.34  E-value: 9.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 717 AAAQGNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELL 796
Cdd:PHA02875   9 AILFGELDIARRLLDI-GINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767948853 797 ISYDANINHAA-DGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHR 866
Cdd:PHA02875  88 LDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 729-863 3.34e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 76.07  E-value: 3.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 729 LLNEEGLDINYSCED-GHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAA 807
Cdd:PHA02878 152 LLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 808 DGGQTPLYLA---CKngNKECIKLLLEAGTNRSVKTT-DGWTPVHAAVDTGnvDSLKLLM 863
Cdd:PHA02878 232 KCGNTPLHISvgyCK--DYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLL 287
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 717-863 2.16e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 74.52  E-value: 2.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 717 AAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELL 796
Cdd:PLN03192 532 VASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767948853 797 ISYdANINHAADGGQTpLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLM 863
Cdd:PLN03192 611 YHF-ASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 722-865 6.63e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.22  E-value: 6.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 722 NVTLLSMLL-----NEEGLDINYSCEDGHSALYSaaknghTDCVRLLLSAEAQVNAADKN-GFTPLCAAAAQGHFECVEL 795
Cdd:PHA02878 113 NVEIFKIILtnrykNIQTIDLVYIDKKSKDDIIE------AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTEL 186

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767948853 796 LISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDT-GNVDSLKLLMYH 865
Cdd:PHA02878 187 LLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEH 257
Ank_4 pfam13637
Ankyrin repeats (many copies);
744-797 8.12e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 63.83  E-value: 8.12e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767948853  744 GHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLI 797
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 712-865 1.55e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 70.76  E-value: 1.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 712 TLLQQAAAQGNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTDCVRLL-----------------------LSAEA 768
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKH-GADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsilpipciekdmiktiLDCGI 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 769 QVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVH 848
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195

                        170
                 ....*....|....*..
gi 767948853 849 AAVDTGNVDSLKLLMYH 865
Cdd:PHA02874 196 NAAEYGDYACIKLLIDH 212
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 37-271 1.61e-12

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: 71.64  E-value: 1.61e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853    37 SKSELRMLLSVMEGELEARDLVIEALRAR--RKEVFIQERYGRFN--LNDPFLALQRDYEAGAGDKEKkpvctnplsiLE 112
Cdd:TIGR02169  238 QKEAIERQLASLEEELEKLTEEISELEKRleEIEQLLEELNKKIKdlGEEEQLRVKEKIGELEAEIAS----------LE 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   113 AVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKL 192
Cdd:TIGR02169  308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   193 EDVMAKLEEEKKKTNELEEELS---AEKRRSTEMEAQM-------EKQLSEFDTERE--------------QLRAKLNRE 248
Cdd:TIGR02169  388 KDYREKLEKLKREINELKRELDrlqEELQRLSEELADLnaaiagiEAKINELEEEKEdkaleikkqewkleQLAADLSKY 467

                          250       260
                   ....*....|....*....|...
gi 767948853   249 EAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:TIGR02169  468 EQELYDLKEEYDRVEKELSKLQR 490
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 123-264 2.02e-12

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: 68.03  E-value: 2.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 123 ERMSAQLAAAESRQKKLEME----KLQLQALEQEHKKLAARLEEERGK------NKQVVLMLvKECKQLSGKVIEEAQKL 192
Cdd:COG1579   34 AELEDELAALEARLEAAKTEledlEKEIKRLELEIEEVEARIKKYEEQlgnvrnNKEYEALQ-KEIESLKRRISDLEDEI 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767948853 193 EDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKlnREEAHTT---DLKEEIDKMRK 264
Cdd:COG1579  113 LELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE--REELAAKippELLALYERIRK 185
Ank_4 pfam13637
Ankyrin repeats (many copies);
779-830 2.31e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 62.29  E-value: 2.31e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767948853  779 TPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLL 830
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 127-271 2.88e-12

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: 70.86  E-value: 2.88e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   127 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKT 206
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL 346

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767948853   207 NELEEELSAEKRRSTEMEAQ---MEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:TIGR02168  347 EELKEELESLEAELEELEAEleeLESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
123-297 3.20e-12

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 70.18  E-value: 3.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 123 ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEE-----ERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMA 197
Cdd:COG4717   74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElreelEKLEKLLQLLPLYQELEALEAELAELPERLEELEE 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 198 KLEEEKKKTNELEEELSAEKRRSTEMEAQM-------EKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 270
Cdd:COG4717  154 RLEELRELEEELEELEAELAELQEELEELLeqlslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233

                        170       180
                 ....*....|....*....|....*..
gi 767948853 271 rgsDSKPSLSLPRKTKDRRLVSISVGT 297
Cdd:COG4717  234 ---NELEAAALEERLKEARLLLLIAAA 257
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 119-271 1.04e-11

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: 67.25  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  119 KKMQERMSA-QLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEergknKQVVLMLVKECKQLSGKVIE---EAQKLED 194
Cdd:pfam13868  80 EQIEEREQKrQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEK-----QRQLREEIDEFNEEQAEWKElekEEEREED 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  195 V-----MAKLEEEKKKTNELEEELSAEK-RRSTEMEAQMEKQLSEFDtEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQ 268
Cdd:pfam13868 155 ErileyLKEKAEREEEREAEREEIEEEKeREIARLRAQQEKAQDEKA-ERDELRAKLYQEEQERKERQKEREEAEKKARQ 233


                  ...
gi 767948853  269 LKR 271
Cdd:pfam13868 234 RQE 236
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 115-322 1.49e-11

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: 68.54  E-value: 1.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   115 MAHCKKMQERMSAQLAAAEsrqKKLEMEKLQLQALEQEHKKLAARLEEERGK---NKQVVLMLVKECKQLSGKVIEEAQK 191
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELE---KALAELRKELEELEEELEQLRKELEELSRQisaLRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   192 LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKlnREEAhtTDLKEEIDKMRKMIEQLKR 271
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL--RAEL--TLLNEEAANLRERLESLER 831

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767948853   272 GSDSKpslslprKTKDRRLVSISVGTEGTVTRSVACQTDLVTENADHMKKL 322
Cdd:TIGR02168  832 RIAAT-------ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 38-272 1.53e-11

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: 68.56  E-value: 1.53e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853    38 KSELRML---LSVMEGELEArdlVIEALRARRKEVFiQERYGRFNLNDPFLALQRDYEAGAGDKEKKPvctnplSILEAV 114
Cdd:TIGR02169  673 PAELQRLrerLEGLKRELSS---LQSELRRIENRLD-ELSQELSDASRKIGEIEKEIEQLEQEEEKLK------ERLEEL 742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   115 MAHCKKMQErmsaQLAAAESRQKKLEMEK----LQLQALEQEHKKLAARLEEERGKNKQVVLMLVKE-CKQLSGKVIEEA 189
Cdd:TIGR02169  743 EEDLSSLEQ----EIENVKSELKELEARIeeleEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEeVSRIEARLREIE 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   190 QKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQME---KQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMI 266
Cdd:TIGR02169  819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEnlnGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898


                   ....*.
gi 767948853   267 EQLKRG 272
Cdd:TIGR02169  899 RELERK 904
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 698-863 1.70e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 67.32  E-value: 1.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 698 LLMSGGPAPLAGRPTL---LQQAAAQGNVTLLSMLL--NEEGLDINYscEDGHSALYSAAKNGHTDCVRLLLSAEAQVNA 772
Cdd:PHA02875  53 LLMKHGAIPDVKYPDIeseLHDAVEEGDVKAVEELLdlGKFADDVFY--KDGMTPLHLATILKKLDIMKLLIARGADPDI 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 773 ADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDG-WTPVHAAV 851
Cdd:PHA02875 131 PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAI 210

                        170
                 ....*....|..
gi 767948853 852 DTGNVDSLKLLM 863
Cdd:PHA02875 211 ENNKIDIVRLFI 222
PTZ00121 PTZ00121
MAEBL; Provisional
 119-289 2.21e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 68.24  E-value: 2.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  119 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKqvvLMLVKECKQLSGKVIEEAQKLEDVMAK 198
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE---AEAAEEKAEAAEKKKEEAKKKADAAKK 1385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  199 LEEEKKKTNELEEELSAEKRRSTEME--AQMEKQLSEFDTEREQLR----AKLNREEAHTTD-LKEEIDKMRKMIEQLKR 271
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKkadeAKKKAEEAKKADeAKKKAEEAKKAEEAKKK 1465

                         170
                  ....*....|....*...
gi 767948853  272 GSDSKPSLSLPRKTKDRR 289
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAK 1483
Ank_2 pfam12796
Ankyrin repeats (3 copies);
814-931 3.11e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.51  E-value: 3.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  814 LYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHripahgnsfneeesessvfdldggeesp 893
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---------------------------- 52

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 767948853  894 egiskpvVPADLINHanreGWTAAHIAASKG----FKMLLKY 931
Cdd:pfam12796  53 -------ADVNLKDN----GRTALHYAARSGhleiVKLLLEK 83
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
712-814 3.52e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.98  E-value: 3.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 712 TLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFE 791
Cdd:COG0666  188 TPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAAL 266

                         90       100
                 ....*....|....*....|...
gi 767948853 792 CVELLISYDANINHAADGGQTPL 814
Cdd:COG0666  267 IVKLLLLALLLLAAALLDLLTLL 289
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 40-271 4.74e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.88  E-value: 4.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  40 ELRMLLSVMEGELEARDLVIEALRARRKEvfiqerygrfnlndpflALQRDYEAGAGdkekkpvctnpLSILEAVMAHCK 119
Cdd:COG1196  257 ELEAELAELEAELEELRLELEELELELEE-----------------AQAEEYELLAE-----------LARLEQDIARLE 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 120 KMQERMSAQLAAAESRQKKLEMEKLQLQA----LEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDV 195
Cdd:COG1196  309 ERRRELEERLEELEEELAELEEELEELEEeleeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 196 MAKL---EEEKKKTNELEEELSAEKRRSTEMEAQM---EKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQL 269
Cdd:COG1196  389 LEALraaAELAAQLEELEEAEEALLERLERLEEELeelEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468


                 ..
gi 767948853 270 KR 271
Cdd:COG1196  469 LE 470
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 730-865 8.24e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.07  E-value: 8.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 730 LNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGH-----FECVELLISYDANIN 804
Cdd:PHA03100  21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVN 100

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767948853 805 HAADGGQTPLYLA--CKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDS--LKLLMYH 865
Cdd:PHA03100 101 APDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDK 165
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 138-331 9.23e-11

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 65.90  E-value: 9.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  138 KLEMEKLQLQALEQEHKKlaarleEERGKNKQVVLMLVKeckqlsgkVIEEAQKLEDVMAKLEEEKKKTNELEEElsaEK 217
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKK------EINDKEKQVSLLLIQ--------ITEKENKMKDLTFLLEESRDKANQLEEK---TK 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  218 RRSTEMEAQMEKQlSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDSKPSLSLPRKTKDRRLVSISVGT 297
Cdd:pfam05483 279 LQDENLKELIEKK-DHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEAT 357

                         170       180       190
                  ....*....|....*....|....*....|....
gi 767948853  298 EGTVTRSVACQTDLVTENADHMKKLPLTMPVKPS 331
Cdd:pfam05483 358 TCSLEELLRTEQQRLEKNEDQLKIITMELQKKSS 391
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
 136-271 1.38e-10

Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.


Pssm-ID: 465814 [Multi-domain]  Cd Length: 117  Bit Score: 59.52  E-value: 1.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  136 QKKLEMEKLQLQALEQEHKKLAARLEeergknkqVVLMLVKECKqlsgKVIEEAQKLEDVMAKLEEEKKKTNELEEELSA 215
Cdd:pfam18595   1 SSTLAEEKEELAELERKARELQAKID--------ALQVVEKDLR----SCIKLLEEIEAELAKLEEAKKKLKELRDALEE 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767948853  216 EKRRSTEMEA---QMEKQLsefdterEQLRAKLNREEAHTtdlKEEIDKMRKMIEQLKR 271
Cdd:pfam18595  69 KEIELRELERreeRLQRQL-------ENAQEKLERLREQA---EEKREAAQARLEELRE 117
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 110-271 1.88e-10

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: 63.40  E-value: 1.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  110 ILEAVMAHCKKMQ------ERMSAQLAAAEsRQKKLEMEKLQLQALEQEHKKLAARLE---EERGKNKQVVLMLVKECKQ 180
Cdd:pfam13868  23 ERDAQIAEKKRIKaeekeeERRLDEMMEEE-RERALEEEEEKEEERKEERKRYRQELEeqiEEREQKRQEEYEEKLQERE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  181 LSGKVIEEAQkLEDVMAKLEEEKKKTNELEE--ELSAEKRRSTEMEAQMEK----QLSEFDTEREQLRAKLNREEAHTTD 254
Cdd:pfam13868 102 QMDEIVERIQ-EEDQAEAEEKLEKQRQLREEidEFNEEQAEWKELEKEEEReedeRILEYLKEKAEREEEREAEREEIEE 180

                         170
                  ....*....|....*...
gi 767948853  255 LKE-EIDKMRKMIEQLKR 271
Cdd:pfam13868 181 EKErEIARLRAQQEKAQD 198
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
137-276 2.42e-10

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 63.38  E-value: 2.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 137 KKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAE 216
Cdd:COG4372    6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767948853 217 KR---RSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDSK 276
Cdd:COG4372   86 NEqlqAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER 148
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 39-270 3.35e-10

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: 64.32  E-value: 3.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853    39 SELRMLLSVMEGELEARDLVIEAL-RARRKEVFIQErygrfNLNDPFLALQRDYEAgagDKEKkpvctnplsiLEAVMAH 117
Cdd:TIGR02169  705 DELSQELSDASRKIGEIEKEIEQLeQEEEKLKERLE-----ELEEDLSSLEQEIEN---VKSE----------LKELEAR 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   118 CKKMQERMSAQLAAAESRQKKLEMEKLQ-----LQALEQEHKKLAARLEEERGKNKQVVL---MLVKECKQLSGKVIEEA 189
Cdd:TIGR02169  767 IEELEEDLHKLEEALNDLEARLSHSRIPeiqaeLSKLEEEVSRIEARLREIEQKLNRLTLekeYLEKEIQELQEQRIDLK 846

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   190 QKLEDVMAKLEEEKKKTNELEEELsAEKRRStemEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQL 269
Cdd:TIGR02169  847 EQIKSIEKEIENLNGKKEELEEEL-EELEAA---LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922


                   .
gi 767948853   270 K 270
Cdd:TIGR02169  923 K 923
Ank_2 pfam12796
Ankyrin repeats (3 copies);
712-774 5.74e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.66  E-value: 5.74e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767948853  712 TLLQQAAAQGNVTLLSMLLNEEGLDInysCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAAD 774
Cdd:pfam12796  32 TALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 30-271 7.21e-10

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: 63.16  E-value: 7.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853    30 EFDVDtlsKSELRMLLSVMEGELEARDLVIEALRAR----RKEVFIQERYgrfnlnDPFLALQRDYEAGAGDKEKKpvct 105
Cdd:TIGR02169  167 EFDRK---KEKALEELEEVEENIERLDLIIDEKRQQlerlRREREKAERY------QALLKEKREYEGYELLKEKE---- 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   106 nplsILEavmahckKMQERMSAQLAAAESRQKKLEMEKLQL--------QALEQEHKKLAARLEEERGKNKQVVLMLVKE 177
Cdd:TIGR02169  234 ----ALE-------RQKEAIERQLASLEEELEKLTEEISELekrleeieQLLEELNKKIKDLGEEEQLRVKEKIGELEAE 302

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   178 CKQLSGKVIEEAQKLEDV---MAKLEEEKKKT----NELEEELSAEKRRstemEAQMEKQLSEFDTEREQLRAKLNREEA 250
Cdd:TIGR02169  303 IASLERSIAEKERELEDAeerLAKLEAEIDKLlaeiEELEREIEEERKR----RDKLTEEYAELKEELEDLRAELEEVDK 378

                          250       260
                   ....*....|....*....|.
gi 767948853   251 HTTDLKEEIDKMRKMIEQLKR 271
Cdd:TIGR02169  379 EFAETRDELKDYREKLEKLKR 399
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 40-274 8.14e-10

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: 63.15  E-value: 8.14e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853    40 ELRMLLSVMEGELEA-----RDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGAgdkekkpvctnpLSILEAV 114
Cdd:TIGR02168  695 ELEKALAELRKELEEleeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE------------LTELEAE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   115 MAHCKKMQERMSAQLAAAESRQKKLEME----KLQLQALEQEHKKLAARLEEERGKnkqvVLMLVKECKQLSGKVIEEAQ 190
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEAQieqlKEELKALREALDELRAELTLLNEE----AANLRERLESLERRIAATER 838

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   191 KLEDvmakLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 270
Cdd:TIGR02168  839 RLED----LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914


                   ....
gi 767948853   271 RGSD 274
Cdd:TIGR02168  915 RELE 918
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
147-272 8.53e-10

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 62.57  E-value: 8.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 147 QALE-QEHKKLAARLEEERGKNKQVVLML---VKECKQLSGKViEEAQKL-EDVMAKLEEEKKKTNELEEELSaEKRRST 221
Cdd:COG2433  380 EALEeLIEKELPEEEPEAEREKEHEERELteeEEEIRRLEEQV-ERLEAEvEELEAELEEKDERIERLERELS-EARSEE 457

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767948853 222 EMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRG 272
Cdd:COG2433  458 RREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSG 508
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 51-271 1.26e-09

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: 62.38  E-value: 1.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853    51 ELEARDLvieALRARRKEVFIQERYgrfNLNDPFLALQRDYEAGAGDKEKKpvcTNPLSILEAVMAHCKKMQERMSAQLA 130
Cdd:TIGR02168  221 ELRELEL---ALLVLRLEELREELE---ELQEELKEAEEELEELTAELQEL---EEKLEELRLEVSELEEEIEELQKELY 291

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   131 AAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmlVKECKQLSGKVIEEaqKLEDVMAKLEEEKKKTNELE 210
Cdd:TIGR02168  292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELES-----KLDELAEELAELEE--KLEELKEELESLEAELEELE 364

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767948853   211 EELSAEKRRSTEMEAQMEKQLSEFDTEREQ---LRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:TIGR02168  365 AELEELESRLEELEEQLETLRSKVAQLELQiasLNNEIERLEARLERLEDRRERLQQEIEELLK 428
PTZ00121 PTZ00121
MAEBL; Provisional
 119-321 1.48e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 62.47  E-value: 1.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  119 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLML----VKECKQLSGKVIEEAQKLED 194
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKeaeeAKKAEELKKKEAEEKKKAEE 1720

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  195 VMAKLEEEKKKTNELEEELSAEKRRSTEM--EAQMEKQLSEFDTEREQLRAKLNREEAHTtdLKEEIDKmrkmieqlkrg 272
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEEDKKKAEEAkkDEEEKKKIAHLKKEEEKKAEEIRKEKEAV--IEEELDE----------- 1787

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767948853  273 SDSKPSLSLPRKTKDRR---------------LVSISVGTEGTVTRSVACQTDLVTENADHMKK 321
Cdd:PTZ00121 1788 EDEKRRMEVDKKIKDIFdnfaniieggkegnlVINDSKEMEDSAIKEVADSKNMQLEEADAFEK 1851
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 110-268 1.85e-09

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 61.06  E-value: 1.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  110 ILEAVMAHCkkMQER---MSAQLAAAESRQKKLEMEKLQLQALEQEHKKL---AARLEEERGKNKQVVLMLVKECKQLSG 183
Cdd:pfam07888  31 LLQNRLEEC--LQERaelLQAQEAANRQREKEKERYKRDREQWERQRRELesrVAELKEELRQSREKHEELEEKYKELSA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  184 KVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEK----------QLSEFDTEREQLRAKLNREEAHTT 253
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERmkerakkagaQRKEEEAERKQLQAKLQQTEEELR 188

                         170
                  ....*....|....*
gi 767948853  254 DLKEEIDKMRKMIEQ 268
Cdd:pfam07888 189 SLSKEFQELRNSLAQ 203
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 28-270 2.05e-09

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: 61.61  E-value: 2.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853    28 KKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVfiQERYGRFNLNDPFLALQRDYEAGAGDKEkkpvcTNP 107
Cdd:TIGR02168  704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL--EERIAQLSKELTELEAEIEELEERLEEA-----EEE 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   108 LSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSgkviE 187
Cdd:TIGR02168  777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS----E 852

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   188 EAQKLEDVMAKLEEEKkktNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKlnreEAHTTDLKEEIDKMRKMIE 267
Cdd:TIGR02168  853 DIESLAAEIEELEELI---EELESELEALLNERASLEEALALLRSELEELSEELREL----ESKRSELRRELEELREKLA 925


                   ...
gi 767948853   268 QLK 270
Cdd:TIGR02168  926 QLE 928
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
28-271 2.07e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 61.62  E-value: 2.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  28 KKEFDvDTLSK-SELRMLLSVMEGELEArdlvieaLRARRKEVfiQERYGRFNlndpflALQRDYEAGAGDKEKkpvctn 106
Cdd:PRK03918 199 EKELE-EVLREiNEISSELPELREELEK-------LEKEVKEL--EELKEEIE------ELEKELESLEGSKRK------ 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 107 plsiLEAVMAHCKKMQERMSAQLAAAESRQKklEMEKLQLQALEQEhkklaaRLEEERGKNKQVVLMLVKECKQLSgkvi 186
Cdd:PRK03918 257 ----LEEKIRELEERIEELKKEIEELEEKVK--ELKELKEKAEEYI------KLSEFYEEYLDELREIEKRLSRLE---- 320

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 187 EEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEaqmekqlsEFDTEREQLRAKLNREEAHTTDLK-EEIDKMRKM 265
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELE--------ERHELYEEAKAKKEELERLKKRLTgLTPEKLEKE 392


                 ....*.
gi 767948853 266 IEQLKR 271
Cdd:PRK03918 393 LEELEK 398
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 38-267 2.80e-09

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: 61.34  E-value: 2.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853    38 KSELRMLLSVMEGELEARDLVIEALRARRKEvfIQErygrfNLNDpfLALQRDYEAGAGDKEKkpvctnplsiLEAVM-- 115
Cdd:pfam01576   70 KQELEEILHELESRLEEEEERSQQLQNEKKK--MQQ-----HIQD--LEEQLDEEEAARQKLQ----------LEKVTte 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   116 AHCKKMQER--MSAQLAAAESRQKKL--------------EMEKLQ-LQALEQEHKKLAARLEEERGKNKQVVLMLVKEC 178
Cdd:pfam01576  131 AKIKKLEEDilLLEDQNSKLSKERKLleeriseftsnlaeEEEKAKsLSKLKNKHEAMISDLEERLKKEEKGRQELEKAK 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   179 KQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQ----------MEKQLSEFDTEREQLRAKLNRE 248
Cdd:pfam01576  211 RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQknnalkkireLEAQISELQEDLESERAARNKA 290

                          250
                   ....*....|....*....
gi 767948853   249 EAHTTDLKEEIDKMRKMIE 267
Cdd:pfam01576  291 EKQRRDLGEELEALKTELE 309
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
59-270 3.18e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.85  E-value: 3.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  59 IEALRARRKEVF-----IQERYGrfNLNDPFLALQRDYEAGAGDKEKKPVCTNPLSI--LEAVMAHCKKMQERMSAQLAA 131
Cdd:PRK03918 393 LEELEKAKEEIEeeiskITARIG--ELKKEIKELKKAIEELKKAKGKCPVCGRELTEehRKELLEEYTAELKRIEKELKE 470

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 132 AESRQKKLEMEKLQLQ-ALEQE-----HKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKK 205
Cdd:PRK03918 471 IEEKERKLRKELRELEkVLKKEselikLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK 550

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 206 TNELEEELSA--EKRRSTEME-AQMEKQLSEFDTE----------------REQLRAK-----LNREEAHTTDLKEEIDK 261
Cdd:PRK03918 551 LEELKKKLAEleKKLDELEEElAELLKELEELGFEsveeleerlkelepfyNEYLELKdaekeLEREEKELKKLEEELDK 630


                 ....*....
gi 767948853 262 MRKMIEQLK 270
Cdd:PRK03918 631 AFEELAETE 639
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 40-271 4.01e-09

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 59.16  E-value: 4.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   40 ELRMLLSVMEgELEARDLVIEALRARRKEVFIQERygrfnlnDPFLALQRDYEAGAGDKEKKpvctnplsILEAVMAHCK 119
Cdd:pfam13868  99 EREQMDEIVE-RIQEEDQAEAEEKLEKQRQLREEI-------DEFNEEQAEWKELEKEEERE--------EDERILEYLK 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  120 KMQERMsaqlAAAESRQKKLEMEKlqlqalEQEHKKLAARLEEERGKNKQVVLMLVKeckqlsgKVIEEAQKLEDvmAKL 199
Cdd:pfam13868 163 EKAERE----EEREAEREEIEEEK------EREIARLRAQQEKAQDEKAERDELRAK-------LYQEEQERKER--QKE 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  200 EEEKKKTNELEEELS-------AEKRRSTEMEAQMEKQLSE-------FDTEREQLRAKLNRE--EAHTTDLKEEIDKMR 263
Cdd:pfam13868 224 REEAEKKARQRQELQqareeqiELKERRLAEEAEREEEEFErmlrkqaEDEEIEQEEAEKRRMkrLEHRRELEKQIEERE 303


                  ....*...
gi 767948853  264 KMIEQLKR 271
Cdd:pfam13868 304 EQRAAERE 311
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 721-863 4.30e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.98  E-value: 4.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 721 GNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYD 800
Cdd:PHA02874  12 GDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 801 AN-------------INHAADGG----------QTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVD 857
Cdd:PHA02874  92 VDtsilpipciekdmIKTILDCGidvnikdaelKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFD 171


                 ....*.
gi 767948853 858 SLKLLM 863
Cdd:PHA02874 172 IIKLLL 177
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 122-271 5.25e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 5.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 122 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEE 201
Cdd:COG1196  241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767948853 202 EKKKTNELEEELSAEKRRSTEMEAQM---EKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:COG1196  321 LEEELAELEEELEELEEELEELEEELeeaEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
Ank_4 pfam13637
Ankyrin repeats (many copies);
712-764 6.68e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 6.68e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767948853  712 TLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLL 764
Cdd:pfam13637   3 TALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 38-270 8.48e-09

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: 59.69  E-value: 8.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853    38 KSELRMLLSVMEGELEArdlviEALRARRKEVFIQE-RYGRFNLNDPFLALQRDYEAGAGDKEKKpvcTNPLSILEAVMA 116
Cdd:TIGR02168  241 LEELQEELKEAEEELEE-----LTAELQELEEKLEElRLEVSELEEEIEELQKELYALANEISRL---EQQKQILRERLA 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   117 HCKKMQERMSAQLAAAESR-----------QKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQV----------VLMLV 175
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKldelaeelaelEEKLEELKEELESLEAELEELEAELEELESRLEELeeqletlrskVAQLE 392

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   176 KECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEME-AQMEKQLSEFDTEREQLRAKLNREEAHTTD 254
Cdd:TIGR02168  393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREELEE 472

                          250
                   ....*....|....*.
gi 767948853   255 LKEEIDKMRKMIEQLK 270
Cdd:TIGR02168  473 AEQALDAAERELAQLQ 488
PTZ00121 PTZ00121
MAEBL; Provisional
 119-289 1.18e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.38  E-value: 1.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  119 KKMQE-RMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKqlsgKVIEEAQKLEDVMA 197
Cdd:PTZ00121 1336 KKAEEaKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK----KKAEEDKKKADELK 1411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  198 KLEEEKKKTNELEEElSAEKRRSTEMEAQME--KQLSEFDTEREQLR-----------------AKLNREEAHTTD-LKE 257
Cdd:PTZ00121 1412 KAAAAKKKADEAKKK-AEEKKKADEAKKKAEeaKKADEAKKKAEEAKkaeeakkkaeeakkadeAKKKAEEAKKADeAKK 1490

                         170       180       190
                  ....*....|....*....|....*....|..
gi 767948853  258 EIDKMRKMIEQLKRGSDSKPSLSLPRKTKDRR 289
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 781-870 1.28e-08

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.76  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 781 LCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLK 860
Cdd:PTZ00322  86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                         90
                 ....*....|
gi 767948853 861 LLMYHRIPAH 870
Cdd:PTZ00322 166 LLSRHSQCHF 175
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 127-264 1.35e-08

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: 56.47  E-value: 1.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 127 AQLAAAESRQKKLEMEklqLQALEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSGKVIEEAQKLEDVMAKLEEekKKT 206
Cdd:COG1579   17 SELDRLEHRLKELPAE---LAELEDELAALEARLEAAKTELED----LEKEIKRLELEIEEVEARIKKYEEQLGN--VRN 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767948853 207 NE----LEEELSAEKRRstemEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRK 264
Cdd:COG1579   88 NKeyeaLQKEIESLKRR----ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
110-278 1.35e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.77  E-value: 1.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  110 ILEAVMAHCKKMQErMSAQLAAAES---------RQKKLEMEKLQLQALEQEHKKLAA---RLEEERGKNKQVVLMLVKE 177
Cdd:COG4913   253 LLEPIRELAERYAA-ARERLAELEYlraalrlwfAQRRLELLEAELEELRAELARLEAeleRLEARLDALREELDELEAQ 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  178 CKQLSGKVIEEAQK--------LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREE 249
Cdd:COG4913   332 IRGNGGDRLEQLEReierlereLEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAE 411

                         170       180
                  ....*....|....*....|....*....
gi 767948853  250 AHTTDLKEEIDKMRKMIEQLKRGSDSKPS 278
Cdd:COG4913   412 AALRDLRRELRELEAEIASLERRKSNIPA 440
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 131-270 1.72e-08

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: 56.09  E-value: 1.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 131 AAESRQKKLemekLQLQALEQEhkklAARLEEERGKnkqvvlmLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELE 210
Cdd:COG1579    1 AMPEDLRAL----LDLQELDSE----LDRLEHRLKE-------LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLE 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767948853 211 EELSAEKRRSTEMEAQM-----EKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 270
Cdd:COG1579   66 LEIEEVEARIKKYEEQLgnvrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELE 130
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
49-270 1.78e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.54  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  49 EGELEARDLVIEALRARRKEVF-----------IQERYGRFNLNDpflaLQRDYEAGAGDKEKkpvctnpLSILEAVMAH 117
Cdd:PRK03918 475 ERKLRKELRELEKVLKKESELIklkelaeqlkeLEEKLKKYNLEE----LEKKAEEYEKLKEK-------LIKLKGEIKS 543

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 118 CKKMQERmsaqLAAAESRQKKLEMEklqLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIE---------- 187
Cdd:PRK03918 544 LKKELEK----LEELKKKLAELEKK---LDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLElkdaekeler 616

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 188 -------EAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEME--------AQMEKQLSEFDTEREQLRAKLNREEAHT 252
Cdd:PRK03918 617 eekelkkLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelreeyLELSRELAGLRAELEELEKRREEIKKTL 696

                        250
                 ....*....|....*...
gi 767948853 253 TDLKEEIDKMRKMIEQLK 270
Cdd:PRK03918 697 EKLKEELEEREKAKKELE 714
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 122-276 3.05e-08

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: 57.72  E-value: 3.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  122 QERMSAQLaaaESRQKKLEMEKlqlQALEQEHKKLAARLEEERG-----KNKQVVLMLV------------KECKQLSGK 184
Cdd:TIGR04523 403 QEKLNQQK---DEQIKKLQQEK---ELLEKEIERLKETIIKNNSeikdlTNQDSVKELIiknldntresleTQLKVLSRS 476

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  185 VIEEAQKLEDvmaKLEEEKKKTNELEEeLSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKM-- 262
Cdd:TIGR04523 477 INKIKQNLEQ---KQKELKSKEKELKK-LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDdf 552

                         170
                  ....*....|....*..
gi 767948853  263 ---RKMIEQLKRGSDSK 276
Cdd:TIGR04523 553 elkKENLEKEIDEKNKE 569
Ank_4 pfam13637
Ankyrin repeats (many copies);
812-862 4.09e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 4.09e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767948853  812 TPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLL 862
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
108-268 5.32e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.85  E-value: 5.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  108 LSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEH--------KKLAARLEEERGKNKQVVLMLVKECK 179
Cdd:COG4913   290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLA 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  180 QLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEkrrstemEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEI 259
Cdd:COG4913   370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA-------LAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442


                  ....*....
gi 767948853  260 DKMRKMIEQ 268
Cdd:COG4913   443 LALRDALAE 451
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
121-271 9.34e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 55.29  E-value: 9.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 121 MQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSgKVIEEAQKLEDVMAKLE 200
Cdd:COG4372   29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQ-AAQAELAQAQEELESLQ 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767948853 201 EEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:COG4372  108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 136-263 1.08e-07

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 51.07  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  136 QKKLEMEKlQLQALEQEHKKLAARLEEERGKnkqvVLMLVKECKQLSgkviEEAQKLEdvmakleeekKKTNELEEELsA 215
Cdd:pfam20492   6 REKQELEE-RLKQYEEETKKAQEELEESEET----AEELEEERRQAE----EEAERLE----------QKRQEAEEEK-E 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767948853  216 EKRRSTEMEA----QMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMR 263
Cdd:pfam20492  66 RLEESAEMEAeekeQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAR 117
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 712-851 1.25e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.45  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 712 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGH-TDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHF 790
Cdd:PHA02876 275 TPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRN 354

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767948853 791 -ECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAV 851
Cdd:PHA02876 355 kDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL 416
PTZ00121 PTZ00121
MAEBL; Provisional
 119-290 1.61e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.53  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  119 KKMQERMSAQLAAAESRQKKlEMEKLQLQALEQEHKKLAARLEEERGKnkqvvlmlVKECKqlsgKVIEEAQKLEDVMAK 198
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAK-KADEAKKKAEEAKKAEEAKKKAEEAKK--------ADEAK----KKAEEAKKADEAKKK 1491

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  199 LEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAklnrEEAHTTDLKEEIDKMRKMiEQLKRGSDSKPS 278
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA----DEAKKAEEKKKADELKKA-EELKKAEEKKKA 1566

                         170
                  ....*....|..
gi 767948853  279 LSLPRKTKDRRL 290
Cdd:PTZ00121 1567 EEAKKAEEDKNM 1578
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 48-270 1.64e-07

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: 55.57  E-value: 1.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853    48 MEGELEARDLVIEALRARRKEVFIQERYGRFNLNDpflaLQRDYE----------AGAGDKEKKpvctnpLSILEAVMAH 117
Cdd:pfam01576  775 LELDLKELEAQIDAANKGREEAVKQLKKLQAQMKD----LQRELEearasrdeilAQSKESEKK------LKNLEAELLQ 844

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   118 ckkMQErmsaQLAAAESRQKKLEMEKLQLQ-----------ALEQEHKKLAAR---LEEERGKNKQVVLML-------VK 176
Cdd:pfam01576  845 ---LQE----DLAASERARRQAQQERDELAdeiasgasgksALQDEKRRLEARiaqLEEELEEEQSNTELLndrlrksTL 917

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   177 ECKQLSGKVIEE---AQKLEDVMAKLE----EEKKKTNELEEELSAEKRRS-TEMEA---QMEKQLSEFDTEREQLRAKL 245
Cdd:pfam01576  918 QVEQLTTELAAErstSQKSESARQQLErqnkELKAKLQEMEGTVKSKFKSSiAALEAkiaQLEEQLEQESRERQAANKLV 997

                          250       260
                   ....*....|....*....|....*
gi 767948853   246 NREEAHTTDLKEEIDKMRKMIEQLK 270
Cdd:pfam01576  998 RRTEKKLKEVLLQVEDERRHADQYK 1022
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 40-271 2.40e-07

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: 55.06  E-value: 2.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853    40 ELRMLLSVMEGELEARDLVIEALRARRKEVfIQERYGRFNLNDP-FLALQRDYEAGAGDKEKKpvcTNPLSILEAVMAHC 118
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAQ-IEQLKEELKALREaLDELRAELTLLNEEAANL---RERLESLERRIAAT 836

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   119 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKnKQVVLMLVKEckqlsgkvieeaqKLEDVMAK 198
Cdd:TIGR02168  837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS-LEEALALLRS-------------ELEELSEE 902

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767948853   199 LEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNRE----EAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:TIGR02168  903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTleeaEALENKIEDDEEEARRRLKRLEN 979
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 181-275 2.56e-07

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 54.83  E-value: 2.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 181 LSGKVIEEAQ--------KLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLnREEAH- 251
Cdd:PRK00409 499 LPENIIEEAKkligedkeKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA-EKEAQq 577

                         90       100
                 ....*....|....*....|....*
gi 767948853 252 -TTDLKEEIDKMRKMIEQLKRGSDS 275
Cdd:PRK00409 578 aIKEAKKEADEIIKELRQLQKGGYA 602
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 136-276 2.69e-07

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 54.64  E-value: 2.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  136 QKKLEMEKLQLQALEQEHKKLAARLEeergkNKQvvlmlvKECKQLSGKVIEEAQKLEDVMAKLEEEKKK-----TNELE 210
Cdd:TIGR04523 245 TTEISNTQTQLNQLKDEQNKIKKQLS-----EKQ------KELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwNKELK 313

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767948853  211 EELSAEKRRSTEMEAQM---EKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDSK 276
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQIsqnNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
127-255 2.88e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.54  E-value: 2.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  127 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSGKvIEEAQKLEDVMAKLEEEKKKT 206
Cdd:COG4913   668 REIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDE----LKGEIGRLEKE-LEQAEEELDELQDRLEAAEDL 742

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 767948853  207 NELEEELSAEKRRSTEMEAQMEKQLSE-FDTEREQLRAKLNREEAHTTDL 255
Cdd:COG4913   743 ARLELRALLEERFAAALGDAVERELREnLEERIDALRARLNRAEEELERA 792
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 746-850 4.23e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 52.68  E-value: 4.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 746 SALYSAAKNGHTDCVRLLL----SAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQ-TPLYLACKN 820
Cdd:PHA02884  35 NILYSSIKFHYTDIIDAILklgaDPEAPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLH 114

                         90       100       110
                 ....*....|....*....|....*....|
gi 767948853 821 GNKECIKLLLEAGTNRSVKTTDGWTPVHAA 850
Cdd:PHA02884 115 GCLKCLEILLSYGADINIQTNDMVTPIELA 144
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 121-250 4.43e-07

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 49.53  E-value: 4.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  121 MQERMsaqlaaaesRQKKLEMEKLQLQALEQEHKklAARLEEERGKNKQvvlmlvkECKQLSgkviEEAQKLEDVMAKLE 200
Cdd:pfam20492  11 LEERL---------KQYEEETKKAQEELEESEET--AEELEEERRQAEE-------EAERLE----QKRQEAEEEKERLE 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 767948853  201 EEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLnrEEA 250
Cdd:pfam20492  69 ESAEMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEEL--EEA 116
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
111-269 5.00e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.91  E-value: 5.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 111 LEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVlMLVKECKQLSGKvIEEAQ 190
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLE-KEVKELEELKEE-IEELE 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 191 ----KLEDVMAKLEEEKKKT----NELE---EELSAEKRRSTEMEAQMEK--QLSEFdteREQLRAKLNREEAHTTDLKE 257
Cdd:PRK03918 245 keleSLEGSKRKLEEKIRELeeriEELKkeiEELEEKVKELKELKEKAEEyiKLSEF---YEEYLDELREIEKRLSRLEE 321

                        170
                 ....*....|..
gi 767948853 258 EIDKMRKMIEQL 269
Cdd:PRK03918 322 EINGIEERIKEL 333
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 51-271 5.32e-07

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: 53.59  E-value: 5.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   51 ELEARDLVIEALRARRKEVfiqERYGRFNLNDPFLALQRDYEAGAGDKEKK------------PVCTNPLSILEAVMAHC 118
Cdd:pfam17380 311 EVERRRKLEEAEKARQAEM---DRQAAIYAEQERMAMERERELERIRQEERkrelerirqeeiAMEISRMRELERLQMER 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  119 KKMQERMSAQLAAA-------ESRQKKL-----EMEKL----------QLQALEQEHKKLAARL-EEERGKNKQVVLMLV 175
Cdd:pfam17380 388 QQKNERVRQELEAArkvkileEERQRKIqqqkvEMEQIraeqeearqrEVRRLEEERAREMERVrLEEQERQQQVERLRQ 467

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  176 KECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSA---EKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHT 252
Cdd:pfam17380 468 QEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAmieEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQE 547

                         250       260
                  ....*....|....*....|
gi 767948853  253 TDLKEEI-DKMRKMIEQLKR 271
Cdd:pfam17380 548 MEERRRIqEQMRKATEERSR 567
Ank_5 pfam13857
Ankyrin repeats (many copies);
729-781 5.78e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 5.78e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767948853  729 LLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPL 781
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 752-830 5.90e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 5.90e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767948853 752 AKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLL 830
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
131-276 6.18e-07

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 52.22  E-value: 6.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 131 AAESRQKKLEMEKLQ--LQALE--QEHKKLaaRLEEERgknkqvvlMLVKECKQLSgKVIEEAQKLEDVMAKLEEEKKKT 206
Cdd:COG1340  101 LAELNKAGGSIDKLRkeIERLEwrQQTEVL--SPEEEK--------ELVEKIKELE-KELEKAKKALEKNEKLKELRAEL 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 207 NELEEELSAEKRRSTEMEAQMEK---QLSEFDTEREQLRAKlnREEAHTT-----------------------DLKEEID 260
Cdd:COG1340  170 KELRKEAEEIHKKIKELAEEAQElheEMIELYKEADELRKE--ADELHKEiveaqekadelheeiielqkelrELRKELK 247

                        170
                 ....*....|....*.
gi 767948853 261 KMRKMIEQLKRGSDSK 276
Cdd:COG1340  248 KLRKKQRALKREKEKE 263
PTZ00121 PTZ00121
MAEBL; Provisional
 119-289 6.50e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 6.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  119 KKMQERMSA-QLAAAESRQKKLEMEKLQ-LQALEQEHKKLAARLEEERgknkqvvlmlvkecKQLSGKVIEEAQKLEDvm 196
Cdd:PTZ00121 1528 KKAEEAKKAdEAKKAEEKKKADELKKAEeLKKAEEKKKAEEAKKAEED--------------KNMALRKAEEAKKAEE-- 1591

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  197 aKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTER---EQLRAKLNREEAHTTDLK--EEIDKMRKMIEQLKR 271
Cdd:PTZ00121 1592 -ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKkkvEQLKKKEAEEKKKAEELKkaEEENKIKAAEEAKKA 1670

                         170
                  ....*....|....*...
gi 767948853  272 GSDSKPSLSLPRKTKDRR 289
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEK 1688
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 122-290 7.12e-07

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: 53.26  E-value: 7.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   122 QERMSA---QLAAAESRQKKLEMEklqLQALEQEHKKLAA---RLEEERgknkQVVLMLVKECKQLSGKVIEEAQKLEDV 195
Cdd:pfam01576    4 EEEMQAkeeELQKVKERQQKAESE---LKELEKKHQQLCEeknALQEQL----QAETELCAEAEEMRARLAARKQELEEI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   196 M----AKLEEEKKKTNELEeelsAEKRRSTEMEAQMEKQLSefdtEREQLRAKLNREEAhTTDlkeeiDKMRKMIEQLKR 271
Cdd:pfam01576   77 LheleSRLEEEEERSQQLQ----NEKKKMQQHIQDLEEQLD----EEEAARQKLQLEKV-TTE-----AKIKKLEEDILL 142

                          170
                   ....*....|....*....
gi 767948853   272 GSDSKPSLSLPRKTKDRRL 290
Cdd:pfam01576  143 LEDQNSKLSKERKLLEERI 161
PHA03247 PHA03247
large tegument protein UL36; Provisional
 351-718 7.58e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 7.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  351 MARPGIDRQASYGDLIGASVPAFP----PPsankiEENGPST-GSTPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAPPm 425
Cdd:PHA03247 2455 FARTILGAPFSLSLLLGELFPGAPvyrrPA-----EARFPFAaGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEP- 2528

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  426 hslhspcantsLHPGLNPRIQAARFRFQGNANDPDQNGNTTQSPPSRDVS-PTSRdnlVAKQLARNTVTQALSRFTSP-Q 503
Cdd:PHA03247 2529 -----------VHPRMLTWIRGLEELASDDAGDPPPPLPPAAPPAAPDRSvPPPR---PAPRPSEPAVTSRARRPDAPpQ 2594

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  504 AGAPSRPGVPPTGDVGTHPPV----GRTSLKTHGVARVDRGNpppippKKPGLSQTPSPPHPQLKVIIDSSRASNTgAKV 579
Cdd:PHA03247 2595 SARPRAPVDDRGDPRGPAPPSplppDTHAPDPPPPSPSPAAN------EPDPHPPPTVPPPERPRDDPAPGRVSRP-RRA 2667

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  580 DNKTVASTPSSLPQGNR-------VINEENL----PKSSSPQLPPKPSIDLTVAPAGCAVSALATSQVGAWPAATPGLNQ 648
Cdd:PHA03247 2668 RRLGRAAQASSPPQRPRrraarptVGSLTSLadppPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAG 2747

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  649 PAC--SDSSLVIPTTIAFCSSINPVSASSCRP----------GASDSLLVTASGWSPSLTPLLMSG---------GPAPL 707
Cdd:PHA03247 2748 PATpgGPARPARPPTTAGPPAPAPPAAPAAGPprrltrpavaSLSESRESLPSPWDPADPPAAVLApaaalppaaSPAGP 2827

                         410
                  ....*....|.
gi 767948853  708 AGRPTLLQQAA 718
Cdd:PHA03247 2828 LPPPTSAQPTA 2838
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 712-848 7.69e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 53.09  E-value: 7.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 712 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQ-VNAADKN----GFTPLCAAAA 786
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSdlyqGETALHIAVV 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767948853 787 QGHFECVELLISYDANINHA-ADG-------------GQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVH 848
Cdd:cd22192   99 NQNLNLVRELIARGADVVSPrATGtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 154-258 7.78e-07

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


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 49.66  E-value: 7.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  154 KKLAARLEEERGKNKQVVLMLVKECKQ-LSGKVIEEAQK-----LEDVMAKLEEEKKKTNELEEELsAEKRRSTEmEAQ- 226
Cdd:pfam15346  22 KRVEEELEKRKDEIEAEVERRVEEARKiMEKQVLEELERereaeLEEERRKEEEERKKREELERIL-EENNRKIE-EAQr 99

                          90       100       110
                  ....*....|....*....|....*....|....
gi 767948853  227 --MEKQLSEFDTEREQLRAKLNREEAHTTDLKEE 258
Cdd:pfam15346 100 keAEERLAMLEEQRRMKEERQRREKEEEEREKRE 133
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 119-289 9.73e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 52.76  E-value: 9.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   119 KKMQE-RMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMA 197
Cdd:TIGR02169  218 KEKREyEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIG 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   198 KLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR--GSDS 275
Cdd:TIGR02169  298 ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAelEEVD 377

                          170
                   ....*....|....
gi 767948853   276 KPSLSLPRKTKDRR 289
Cdd:TIGR02169  378 KEFAETRDELKDYR 391
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 186-271 1.07e-06

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


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 48.33  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  186 IEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDT-----EREQLRA--KLNREEAHTTDLKEE 258
Cdd:pfam13863   2 LEKKREMFLVQLALDAKREEIERLEELLKQREEELEKKEQELKEDLIKFDKflkenDAKRRRAlkKAEEETKLKKEKEKE 81

                          90
                  ....*....|...
gi 767948853  259 IDKMRKMIEQLKR 271
Cdd:pfam13863  82 IKKLTAQIEELKS 94
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 145-270 1.12e-06

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: 52.65  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  145 QLQALEQEHKKLAARLEEErgknkQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKkktneleEELSAEKRRSTEME 224
Cdd:COG3096   513 RLQQLRAQLAELEQRLRQQ-----QNAERLLEEFCQRIGQQLDAAEELEELLAELEAQL-------EELEEQAAEAVEQR 580

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  225 AQMEKQLSEFDTEREQLRAK----------LNREEAHT----TDLKEEIDKMRKMIEQLK 270
Cdd:COG3096   581 SELRQQLEQLRARIKELAARapawlaaqdaLERLREQSgealADSQEVTAAMQQLLERER 640
mukB PRK04863
chromosome partition protein MukB;
145-244 1.13e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 52.65  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  145 QLQALEQEHKKLAARLEEERGKNKqvvlmLVKECKQLSGKVIEEAQKLEDVMAKLEEEKkktneleEELSAEKRRSTEME 224
Cdd:PRK04863  514 QLQQLRMRLSELEQRLRQQQRAER-----LLAEFCKRLGKNLDDEDELEQLQEELEARL-------ESLSESVSEARERR 581

                          90       100
                  ....*....|....*....|
gi 767948853  225 AQMEKQLSEFDTEREQLRAK 244
Cdd:PRK04863  582 MALRQQLEQLQARIQRLAAR 601
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 73-233 1.18e-06

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 51.73  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  73 ERYGRfnlndpflalQRDYEAGAGDKEKKPvctnplsileavmahcKKMQERMSAQL----AAAESRQKKLEMEKLQLQA 148
Cdd:PRK09510  62 EQYNR----------QQQQQKSAKRAEEQR----------------KKKEQQQAEELqqkqAAEQERLKQLEKERLAAQE 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 149 lEQEHKKLAARLEEErgKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQME 228
Cdd:PRK09510 116 -QKKQAEEAAKQAAL--KQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAA 192


                 ....*
gi 767948853 229 KQLSE 233
Cdd:PRK09510 193 AKAAA 197
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
125-270 1.32e-06

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 51.06  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 125 MSAQLAAAESRQKKLEME----KLQLQALEQEHKKLAARLEEERGKnkqvvlmlVKECKQLSGKVIEEAQKLEDVMAKLE 200
Cdd:COG1340    6 LSSSLEELEEKIEELREEieelKEKRDELNEELKELAEKRDELNAQ--------VKELREEAQELREKRDELNEKVKELK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 201 EEK----KKTNELEEEL------SAEKRRSTEMEAQMEKQLSEFdtEREQLRAKLNREE-----AHTTDLKEEIDKMRKM 265
Cdd:COG1340   78 EERdelnEKLNELREELdelrkeLAELNKAGGSIDKLRKEIERL--EWRQQTEVLSPEEekelvEKIKELEKELEKAKKA 155


                 ....*
gi 767948853 266 IEQLK 270
Cdd:COG1340  156 LEKNE 160
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
106-269 1.39e-06

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 50.21  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 106 NPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMeklQLQALEQEHKKLAARLEeergknkqvvLMLVKECKQLSGKV 185
Cdd:COG1842   23 DPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLER---QLEELEAEAEKWEEKAR----------LALEKGREDLAREA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 186 IEEAQKLEDVMAKLEEEKKKTNELEEELsaekrrsTEMEAQMEKQLSEFDTEREQLRAKLNREEA-----------HTTD 254
Cdd:COG1842   90 LERKAELEAQAEALEAQLAQLEEQVEKL-------KEALRQLESKLEELKAKKDTLKARAKAAKAqekvnealsgiDSDD 162

                        170
                 ....*....|....*
gi 767948853 255 LKEEIDKMRKMIEQL 269
Cdd:COG1842  163 ATSALERMEEKIEEM 177
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
133-270 1.58e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.99  E-value: 1.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 133 ESRQKKLEmEKLQLQALEQEHKKLAA--RLEEERGKNKQVVLM-------LVKECKQLSGKVIEEAQKLEDVMAKLEEEK 203
Cdd:PRK03918 145 ESREKVVR-QILGLDDYENAYKNLGEviKEIKRRIERLEKFIKrtenieeLIKEKEKELEEVLREINEISSELPELREEL 223

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767948853 204 KKTNELEEELsaEKRRstEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 270
Cdd:PRK03918 224 EKLEKEVKEL--EELK--EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK 286
PHA02798 PHA02798
ankyrin-like protein; Provisional
 757-863 1.65e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 51.76  E-value: 1.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 757 TDCVRLLLSAEAQVNAADKNGFTPLCAAAA-----QGHFECVELLISYDANINHAADGGQTPLYLACKNG---NKECIKL 828
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPLCTILSnikdyKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLF 130

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767948853 829 LLEAGTNRSVKTTDGWTPVHAAVDTGN---VDSLKLLM 863
Cdd:PHA02798 131 MIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLL 168
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 122-250 1.89e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 1.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 122 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERgknkqvvlmlvkecKQLSGKVIEEAQKLEDVMAKLEE 201
Cdd:COG1196  381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL--------------EELEEALAELEEEEEEEEEALEE 446

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767948853 202 EKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEA 250
Cdd:COG1196  447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
APG6_N pfam17675
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
 118-251 1.95e-06

Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.


Pssm-ID: 465452 [Multi-domain]  Cd Length: 127  Bit Score: 47.98  E-value: 1.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  118 CKKMQERMSAQLAAAES-RQ------KKLEMEKL-QLQALEQEHKKLaaRLEEERgknkqvvlmLVKECKQLSgkviEEA 189
Cdd:pfam17675   7 TDLLLEELDKQLEDAEKeRDayisflKKLEKETPeELEELEKELEKL--EKEEEE---------LLQELEELE----KER 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767948853  190 QKLEDVMAKLEEEKKKTNELEEELSAEKRrstemeaQMEKQLSEFDTEREQLRAKLNREEAH 251
Cdd:pfam17675  72 EELDAELEALEEELEALDEEEEEFWREYN-------ALQLQLLEFQDERDSLEAQYEHALNQ 126
Ank_5 pfam13857
Ankyrin repeats (many copies);
800-850 2.22e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 2.22e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767948853  800 DANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAA 850
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 39-219 2.42e-06

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: 50.92  E-value: 2.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  39 SELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRdyeagAGDKEKKPVCTNP---------LS 109
Cdd:COG4942   65 AALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYR-----LGRQPPLALLLSPedfldavrrLQ 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 110 ILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKV---I 186
Cdd:COG4942  140 YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELaelQ 219

                        170       180       190
                 ....*....|....*....|....*....|...
gi 767948853 187 EEAQKLEDVMAKLEEEKKKTNELEEELSAEKRR 219
Cdd:COG4942  220 QEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 714-799 2.59e-06

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 2.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 714 LQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECV 793
Cdd:PTZ00322  86 LCQLAASGDAVGARILL-TGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164


                 ....*.
gi 767948853 794 ELLISY 799
Cdd:PTZ00322 165 QLLSRH 170
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 119-271 2.64e-06

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


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 50.81  E-value: 2.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  119 KKMQERMSaQLAAAESRQKKLEMEKLQLQALEQEHKKL--AARL-EEERGKNK---QVVLMLVKEckqlsgkvIEEAQKL 192
Cdd:pfam15558  87 KQVIEKES-RWREQAEDQENQRQEKLERARQEAEQRKQcqEQRLkEKEEELQAlreQNSLQLQER--------LEEACHK 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  193 EDVMAKLEEEKKKTNELEEELSAEKR-RSTEMEAQMEKQLSEFDTEREQLRAKLNRE---EAHTTDLKEEIDKMRKMIEQ 268
Cdd:pfam15558 158 RQLKEREEQKKVQENNLSELLNHQARkVLVDCQAKAEELLRRLSLEQSLQRSQENYEqlvEERHRELREKAQKEEEQFQR 237


                  ...
gi 767948853  269 LKR 271
Cdd:pfam15558 238 AKW 240
KASH_CCD pfam14662
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ...
 108-270 2.83e-06

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: 49.02  E-value: 2.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  108 LSILEAVMAHCKKMQERMS---AQLAAAESRQKKLEMEKLQL--QALEQEHKKLAAR-LEEERGKNKQVVLMLVKECKQL 181
Cdd:pfam14662   7 LTCVEDLQANNQKLLQENSklkATVETREETNAKLLEENLNLrkQAKSQQQAVQKEKlLEEELEDLKLIVNSLEEARRSL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  182 SGK---VIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEE 258
Cdd:pfam14662  87 LAQnkqLEKENQSLLQEIESLQEENKKNQAERDKLQKKKKELLKSKACLKEQLHSCEDLACNRETILIEKTTQIEELKST 166

                         170
                  ....*....|..
gi 767948853  259 IDKMRKMIEQLK 270
Cdd:pfam14662 167 VEEYSSIEEELR 178
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 123-270 3.23e-06

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: 51.33  E-value: 3.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   123 ERMSAQLAAAESRQKKLEMEKlqlQALEQEHKKLAARLEEERG--KNKQVVLMLVKECK---------------QLSGKV 185
Cdd:pfam01576  920 EQLTTELAAERSTSQKSESAR---QQLERQNKELKAKLQEMEGtvKSKFKSSIAALEAKiaqleeqleqesrerQAANKL 996

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   186 IEEAQK-LEDVMAKLEEEKKKTNELEEElsAEKrrSTEMEAQMEKQLSEfdTEREQLRA-----KLNREeahTTDLKEEI 259
Cdd:pfam01576  997 VRRTEKkLKEVLLQVEDERRHADQYKDQ--AEK--GNSRMKQLKRQLEE--AEEEASRAnaarrKLQRE---LDDATESN 1067

                          170
                   ....*....|.
gi 767948853   260 DKMRKMIEQLK 270
Cdd:pfam01576 1068 ESMNREVSTLK 1078
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
119-254 3.38e-06

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 49.91  E-value: 3.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 119 KKMQERMSAQLAAAESRQKKLEME------KLQLQALEQEHKKLAARLEE---ERGKNKQVVLMLVKECKQLSGKVIEEA 189
Cdd:COG1340  143 KELEKELEKAKKALEKNEKLKELRaelkelRKEAEEIHKKIKELAEEAQElheEMIELYKEADELRKEADELHKEIVEAQ 222

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767948853 190 QKLEDVMAKLEEEKKKTNELEEELSaeKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTD 254
Cdd:COG1340  223 EKADELHEEIIELQKELRELRKELK--KLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKLTTE 285
PRK12704 PRK12704
phosphodiesterase; Provisional
 126-271 4.19e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 50.55  E-value: 4.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 126 SAQLAAAESRQKK-LEMEKLQLQALEQEhKKLAARLEEERGKNKqvvlmLVKECKQLSGKVIEEAQKLEDVMAKLEEEKK 204
Cdd:PRK12704  30 EAKIKEAEEEAKRiLEEAKKEAEAIKKE-ALLEAKEEIHKLRNE-----FEKELRERRNELQKLEKRLLQKEENLDRKLE 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767948853 205 KTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNR------EEAhttdlKEEIdkMRKMIEQLKR 271
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisgltaEEA-----KEIL--LEKVEEEARH 169
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 127-271 4.89e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 4.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 127 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmlvkecKQLSGKVIEEAQKLEDVMAKLEEEKKKT 206
Cdd:COG1196  639 AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL---------EELAERLAEEELELEEALLAEEEEEREL 709

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767948853 207 NELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:COG1196  710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 135-269 4.91e-06

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 47.34  E-value: 4.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  135 RQKKLEMEKLQLQALEQEhkklaarlEEERgknkqvvlmLVKEckQLSGKVIEEAQKLEDVMAKLEEEKKKTnelEEELS 214
Cdd:pfam05672  21 RQAREQREREEQERLEKE--------EEER---------LRKE--ELRRRAEEERARREEEARRLEEERRRE---EEERQ 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767948853  215 AEKRRSTEMEAQMEKQlsefdterEQLRAKLNREEAHTTdLKEEIDKMRKMIEQL 269
Cdd:pfam05672  79 RKAEEEAEEREQREQE--------EQERLQKQKEEAEAK-AREEAERQRQEREKI 124
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 367-736 5.11e-06

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 50.54  E-value: 5.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  367 GASVPAFPPPSankieenGPSTGSTPDPTSSTPPLPSNAAPPTAQTPgiAPQNSQAPPMHSLHSpcaNTSLHPglnPRIQ 446
Cdd:pfam03154 179 GAASPPSPPPP-------GTTQAATAGPTPSAPSVPPQGSPATSQPP--NQTQSTAAPHTLIQQ---TPTLHP---QRLP 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  447 AARFRFQGnandpdqngnTTQSPPSRDVSPTSRDNLVAK-QLARNTVTQALSRFTSPQAGAPSRPGVPPTGDVGTHPPVG 525
Cdd:pfam03154 244 SPHPPLQP----------MTQPPPPSQVSPQPLPQPSLHgQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGP 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  526 RTSLKTHGVARVDRGNPPPIPPKKPGLSQTPSPPHPQLKVIID-----------SSRASNTGAKVDNKTVASTPSSLPQG 594
Cdd:pfam03154 314 SPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKpppttpipqlpNPQSHKHPPHLSGPSPFQMNSNLPPP 393

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  595 NRVINEENLPKSSSPQLPPKPsidLTVAPAGcavsalatSQVGAWPAATPGLNQ-PACSDSSLVIPTTIAFCS--SINPV 671
Cdd:pfam03154 394 PALKPLSSLSTHHPPSAHPPP---LQLMPQS--------QQLPPPPAQPPVLTQsQSLPPPAASHPPTSGLHQvpSQSPF 462

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767948853  672 SASSCRPGASDSllVTASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLD 736
Cdd:pfam03154 463 PQHPFVPGGPPP--ITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALD 525
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 119-276 5.56e-06

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 50.49  E-value: 5.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  119 KKMQERMSAQLAAAESR----QKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmLVKE-------CKQLSGKVIE 187
Cdd:pfam05483  91 KKWKVSIEAELKQKENKlqenRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKD----LIKEnnatrhlCNLLKETCAR 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  188 EAQKledvMAKLEEEKKKTNELEEELSaekrrstemeAQMEKQLSEFDTEREQlrAKLNREEAHTTdLKEEIDKMRKMIE 267
Cdd:pfam05483 167 SAEK----TKKYEYEREETRQVYMDLN----------NNIEKMILAFEELRVQ--AENARLEMHFK-LKEDHEKIQHLEE 229


                  ....*....
gi 767948853  268 QLKRGSDSK 276
Cdd:pfam05483 230 EYKKEINDK 238
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
146-271 5.68e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 5.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 146 LQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEA 225
Cdd:COG4717   44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767948853 226 QmeKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:COG4717  124 L--LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEE 167
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 713-862 5.68e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.06  E-value: 5.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 713 LLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFEC 792
Cdd:PHA02876 148 LIKERIQQDELLIAEMLL-EGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDT 226

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767948853 793 VELLISYDANINHaadgGQTPLYLACKNGNKECIKLLLEAGTnrSVKTTDGW--TPVHAAVDTGNVDSL--KLL 862
Cdd:PHA02876 227 IKAIIDNRSNINK----NDLSLLKAIRNEDLETSLLLYDAGF--SVNSIDDCknTPLHHASQAPSLSRLvpKLL 294
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 151-270 5.76e-06

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: 49.21  E-value: 5.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  151 QEHKKLAARLEEERGKNKQVVLMLVKECKqlSGKVIEEA-----QKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEA 225
Cdd:pfam02841 155 EERDKLEAKYNQVPRKGVKAEEVLQEFLQ--SKEAVEEAilqtdQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQ 232

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 767948853  226 QMEKQLSEFDTEREQLRAKLNREEAHttdLKEEIDKM--RKMIEQLK 270
Cdd:pfam02841 233 MMEAQERSYQEHVKQLIEKMEAEREQ---LLAEQERMleHKLQEQEE 276
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 729-805 6.05e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.66  E-value: 6.05e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767948853 729 LLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINH 805
Cdd:PHA03100 177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 117-289 6.27e-06

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 50.11  E-value: 6.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  117 HCKKMQERMSAQLAAAESRQKKL--EMEKLQlQALEQEHKKLAARL---EEERGKNKQVVLMLVKECKQLSGKVIEEAQK 191
Cdd:pfam05483 524 NCKKQEERMLKQIENLEEKEMNLrdELESVR-EEFIQKGDEVKCKLdksEENARSIEYEVLKKEKQMKILENKCNNLKKQ 602

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  192 LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:pfam05483 603 IENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKA 682

                         170
                  ....*....|....*...
gi 767948853  272 GSDSKPSLslpRKTKDRR 289
Cdd:pfam05483 683 IADEAVKL---QKEIDKR 697
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 714-851 6.38e-06

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 50.08  E-value: 6.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  714 LQQAAAQGNVTLLSMLLNEEGLDInyscEDGHSALYSAAKNGH---TDCVRLLLSAEAQ------VNAADKNGF----TP 780
Cdd:TIGR00870  56 LFVAAIENENLELTELLLNLSCRG----AVGDTLLHAISLEYVdavEAILLHLLAAFRKsgplelANDQYTSEFtpgiTA 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  781 LCAAAAQGHFECVELLISYDANINHAADG--------------GQTPLYLACKNGNKECIKLLLEAGTNrsVKTTD--GW 844
Cdd:TIGR00870 132 LHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPAD--ILTADslGN 209


                  ....*..
gi 767948853  845 TPVHAAV 851
Cdd:TIGR00870 210 TLLHLLV 216
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 132-271 6.74e-06

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: 50.07  E-value: 6.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   132 AESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIE--------------EAQKLEDVMA 197
Cdd:TIGR02169  665 GILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEiekeieqleqeeekLKERLEELEE 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   198 KLEeekkktnELEEELSAEKRRSTEMEA---QMEKQLSEFDTEREQLRAKLNRE-----EAHTTDLKEEIDKMRKMIEQL 269
Cdd:TIGR02169  745 DLS-------SLEQEIENVKSELKELEArieELEEDLHKLEEALNDLEARLSHSripeiQAELSKLEEEVSRIEARLREI 817


                   ..
gi 767948853   270 KR 271
Cdd:TIGR02169  818 EQ 819
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 123-274 6.99e-06

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: 50.17  E-value: 6.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   123 ERMSAQLAAaesrqKKLEMEKLqLQALEqehkklaARLEEERGKNKQvvlmLVKECKQLSGKVI--------EEA--QKL 192
Cdd:pfam01576   60 EEMRARLAA-----RKQELEEI-LHELE-------SRLEEEEERSQQ----LQNEKKKMQQHIQdleeqldeEEAarQKL 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   193 --EDV-----MAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDL-----KEEid 260
Cdd:pfam01576  123 qlEKVtteakIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLeerlkKEE-- 200

                          170
                   ....*....|....
gi 767948853   261 KMRKMIEQLKRGSD 274
Cdd:pfam01576  201 KGRQELEKAKRKLE 214
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
127-271 7.40e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 7.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 127 AQLAAAESRQKKLEmEKLQLQALEQEHKKL--------------AARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKL 192
Cdd:COG4717  347 EELQELLREAEELE-EELQLEELEQEIAALlaeagvedeeelraALEQAEEYQELKEELEELEEQLEELLGELEELLEAL 425

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 193 --EDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEK-----QLSEFDTEREQLRAKLNR--EEAHTTDLKEEIdkMR 263
Cdd:COG4717  426 deEELEEELEELEEELEELEEELEELREELAELEAELEQleedgELAELLQELEELKAELRElaEEWAALKLALEL--LE 503


                 ....*...
gi 767948853 264 KMIEQLKR 271
Cdd:COG4717  504 EAREEYRE 511
PHA03247 PHA03247
large tegument protein UL36; Provisional
 368-720 1.05e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  368 ASVPAFPPPSANKIEENGPStGSTPDPTSSTPPlPSNAAPPTAQTPGIAPQNSQAPPMHSLHSPCANTSLHPGLNPRIQA 447
Cdd:PHA03247 2586 ARRPDAPPQSARPRAPVDDR-GDPRGPAPPSPL-PPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSR 2663

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  448 AR-FRFQGNANDPdqngnttQSPPSRDVSPTSRDNLVA-KQLAR---------NTVTQALSRFTSPQAGAPSRPGVPPTG 516
Cdd:PHA03247 2664 PRrARRLGRAAQA-------SSPPQRPRRRAARPTVGSlTSLADpppppptpePAPHALVSATPLPPGPAAARQASPALP 2736

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  517 DVGTHPPVGRTSLKTHGVARVDRGNPPPIPPKKPGLSQTPSPPHPQLKVIIDSSRASNTGAKVDNKTVASTPSSLPQGNR 596
Cdd:PHA03247 2737 AAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAA 2816

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  597 VINEENLPkssSPQLPPKPSIdLTVAPAGCAVSALATSQVGAWPAATPGLNQPACSDSSLVIPTTiafcsSINPVSASSC 676
Cdd:PHA03247 2817 ALPPAASP---AGPLPPPTSA-QPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAA-----PARPPVRRLA 2887

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 767948853  677 RPGASDSllvTASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQ 720
Cdd:PHA03247 2888 RPAVSRS---TESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ 2928
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 118-275 1.08e-05

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 49.30  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  118 CKKMQERMSAQLAAAES--------RQKKLEMEKLQLQALEQEHKKLAARLEEERGKN--KQVVLMLVKE---CKQLSGK 184
Cdd:pfam05622 213 YKKLEEKLEALQKEKERliierdtlRETNEELRCAQLQQAELSQADALLSPSSDPGDNlaAEIMPAEIREkliRLQHENK 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  185 VIEEAQ------KLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQME---KQLSEFDTERE---QLRAKLNREEAHT 252
Cdd:pfam05622 293 MLRLGQegsyreRLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEelqKALQEQGSKAEdssLLKQKLEEHLEKL 372

                         170       180
                  ....*....|....*....|...
gi 767948853  253 TDLKEEIDKMRKMIEQLKRGSDS 275
Cdd:pfam05622 373 HEAQSELQKKKEQIEELEPKQDS 395
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 810-835 1.18e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.57  E-value: 1.18e-05
                           10        20
                   ....*....|....*....|....*.
gi 767948853   810 GQTPLYLACKNGNKECIKLLLEAGTN 835
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 98-320 1.22e-05

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: 49.27  E-value: 1.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853    98 KEKKPVCTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVK- 176
Cdd:TIGR00606  216 KEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKv 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   177 ------ECKQL----SGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEK---QLSEFDTERE--QL 241
Cdd:TIGR00606  296 fqgtdeQLNDLyhnhQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRhqeHIRARDSLIQslAT 375

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   242 RAKLNREEaHTTDLKEEID-----KMRKMIEQLKRGSDSKPSLSLPRKTKDRRLVSISVGTEGtVTRSVACQTDLVTENA 316
Cdd:TIGR00606  376 RLELDGFE-RGPFSERQIKnfhtlVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKG-LGRTIELKKEILEKKQ 453


                   ....
gi 767948853   317 DHMK 320
Cdd:TIGR00606  454 EELK 457
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 29-266 1.27e-05

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 49.45  E-value: 1.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853    29 KEFDVDTLSKsELRMLLSVMEGELEARDlviEALRARRKEV-FIQERYGRFnlndpflaLQRDYEAGAGDKEKKPVCTNP 107
Cdd:pfam12128  288 LNQLLRTLDD-QWKEKRDELNGELSAAD---AAVAKDRSELeALEDQHGAF--------LDADIETAAADQEQLPSWQSE 355

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   108 LSILEAVMA----------------------HCKKMQERMSAQLAAA-ESRQKKLEMEKLQLQALEQE-HKKLAARLEEE 163
Cdd:pfam12128  356 LENLEERLKaltgkhqdvtakynrrrskikeQNNRDIAGIKDKLAKIrEARDRQLAVAEDDLQALESElREQLEAGKLEF 435

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   164 RGKNKQVVLMLVKECKQLSGKVIEEAQKLEdvmakLEEEKKKTNELEEELsaEKRRSTEMEAQMEkqLSEFDTEREQLRA 243
Cdd:pfam12128  436 NEEEYRLKSRLGELKLRLNQATATPELLLQ-----LENFDERIERAREEQ--EAANAEVERLQSE--LRQARKRRDQASE 506

                          250       260
                   ....*....|....*....|...
gi 767948853   244 KLNREEAHTTDLKEEIDKMRKMI 266
Cdd:pfam12128  507 ALRQASRRLEERQSALDELELQL 529
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
127-264 1.28e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  127 AQLAAAESRQKKLEME----KLQLQALEQEHKKLAARLE-----EERGKNKQVVLMLVKECKQLSgKVIEEAQKLEDVMA 197
Cdd:COG4913   610 AKLAALEAELAELEEElaeaEERLEALEAELDALQERREalqrlAEYSWDEIDVASAEREIAELE-AELERLDASSDDLA 688

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767948853  198 KLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNR-EEAHTTDLKEEIDKMRK 264
Cdd:COG4913   689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaEDLARLELRALLEERFA 756
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 114-270 1.31e-05

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 49.29  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  114 VMAHCKKMQERMSA-QLAAAESRQKKLEMEKLQLQaleqehkKLAArleEERGKNKQVVLmlvKECKQLSGKVIEEA-QK 191
Cdd:pfam05911   5 VKQHAKVAEEAVSGwEKAEAEALALKQQLESVTLQ-------KLTA---EERAAHLDGAL---KECMQQLRNVKEEQeQK 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  192 LEDV-MAKLEEEKKKTNELEEELSAEKRRSTEMEAQmEKQLSEFDTEREQLRAKLNRE----EAHTTDLKEEIDKMRKMI 266
Cdd:pfam05911  72 IHDVvLKKTKEWEKIKAELEAKLVETEQELLRAAAE-NDALSRSLQERENLLMKLSEEksqaEAEIEALKSRLESCEKEI 150


                  ....
gi 767948853  267 EQLK 270
Cdd:pfam05911 151 NSLK 154
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 133-271 1.32e-05

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 49.20  E-value: 1.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   133 ESRQKKLEMEKLQLQALEQEHKK--LAAR---LEEERGKNKQVVLMLVKECKQLSGKVIE-EAQKLEDVMAKLEEEKKKT 206
Cdd:pfam02463  202 LKEQAKKALEYYQLKEKLELEEEylLYLDylkLNEERIDLLQELLRDEQEEIESSKQEIEkEEEKLAQVLKENKEEEKEK 281

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767948853   207 NELEEELS--AEKRRSTEMEAQMEKQLSEFDTEREQL-RAKLNREEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:pfam02463  282 KLQEEELKllAKEEEELKSELLKLERRKVDDEEKLKEsEKEKKKAEKELKKEKEEIEELEKELKELEI 349
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 776-804 1.36e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.57  E-value: 1.36e-05
                           10        20
                   ....*....|....*....|....*....
gi 767948853   776 NGFTPLCAAAAQGHFECVELLISYDANIN 804
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 119-277 1.49e-05

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: 48.22  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 119 KKMQERMSAQLAAAESRQKKLEMEK----LQLQALEQ----------------------------EHKKLAARLEEER-- 164
Cdd:COG4942   26 EAELEQLQQEIAELEKELAALKKEEkallKQLAALERriaalarriraleqelaaleaelaelekEIAELRAELEAQKee 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 165 -----------GKNKQVVLML------------------VKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSA 215
Cdd:COG4942  106 laellralyrlGRQPPLALLLspedfldavrrlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767948853 216 EKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDSKP 277
Cdd:COG4942  186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 776-804 1.56e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 1.56e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 767948853  776 NGFTPL-CAAAAQGHFECVELLISYDANIN 804
Cdd:pfam00023   1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVN 30
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
159-271 1.74e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.97  E-value: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 159 RLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNE-----------LEEELSAEKRRSTEMEAQM 227
Cdd:COG4372    3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREeleqareeleqLEEELEQARSELEQLEEEL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767948853 228 E---KQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:COG4372   83 EelnEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQ 129
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 111-431 1.80e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.29  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 111 LEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSG------- 183
Cdd:COG3883   32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYldvllgs 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 184 -------------KVIEEAQKleDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEA 250
Cdd:COG3883  112 esfsdfldrlsalSKIADADA--DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 251 httDLKEEIDKMRKMIEQLKRGSDSKPSLSLPRKTKDRRLVSISVGTEGTVTRSVACQTDLVTEnadhmkklpltmpvkp 330
Cdd:COG3883  190 ---EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG---------------- 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 331 stGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPSANKIEENGPSTGSTPDPTSSTPPLPSNAAPPTA 410
Cdd:COG3883  251 --AAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASA 328

                        330       340
                 ....*....|....*....|.
gi 767948853 411 QTPGIAPQNSQAPPMHSLHSP 431
Cdd:COG3883  329 GGGGGSGGGGGSSGGGSGGGG 349
PHA03095 PHA03095
ankyrin-like protein; Provisional
 722-870 1.82e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.48  E-value: 1.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 722 NVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTD--CVRLLLSAEAQVNAADKNGFTPLCAAAAqgHFECVELLISY 799
Cdd:PHA03095 166 NVELLRLLI-DAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMAT--GSSCKRSLVLP 242

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767948853 800 ----DANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHRIPAH 870
Cdd:PHA03095 243 lliaGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 129-276 1.87e-05

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 46.67  E-value: 1.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 129 LAAAESRQKKLEMEKLQLQALE---QEHKKLAARLEEERGKNKQVVLM----LVKECKQLSGKVIEEAQKLEDV------ 195
Cdd:cd00176   32 LESVEALLKKHEALEAELAAHEervEALNELGEQLIEEGHPDAEEIQErleeLNQRWEELRELAEERRQRLEEAldlqqf 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 196 MAKLEEEKKKTNELEEELSAEKRRS--TEMEAQMEKqLSEFDTEREQLRAKLNR------------EEAHTTDLKEEIDK 261
Cdd:cd00176  112 FRDADDLEQWLEEKEAALASEDLGKdlESVEELLKK-HKELEEELEAHEPRLKSlnelaeelleegHPDADEEIEEKLEE 190

                        170
                 ....*....|....*
gi 767948853 262 MRKMIEQLKRGSDSK 276
Cdd:cd00176  191 LNERWEELLELAEER 205
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 119-270 2.12e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.48  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  119 KKMQERMSAQLaaaESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKEckQLsgKVIEEaqKLEDVMAK 198
Cdd:TIGR04523 259 KDEQNKIKKQL---SEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKS--EL--KNQEK--KLEEIQNQ 329

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767948853  199 LEEEKKKTNELEEELSaekrrstemeaQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 270
Cdd:TIGR04523 330 ISQNNKIISQLNEQIS-----------QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 123-269 2.16e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 2.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 123 ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEE 202
Cdd:COG1196  654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 203 KKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNR---------------EEAHTT------DLKEEIDK 261
Cdd:COG1196  734 REELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllaieeyeelEERYDFlseqreDLEEARET 813


                 ....*...
gi 767948853 262 MRKMIEQL 269
Cdd:COG1196  814 LEEAIEEI 821
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 111-264 2.21e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 2.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   111 LEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEErgknKQVVLMLVKECKQlsgKVIEEAQ 190
Cdd:TIGR02168  896 LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE----YSLTLEEAEALEN---KIEDDEE 968

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   191 KLEDVMAKLEEEKKK---TNEL-EEELSAEKRRSTEMEAQMEkqlsEFDTEREQLR---AKLNREEahTTDLKEEIDKMR 263
Cdd:TIGR02168  969 EARRRLKRLENKIKElgpVNLAaIEEYEELKERYDFLTAQKE----DLTEAKETLEeaiEEIDREA--RERFKDTFDQVN 1042


                   .
gi 767948853   264 K 264
Cdd:TIGR02168 1043 E 1043
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 64-270 2.34e-05

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: 48.43  E-value: 2.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853    64 ARRKEVFIQERygrfNLNDPFLALQRDYEAgagDKEKKPVCTNPLSILEAVMAHCKKMQERMSA---QLAAAESrQKKLE 140
Cdd:TIGR00618  365 TSIREISCQQH----TLTQHIHTLQQQKTT---LTQKLQSLCKELDILQREQATIDTRTSAFRDlqgQLAHAKK-QQELQ 436

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   141 MEKLQLQAL------------EQEHKKLAARLEEERGK--NKQVVLMLVKECKQLSGKVIEEAQ---------------- 190
Cdd:TIGR00618  437 QRYAELCAAaitctaqcekleKIHLQESAQSLKEREQQlqTKEQIHLQETRKKAVVLARLLELQeepcplcgscihpnpa 516

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   191 ---------------KLEDVMAKLEEEKKKTnelEEELSAEKRRSTEMEAQMEkqlsEFDTEREQLRAKLNReeahttdL 255
Cdd:TIGR00618  517 rqdidnpgpltrrmqRGEQTYAQLETSEEDV---YHQLTSERKQRASLKEQMQ----EIQQSFSILTQCDNR-------S 582

                          250
                   ....*....|....*
gi 767948853   256 KEEIDKMRKMIEQLK 270
Cdd:TIGR00618  583 KEDIPNLQNITVRLQ 597
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 134-270 2.45e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 48.18  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  134 SRQKKLEMEKLQLQALEQEHKKLAARLEE--ERGKNKQVVLMLVKeckqlsgKVIEEAQKLEDvmakleeEKKKTNELEE 211
Cdd:pfam05483 367 TEQQRLEKNEDQLKIITMELQKKSSELEEmtKFKNNKEVELEELK-------KILAEDEKLLD-------EKKQFEKIAE 432

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767948853  212 ELSAEKRRSTEMEAQMEKQLSEFDTereQLRAKLNREEAHTT---DLKEEIDKmrkmiEQLK 270
Cdd:pfam05483 433 ELKGKEQELIFLLQAREKEIHDLEI---QLTAIKTSEEHYLKeveDLKTELEK-----EKLK 486
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 787-866 2.58e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.14  E-value: 2.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 787 QGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHR 866
Cdd:PHA02876 155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
190-290 2.82e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 47.21  E-value: 2.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 190 QKLEDVMAKLEEEKKKTNELEEELS--AEKRRS-----TEMEAQMEKQLSEFDTEREQLR-AKLNREEahttdLKEEIDK 261
Cdd:COG1340   15 EKIEELREEIEELKEKRDELNEELKelAEKRDElnaqvKELREEAQELREKRDELNEKVKeLKEERDE-----LNEKLNE 89

                         90       100
                 ....*....|....*....|....*....
gi 767948853 262 MRKMIEQLKRGSDSKPSLSLPRKTKDRRL 290
Cdd:COG1340   90 LREELDELRKELAELNKAGGSIDKLRKEI 118
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 119-301 2.89e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 2.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 119 KKMQERMSAQLAAAESRQKKLEMEKLQ-LQALEQEHKKLAARLEEERGKNKQVVLMLVKEckqlsgkvIEEAQKLEDVMA 197
Cdd:COG1196  353 LEEAEAELAEAEEALLEAEAELAEAEEeLEELAEELLEALRAAAELAAQLEELEEAEEAL--------LERLERLEEELE 424

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 198 KLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMR---KMIEQLKRGSD 274
Cdd:COG1196  425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAarlLLLLEAEADYE 504

                        170       180
                 ....*....|....*....|....*...
gi 767948853 275 SKPSLSLPRKTKD-RRLVSISVGTEGTV 301
Cdd:COG1196  505 GFLEGVKAALLLAgLRGLAGAVAVLIGV 532
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 87-271 3.03e-05

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 47.76  E-value: 3.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   87 LQRDYEAGAGDKEKKPVCTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKL-QLQALEQEHKKLAARLEEERG 165
Cdd:pfam05622 249 LQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLtELQQLLEDANRRKNELETQNR 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  166 KNKQVVLMLVKECKQLSGKVIEEAQKLEDVMA---KLEEEKKKTNELEEELSAEKRRSTEMEAqmeKQLSEFDTEREQLR 242
Cdd:pfam05622 329 LANQRILELQQQVEELQKALQEQGSKAEDSSLlkqKLEEHLEKLHEAQSELQKKKEQIEELEP---KQDSNLAQKIDELQ 405

                         170       180
                  ....*....|....*....|....*....
gi 767948853  243 AKLNREEahttdlkeeiDKMRKMIEQLKR 271
Cdd:pfam05622 406 EALRKKD----------EDMKAMEERYKK 424
PTZ00121 PTZ00121
MAEBL; Provisional
 92-287 3.05e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 3.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   92 EAGAGDKEKKPVCTNPLSilEAVMAHCKKMQERMSAqlaaaESRQKKLEMEKLqlqalEQEHKKLAARLEEERGKnkqvv 171
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFE--EARMAHFARRQAAIKA-----EEARKADELKKA-----EEKKKADEAKKAEEKKK----- 1303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  172 lmlvkeckqlsgkvIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEA- 250
Cdd:PTZ00121 1304 --------------ADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAa 1369

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 767948853  251 --HTTDLKEEIDKMRKMIEQLKRGSDSKPSLSLPRKTKD 287
Cdd:PTZ00121 1370 ekKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 122-264 3.35e-05

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: 48.04  E-value: 3.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   122 QERMSAQLAAAESRQKKLEMEKLQLQALEQ-------EHKKLAARLEEErgknkQVVLMLVKEC-KQLSGKVIEEAQKLE 193
Cdd:TIGR00618  151 QGEFAQFLKAKSKEKKELLMNLFPLDQYTQlalmefaKKKSLHGKAELL-----TLRSQLLTLCtPCMPDTYHERKQVLE 225

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767948853   194 DVMAKLEEEKKKTNELEEELSaEKRRSTEMEAQMEKQLSEFDTEREQLRAklnrEEAHTTDLKEEIDKMRK 264
Cdd:TIGR00618  226 KELKHLREALQQTQQSHAYLT-QKREAQEEQLKKQQLLKQLRARIEELRA----QEAVLEETQERINRARK 291
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
119-269 3.52e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.73  E-value: 3.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 119 KKMQERMSAQLAAAESRQKKLEMEKLQLQALE---QEHKKLAARLEEERGKNKQVVlmlvKECKQLSGKVIEEAQKLEDV 195
Cdd:PRK02224 519 EDLEELIAERRETIEEKRERAEELRERAAELEaeaEEKREAAAEAEEEAEEAREEV----AELNSKLAELKERIESLERI 594

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767948853 196 MAKLEEEKKKTNELEEElsAEKRRS-TEMEAQMEKQLSEFDTEREQLRAKLnrEEAHTTDLKEEIDKMRKMIEQL 269
Cdd:PRK02224 595 RTLLAAIADAEDEIERL--REKREAlAELNDERRERLAEKRERKRELEAEF--DEARIEEAREDKERAEEYLEQV 665
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 133-263 3.73e-05

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 45.06  E-value: 3.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  133 ESRQKKLEMEKLQLQAlEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSGKVIEEAQ-KLEDVMAKLEEEKKKTNELEE 211
Cdd:pfam11600   5 KSVQSQEEKEKQRLEK-DKERLRRQLKLEAEKEEKER----LKEEAKAEKERAKEEARrKKEEEKELKEKERREKKEKDE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767948853  212 ELSAEKRRSTEmEAQMEKQlsefdterEQLRAKL--NREEAHTTDLKEEIDKMR 263
Cdd:pfam11600  80 KEKAEKLRLKE-EKRKEKQ--------EALEAKLeeKRKKEEEKRLKEEEKRIK 124
Ank_5 pfam13857
Ankyrin repeats (many copies);
768-817 4.09e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 4.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 767948853  768 AQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLA 817
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 186-276 4.23e-05

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 45.79  E-value: 4.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  186 IEEAQ-KLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLraklnrEEAHTTdlKEEIDKMRK 264
Cdd:pfam00261  10 LDEAEeRLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKL------EEAEKA--ADESERGRK 81

                          90
                  ....*....|..
gi 767948853  265 MIEQLKRGSDSK 276
Cdd:pfam00261  82 VLENRALKDEEK 93
PTZ00121 PTZ00121
MAEBL; Provisional
 119-289 4.24e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 4.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  119 KKMQERMSAQLAAAESRQKKlEMEKLQLQAlEQEHKKLAARLEEERGKNKQVVLMLVKECKqlsgKVIEEAQKLEDVM-- 196
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKAEEAK-KADEAKKKA-EEAKKADEAKKKAEEAKKKADEAKKAAEAK----KKADEAKKAEEAKka 1524

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  197 --AKLEEEKKKTNEL---EEELSAEK-RRSTEMEAQMEKQLSEFDTEREQLRAKLNR--------EEAHTTDLKEEIDKM 262
Cdd:PTZ00121 1525 deAKKAEEAKKADEAkkaEEKKKADElKKAEELKKAEEKKKAEEAKKAEEDKNMALRkaeeakkaEEARIEEVMKLYEEE 1604

                         170       180
                  ....*....|....*....|....*...
gi 767948853  263 RKM-IEQLKRGSDSKPSLSLPRKTKDRR 289
Cdd:PTZ00121 1605 KKMkAEEAKKAEEAKIKAEELKKAEEEK 1632
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 136-271 4.53e-05

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 45.28  E-value: 4.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  136 QKKLEMEKLQLQALEQEHKKLAARLEEErgkNKQvvlmLVKECKQLSGKVIEEAQKLE----DVMAkLEEEKKKTNELEE 211
Cdd:pfam13851  28 IKSLKEEIAELKKKEERNEKLMSEIQQE---NKR----LTEPLQKAQEEVEELRKQLEnyekDKQS-LKNLKARLKVLEK 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767948853  212 ELSAEKRRSTEMEAQMEKqLSEfdtEREQLRAKLNR--EEAHT-TDLKEEI--DKMRKMIEQLKR 271
Cdd:pfam13851 100 ELKDLKWEHEVLEQRFEK-VER---ERDELYDKFEAaiQDVQQkTGLKNLLleKKLQALGETLEK 160
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 136-270 4.60e-05

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


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 45.44  E-value: 4.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  136 QKKLEM--EKLQLQAL--EQEHKKLAARLEEERGKNKQVvlmlvkeckqlsGKVIEEAqklEDVMAKLEEEKKKTNELEE 211
Cdd:pfam05010   3 QKDMDAalEKARNEIEekELEINELKAKYEELRRENLEM------------RKIVAEF---EKTIAQMIEEKQKQKELEH 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767948853  212 elsaekrrstemeAQMEKQLSEfdteREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 270
Cdd:pfam05010  68 -------------AEIQKVLEE----KDQALADLNSVEKSFSDLFKRYEKQKEVISGYK 109
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
 111-226 4.84e-05

flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.


Pssm-ID: 131526 [Multi-domain]  Cd Length: 141  Bit Score: 44.23  E-value: 4.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  111 LEAVMAHCKKMQERMSAQLAAAES-RQKKLEMEKLQLQALE-QEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEE 188
Cdd:TIGR02473  22 LAKAQAEFERLETQLQQLIKYREEyEQQALEKVGAGTSALElSNYQRFIRQLDQRIQQQQQELALLQQEVEAKRERLLEA 101

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767948853  189 AQKLEdVMAKLEEeKKKTNELEEELSAEKRRSTEMEAQ 226
Cdd:TIGR02473 102 RRELK-ALEKLKE-KKQKEYRAEEAKREQKEMDELATQ 137
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 39-225 4.99e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.37  E-value: 4.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853    39 SELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYgrfnLNDPFLALQRDYEAGAGDKEKKPV----CTNPLSILEAV 114
Cdd:TIGR02169  808 SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID----LKEQIKSIEKEIENLNGKKEELEEeleeLEAALRDLESR 883

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   115 MAHCKKMQERMSAQLAAAESRQKKLEmekLQLQALEQEHKKLAARLEEERGKNKQV---------------VLMLVKECK 179
Cdd:TIGR02169  884 LGDLKKERDELEAQLRELERKIEELE---AQIEKKRKRLSELKAKLEALEEELSEIedpkgedeeipeeelSLEDVQAEL 960

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767948853   180 QlsgKVIEEAQKLEDV---------------------MAKLEEEKKKTNELEEELSaEKRRSTEMEA 225
Cdd:TIGR02169  961 Q---RVEEEIRALEPVnmlaiqeyeevlkrldelkekRAKLEEERKAILERIEEYE-KKKREVFMEA 1023
PHA03247 PHA03247
large tegument protein UL36; Provisional
 271-713 5.48e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 5.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  271 RGSDSKPSLSLPRKTKDR-RLVSISVGTEGTVTRSVACQTDLVTENAD--HMKKLPLTMPVKPSTGSPLVSANAKGSVCT 347
Cdd:PHA03247 2653 RDDPAPGRVSRPRRARRLgRAAQASSPPQRPRRRAARPTVGSLTSLADppPPPPTPEPAPHALVSATPLPPGPAAARQAS 2732

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  348 SATMARPGidrqasygdligasvpafPPPSANkieenGPSTGSTPDPTsSTPPLPSNAAPPTA-QTPGIAPQNSQAPPMH 426
Cdd:PHA03247 2733 PALPAAPA------------------PPAVPA-----GPATPGGPARP-ARPPTTAGPPAPAPpAAPAAGPPRRLTRPAV 2788

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  427 SLHSPCANTSLHPGLNPRIQAArfrfqgnANDPDQNGNTTQSPPSRDVSPTsrdnlvakqlarnTVTQALSRFTSPQAGA 506
Cdd:PHA03247 2789 ASLSESRESLPSPWDPADPPAA-------VLAPAAALPPAASPAGPLPPPT-------------SAQPTAPPPPPGPPPP 2848

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  507 PSRPG--VPPTGDVGTHPPVGRTSLKTHGVAR--VDRGNPPPIPPKKPGLSQTPSPPHPQlkviidssrasntgakvdnk 582
Cdd:PHA03247 2849 SLPLGgsVAPGGDVRRRPPSRSPAAKPAAPARppVRRLARPAVSRSTESFALPPDQPERP-------------------- 2908

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  583 tvasTPSSLPQGNRVINEENLPKSSSPQLPPKPSIDLTVAPAgcAVSALATSQVGAWPAATPGLNQPAcsdSSLVIPTTI 662
Cdd:PHA03247 2909 ----PQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPT--TDPAGAGEPSGAVPQPWLGALVPG---RVAVPRFRV 2979

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767948853  663 AFCSSINPVSASSCRPgASDSLLVTASGWSPSLTpLLMSGGPAPLAGRPTL 713
Cdd:PHA03247 2980 PQPAPSREAPASSTPP-LTGHSLSRVSSWASSLA-LHEETDPPPVSLKQTL 3028
LUC7 pfam03194
LUC7 N_terminus; This family contains the N terminal region of several LUC7 protein homologs ...
 132-274 5.52e-05

LUC7 N_terminus; This family contains the N terminal region of several LUC7 protein homologs and only contains eukaryotic proteins. LUC7 has been shown to be a U1 snRNA associated protein with a role in splice site recognition. The family also contains human and mouse LUC7 like (LUC7L) proteins and human cisplatin resistance-associated overexpressed protein (CROP).


Pssm-ID: 460842 [Multi-domain]  Cd Length: 246  Bit Score: 45.67  E-value: 5.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  132 AESRQKKLEMEKLQLQALEQEHKKLAARLEE--ERGKnkqvvlmlvkeckqlsgkvIEEAQKLedvMAKLEEEKKKTNEL 209
Cdd:pfam03194 111 QEEIEQTDELKQEQISVLEEKIKKLLEEAEElgEEGN-------------------VDEAQKL---MKKVEELKEEKEEL 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  210 EEEL-SAEKRRSTEMEAQME------KQLSEFDTERE--------------QLRAKLNReeahttdLKEEIDKmRKMIEQ 268
Cdd:pfam03194 169 EQQYeSLTKESAASQEKKMEvcevcgAFLIVNDADRRladhltgkqhlgyaKIRDTLEE-------LKEKIEE-RREERE 240


                  ....*.
gi 767948853  269 LKRGSD 274
Cdd:pfam03194 241 ERREKR 246
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 136-247 5.70e-05

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


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 43.33  E-value: 5.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  136 QKKLEMEKLQ--LQALEQEHKKLAARLEEERGKNKQVVLMLvKECKQLSGKVIEE-AQKLEDVMAKLEEEKKKTNELEEE 212
Cdd:pfam13863   3 EKKREMFLVQlaLDAKREEIERLEELLKQREEELEKKEQEL-KEDLIKFDKFLKEnDAKRRRALKKAEEETKLKKEKEKE 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 767948853  213 LsaekrrstemeAQMEKQLSEFDTEREQLRAKLNR 247
Cdd:pfam13863  82 I-----------KKLTAQIEELKSEISKLEEKLEE 105
PHA02946 PHA02946
ankyin-like protein; Provisional
 713-855 6.30e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.59  E-value: 6.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 713 LLQQAAAQGNVTLLSMLLNEEGLD-------------INYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFT 779
Cdd:PHA02946  28 MLQAIEPSGNYHILHAYCGIKGLDerfveellhrgysPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKT 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767948853 780 PL--CAAAAQGHFECVELLISYDANINHAAD-GGQTPLyLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGN 855
Cdd:PHA02946 108 PLyyLSGTDDEVIERINLLVQYGAKINNSVDeEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDN 185
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 167-268 6.42e-05

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


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 43.73  E-value: 6.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   167 NKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEE-KKKTNELEEE---LSAEKRRstEMEAQMEKQLSEFDTEREQLR 242
Cdd:smart00935   5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKElQKLKEKLQKDaatLSEAARE--KKEKELQKKVQEFQRKQQKLQ 82

                           90       100
                   ....*....|....*....|....*.
gi 767948853   243 AKLNREEAhttdlkEEIDKMRKMIEQ 268
Cdd:smart00935  83 QDLQKRQQ------EELQKILDKINK 102
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 743-775 6.88e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.74  E-value: 6.88e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 767948853  743 DGHSALYSAA-KNGHTDCVRLLLSAEAQVNAADK 775
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 331-730 6.92e-05

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: 46.83  E-value: 6.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  331 STGSPLVSANAKGSVCTSATMARPGIdrqASYGDLIGASVPAFPPPSANKIEENGPsTGSTPDPTSSTPPLPSNAAPPTa 410
Cdd:pfam05109 414 TTTHKVIFSKAPESTTTSPTLNTTGF---AAPNTTTGLPSSTHVPTNLTAPASTGP-TVSTADVTSPTPAGTTSGASPV- 488

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  411 qTPGIAPQN----SQAP----PMHSLHSPCAN-TSLHPGLNPRIQAARFRFQGNANdpDQNGNTTQSPPSRDVSP---TS 478
Cdd:pfam05109 489 -TPSPSPRDngteSKAPdmtsPTSAVTTPTPNaTSPTPAVTTPTPNATSPTLGKTS--PTSAVTTPTPNATSPTPavtTP 565

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  479 RDNLVAKQLARNTVTQALSRFTsPQAGAPSRPGVPPTGDVGTH-------------PPVGRTSLKTHGVARVDRGNPPPI 545
Cdd:pfam05109 566 TPNATIPTLGKTSPTSAVTTPT-PNATSPTVGETSPQANTTNHtlggtsstpvvtsPPKNATSAVTTGQHNITSSSTSSM 644

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  546 PPKKPGLSQTPSPP---------------HPQ-LKVIIDSSRASNTGAKVDNKTVASTPSSLPQ----GNRVIN----EE 601
Cdd:pfam05109 645 SLRPSSISETLSPStsdnstshmplltsaHPTgGENITQVTPASTSTHHVSTSSPAPRPGTTSQasgpGNSSTStkpgEV 724

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  602 NLPKSSSPQLPPKPSidltvAPAGCAVSA-LATSQVGAWPAATPGLNQPACSDSSLVIPTTIAFCSSINP---VSASSCR 677
Cdd:pfam05109 725 NVTKGTPPKNATSPQ-----APSGQKTAVpTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPrtrYNATTYL 799

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767948853  678 PGASDSLLvtASGWSPSLTPLLMSGG--PAPLAGRP------TLLQQAAAQGNVTLLSMLL 730
Cdd:pfam05109 800 PPSTSSKL--RPRWTFTSPPVTTAQAtvPVPPTSQPrfsnlsMLVLQWASLAVLTLLLLLV 858
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 126-271 7.20e-05

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 46.89  E-value: 7.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   126 SAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKqvVLMLVKECKQLSGKVIEEAQKledVMAKLEEEKKK 205
Cdd:pfam02463  216 KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQ--EIEKEEEKLAQVLKENKEEEK---EKKLQEEELKL 290

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767948853   206 TNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:pfam02463  291 LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEE 356
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 37-276 7.70e-05

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 46.49  E-value: 7.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  37 SKSELRMLLSVMEGEleaRDLVIEALRarrkevfIQERYGRFNLNDPFLALQRDYEAGAGDKEKKPVCTNPLSILEAVMA 116
Cdd:COG5185  115 SADILISLLYLYKSE---IVALKDELI-------KVEKLDEIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGL 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 117 HCKKMQErmsaqlaaaESRQKKLEMEKLQ-LQALEQEHKKLAARLEEERGKNKQVVlmlvKECKQLSGKVIEEAQKLEDV 195
Cdd:COG5185  185 TLGLLKG---------ISELKKAEPSGTVnSIKESETGNLGSESTLLEKAKEIINI----EEALKGFQDPESELEDLAQT 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 196 MAKLEEEKKKTNELEEELSAEKR-RSTEMEAQMEKQLSEFDTEREQLRA--KLNREEAHTTDLKEEIDKMR--KMIEQLK 270
Cdd:COG5185  252 SDKLEKLVEQNTDLRLEKLGENAeSSKRLNENANNLIKQFENTKEKIAEytKSIDIKKATESLEEQLAAAEaeQELEESK 331


                 ....*.
gi 767948853 271 RGSDSK 276
Cdd:COG5185  332 RETETG 337
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 40-269 7.79e-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: 46.71  E-value: 7.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853    40 ELRMLLSVMEGELEARDLVIEALRARRKEVFIQERygrfNLNDPFLALQRDYEAGAGDKEKKPVCTNPLSI-LEAVMAHC 118
Cdd:pfam01576  233 ELRAQLAKKEEELQAALARLEEETAQKNNALKKIR----ELEAQISELQEDLESERAARNKAEKQRRDLGEeLEALKTEL 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   119 KKMQERMSAQlaaAESRQKKlEMEKLQLQ-ALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSgkviEEAQKLEDVMA 197
Cdd:pfam01576  309 EDTLDTTAAQ---QELRSKR-EQEVTELKkALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAK----RNKANLEKAKQ 380

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767948853   198 KLEEEkkkTNELEEELSAEKRRSTEMEAQMEKQlsefDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQL 269
Cdd:pfam01576  381 ALESE---NAELQAELRTLQQAKQDSEHKRKKL----EGQLQELQARLSESERQRAELAEKLSKLQSELESV 445
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 45-268 7.88e-05

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 46.74  E-value: 7.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   45 LSVMEGELEARDLVIEAL--------RARRKEVfiqERYGRFN--LNDPFLALQRDY---EAGAGD-KE----------K 100
Cdd:pfam10174 438 LTTLEEALSEKERIIERLkeqreredRERLEEL---ESLKKENkdLKEKVSALQPELtekESSLIDlKEhasslassglK 514

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  101 KPVCTNPLSI-LEAVMAHCKKMQERMSAQLAAAESRQKKLEMeKLQLQALEQEhkklAARLEEERGKNKQVV---LMLVK 176
Cdd:pfam10174 515 KDSKLKSLEIaVEQKKEECSKLENQLKKAHNAEEAVRTNPEI-NDRIRLLEQE----VARYKEESGKAQAEVerlLGILR 589

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  177 EC---KQLSGKVIEEAQKLEDVMAKLE------------EEKKKTNELEEElsAEKRRSTEMEAQMEKQLSEFDTEREQL 241
Cdd:pfam10174 590 EVeneKNDKDKKIAELESLTLRQMKEQnkkvanikhgqqEMKKKGAQLLEE--ARRREDNLADNSQQLQLEELMGALEKT 667

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767948853  242 RAKLN--------------REEAHTTDLKEEidkMRKMIEQ 268
Cdd:pfam10174 668 RQELDatkarlsstqqslaEKDGHLTNLRAE---RRKQLEE 705
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 119-226 8.02e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 8.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   119 KKMQERMSAQLAAAESRQKKLEMEklqLQALEQEHKKLAARLEEERgknkqvvlmlvKECKQLSGKVIEEAQKLEDVMAK 198
Cdd:TIGR02169  405 KRELDRLQEELQRLSEELADLNAA---IAGIEAKINELEEEKEDKA-----------LEIKKQEWKLEQLAADLSKYEQE 470

                           90       100
                   ....*....|....*....|....*...
gi 767948853   199 LEEEKKKTNELEEELSAEKRRSTEMEAQ 226
Cdd:TIGR02169  471 LYDLKEEYDRVEKELSKLQRELAEAEAQ 498
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
 115-269 8.74e-05

ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria only. Scoring just below the trusted cutoff are the N-terminal domains of Mycobacterial b/delta fusion proteins and a subunit from an archaeon, Methanosarcina barkeri, in which the ATP synthase homolog differs in architecture and is not experimentally confirmed. This model helps resolve b from the related b' subunit. Within the family is an example from a sodium-translocating rather than proton-translocating ATP synthase. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 130214 [Multi-domain]  Cd Length: 147  Bit Score: 43.55  E-value: 8.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  115 MAHCKKMqerMSAQLAAA-ESRQKKLEMEklqLQALEQEHKKLAARLEEERGknkqvvlmLVKECKQLSGKVIEEAqkle 193
Cdd:TIGR01144   9 VWFCMKY---VWPPLAKAiETRQKKIADG---LASAERAKKEAALAQKKAQV--------ILKEAKDEAQEIIENA---- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  194 dvmakleeeKKKTNELEEELSAEKRrsTEMEAQMEKQLSEFDTEREQLRAKLNREeahTTDL---------KEEIDKM-- 262
Cdd:TIGR01144  71 ---------NKRGSEILEEAKAEAR--EEREKIKAQARAEIEAEKEQAREELRKQ---VADLsvlgaekiiERNIDKQaq 136


                  ....*..
gi 767948853  263 RKMIEQL 269
Cdd:TIGR01144 137 KDLIDKL 143
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
 135-250 1.19e-04

flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.


Pssm-ID: 131526 [Multi-domain]  Cd Length: 141  Bit Score: 43.07  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  135 RQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvLMLVKECKQLSGKVIEEAQKLEDVMAKLEEE----KKKTNELE 210
Cdd:TIGR02473  11 REKEEEQAKLELAKAQAEFERLETQLQQLIKYREE--YEQQALEKVGAGTSALELSNYQRFIRQLDQRiqqqQQELALLQ 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 767948853  211 EELsaEKRRSTEMEAQMEKQLseFDTEREQLRAKLNREEA 250
Cdd:TIGR02473  89 QEV--EAKRERLLEARRELKA--LEKLKEKKQKEYRAEEA 124
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 717-841 1.20e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 45.84  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  717 AAAQGNVTLLS-MLLNEEGLDINysCED--GHSALYSAAK-NGHTDCVRLLLSAEAQVNAADKngftpLCAAAAQGHFEC 792
Cdd:TIGR00870  24 AAERGDLASVYrDLEEPKKLNIN--CPDrlGRSALFVAAIeNENLELTELLLNLSCRGAVGDT-----LLHAISLEYVDA 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767948853  793 VELLISY-------DANINHAADG-------GQTPLYLACKNGNKECIKLLLEAGTNRSVKTT 841
Cdd:TIGR00870  97 VEAILLHllaafrkSGPLELANDQytseftpGITALHLAAHRQNYEIVKLLLERGASVPARAC 159
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 125-271 1.25e-04

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 44.12  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  125 MSAQLAA--AESR--QKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVlMLVKEcKQLSGKviEEAQ-KLEDVMAKL 199
Cdd:pfam15619  58 LPQLIARhnEEVRvlRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLE-KLSED-KNLAER--EELQkKLEQLEAKL 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767948853  200 EEEKKKTNELEEELS-AEKRRSTEMEAQMEKQLsefdtereQLRAKLNreeahttDLKEEIDKMRKMIEQLKR 271
Cdd:pfam15619 134 EDKDEKIQDLERKLElENKSFRRQLAAEKKKHK--------EAQEEVK-------ILQEEIERLQQKLKEKER 191
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 170-271 1.31e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.14  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 170 VVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQM---EKQLSEFDTEREQLRAKLN 246
Cdd:COG4942    7 LALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIaalARRIRALEQELAALEAELA 86

                         90       100
                 ....*....|....*....|....*
gi 767948853 247 REEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:COG4942   87 ELEKEIAELRAELEAQKEELAELLR 111
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
130-269 1.31e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.80  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 130 AAAESRQKKLEMEkLQLQALEQEHKKLAARLEEergknkqvvlmlvkeckqlsgkvIEEAQKLEDVMAKLEEEKKKTNEL 209
Cdd:PRK02224 469 TIEEDRERVEELE-AELEDLEEEVEEVEERLER-----------------------AEDLVEAEDRIERLEERREDLEEL 524

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767948853 210 EEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLN---------REEAHT-----TDLKEEIDKMRKMIEQL 269
Cdd:PRK02224 525 IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAeaeeeaeeaREEVAElnsklAELKERIESLERIRTLL 598
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 99-266 1.39e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.94  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853    99 EKKPVCTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEklqLQALEQ--EHKKLAA-RLEEERGKNKQV---VL 172
Cdd:pfam01576  510 EAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRE---LEALTQqlEEKAAAYdKLEKTKNRLQQElddLL 586

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   173 MLVKECKQLSGKvIEEAQKLEDVMakLEEEKKKTNELeeelsAEKRRSTEMEAQmekqlsefdtEREQLRAKLNREEAHT 252
Cdd:pfam01576  587 VDLDHQRQLVSN-LEKKQKKFDQM--LAEEKAISARY-----AEERDRAEAEAR----------EKETRALSLARALEEA 648

                          170
                   ....*....|....
gi 767948853   253 TDLKEEIDKMRKMI 266
Cdd:pfam01576  649 LEAKEELERTNKQL 662
Prefoldin_2 pfam01920
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
 127-246 1.41e-04

Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.


Pssm-ID: 396482 [Multi-domain]  Cd Length: 102  Bit Score: 41.82  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  127 AQLAAAESRQKKLEMEKLQLQALEQEHKKLaarLEEergknkqvvLMLVKE---CKQLSGKVIEEaQKLEDVMAKLEEEK 203
Cdd:pfam01920   2 NKFQQLQQQLQLLAQQIKQLETQLKELELA---LEE---------LELLDEdtkVYKLIGDVLVK-QDKEEVKEQLEERK 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 767948853  204 KKtneLEEELSAekrrstemeaqMEKQLSEFDTEREQLRAKLN 246
Cdd:pfam01920  69 ET---LEKEIKT-----------LEKQLEKLEKELEELKEELY 97
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
134-281 1.50e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  134 SRQKKLEMEKLQLQALEQEHKKLAARLE--EERGKNKQVVLMLVKECKQLS------GKVIEEAQKLEDVMAKLEEEKKK 205
Cdd:COG4913   607 DNRAKLAALEAELAELEEELAEAEERLEalEAELDALQERREALQRLAEYSwdeidvASAEREIAELEAELERLDASSDD 686

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767948853  206 TNELEEELsaekrrstemeAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDSKPSLSL 281
Cdd:COG4913   687 LAALEEQL-----------EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 781-863 1.51e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.37  E-value: 1.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 781 LCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLK 860
Cdd:PHA02875   6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85


                 ...
gi 767948853 861 LLM 863
Cdd:PHA02875  86 ELL 88
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 122-225 1.58e-04

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 45.33  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  122 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEaqKLEDVMAKLEE 201
Cdd:pfam15709 409 KQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEE--RLEYQRQKQEA 486

                          90       100
                  ....*....|....*....|....
gi 767948853  202 EKKKtneleeELSAEKRRSTEMEA 225
Cdd:pfam15709 487 EEKA------RLEAEERRQKEEEA 504
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 36-270 1.85e-04

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: 45.42  E-value: 1.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853    36 LSKSElRMLLSVMEGELEARDL-----VIEALRARRKEVfiQERYGRFNLNDPFLALQRDYEAGAGDKEKKpvcTNPLSI 110
Cdd:TIGR00606  767 IEEQE-TLLGTIMPEEESAKVCltdvtIMERFQMELKDV--ERKIAQQAAKLQGSDLDRTVQQVNQEKQEK---QHELDT 840

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   111 LEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEergKNKQVvLMLVKECKQLSGKVIEEAQ 190
Cdd:TIGR00606  841 VVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVE---LSTEV-QSLIREIKDAKEQDSPLET 916

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   191 KLED-------VMAKLEEEKK----KTNELEEELSAE--KRRSTEMEAQ--MEKQLSEFDTEREQLRAKLNREEAHTTDL 255
Cdd:TIGR00606  917 FLEKdqqekeeLISSKETSNKkaqdKVNDIKEKVKNIhgYMKDIENKIQdgKDDYLKQKETELNTVNAQLEECEKHQEKI 996

                          250
                   ....*....|....*
gi 767948853   256 KEEIDKMRKMIEQLK 270
Cdd:TIGR00606  997 NEDMRLMRQDIDTQK 1011
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 40-270 1.87e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 45.27  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   40 ELRMLLSVMEGELEARD--LVI---EALRARRKEVfIQERYgrfnlndpflALQRDYEAGAGDKEKKPVCTNPLSilEAV 114
Cdd:pfam07888   5 ELVTLEEESHGEEGGTDmlLVVpraELLQNRLEEC-LQERA----------ELLQAQEAANRQREKEKERYKRDR--EQW 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  115 MAHCKKMQERMS-AQLAAAESRQKKLEMEKLQ--LQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQK 191
Cdd:pfam07888  72 ERQRRELESRVAeLKEELRQSREKHEELEEKYkeLSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  192 LEDV---------MAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQ-LSEFDTEREQLRAKLNREEAHTTDLKEEIDK 261
Cdd:pfam07888 152 LERMkerakkagaQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNsLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE 231


                  ....*....
gi 767948853  262 MRKMIEQLK 270
Cdd:pfam07888 232 NEALLEELR 240
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
121-271 1.97e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.39  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 121 MQERMSAQLAAAESRQKKLEmekLQLQALEQEHKKLAARLEEERGKNKqvVLMLVKECKQLSGKVIEEAQKLEDVMAKLE 200
Cdd:COG3206  162 LEQNLELRREEARKALEFLE---EQLPELRKELEEAEAALEEFRQKNG--LVDLSEEAKLLLQQLSELESQLAEARAELA 236

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767948853 201 EEKKKTNELEEELSAEKRRSTEMEA-----QMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:COG3206  237 EAEARLAALRAQLGSGPDALPELLQspviqQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ 312
Rootletin pfam15035
Ciliary rootlet component, centrosome cohesion;
132-270 1.99e-04

Ciliary rootlet component, centrosome cohesion;


Pssm-ID: 464459 [Multi-domain]  Cd Length: 190  Bit Score: 43.49  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  132 AESRQKKLeMEKLQLQALEQ-------EHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEaqkLEDVMAKLEEEKK 204
Cdd:pfam15035  10 AQQRQAQL-VQKLQAKVLQYkkrcselEQQLLEKTSELEKTELLLRKLTLEPRLQRLEREHSAD---LEEALIRLEEERQ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  205 KTNEL-----------EEELSAEKRRSTEMEA----------QMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMR 263
Cdd:pfam15035  86 RSESLsqvnsllreqlEQASRANEALREDLQKltndwerareELEQKESEWRKEEEAFNEYLSSEHSRLLSLWREVVAVR 165


                  ....*..
gi 767948853  264 KMIEQLK 270
Cdd:pfam15035 166 RQFTELK 172
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 129-294 2.14e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 2.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 129 LAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNE 208
Cdd:COG4942   12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 209 LEEELSAEKRRSTEMEAQMEKQL----------------------------------SEFDTER-EQLRAKLNREEAHTT 253
Cdd:COG4942   88 LEKEIAELRAELEAQKEELAELLralyrlgrqpplalllspedfldavrrlqylkylAPARREQaEELRADLAELAALRA 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767948853 254 DLKEEIDKMRKMIEQLKRgsdSKPSLSLPRKTKDRRLVSIS 294
Cdd:COG4942  168 ELEAERAELEALLAELEE---ERAALEALKAERQKLLARLE 205
COG5022 COG5022
Myosin heavy chain [General function prediction only];
123-342 2.17e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 45.45  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  123 ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQV---VLMLVKECkqlsgKVIEEAQKLEDVMAKL 199
Cdd:COG5022   810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAkkrFSLLKKET-----IYLQSAQRVELAERQL 884

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  200 EEEKK----------KTNELEEELSaEKRRS------------TEMEAQMEKQLSEFDTEREQLR--------AKLNREE 249
Cdd:COG5022   885 QELKIdvksisslklVNLELESEII-ELKKSlssdlienlefkTELIARLKKLLNNIDLEEGPSIeyvklpelNKLHEVE 963

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  250 AHTTDLKEEIDKMRKMIEQLKRgsDSKPSLSLPRKTKdRRLVSISvgtegtvtrsvaCQTDLVTENADHMKKLPLTMPVK 329
Cdd:COG5022   964 SKLKETSEEYEDLLKKSTILVR--EGNKANSELKNFK-KELAELS------------KQYGALQESTKQLKELPVEVAEL 1028

                         250
                  ....*....|...
gi 767948853  330 PSTGSPLVSANAK 342
Cdd:COG5022  1029 QSASKIISSESTE 1041
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 167-268 2.24e-04

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: 42.18  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  167 NKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEE-KKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKL 245
Cdd:pfam03938   6 DMQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKElQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQEL 85

                          90       100
                  ....*....|....*....|....
gi 767948853  246 NREEAhttDLKEEI-DKMRKMIEQ 268
Cdd:pfam03938  86 QKKQQ---ELLQPIqDKINKAIKE 106
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 28-248 2.34e-04

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 44.95  E-value: 2.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  28 KKEFDvdtlskSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERygrfnlndpflalQRDYEAGAgDKEKKPVCTNP 107
Cdd:COG5185  331 KRETE------TGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVE-------------LSKSSEEL-DSFKDTIESTK 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 108 LSILEAVMAHCKKMQErmsaqLAAAESRQKKlemeklqlqALEQEHKKLAARLEEERGKNKQVvlmlvkeckqlsGKVIE 187
Cdd:COG5185  391 ESLDEIPQNQRGYAQE-----ILATLEDTLK---------AADRQIEELQRQIEQATSSNEEV------------SKLLN 444

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767948853 188 EAQK-LEDVMAKLEEEKK-----KTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNRE 248
Cdd:COG5185  445 ELISeLNKVMREADEESQsrleeAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQ 511
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 128-275 2.37e-04

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


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 43.51  E-value: 2.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  128 QLAAAESRQKKLEMEklqlqaLEQEhKKLAARLEEergknkQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTN 207
Cdd:pfam04012  44 ALAQTIARQKQLERR------LEQQ-TEQAKKLEE------KAQAALTKGNEELAREALAEKKSLEKQAEALETQLAQQR 110

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767948853  208 EleeelsaekrrsteMEAQMEKQLSEFDTEREQLRAKLNreeahTTDLKEEIDKMRKMIEQLKRGSDS 275
Cdd:pfam04012 111 S--------------AVEQLRKQLAALETKIQQLKAKKN-----LLKARLKAAKAQEAVQTSLGSLST 159
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 141-290 2.46e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 2.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   141 MEKLQLQA-LEQEHKKLAARLEEERgknkqvvlmlvkecKQLSGKVIEEaqkLEDVMAKLEEEKKKTNELEEELSAEKRR 219
Cdd:TIGR02168  202 LKSLERQAeKAERYKELKAELRELE--------------LALLVLRLEE---LREELEELQEELKEAEEELEELTAELQE 264

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767948853   220 StemeaqmEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMI----EQLKRGSDSKPSLSLPRKTKDRRL 290
Cdd:TIGR02168  265 L-------EEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqilrERLANLERQLEELEAQLEELESKL 332
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 810-840 2.47e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 2.47e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 767948853  810 GQTPLYLAC-KNGNKECIKLLLEAGTNRSVKT 840
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 122-246 2.72e-04

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 41.86  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  122 QERMSAQLAAAESRQKKLeMEKLQLQAleqehkKLAARLEE--ERgknkQVVlmlvkeckqlsgKVIEEAQKLEDVMAKL 199
Cdd:pfam07926  10 IKRLKEEAADAEAQLQKL-QEDLEKQA------EIAREAQQnyER----ELV------------LHAEDIKALQALREEL 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 767948853  200 EEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLN 246
Cdd:pfam07926  67 NELKAEIAELKAEAESAKAELEESEESWEEQKKELEKELSELEKRIE 113
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
119-281 3.01e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 3.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 119 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAA---RLEEERGKNKQVVlmlvkecKQLSGKVIEEAQKLEDV 195
Cdd:COG4372   83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKerqDLEQQRKQLEAQI-------AELQSEIAEREEELKEL 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 196 MAKLEEEKKKTNELEEELSAEKRRSTemEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDS 275
Cdd:COG4372  156 EEQLESLQEELAALEQELQALSEAEA--EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233


                 ....*.
gi 767948853 276 KPSLSL 281
Cdd:COG4372  234 ALSALL 239
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 112-268 3.11e-04

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 43.20  E-value: 3.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 112 EAVMAHCKKMQERMSAQLAAAESRQKKLEmEKLQLQALEQEHKKLAARLEEergknkqvvlmlvKECKQLSGKVIEEAQK 191
Cdd:cd00176   75 EEIQERLEELNQRWEELRELAEERRQRLE-EALDLQQFFRDADDLEQWLEE-------------KEAALASEDLGKDLES 140

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767948853 192 LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTER-EQLRAKLNReeahttdLKEEIDKMRKMIEQ 268
Cdd:cd00176  141 VEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKlEELNERWEE-------LLELAEERQKKLEE 211
mukB PRK04863
chromosome partition protein MukB;
53-275 3.15e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.95  E-value: 3.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   53 EARDLVIEALRARRkevFIQERYGRFNLNDPFLA-----------LQRDYEAGAGDKEKKPVCTNPLSILEAVMAHCK-- 119
Cdd:PRK04863  898 EIREQLDEAEEAKR---FVQQHGNALAQLEPIVSvlqsdpeqfeqLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSye 974

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  120 KMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEergkNKQVVLMLVKECKQLSGKVIEEAQKLED--VMA 197
Cdd:PRK04863  975 DAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQ----YNQVLASLKSSYDAKRQMLQELKQELQDlgVPA 1050

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767948853  198 KLEEEKKkTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEahttdlkEEIDKMRKMIEQLKRGSDS 275
Cdd:PRK04863 1051 DSGAEER-ARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLE-------RDYHEMREQVVNAKAGWCA 1120
MFAP1 pfam06991
Microfibril-associated/Pre-mRNA processing; MFAP1 was first named for proteins associated with ...
 187-288 3.30e-04

Microfibril-associated/Pre-mRNA processing; MFAP1 was first named for proteins associated with microfibrils which are an important component of the extracellular matrix (ECM) of many tissues. For example, MFAP1 has been shown to be associated with elastin-like fibres at the base of Schlemm's canal endothelium cells, in the juxtacanalicular tissue, and in the uveal region. Based on its role in the ECM and the proximity of the MFAP1 gene to FBN1 it was hypothesized that mutations in MFAP1 contributed to heritable diseases affecting microfibrils, Marfan syndrome but this has now been shown not to be the case. MFAP1 has also been shown to interact directly with certain pre-mRNA processing factor proteins, Prps, which are also spliceosome components and is thus required for pre-mRNA processing. MAFP1 bound to Pr38 of yeast is necessary for cells in vivo to progress from G2 to M phase.


Pssm-ID: 462060 [Multi-domain]  Cd Length: 215  Bit Score: 42.93  E-value: 3.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  187 EEAQKLEDVMAKLEEEKKKTNEL-EEELsaeKRRSTEMEAQMEKQ-LSEFDTE--------------REQLRAKLNREEA 250
Cdd:pfam06991  34 EEEEEEEEAKKEAEERKKEADKLvEEEI---RREAAAKEAGDEDEnEEDVDDTdgldpeaeyeawklRELKRIKRDREER 110

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767948853  251 HTTD-LKEEIDKMRKMIEQLKRGSDSKpslsLPRKTKDR 288
Cdd:pfam06991 111 EAREkEREEIERRRNMTEEERLAEDRE----NPKKQREK 145
PRK11637 PRK11637
AmiB activator; Provisional
 119-278 3.39e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 44.30  E-value: 3.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 119 KKMQERM-SAQLAAAeSRQKKLEMEKLQLQALE-QEHKKLAAR---LEEERGKNkqvvlmlVKECKQLSGKVIEEAQKLE 193
Cdd:PRK11637 119 QAAQERLlAAQLDAA-FRQGEHTGLQLILSGEEsQRGERILAYfgyLNQARQET-------IAELKQTREELAAQKAELE 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 194 DVMAK----LEEEKKKTNELEEELSAEKRRSTEMEAQMEK---QLSEFDTEREQLRAKLNREEAHTTDLKE----EIDKM 262
Cdd:PRK11637 191 EKQSQqktlLYEQQAQQQKLEQARNERKKTLTGLESSLQKdqqQLSELRANESRLRDSIARAEREAKARAErearEAARV 270

                        170
                 ....*....|....*..
gi 767948853 263 RKMIEQLKR-GSDSKPS 278
Cdd:PRK11637 271 RDKQKQAKRkGSTYKPT 287
CCCAP pfam15964
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ...
 123-263 3.42e-04

Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.


Pssm-ID: 435040 [Multi-domain]  Cd Length: 703  Bit Score: 44.51  E-value: 3.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  123 ERMSAQLAAAESRQKKLEMeklQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEE 202
Cdd:pfam15964 548 NEAKAQALQAQQREQELTQ---KMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEITQKSRSEVEQLSQE 624

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767948853  203 KKKTNELEEELsaeKRRSTEMEAQ----------MEKQLSEFD----TEREQLRAKLNREEA---HTTDLKEEIDKMR 263
Cdd:pfam15964 625 KEYLQDRLEKL---QKRNEELEEQcvqhgrmherMKQRLRQLDkhcqATAQQLVQLLSKQNQlfkERQNLTEEVQSLR 699
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 40-271 3.54e-04

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 44.35  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   40 ELRMLLSVMEGELEARDlviEALRARRKEVFIQERYgrfnlNDPFLALQRDYEAGAGD-KEKKPVCTNPLSILeAVMAHC 118
Cdd:pfam05557  52 ELQKRIRLLEKREAEAE---EALREQAELNRLKKKY-----LEALNKKLNEKESQLADaREVISCLKNELSEL-RRQIQR 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  119 KKMQerMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQK------- 191
Cdd:pfam05557 123 AELE--LQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKselarip 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  192 -LEDVMAKLEEEKKKTNE-------LEEELSAEKRRSTEMEAQMEKqLSEFDTEREQLRAKLNR----EEAHTTDLKEEI 259
Cdd:pfam05557 201 eLEKELERLREHNKHLNEnienkllLKEEVEDLKRKLEREEKYREE-AATLELEKEKLEQELQSwvklAQDTGLNLRSPE 279

                         250
                  ....*....|..
gi 767948853  260 DKMRKMIEQLKR 271
Cdd:pfam05557 280 DLSRRIEQLQQR 291
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 128-268 3.57e-04

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: 44.24  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  128 QLAAAESRQKKLEMEKLQ----LQALEQEHKKLAARL------EEERGKNKQVVLM----------------LVKECKQL 181
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEkeskISDLEDELNKDDFELkkenleKEIDEKNKEIEELkqtqkslkkkqeekqeLIDQKEKE 597

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  182 SGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDK 261
Cdd:TIGR04523 598 KKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD 677


                  ....*..
gi 767948853  262 MRKMIEQ 268
Cdd:TIGR04523 678 IIELMKD 684
PHA02795 PHA02795
ankyrin-like protein; Provisional
 790-856 3.67e-04

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 44.22  E-value: 3.67e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767948853 790 FECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNV 856
Cdd:PHA02795 201 LEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGSV 267
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 135-247 3.90e-04

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: 43.33  E-value: 3.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 135 RQKKLEMEKLQLQALEQEhkklAARLEEERGKNKQVvlmlvkeckqlsgkvIEEAQK-----LEDVMAKLEEEKKKTNEL 209
Cdd:cd16269  196 KEKEIEAERAKAEAAEQE----RKLLEEQQRELEQK---------------LEDQERsyeehLRQLKEKMEEERENLLKE 256

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767948853 210 EEELSAEKRRstEMEAQMEKqlsEFDTEREQLRAKLNR 247
Cdd:cd16269  257 QERALESKLK--EQEALLEE---GFKEQAELLQEEIRS 289
PRK01156 PRK01156
chromosome segregation protein; Provisional
 121-267 4.09e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 44.12  E-value: 4.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 121 MQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLA-----ARLEEERG--KNKQVVLMLVKECKQLSGKVieeaQKLE 193
Cdd:PRK01156 250 MKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIIndpvyKNRNYINDyfKYKNDIENKKQILSNIDAEI----NKYH 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 194 DVMAKLEEEKKKTNELEEelsaEKRRSTEmeaqMEKQLSEFDT----------EREQLRAKLNREEAHTTDLKEEIDKMR 263
Cdd:PRK01156 326 AIIKKLSVLQKDYNDYIK----KKSRYDD----LNNQILELEGyemdynsylkSIESLKKKIEEYSKNIERMSAFISEIL 397


                 ....
gi 767948853 264 KMIE 267
Cdd:PRK01156 398 KIQE 401
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 743-772 4.22e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 4.22e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 767948853   743 DGHSALYSAAKNGHTDCVRLLLSAEAQVNA 772
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 717-931 4.33e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.98  E-value: 4.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 717 AAAQGNVTLLSMLLNeegldINYSCEDGHSALYSAAKNghTDCVRLLLSAEaqVNAADKNGFTPLCAAAAQGHFECVELL 796
Cdd:cd22194   90 ASDTGKTCLMKALLN-----INENTKEIVRILLAFAEE--NGILDRFINAE--YTEEAYEGQTALNIAIERRQGDIVKLL 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 797 ISYDANINHAADG--------------GQTPLYLACKNGNKECIKLLLEAG-TNRSVKTTDGWTPVHAAV----DTGNVD 857
Cdd:cd22194  161 IAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKEsTDITSQDSRGNTVLHALVtvaeDSKTQN 240

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767948853 858 SLKLLMYHRIPahgnsfneeesessvfdLDGGEESPEGISkpvvpadlinhaNREGWTAAHIAASKGFKMLLKY 931
Cdd:cd22194  241 DFVKRMYDMIL-----------------LKSENKNLETIR------------NNEGLTPLQLAAKMGKAEILKY 285
UPF0242 pfam06785
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...
 187-268 4.79e-04

Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.


Pssm-ID: 429117 [Multi-domain]  Cd Length: 194  Bit Score: 42.12  E-value: 4.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  187 EEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMI 266
Cdd:pfam06785  87 ILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEEQLAEKQLLINEYQQTIEEQRSVL 166


                  ..
gi 767948853  267 EQ 268
Cdd:pfam06785 167 EK 168
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
145-272 5.09e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 5.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 145 QLQALEQEHKKLAARLEEERgknkqvvlmLVKECKQLSGKV----IEEAQKLEDVMAKLEEEKKKTNELEEEL-SAEKRR 219
Cdd:COG4717  348 ELQELLREAEELEEELQLEE---------LEQEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLeELLGEL 418

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767948853 220 STEMEAQMEKQLSEfdtEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRG 272
Cdd:COG4717  419 EELLEALDEEELEE---ELEELEEELEELEEELEELREELAELEAELEQLEED 468
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 713-931 5.23e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 43.72  E-value: 5.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 713 LLQQAAAQGNvtlLSMLLNEEGLDINYsceDGHSALYSAAKNGHTDCVRLLLSAEAQVNAAdkngftpLCAAAAQGHfec 792
Cdd:cd21882   48 LLEAAPDSGN---PKELVNAPCTDEFY---QGQTALHIAIENRNLNLVRLLVENGADVSAR-------ATGRFFRKS--- 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 793 VELLISYdaninhaadgGQTPLYLACKNGNKECIKLLLEAGTN-RSVKTTD--GWTPVHAAVDTGN--VDSLKLL--MYH 865
Cdd:cd21882  112 PGNLFYF----------GELPLSLAACTNQEEIVRLLLENGAQpAALEAQDslGNTVLHALVLQADntPENSAFVcqMYN 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767948853 866 RIPAHGNSfneeesessvfdldggeespegiSKPVVPADLInhANREGWTAAHIAASKGFKMLLKY 931
Cdd:cd21882  182 LLLSYGAH-----------------------LDPTQQLEEI--PNHQGLTPLKLAAVEGKIVMFQH 222
PRK00106 PRK00106
ribonuclease Y;
140-271 5.29e-04

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 43.70  E-value: 5.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 140 EMEKLQLQALEQEHKKLaarleeeRGKNKQVVLMLVKECKQLSgkvieEAQKLEDVMAKLEEEKKKTNELEEELSAEKRR 219
Cdd:PRK00106  31 EAAELTLLNAEQEAVNL-------RGKAERDAEHIKKTAKRES-----KALKKELLLEAKEEARKYREEIEQEFKSERQE 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767948853 220 STEMEAQMEKQLSEFDTEREQLRAK---LNREEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:PRK00106  99 LKQIESRLTERATSLDRKDENLSSKektLESKEQSLTDKSKHIDEREEQVEKLEE 153
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 748-820 5.33e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 43.05  E-value: 5.33e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767948853 748 LYSAAKNGHtDCVRLLLSAEAQVNA-ADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLA---CKN 820
Cdd:PHA02884  75 IYAIDCDND-DAAKLLIRYGADVNRyAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELAlmiCNN 150
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 135-479 5.35e-04

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 43.88  E-value: 5.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  135 RQKKLEMEKLQLQALEQEHKKLAARLEEE---RGKNKQVvlmLVKECKQLSGKVIEEAQ--KLEDVMAKLEEEKKKTNEL 209
Cdd:PTZ00108  997 KEYLLGKLERELARLSNKVRFIKHVINGElviTNAKKKD---LVKELKKLGYVRFKDIIkkKSEKITAEEEEGAEEDDEA 1073

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  210 EEELSAEKRRST----------------EMEAQMEKQLSEFDTEREQLRAKlNREEAHTTDLK---EEIDKMRKMIEQLK 270
Cdd:PTZ00108 1074 DDEDDEEELGAAvsydyllsmpiwsltkEKVEKLNAELEKKEKELEKLKNT-TPKDMWLEDLDkfeEALEEQEEVEEKEI 1152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  271 RGSDSKPSlslPRKTKDRRLVSisvgtegtvtrsvacQTDLVTENADHMKKLPLTMPVKPSTGSPLVSANAKGSVCTSAT 350
Cdd:PTZ00108 1153 AKEQRLKS---KTKGKASKLRK---------------PKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPD 1214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  351 MARPGIDRQASYGDLIGASVPAFPPPSANKIEENGPSTGSTPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAPPMHSL-- 428
Cdd:PTZ00108 1215 NKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPdg 1294

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767948853  429 ---HSPCANTSLHPGLNPRIQ----AARFRFQGNANDPDQNGNTTQSPPSRDVSPTSR 479
Cdd:PTZ00108 1295 esnGGSKPSSPTKKKVKKRLEgslaALKKKKKSEKKTARKKKSKTRVKQASASQSSRL 1352
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 108-267 5.42e-04

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: 43.88  E-value: 5.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   108 LSILEAVMAHCKKMQERMSAQLAAAESRQKKL---EMEKLQLQALEQEHKKLAARLEEERGKN---KQVVLMLVKE---C 178
Cdd:TIGR00606  600 LASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsQDEESDLERLKEEIEKSSKQRAMLAGATavySQFITQLTDEnqsC 679

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   179 KQLSGKVIEEAQKLEDVMAKLEEEKK----KTNELEEELSAEKRRSTEMEAQMEKQLSEFD---TEREQLRAKLNREEAH 251
Cdd:TIGR00606  680 CPVCQRVFQTEAELQEFISDLQSKLRlapdKLKSTESELKKKEKRRDEMLGLAPGRQSIIDlkeKEIPELRNKLQKVNRD 759

                          170
                   ....*....|....*.
gi 767948853   252 TTDLKEEIDKMRKMIE 267
Cdd:TIGR00606  760 IQRLKNDIEEQETLLG 775
PRK12704 PRK12704
phosphodiesterase; Provisional
 51-228 5.61e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.61  E-value: 5.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  51 ELEARDLVIEAlrarRKEVFIQERYGRFNLNDPFLALQRDYEAGAGDKEKKpvctnpLSILEAVMahcKKMQERMSAQLA 130
Cdd:PRK12704  37 EEEAKRILEEA----KKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNE------LQKLEKRL---LQKEENLDRKLE 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 131 AAESRQKKLEMEKLQLQALEQEHKKLAARLEEergknkqvvlmlvkeckqlsgKVIEEAQKLEDVMAKLEEEKKKT--NE 208
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEE---------------------LIEEQLQELERISGLTAEEAKEIllEK 162

                        170       180
                 ....*....|....*....|...
gi 767948853 209 LEEELSAEKR---RSTEMEAQME 228
Cdd:PRK12704 163 VEEEARHEAAvliKEIEEEAKEE 185
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
 134-266 5.62e-04

Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.


Pssm-ID: 463600 [Multi-domain]  Cd Length: 139  Bit Score: 41.01  E-value: 5.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  134 SRQKKLEMEKLQlQALEQEHKKLAARLEEERGKNkqvvLMLVKEckqlsgkvieeAQKLEDVMAKLEEEKKKTNELEEEL 213
Cdd:pfam12474  31 ERQQKQQIEKLE-QRQTQELRRLPKRIRAEQKKR----LKMFRE-----------SLKQEKKELKQEVEKLPKFQRKEAK 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767948853  214 saeKRRSTEMEAQMEKQlsefdtEREQLRAKLnreEAHTTDLKEEIDKMRKMI 266
Cdd:pfam12474  95 ---RQRKEELELEQKHE------ELEFLQAQS---EALERELQQLQNEKRKEL 135
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 119-246 5.63e-04

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: 41.13  E-value: 5.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  119 KKMQERMSAQLAAAESR-----QKKLEMEK-LQLQALEQEHKKLAARLE-EERGKNKQVVLMLVKECKQLSGKVIEEAQK 191
Cdd:pfam10473   2 EKKQLHVLEKLKESERKadslkDKVENLEReLEMSEENQELAILEAENSkAEVETLKAEIEEMAQNLRDLELDLVTLRSE 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767948853  192 LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLN 246
Cdd:pfam10473  82 KENLTKELQKKQERVSELESLNSSLENLLEEKEQEKVQMKEESKTAVEMLQTQLK 136
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 123-248 5.71e-04

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 43.90  E-value: 5.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  123 ERMSAQLAAAEsrqKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLvkECKQLSGKVIEEaqKLEDVMAKLEEE 202
Cdd:pfam05911 698 ENLEVELASCT---ENLESTKSQLQESEQLIAELRSELASLKESNSLAETQL--KCMAESYEDLET--RLTELEAELNEL 770

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767948853  203 KKKTNELEEELSAEKR-------RSTEMEAQME----KQLSEFDTEREQLRAKLNRE 248
Cdd:pfam05911 771 RQKFEALEVELEEEKNcheeleaKCLELQEQLErnekKESSNCDADQEDKKLQQEKE 827
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 187-270 5.91e-04

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 40.67  E-value: 5.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  187 EEAQK----LEDVMAKLEEEKKKTNEleeelsaEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEidKM 262
Cdd:pfam20492   2 EEAERekqeLEERLKQYEEETKKAQE-------ELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEES--AE 72


                  ....*...
gi 767948853  263 RKMIEQLK 270
Cdd:pfam20492  73 MEAEEKEQ 80
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 779-863 5.96e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.11  E-value: 5.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 779 TPL--CAAAAQGHFECVELLISYDANINHAADG-GQTPL--YLAC-KNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVD 852
Cdd:PHA02859  53 TPIfsCLEKDKVNVEILKFLIENGADVNFKTRDnNLSALhhYLSFnKNVEPEILKILIDSGSSITEEDEDGKNLLHMYMC 132

                         90
                 ....*....|...
gi 767948853 853 TGNV--DSLKLLM 863
Cdd:PHA02859 133 NFNVriNVIKLLI 145
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
 157-287 6.03e-04

Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.


Pssm-ID: 434558 [Multi-domain]  Cd Length: 154  Bit Score: 41.32  E-value: 6.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  157 AARLEE-ERGKNKQVvlmlvkECKQLSGKVIEEAQKLEdvmaKLEEEKKKTNELEEELsaEKRRSTEMeaqMEKQLsefd 235
Cdd:pfam15236  41 PAQLEErERKRQKAL------EHQNAIKKQLEEKERQK----KLEEERRRQEEQEEEE--RLRREREE---EQKQF---- 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767948853  236 tEREQLRAKlNREEAHTTDLKEEIDKMRKMIEQLKRGSDSKPSLSLPRKTKD 287
Cdd:pfam15236 102 -EEERRKQK-EKEEAMTRKTQALLQAMQKAQELAQRLKQEQRIRELAEKGHD 151
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 121-271 6.53e-04

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 43.53  E-value: 6.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 121 MQERMSAQLAAAESRQKKLEMEKLQLQAlEQE--HKKLAARLEEERGKNKqvvlmlvkeckqlsgkvieeaQKLEDVMAK 198
Cdd:COG0542  405 EIDSKPEELDELERRLEQLEIEKEALKK-EQDeaSFERLAELRDELAELE---------------------EELEALKAR 462

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 199 LEEEKKKTNE---LEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREE-----AHTTD------LKEEIDKMRK 264
Cdd:COG0542  463 WEAEKELIEEiqeLKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTEEDiaevvSRWTGipvgklLEGEREKLLN 542


                 ....*..
gi 767948853 265 MIEQLKR 271
Cdd:COG0542  543 LEEELHE 549
DUF874 pfam05917
Helicobacter pylori protein of unknown function (DUF874); This family consists of several ...
 125-251 6.64e-04

Helicobacter pylori protein of unknown function (DUF874); This family consists of several hypothetical proteins specific to Helicobacter pylori. The function of this family is unknown.


Pssm-ID: 283549 [Multi-domain]  Cd Length: 398  Bit Score: 43.30  E-value: 6.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  125 MSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmlvkeckqlSGKVIEEAQ-KLEDVMAKLEEEK 203
Cdd:pfam05917 115 LAACSAGDTDEQIELEQEKKEAENAEDRANKNGIELEQEKQKTNK------------SGIELANNQiKAEQEQQKTEQEK 182

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 767948853  204 KKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQlraklNREEAH 251
Cdd:pfam05917 183 QKAEKEAIELEQEKQKTIKTQRDLIKEQKDFIKETEQ-----NCQENH 225
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
 115-233 6.67e-04

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


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 42.00  E-value: 6.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  115 MAHCKKMQERMSAQ------LAA-AESRQKKLEMEKLQLQALEQEH---KKLA-----------ARLEEERGKNKQVVLM 173
Cdd:pfam13904  41 ARKLEGLKLERQPLeayenwLAAkQRQRQKELQAQKEEREKEEQEAelrKRLAkekyqewlqrkARQQTKKREESHKQKA 120

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767948853  174 LVKECKQLSGKVIEEAQklEDVMAKLEE-EKKKTNEL----EEELSAEKRRstEMEAQMEKQLSE 233
Cdd:pfam13904 121 AESASKSLAKPERKVSQ--EEAKEVLQEwERKKLEQQqrkrEEEQREQLKK--EEEEQERKQLAE 181
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 169-264 6.83e-04

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 41.21  E-value: 6.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  169 QVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTE---MEAQMEKQLSEfdTEREQLRAKL 245
Cdd:pfam11600   1 RRSQKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEearRKKEEEKELKE--KERREKKEKD 78

                          90
                  ....*....|....*....
gi 767948853  246 NREEAHTTDLKEEIDKMRK 264
Cdd:pfam11600  79 EKEKAEKLRLKEEKRKEKQ 97
PHA03291 PHA03291
envelope glycoprotein I; Provisional
 314-451 7.33e-04

envelope glycoprotein I; Provisional


Pssm-ID: 223033 [Multi-domain]  Cd Length: 401  Bit Score: 43.02  E-value: 7.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 314 ENADHMKKLPLTMPVKPSTGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIgasVPAFPPPSANKIE--ENGPSTGST 391
Cdd:PHA03291 151 EGATNASLFPLGLAAFPAEGTLAAPPLGEGSADGSCDPALPLSAPRLGPADVF---VPATPRPTPRTTAspETTPTPSTT 227

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767948853 392 PDPTSSTPPLPS-NAAPPTAQTPGIAPQNSQAPPMHSLHSPCANTSlhpglnPRIQAARFR 451
Cdd:PHA03291 228 TSPPSTTIPAPStTIAAPQAGTTPEAEGTPAPPTPGGGEAPPANAT------PAPEASRYE 282
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 130-261 7.42e-04

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 43.53  E-value: 7.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 130 AAAesrQKKLEMEKL--QLQALEQEHkklaARLEEERGKnkqvvlmLVKECKQLSgkvIEEAQKLEDVMAKLEEEKkktN 207
Cdd:COG0542  398 AAA---RVRMEIDSKpeELDELERRL----EQLEIEKEA-------LKKEQDEAS---FERLAELRDELAELEEEL---E 457

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767948853 208 ELEEELSAEK---RRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDK 261
Cdd:COG0542  458 ALKARWEAEKeliEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE 514
PHA03369 PHA03369
capsid maturational protease; Provisional
 224-651 8.61e-04

capsid maturational protease; Provisional


Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 43.06  E-value: 8.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 224 EAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKrgsDSKPSLSLPRKTKDRRLVS--ISVGTEGTV 301
Cdd:PHA03369 260 EAPLNALLEILKAKNAEMPGTLNPSFGSSDESPEWKTFYEALADQLN---NLYKLLRTIYKHKDETVIEqyLIEGRKLFS 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 302 TrsvacqtdlVTENADHMKKLPLTMPVKPStgSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPSANKI 381
Cdd:PHA03369 337 T---------INGLKAHNEILKTASLTAPS--RVLAAAAKVAVIAAPQTHTGPADRQRPQRPDGIPYSVPARSPMTAYPP 405

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 382 EENGPSTGSTPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAP-PMHSLhspcantsLHPGLNPRIQAARFRFQGNANDPD 460
Cdd:PHA03369 406 VPQFCGDPGLVSPYNPQSPGTSYGPEPVGPVPPQPTNPYVMPiSMANM--------VYPGHPQEHGHERKRKRGGELKEE 477

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 461 QNGNTTQSPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTSPQAGAPSrPGVPPTGDVGTHPPVGRTSLKT--HGVARVD 538
Cdd:PHA03369 478 LIETLKLVKKLKEEQESLAKELEATAHKSEIKKIAESEFKNAGAKTAA-ANIEPNCSADAAAPATKRARPEtkTELEAVV 556

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 539 RGNPPPIPPKKPGLSQTPSPPHPQLKVIIDSSRASNTGAKVdnKTVASTPSSLPQGNRVINEENLPKSSSPQLPPKPSID 618
Cdd:PHA03369 557 RFPYQIRNMESPAFVHSFTSTTLAAAAGQGSDTAEALAGAI--ETLLTQASAQPAGLSLPAPAVPVNASTPASTPPPLAP 634

                        410       420       430
                 ....*....|....*....|....*....|...
gi 767948853 619 LTVAPAGCAVSALATSQvgawPAATPGLNQPAC 651
Cdd:PHA03369 635 QEPPQPGTSAPSLETSL----PQQKPVLSKGAF 663
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
 119-168 8.71e-04

Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269834 [Multi-domain]  Cd Length: 52  Bit Score: 37.91  E-value: 8.71e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767948853 119 KKMQERMSAQlaaaESRQ-KKLEMEKL--QLQALEQEHKKLAARLEEERGKNK 168
Cdd:cd14686    4 RRERNREAAR----RSRErKKERIEELeeEVEELEEENEELKAELEELRAEVE 52
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 137-268 9.09e-04

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 41.18  E-value: 9.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  137 KKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNE-----LEE 211
Cdd:pfam09756   1 KKLGAKKRAKLELKEAKRQQREAEEEEREEREKLEEKREEEYKEREEREEEAEKEKEEEERKQEEEQERKEQeeyekLKS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767948853  212 ELSAEKRRSTEMEAQMEKQLSE----FDTER-----EQLRAKLNreeahtTDLKEEIDKMRKMIEQ 268
Cdd:pfam09756  81 QFVVEEEGTDKLSAEDESQLLEdfinYIKLKkvvllEELAAEFG------LKTQDVIDRIQDLEEQ 140
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 113-250 9.67e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.49  E-value: 9.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 113 AVMAHCKKMQERMSAQLAAAESRQKKLEM---EKLQLQALEQEHKKlaaRLEEERGKNKQVVLMLVKECKQ--LSGKVIE 187
Cdd:PRK09510  59 AVVEQYNRQQQQQKSAKRAEEQRKKKEQQqaeELQQKQAAEQERLK---QLEKERLAAQEQKKQAEEAAKQaaLKQKQAE 135

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767948853 188 EAQK--LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQmEKQLSEFDTEREQLRAKLNREEA 250
Cdd:PRK09510 136 EAAAkaAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAA-KKAAAEAKKKAEAEAAAKAAAEA 199
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
98-249 9.79e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 9.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  98 KEKKPVCTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKL--QLQALEQEHKKLAARLEEERGKNKQVVLML- 174
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELreEYLELSRELAGLRAELEELEKRREEIKKTLe 697

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767948853 175 -VKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELsaeKRRSTEMEAQMEKQL-SEFdTEREQLRAKLNREE 249
Cdd:PRK03918 698 kLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALL---KERALSKVGEIASEIfEEL-TEGKYSGVRVKAEE 770
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 190-276 9.79e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.83  E-value: 9.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 190 QKLEDVMAKLEEEKKKTNELEEELSAEKrrstemeAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRkmiEQL 269
Cdd:COG1579   13 QELDSELDRLEHRLKELPAELAELEDEL-------AALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE---EQL 82


                 ....*..
gi 767948853 270 KRGSDSK 276
Cdd:COG1579   83 GNVRNNK 89
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 122-271 1.01e-03

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 42.90  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   122 QERMSAQLAAA----ESRQKKLEMEK-------LQLQALEQEHKKLA-----ARLEEERGKNKQVVlMLVKECKQLSGKV 185
Cdd:pfam12128  620 QAAAEEQLVQAngelEKASREETFARtalknarLDLRRLFDEKQSEKdkknkALAERKDSANERLN-SLEAQLKQLDKKH 698

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   186 ---IEE--AQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEID 260
Cdd:pfam12128  699 qawLEEqkEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIR 778

                          170
                   ....*....|.
gi 767948853   261 KMRKMIEQLKR 271
Cdd:pfam12128  779 TLERKIERIAV 789
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 810-835 1.02e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.02e-03
                          10        20
                  ....*....|....*....|....*.
gi 767948853  810 GQTPLYLACKNGNKECIKLLLEAGTN 835
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGAD 27
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
 122-212 1.02e-03

Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.


Pssm-ID: 434558 [Multi-domain]  Cd Length: 154  Bit Score: 40.55  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  122 QERMSAQLAAAEsRQKKLEMEK------LQLQALEQEHKKLAARLEEERGKNKQvvlmlVKECKQLSGKVIEEAQKLEDV 195
Cdd:pfam15236  58 QNAIKKQLEEKE-RQKKLEEERrrqeeqEEEERLRREREEEQKQFEEERRKQKE-----KEEAMTRKTQALLQAMQKAQE 131

                          90
                  ....*....|....*..
gi 767948853  196 MAKLEEEKKKTNELEEE 212
Cdd:pfam15236 132 LAQRLKQEQRIRELAEK 148
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
 133-236 1.04e-03

Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.


Pssm-ID: 198139 [Multi-domain]  Cd Length: 154  Bit Score: 40.48  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   133 ESRQK-KLEMEKLQLQ-----ALEQEHKKLAARLEEERGK-NKQVVLMLVKEC-KQLSGKVIEEAQKLEDVMAKLEEEKK 204
Cdd:smart01071  39 QARVErMEEIKNLKYElimndHLNKRIDKLLKGLREEELSpETPTYNEMLAELqDQLKKELEEANGDSEGLLEELKKHRD 118

                           90       100       110
                   ....*....|....*....|....*....|..
gi 767948853   205 KTNELEEELsaeKRRSTEMEAQMEKQLSEFDT 236
Cdd:smart01071 119 KLKKEQKEL---RKKLDELEKEEKKKIWSVDT 147
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 184-271 1.05e-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: 40.25  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  184 KVIEEAQKLEDVMAKLEEEKKKtneleeelsaekrrsteMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMR 263
Cdd:pfam03938   9 KILEESPEGKAAQAQLEKKFKK-----------------RQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKE 71


                  ....*...
gi 767948853  264 KMIEQLKR 271
Cdd:pfam03938  72 QELQQLQQ 79
PRK00106 PRK00106
ribonuclease Y;
112-266 1.06e-03

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 42.55  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 112 EAVMAHCKKMQERMSAQL-------AAAESRQKKLEMEKlQLQALEQEHKKLAARLEEErgknkqvVLMLVKECKQLSGK 184
Cdd:PRK00106  52 ERDAEHIKKTAKRESKALkkellleAKEEARKYREEIEQ-EFKSERQELKQIESRLTER-------ATSLDRKDENLSSK 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 185 --VIEEA-QKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDK 261
Cdd:PRK00106 124 ekTLESKeQSLTDKSKHIDEREEQVEKLEEQKKAELERVAALSQAEAREIILAETENKLTHEIATRIREAEREVKDRSDK 203


                 ....*
gi 767948853 262 MRKMI 266
Cdd:PRK00106 204 MAKDL 208
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 117-275 1.16e-03

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 42.89  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  117 HCKkmqERMSAQLAAAESRQ-KKLEMEKLQLQALEQEHKKLAARLEEErGKNKQVVLMLVKECKQLSgkviEEAQKLEDV 195
Cdd:pfam10174 596 NDK---DKKIAELESLTLRQmKEQNKKVANIKHGQQEMKKKGAQLLEE-ARRREDNLADNSQQLQLE----ELMGALEKT 667

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  196 MAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSE-FDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQ---LKR 271
Cdd:pfam10174 668 RQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEiLEMKQEALLAAISEKDANIALLELSSSKKKKTQEEvmaLKR 747


                  ....
gi 767948853  272 GSDS 275
Cdd:pfam10174 748 EKDR 751
Nop53 pfam07767
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ...
 142-272 1.18e-03

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


Pssm-ID: 462259 [Multi-domain]  Cd Length: 353  Bit Score: 42.28  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  142 EKLQLQALEQEHKKLAARLEEERgknkqvvlmlvkeckqlsgkvIEEAQKLEDVMAKLEEEKKKT-----NELEEElsaE 216
Cdd:pfam07767 198 QELLQKAVEAEKKRLKEEEKLER---------------------VLEKIAESAATAEAREEKRKTkaqrnKEKRRK---E 253

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767948853  217 KRRSTEMEAQMEKQLSEFDTEREqLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRG 272
Cdd:pfam07767 254 EEREAKEEKALKKKLAQLERLKE-IAKEIAEKEKEREEKAEARKREKRKKKKEEKK 308
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 174-270 1.37e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 41.93  E-value: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   174 LVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEE----ELSA--EKRRSTEMEAQMEKQ-LSEFDTEREQLRAKLN 246
Cdd:smart00787 163 LMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDcdptELDRakEKLKKLLQEIMIKVKkLEELEEELQELESKIE 242

                           90       100
                   ....*....|....*....|....
gi 767948853   247 REEAHTTDLKEEIDKMRKMIEQLK 270
Cdd:smart00787 243 DLTNKKSELNTEIAEAEKKLEQCR 266
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 119-274 1.42e-03

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


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 40.81  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  119 KKMQ-ERMSAQLAAAESRQK--KLEMEKLQLQALEQEHKKLAARLEEERGKNKQVV---LMLVKECKQLSGKVIEEAQK- 191
Cdd:pfam05010  11 EKARnEIEEKELEINELKAKyeELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEhaeIQKVLEEKDQALADLNSVEKs 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  192 LEDVMAKLE------------EE--KKKTNELEEELSAEKRRSTEMEAQMEKQL-----------SEFDTEREQLRAKLN 246
Cdd:pfam05010  91 FSDLFKRYEkqkevisgykknEEslKKCAQDYLARIKKEEQRYQALKAHAEEKLdqaneeiaqvrSKAKAETAALQASLR 170

                         170       180
                  ....*....|....*....|....*...
gi 767948853  247 REEAHTTDLKEEIDKMRKMIEQLKRGSD 274
Cdd:pfam05010 171 KEQMKVQSLERQLEQKTKENEELTKICD 198
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 85-268 1.49e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 41.59  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  85 LALQRDYEAGAGDKEKKPVCTNPLSILEAVMAHCKKMQERmsAQLAAAESRQKKLEMEKLQlQALEQEHKKLAARLEEER 164
Cdd:cd22656   97 LELIDDLADATDDEELEEAKKTIKALLDDLLKEAKKYQDK--AAKVVDKLTDFENQTEKDQ-TALETLEKALKDLLTDEG 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 165 GKNKQvvlmlvKECKQLSGKvIEEAQK--LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAqMEKQLSEFDTEREQLR 242
Cdd:cd22656  174 GAIAR------KEIKDLQKE-LEKLNEeyAAKLKAKIDELKALIADDEAKLAAALRLIADLTA-ADTDLDNLLALIGPAI 245

                        170       180
                 ....*....|....*....|....*.
gi 767948853 243 AKLNREEAHTTDLKEEIDKMRKMIEQ 268
Cdd:cd22656  246 PALEKLQGAWQAIATDLDSLKDLLED 271
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
190-270 1.52e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.82  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 190 QKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAqmekQLSEFDTEREQLRAKL--NREEAHTtdLKEEIDKMRKMIE 267
Cdd:COG1340    1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNE----ELKELAEKRDELNAQVkeLREEAQE--LREKRDELNEKVK 74


                 ...
gi 767948853 268 QLK 270
Cdd:COG1340   75 ELK 77
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 99-274 1.58e-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: 42.34  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853    99 EKKPVCTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHK--------KLAARLEEERGKNKQV 170
Cdd:TIGR00606  782 ESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHEldtvvskiELNRKLIQDQQEQIQH 861

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   171 VLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKqlseFDTEREQLRAKLNRE-- 248
Cdd:TIGR00606  862 LKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEK----DQQEKEELISSKETSnk 937

                          170       180       190
                   ....*....|....*....|....*....|..
gi 767948853   249 --EAHTTDLKEEIDK----MRKMIEQLKRGSD 274
Cdd:TIGR00606  938 kaQDKVNDIKEKVKNihgyMKDIENKIQDGKD 969
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
 127-216 1.70e-03

Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.


Pssm-ID: 461461 [Multi-domain]  Cd Length: 121  Bit Score: 39.30  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  127 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQV---VLMLVKECKQLSGKVIEEAQK-------LEDVM 196
Cdd:pfam04871   1 AKKSELESEASSLKNENTELKAELQELSKQYNSLEQKESQAKELeaeVKKLEEALKKLKAELSEEKQKekekqseLDDLL 80

                          90       100
                  ....*....|....*....|....*..
gi 767948853  197 -------AKLEEEKKKTNELEEELSAE 216
Cdd:pfam04871  81 lllgdleEKVEKYKARLKELGEEVLSD 107
COG5124 COG5124
Protein predicted to be involved in meiotic recombination [Cell division and chromosome ...
 138-274 1.74e-03

Protein predicted to be involved in meiotic recombination [Cell division and chromosome partitioning / General function prediction only];


Pssm-ID: 227453 [Multi-domain]  Cd Length: 209  Bit Score: 40.71  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 138 KLEMEKLQLQALEQEHKKLAARLEEER-GKNKQVVLMLVKECKQ--LSGKVI----------------EEAQKLEDV--- 195
Cdd:COG5124    7 SLAEKRRRLEAIFHDSKDFFQLKEVEKlGSKKQIVLMTVKDLLQqlVDDGVVsvekcgtsniywsfksQTLQKLYDSsel 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 196 -MAKLEEEKKKTNELEEELSAEK----------RRSTEMEAQMEKQLSEFDtEREQLRAKLNREEAHTTDLKEEIDKmrK 264
Cdd:COG5124   87 lKKKIQEVKQDIATYKEEIDKEKatrrkkftegQKNYNREALLEKRKKEQD-EIKKKLNSLQKIEPIRWDAAKIQEK--K 163

                        170
                 ....*....|
gi 767948853 265 MIEQLKRGSD 274
Cdd:COG5124  164 KKVHLNKTTD 173
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 109-271 1.81e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.08  E-value: 1.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   109 SILEAVMAHCKKMQERMSA---------QLAAAESRQKkLEMEKlQLQALEQEHKKLAARLEEERGKNKQVVlmlvKECK 179
Cdd:pfam01576  447 SLLNEAEGKNIKLSKDVSSlesqlqdtqELLQEETRQK-LNLST-RLRQLEDERNSLQEQLEEEEEAKRNVE----RQLS 520

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   180 QLSGKVIEEAQKLED---VMAKLEEEKKKtneLEEELSAEKRRSTEMEAQMEKqlseFDTEREQLRAKLNreeahttDLK 256
Cdd:pfam01576  521 TLQAQLSDMKKKLEEdagTLEALEEGKKR---LQRELEALTQQLEEKAAAYDK----LEKTKNRLQQELD-------DLL 586

                          170
                   ....*....|....*
gi 767948853   257 EEIDKMRKMIEQLKR 271
Cdd:pfam01576  587 VDLDHQRQLVSNLEK 601
YkyA pfam10368
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ...
 123-270 1.82e-03

Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.


Pssm-ID: 431235 [Multi-domain]  Cd Length: 185  Bit Score: 40.27  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  123 ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKL-----AARLEEergkNKQVvlmlvkecKQLSGKVIEEAQKLEDvma 197
Cdd:pfam10368   4 EKIYDHLEEAVELEKPFEEQQEPLVELEKKEQELyeeiiELGMDE----FDEI--------KKLSDEALENVEEREE--- 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767948853  198 KLEEEKKKTNELEEELSaekrrstEMEAQMEK-QLSEFDTEREQLRAKLN-REEAH---TTDLKEEIDKMRKMIEQLK 270
Cdd:pfam10368  69 LLEKEKESIEEAKEEFK-------KIKEIIEEiEDEELKKEAEELIDAMEeRYEAYdelYDAYKKALELDKELYEMLK 139
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 379-515 1.86e-03

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 42.02  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 379 NKIEENGPSTGSTPD-PTSSTPPLPSNAAPPTAQT-----PGIAPQN--SQAPPMHSLHSPCANTSLHPGLNPRIQAARf 450
Cdd:PHA03269  16 NLIIANLNTNIPIPElHTSAATQKPDPAPAPHQAAsrapdPAVAPTSaaSRKPDLAQAPTPAASEKFDPAPAPHQAASR- 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767948853 451 rfqgnANDPDQNGNTTQSP-PSRDVSPTSRDNlvAKQLARNTVTQALSRFTSPQAGAPSRPgvPPT 515
Cdd:PHA03269  95 -----APDPAVAPQLAAAPkPDAAEAFTSAAQ--AHEAPADAGTSAASKKPDPAAHTQHSP--PPF 151
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
135-271 1.87e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 135 RQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLvKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELs 214
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEI-ERYEEQREQARETRDEADEVLEEHEERREELETLEAEI- 260

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767948853 215 aEKRRSTEMEAQMEK------------QLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 271
Cdd:PRK02224 261 -EDLRETIAETEREReelaeevrdlreRLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
 113-270 1.89e-03

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: 40.80  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  113 AVMAHCKKMQERMSAQlAAAESRQKKLEMEKLQLqALEQEHKklaarleeergknkQVVLMLVKECKQLSGKVIEEAQKL 192
Cdd:pfam15665  56 QTLEESLEQHERMKRQ-ALTEFEQYKRRVEEREL-KAEAEHR--------------QRVVELSREVEEAKRAFEEKLESF 119

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767948853  193 EDVMAKLEEEKKKTneLEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLraklnrEEAHttdlKEEIDKMRKMIEQLK 270
Cdd:pfam15665 120 EQLQAQFEQEKRKA--LEELRAKHRQEIQELLTTQRAQSASSLAEQEKL------EELH----KAELESLRKEVEDLR 185
PHA02798 PHA02798
ankyrin-like protein; Provisional
 758-863 2.02e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.74  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 758 DCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHF---ECVELLISYDANINHAADGGQTPLYLACKNGNK---ECIKLLLE 831
Cdd:PHA02798  90 DIVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLE 169

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767948853 832 AGTN-RSVKTTDGWTPVHA----AVDTGNVDSLKLLM 863
Cdd:PHA02798 170 KGVDiNTHNNKEKYDTLHCyfkyNIDRIDADILKLFV 206
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 130-270 2.08e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 41.60  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  130 AAAESRQKKLEMEKL--------QLQALEQEHKKlaaRLEEERGKNKQVvlmlvkecKQLSGKVIEEAQKledvMAKLEE 201
Cdd:pfam05622 109 LAEEAQALKDEMDILressdkvkKLEATVETYKK---KLEDLGDLRRQV--------KLLEERNAEYMQR----TLQLEE 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767948853  202 EKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDT---EREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 270
Cdd:pfam05622 174 ELKKANALRGQLETYKRQVQELHGKLSEESKKADKlefEYKKLEEKLEALQKEKERLIIERDTLRETNEELR 245
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 186-270 2.12e-03

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 39.61  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  186 IEEAQKLEDVMAKLEEEK----KKTNELEEELSAekrrstemeAQMEKQLSEFDtEReQLRAKLNREEAHTTDLKEEIDK 261
Cdd:pfam11559  51 LEFRESLNETIRTLEAEIerlqSKIERLKTQLED---------LERELALLQAK-ER-QLEKKLKTLEQKLKNEKEELQR 119


                  ....*....
gi 767948853  262 MRKMIEQLK 270
Cdd:pfam11559 120 LKNALQQIK 128
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 136-293 2.25e-03

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


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 41.34  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  136 QKKLEMEKlQLQALEQEHKKLAARLeeergknkqvvLMLVKECKQLSGKVIE-EAQKLEDVMA------KLEEE--KKKT 206
Cdd:pfam15905  87 QERGEQDK-RLQALEEELEKVEAKL-----------NAAVREKTSLSASVASlEKQLLELTRVnellkaKFSEDgtQKKM 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  207 NELEEEL-SAEKRRSTEMEA------QMEKQLSEFDTEREQLRAKL--------------NREEAHTTDLKEEIDKMRKM 265
Cdd:pfam15905 155 SSLSMELmKLRNKLEAKMKEvmakqeGMEGKLQVTQKNLEHSKGKVaqleeklvstekekIEEKSETEKLLEYITELSCV 234

                         170       180
                  ....*....|....*....|....*...
gi 767948853  266 IEQLKRGSDSKPSLSLPRKTKDRRLVSI 293
Cdd:pfam15905 235 SEQVEKYKLDIAQLEELLKEKNDEIESL 262
PHA03247 PHA03247
large tegument protein UL36; Provisional
 325-623 2.27e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  325 TMPVKPSTGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPSAnkieengPSTGSTPdPTSSTPPLPSN 404
Cdd:PHA03247 2770 APPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAAS-------PAGPLPP-PTSAQPTAPPP 2841

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  405 AAPP---------------------TAQTPGIAPQNSQAPPMHSLHSPCANTSLHPGLNPRIQAARFRfQGNANDPDQNG 463
Cdd:PHA03247 2842 PPGPpppslplggsvapggdvrrrpPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPP-QPQAPPPPQPQ 2920

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  464 NTTQSPPSRDVSPTSR---DNLVAKQLARNTVTQALSRFTSPQAGA--PSRPGVPPTGDVGTHPPV-----GRTSLKTHG 533
Cdd:PHA03247 2921 PQPPPPPQPQPPPPPPprpQPPLAPTTDPAGAGEPSGAVPQPWLGAlvPGRVAVPRFRVPQPAPSReapasSTPPLTGHS 3000

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  534 VARVdrgnppPIPPKKPGLSQTPSPPHPQLKVII---DSSRASNTGAKVDNKTVASTPSSLpqgNRVINEENLPKSSSPQ 610
Cdd:PHA03247 3001 LSRV------SSWASSLALHEETDPPPVSLKQTLwppDDTEDSDADSLFDSDSERSDLEAL---DPLPPEPHDPFAHEPD 3071

                         330
                  ....*....|...
gi 767948853  611 lPPKPSIDLTVAP 623
Cdd:PHA03247 3072 -PATPEAGARESP 3083
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 130-295 2.29e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.74  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 130 AAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEA--------------QKLEDV 195
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAkkeadeiikelrqlQKGGYA 602

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 196 MAK---LEEEKKKTNE----LEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLrAKLNREEAhttDLKEEIDKMRKMIEQ 268
Cdd:PRK00409 603 SVKaheLIEARKRLNKanekKEKKKKKQKEKQEELKVGDEVKYLSLGQKGEVL-SIPDDKEA---IVQAGIMKMKVPLSD 678

                        170       180
                 ....*....|....*....|....*..
gi 767948853 269 LKRGSDSKPSLSLPRKTKDRRLVSISV 295
Cdd:PRK00409 679 LEKIQKPKKKKKKKPKTVKPKPRTVSL 705
PHA02791 PHA02791
ankyrin-like protein; Provisional
 744-844 2.32e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.18  E-value: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 744 GHSALYSAAKNGHTDCVRLLLSAEAQVNAADkNGFtPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNK 823
Cdd:PHA02791  30 GHSALYYAIADNNVRLVCTLLNAGALKNLLE-NEF-PLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNM 107

                         90       100
                 ....*....|....*....|.
gi 767948853 824 ECIKLLLEAGTNRSVKTTDGW 844
Cdd:PHA02791 108 QTVKLFVKKNWRLMFYGKTGW 128
DUF4618 pfam15397
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ...
 99-271 2.38e-03

Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.


Pssm-ID: 464704 [Multi-domain]  Cd Length: 258  Bit Score: 40.71  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   99 EKKPVCTNPLSILEAvmAHCKKMQErMSAQLaaaesrQKKLEMEKLQLQALEQEHKKLAARLEEERGK------------ 166
Cdd:pfam15397  45 QQYEKFGTIISILEY--SNKKQLQQ-AKAEL------QEWEEKEESKLNKLEQQLEQLNAKIQKTQEElnflstykdkey 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  167 -NKQV-VLMLVKECKQLSGKVIEEAQKLED----VMAKLEEEK-KKTNELEEELSAEKRRSTEmEAQMEKQLSEFDTERE 239
Cdd:pfam15397 116 pVKAVqIANLVRQLQQLKDSQQDELDELEEmrrmVLESLSRKIqKKKEKILSSLAEKTLSPYQ-ESLLQKTRDNQVMLKE 194

                         170       180       190
                  ....*....|....*....|....*....|..
gi 767948853  240 QLRAKLNREEahttdLKEEIDKMRKMIEQLKR 271
Cdd:pfam15397 195 IEQFREFIDE-----LEEEIPKLKAEVQQLQA 221
PRK12705 PRK12705
hypothetical protein; Provisional
 119-280 2.38e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 41.62  E-value: 2.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 119 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEER-----GKNKQVVLMLVKECKQL---SGKVIEEAQ 190
Cdd:PRK12705  33 KEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREElqreeERLVQKEEQLDARAEKLdnlENQLEEREK 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 191 KLEDVMAKLEEEKKKT-NELEEelsAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQL 269
Cdd:PRK12705 113 ALSARELELEELEKQLdNELYR---VAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQAMQRI 189

                        170
                 ....*....|.
gi 767948853 270 KRGSDSKPSLS 280
Cdd:PRK12705 190 ASETASDLSVS 200
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 119-250 2.39e-03

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 41.48  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  119 KKMQERMS--AQLAAAESRQKKLEMEKLQLQALEQEHKK-LAARLEEERGKNKQVVLMlvKECKQLSGK--------VIE 187
Cdd:pfam15709 372 EKMREELEleQQRRFEEIRLRKQRLEEERQRQEEEERKQrLQLQAAQERARQQQEEFR--RKLQELQRKkqqeeaerAEA 449

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767948853  188 EAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEA 250
Cdd:pfam15709 450 EKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEA 512
fliH PRK06669
flagellar assembly protein H; Validated
 119-295 2.44e-03

flagellar assembly protein H; Validated


Pssm-ID: 235850 [Multi-domain]  Cd Length: 281  Bit Score: 40.77  E-value: 2.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 119 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAK 198
Cdd:PRK06669  28 KVLSIKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFEIVEAAEEEAKEELLKKTDEASSIIEKLQMQIEREQEE 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 199 LEEEKKktnELEEELSAEKRRSTEMEAQmEKQLSEFDTEREQLRA---KLNRE-EAHTTDLKEEIDKMRKMI--EQLKRG 272
Cdd:PRK06669 108 WEEELE---RLIEEAKAEGYEEGYEKGR-EEGLEEVRELIEQLNKiieKLIKKrEEILESSEEEIVELALDIakKVIKEI 183

                        170       180
                 ....*....|....*....|....*....
gi 767948853 273 SDSKPSLSLP------RKTKDRRLVSISV 295
Cdd:PRK06669 184 SENSKEIALAlvkellKEVKDATDITIRV 212
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 94-250 2.52e-03

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 40.98  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   94 GAGDKEKKPVCTNPLSILEAVMAHCKKMQERMsAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLM 173
Cdd:TIGR02794  21 GSLYHSVKPEPGGGAEIIQAVLVDPGAVAQQA-NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAA 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767948853  174 LVKECKQlsgkvIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEA 250
Cdd:TIGR02794 100 AEKAAKQ-----AEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEA 171
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 778-866 2.57e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.40  E-value: 2.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 778 FTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTdgWTPVHAAVDTGNVD 857
Cdd:PHA02878  38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYT--LVAIKDAFNNRNVE 115


                 ....*....
gi 767948853 858 SLKLLMYHR 866
Cdd:PHA02878 116 IFKIILTNR 124
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 151-276 2.59e-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: 41.02  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 151 QEHKKLAARLEEERGKN---KQVVLMLVKEcKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEE-ELSAEKRRSTEMEAQ 226
Cdd:cd16269  149 EDREKLVEKYRQVPRKGvkaEEVLQEFLQS-KEAEAEAILQADQALTEKEKEIEAERAKAEAAEqERKLLEEQQRELEQK 227

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767948853 227 MEKQLSEFDTEREQLRAKLNREEAHTTDLKEEI--DKMRKMIEQLKRGSDSK 276
Cdd:cd16269  228 LEDQERSYEEHLRQLKEKMEEERENLLKEQERAleSKLKEQEALLEEGFKEQ 279
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 120-270 2.63e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.70  E-value: 2.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   120 KMQ---ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAArlEEERGKnkqvvLMLVKECKQLSgkviEEAQKLEDvm 196
Cdd:pfam01576  437 KLQselESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ--EETRQK-----LNLSTRLRQLE----DERNSLQE-- 503

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767948853   197 aKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTeREQLRAKLNRE-EAHTTDLKE---EIDKMRKMIEQLK 270
Cdd:pfam01576  504 -QLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA-LEEGKKRLQRElEALTQQLEEkaaAYDKLEKTKNRLQ 579
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 136-276 2.67e-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: 41.54  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  136 QKKLEMEKL---------QLQALEQEHKKLAARLEE---ERGKNKQVVLMLVKECKQLSGKV----------IEEAQKLE 193
Cdd:TIGR04523 451 VKELIIKNLdntresletQLKVLSRSINKIKQNLEQkqkELKSKEKELKKLNEEKKELEEKVkdltkkisslKEKIEKLE 530

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  194 DVMAK-----------------------LEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEA 250
Cdd:TIGR04523 531 SEKKEkeskisdledelnkddfelkkenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEK 610

                         170       180
                  ....*....|....*....|....*....
gi 767948853  251 HTTDLKEEIDKMRK---MIEQLKRGSDSK 276
Cdd:TIGR04523 611 KISSLEKELEKAKKeneKLSSIIKNIKSK 639
FliJ COG2882
Flagellar biosynthesis chaperone FliJ [Cell motility];
111-254 2.73e-03

Flagellar biosynthesis chaperone FliJ [Cell motility];


Pssm-ID: 442129 [Multi-domain]  Cd Length: 142  Bit Score: 39.12  E-value: 2.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 111 LEAVMAHCKKMQERMSAQLAAAesrQKKLEMEKLQLQALEQEHKKLAARLEEergknkqvvlmlvkecKQLSGKVIEEAQ 190
Cdd:COG2882    7 LQTLLDLAEKEEDEAARELGQA---QQALEQAEEQLEQLEQYREEYEQRLQQ----------------KLQQGLSAAQLR 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767948853 191 KLEDVMAKLEEE----KKKTNELEEELsaEKRRSTEMEAQMEKQLseFDT----EREQLRAKLNREEAHTTD 254
Cdd:COG2882   68 NYQQFIARLDEAieqqQQQVAQAEQQV--EQARQAWLEARQERKA--LEKlkerRREEERQEENRREQKELD 135
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
331-515 2.91e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.40  E-value: 2.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 331 STGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPS----ANKIEENGPSTGSTPDPTSSTPPLPSNAA 406
Cdd:PRK12323 383 AQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPApealAAARQASARGPGGAPAPAPAPAAAPAAAA 462

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 407 PPTAQTPGIAPQNSQAPPmhSLHSPCANTSLHPGLNPRIQAARFRFQGNANDPDQNGnttqsPPSRDVSPTSRDNLVAKQ 486
Cdd:PRK12323 463 RPAAAGPRPVAAAAAAAP--ARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAA-----PAGWVAESIPDPATADPD 535

                        170       180
                 ....*....|....*....|....*....
gi 767948853 487 LARNTVTQALSRFTSPQAGAPSRPGVPPT 515
Cdd:PRK12323 536 DAFETLAPAPAAAPAPRAAAATEPVVAPR 564
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
40-268 3.03e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 3.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   40 ELRMLLSVMEGELEARDLVIEALRARRkEVFIQERYGRFNLNDpFLALQRDYEA--------GAGDKEkkpvctnpLSIL 111
Cdd:COG4913   621 ELEEELAEAEERLEALEAELDALQERR-EALQRLAEYSWDEID-VASAEREIAEleaelerlDASSDD--------LAAL 690

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  112 EAVMAHCKKMQERMSAQLAAAESRQKKLEMeklQLQALEQEHKKLAARLEE-ERGKNKQVVLMLVKECKQLSGKVIEE-- 188
Cdd:COG4913   691 EEQLEELEAELEELEEELDELKGEIGRLEK---ELEQAEEELDELQDRLEAaEDLARLELRALLEERFAAALGDAVERel 767

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  189 AQKLEDVMAKLEEEK-KKTNELEEELSAEKRR----STEMEAQMEkQLSEFDTEREQL-------------RAKLNREEA 250
Cdd:COG4913   768 RENLEERIDALRARLnRAEEELERAMRAFNREwpaeTADLDADLE-SLPEYLALLDRLeedglpeyeerfkELLNENSIE 846

                         250
                  ....*....|....*...
gi 767948853  251 HTTDLKEEIDKMRKMIEQ 268
Cdd:COG4913   847 FVADLLSKLRRAIREIKE 864
CCCAP pfam15964
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ...
 119-274 3.03e-03

Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.


Pssm-ID: 435040 [Multi-domain]  Cd Length: 703  Bit Score: 41.43  E-value: 3.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  119 KKMQERMSAQLAAaesRQKKLEMEKLQLQALEQehKKLAARLEEERGKNKQVVLMlvkECKQLSGKVIEEAQKLEDVMAK 198
Cdd:pfam15964 307 KERDDLMSALVSV---RSSLAEAQQRESSAYEQ--VKQAVQMTEEANFEKTKALI---QCEQLKSELERQKERLEKELAS 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  199 ------------LEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMI 266
Cdd:pfam15964 379 qqekraqekealRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQL 458


                  ....*...
gi 767948853  267 EQLKRGSD 274
Cdd:pfam15964 459 NQTKMKKD 466
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 311-644 3.15e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 3.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  311 LVTENADHMKKLPLTMPVKPSTGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPSANKIEENGPSTGS 390
Cdd:PHA03307   92 LSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQ 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  391 TPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAPPMHSLHSPCANTSLHPG-LNPRIQAARFRF--------QGNANDPDQ 461
Cdd:PHA03307  172 AALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPApAPGRSAADDAGAsssdssssESSGCGWGP 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  462 NGNTTQSPPSRDVSPTSRDNLVAkqlARNTVTQALSRFTSPQAGAPSRPGVPPTGDVGTHPPVGRTSLKTHGVARVDRGN 541
Cdd:PHA03307  252 ENECPLPRPAPITLPTRIWEASG---WNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSS 328

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  542 PPPIPPKKPGLSQTPSPPH--------PQLKVIIDSSRASNTGAKVDNKTVASTPSSLPQGNR-VINEENLPKSSSPQLP 612
Cdd:PHA03307  329 TSSSSESSRGAAVSPGPSPsrspspsrPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARaAVAGRARRRDATGRFP 408

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 767948853  613 -----PKPSIDLTVAPAGCAVSALATSQVGAWPAATP 644
Cdd:PHA03307  409 agrprPSPLDAGAASGAFYARYPLLTPSGEPWPGSPP 445
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 140-272 3.36e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 3.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 140 EMEKlQLQALEQE------HKKLAARLEEergknKQVVLMLVKeckqlsgkvieeaqkLEDVMAKLEEEKKKTNELEEEL 213
Cdd:COG1196  197 ELER-QLEPLERQaekaerYRELKEELKE-----LEAELLLLK---------------LRELEAELEELEAELEELEAEL 255

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767948853 214 SAEkrrstemeaqmEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRG 272
Cdd:COG1196  256 EEL-----------EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
V_Alix_like cd08915
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ...
 145-274 3.41e-03

Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains the V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Bro1, and Rim20 all interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. The Alix V-domain contains a binding site, partially conserved in this superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Members of this superfamily have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members, including Alix, HD-PTP, and Bro1, also have a proline-rich region (PRR), which binds multiple partners in Alix, including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2. The C-terminal portion (V-domain and PRR) of Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes; it interacts with a YPxL motif in Doa4s catalytic domain to stimulate its deubiquitination activity. Rim20 may bind the ESCRT-III subunit Snf7, bringing the protease Rim13 (a YPxL-containing transcription factor) into proximity with Rim101, and promoting the proteolytic activation of Rim101. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate often absent in human kidney, breast, lung, and cervical tumors. HD-PTP has a C-terminal catalytically inactive tyrosine phosphatase domain.


Pssm-ID: 185746 [Multi-domain]  Cd Length: 342  Bit Score: 40.79  E-value: 3.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 145 QLQALEQEHKKLAARLEEERGKNKqvvlmlvkeckqLSGKVIEEAQKLEDV-MAKL-EEEKKKTNELEEELSAEKRRSTE 222
Cdd:cd08915  201 EVSELEKERERFISELEIKSRNND------------ILPKLITEYKKNGTTeFEDLfEEHLKKFDKDLTYVEKTKKKQIE 268

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767948853 223 MEAQMEKQLSEFDTEREQLRAKLNREEAhTTDLKEEIDKMRKMIEQLKRGSD 274
Cdd:cd08915  269 LIKEIDAANQEFSQVKNSNDSLDPREEA-LQDLEASYKKYLELKENLNEGSK 319
PHA02917 PHA02917
ankyrin-like protein; Provisional
 793-866 3.46e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 41.14  E-value: 3.46e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767948853 793 VELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAV-DTGNVDSLKLLMYHR 866
Cdd:PHA02917 435 INICLPYLKDINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAInESRNIELLKMLLCHK 509
DUF4355 pfam14265
Domain of unknown function (DUF4355); This family of proteins is found in bacteria and viruses. ...
 195-270 3.46e-03

Domain of unknown function (DUF4355); This family of proteins is found in bacteria and viruses. Proteins in this family are typically between 180 and 214 amino acids in length.


Pssm-ID: 405026 [Multi-domain]  Cd Length: 119  Bit Score: 38.44  E-value: 3.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767948853  195 VMAKLEEEKKKTNELEEELSAEKRRSTEMEAQmEKQlsefDTEREQLRAKLNREEAHTTdLKEEIDKMRKMIEQLK 270
Cdd:pfam14265   8 VAKALATKKNNLEKEIEDEIKEAKKLAKMNAE-EKA----KYELEKLQKELEEEKAELA-RKELKAEARKMLSEKG 77
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 145-270 3.54e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.97  E-value: 3.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 145 QLQALEQEHKKLAARLEEERG---KNKQVVLMLVKECKQLSGKVIEE-------AQKLEDVMAKLEEEKKKTNELEEE-- 212
Cdd:PRK04778 113 LLDLIEEDIEQILEELQELLEseeKNREEVEQLKDLYRELRKSLLANrfsfgpaLDELEKQLENLEEEFSQFVELTESgd 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 213 -------LSAEKRRSTEMEAQMEK---QLSEFDTE-REQLR------AKLNRE---------EAHTTDLKEEIDKMRKMI 266
Cdd:PRK04778 193 yveareiLDQLEEELAALEQIMEEipeLLKELQTElPDQLQelkagyRELVEEgyhldhldiEKEIQDLKEQIDENLALL 272


                 ....
gi 767948853 267 EQLK 270
Cdd:PRK04778 273 EELD 276
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 195-271 3.56e-03

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


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 39.00  E-value: 3.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 195 VMAKLEEEKKK-TNELEEelsAEKRRS--TEMEAQMEKQLSEFDTEREQLRAKLNRE-----EAHTTDLKEEIDKMRKM- 265
Cdd:COG0711   25 ILKALDERQEKiADGLAE---AERAKEeaEAALAEYEEKLAEARAEAAEIIAEARKEaeaiaEEAKAEAEAEAERIIAQa 101


                 ....*....
gi 767948853 266 ---IEQLKR 271
Cdd:COG0711  102 eaeIEQERA 110
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 119-271 3.57e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 41.26  E-value: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  119 KKMQERMSAQLAAAESRQKKL----EMEKL--QLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLsgkviEEAQKL 192
Cdd:pfam05557 359 RAILESYDKELTMSNYSPQLLerieEAEDMtqKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQAL-----RQQESL 433

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  193 EDVMAKLEEE---KKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQ---LRAKLNREEAHTTDLKEEIDKMRKMI 266
Cdd:pfam05557 434 ADPSYSKEEVdslRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKtkvLHLSMNPAAEAYQQRKNQLEKLQAEI 513


                  ....*
gi 767948853  267 EQLKR 271
Cdd:pfam05557 514 ERLKR 518
NOPS_NONA_like cd12945
NOPS domain, including C-terminal coiled-coil region, in p54nrb/PSF/PSP1 homologs from ...
 199-242 3.81e-03

NOPS domain, including C-terminal coiled-coil region, in p54nrb/PSF/PSP1 homologs from invertebrate species; The family contains a DBHS domain (for Drosophila behavior, human splicing), which comprises two conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a charged protein-protein interaction NOPS (NONA and PSP1) domain. This model corresponds to the NOPS domain, with a long helical C-terminal extension , found in Drosophila melanogaster gene no-ontransient A (nonA) encoding puff-specific protein Bj6 (also termed NONA), Chironomus tentans hrp65 gene encoding protein Hrp65 and similar proteins. D. melanogaster NONA is involved in eye development and behavior, and may play a role in circadian rhythm maintenance, similar to vertebrate p54nrb. C. tentans hrp65 is a component of nuclear fibers associated with ribonucleoprotein particles in transit from the gene to the nuclear pore. The NOPS domain specifically binds to the second RNA recognition motif (RRM2) domain of the partner DBHS protein via a substantial interaction surface. Its highly conserved C-terminal residues are critical for functional DBHS dimerization while the highly conserved C-terminal helical extension, forming a right-handed antiparallel heterodimeric coiled-coil, is essential for localization of these proteins to subnuclear bodies.


Pssm-ID: 240580 [Multi-domain]  Cd Length: 100  Bit Score: 37.73  E-value: 3.81e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 767948853 199 LEEEKKKTNELEEELSAEKRRsteMEAQMEKQLSEFDTE--REQLR 242
Cdd:cd12945   58 HELYKQKEEALKRELKMEEEK---LEAQMEYARYEHETEllREQLR 100
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 712-867 3.91e-03

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.83  E-value: 3.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  712 TLLQQAAAQGNVTLLSMLLnEEGLDINYSC-------EDGHSALY------SAAKN-GHTDCVRLLLSAEAQVNAADKNG 777
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLL-ERGASVPARAcgdffvkSQGVDSFYhgesplNAAAClGSPSIVALLSEDPADILTADSLG 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  778 FTPLCAAAAQGHF---------ECVELLISYDANI----------NHAadgGQTPLYLACKNGNKECIKLLLEagTNRSV 838
Cdd:TIGR00870 209 NTLLHLLVMENEFkaeyeelscQMYNFALSLLDKLrdskelevilNHQ---GLTPLKLAAKEGRIVLFRLKLA--IKYKQ 283

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 767948853  839 KTTDGWT--PVH-AAVDTGNVDS-------LKLLMYHRI 867
Cdd:TIGR00870 284 KKFVAWPngQQLlSLYWLEELDGwrrkqsvLELIVVFVI 322
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 137-271 4.22e-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: 40.77  E-value: 4.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  137 KKLEMEKLQLQALEQEHKKLaarlEEERGKNKqvvlmlvkecKQLSgKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAE 216
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKL----EKQKKENK----------KNID-KFLTEIKKKEKELEKLNNKYNDLKKQKEELENE 174

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767948853  217 KRrstemeaQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKM---IEQLKR 271
Cdd:TIGR04523 175 LN-------LLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLesqISELKK 225
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 136-314 4.36e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.19  E-value: 4.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   136 QKKLEMEKLQLQALEQEHKKLAARLEEERGK---NKQVVLMLVKECKQLSGKV-------------IEEAQK-LEDVMAK 198
Cdd:TIGR00606  701 QSKLRLAPDKLKSTESELKKKEKRRDEMLGLapgRQSIIDLKEKEIPELRNKLqkvnrdiqrlkndIEEQETlLGTIMPE 780

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   199 LEEEK------KKTNELEEELSAEKRRSTEMEAqmEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQlkrg 272
Cdd:TIGR00606  781 EESAKvcltdvTIMERFQMELKDVERKIAQQAA--KLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQD---- 854

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 767948853   273 sDSKPSLSLPRKTKDRRLVSISVGTEGTVTRSVACQT-DLVTE 314
Cdd:TIGR00606  855 -QQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLvELSTE 896
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 140-294 4.59e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 40.68  E-value: 4.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 140 EMEKLQLQALEQEHKKLAARLEEErGknkqvvLMLVKECKQLS-----GKVIEEAQKLEDVMAKLEEEKKKTNELEEELS 214
Cdd:PRK05771   5 RMKKVLIVTLKSYKDEVLEALHEL-G------VVHIEDLKEELsnerlRKLRSLLTKLSEALDKLRSYLPKLNPLREEKK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 215 AEKRRSTEmEAQmEKQLSEFDTEREQLRAKLNREeahtTDLKEEIDKMRKMIEQLK--RGSDSKPSLSLPRKTKDRRLVS 292
Cdd:PRK05771  78 KVSVKSLE-ELI-KDVEEELEKIEKEIKELEEEI----SELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYVSVFVGT 151


                 ..
gi 767948853 293 IS 294
Cdd:PRK05771 152 VP 153
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 112-270 4.61e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.93  E-value: 4.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   112 EAVMAHCKKMQERMSAQlaaAESRQKK---------LEMEKLQLQALEQEHKKLAARLEEergknkqvvlmLVKEcKQLS 182
Cdd:pfam01576  612 EEKAISARYAEERDRAE---AEAREKEtralslaraLEEALEAKEELERTNKQLRAEMED-----------LVSS-KDDV 676

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   183 GKVIEEAQKLEDVM-AKLEEEKKKTNELEEELSA-------------------------------EKRRstemeaQMEKQ 230
Cdd:pfam01576  677 GKNVHELERSKRALeQQVEEMKTQLEELEDELQAtedaklrlevnmqalkaqferdlqardeqgeEKRR------QLVKQ 750

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 767948853   231 LSEFDTERE--------------QLRAKLNREEAHTTDL---KEE-IDKMRKMIEQLK 270
Cdd:pfam01576  751 VRELEAELEderkqraqavaakkKLELDLKELEAQIDAAnkgREEaVKQLKKLQAQMK 808
Ax_dynein_light pfam10211
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ...
 184-270 4.72e-03

Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in flagellar and cilia motility. Eukaryotic cilia and flagella are complex organelles consisting of a core structure, the axoneme, which is composed of nine microtubule doublets forming a cylinder that surrounds a pair of central singlet microtubules. This ultra-structural arrangement seems to be one of the most stable micro-tubular assemblies known and is responsible for the flagellar and ciliary movement of a large number of organizms ranging from protozoan to mammals. This light chain interacts directly with the N-terminal half of the heavy chains.


Pssm-ID: 463000 [Multi-domain]  Cd Length: 187  Bit Score: 39.09  E-value: 4.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  184 KVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEfdtereqlraklnREEAHttdlKEEIDKMR 263
Cdd:pfam10211 113 KALQAEQGKAELEKKIADLEEEKEELEKQVAELKAKCEAIEKREEERRQA-------------EEKKH----AEEIAFLK 175


                  ....*..
gi 767948853  264 KMIEQLK 270
Cdd:pfam10211 176 KTNQQLK 182
Nnf1 pfam03980
Nnf1; NNF1 is an essential yeast gene that is necessary for chromosome segregation. It is ...
 168-259 5.00e-03

Nnf1; NNF1 is an essential yeast gene that is necessary for chromosome segregation. It is associated with the spindle poles and forms part of a kinetochore subcomplex called MIND.


Pssm-ID: 461118  Cd Length: 103  Bit Score: 37.61  E-value: 5.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  168 KQVVLMLVKECKQLSGKVIEEaqklEDVMAKLeeekkktNELEE-ELSAEKRRSTEMEAQMEKQL-----------SEFD 235
Cdd:pfam03980   8 RQMVEFLQESCREEFEEILEE----RDVVAKL-------NELDElIEEAKERREEGEGPAWRPSVppeelirahlaPYKQ 76

                          90       100
                  ....*....|....*....|....
gi 767948853  236 TEREQLRAKLNREEAHTTDLKEEI 259
Cdd:pfam03980  77 KQLEQLNARLQKLEAENAALAEEV 100
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 188-269 5.43e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 5.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   188 EAQKLEDVMAKLEEE-----------KKKTNELEEELSAEKRRSTEMEAQ---MEKQLSEFDTEREQLRAKLNREEAHTT 253
Cdd:TIGR02168  678 EIEELEEKIEELEEKiaelekalaelRKELEELEEELEQLRKELEELSRQisaLRKDLARLEAEVEQLEERIAQLSKELT 757

                           90
                   ....*....|....*.
gi 767948853   254 DLKEEIDKMRKMIEQL 269
Cdd:TIGR02168  758 ELEAEIEELEERLEEA 773
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
 137-284 6.21e-03

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 38.88  E-value: 6.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  137 KKLEMEKLQLQALEQEhkkLAARLEEERgknkqvvlmlvkeckqlsgKVIEEAQKLEDVMAKLEEEKKKTNELEEE---- 212
Cdd:pfam15927   1 ARLREEEEERLRAEEE---EAERLEEER-------------------REEEEEERLAAEQDRRAEELEELKHLLEErkea 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  213 ---LSAEKRRSTEMEAQME-------KQLSEFDTEREQLRAKlnrEEAHTTDLKEEIDKMRKMIEQLKRGSDSKPSLSLP 282
Cdd:pfam15927  59 lekLRAEAREEAEWERYMRcdglpdpRDEQEINTFISLWREE---EEEDIDEVMETCTLVLELIEELEELLLDTPPEELA 135


                  ..
gi 767948853  283 RK 284
Cdd:pfam15927 136 EK 137
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 122-276 6.38e-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: 40.42  E-value: 6.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   122 QERMSAQLAAaeSRQKKLEMEKLQLQALEQEHKKLAARLEEERGKnkqvvlmLVKECKQLSgKVIEEAQKLEDVMAKLEE 201
Cdd:TIGR00606  406 EAKTAAQLCA--DLQSKERLKQEQADEIRDEKKGLGRTIELKKEI-------LEKKQEELK-FVIKELQQLEGSSDRILE 475

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   202 EKKKTNELEEELS-AEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEA----HTTDLKEEIDKMRKMIEQLKRGSDSK 276
Cdd:TIGR00606  476 LDQELRKAERELSkAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEqlnhHTTTRTQMEMLTKDKMDKDEQIRKIK 555
fliH PRK06800
flagellar assembly protein H; Validated
 188-270 6.55e-03

flagellar assembly protein H; Validated


Pssm-ID: 180700  Cd Length: 228  Bit Score: 39.09  E-value: 6.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 188 EAQKLEDVMAKLEEEKKKtnELEEELSAEKRRSTEMeAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIE 267
Cdd:PRK06800  21 ELQFPKPIEVEVEEEIQK--DHEELLAQQKSLHKEL-NQLRQEQQKLERERQQLLADREQFQEHVQQQMKEIEAARQQFQ 97


                 ...
gi 767948853 268 QLK 270
Cdd:PRK06800  98 KEQ 100
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 111-270 6.78e-03

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: 38.89  E-value: 6.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  111 LEAVMAHCKKMQERMSAQLAAAESRQKKLEmeklqlQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQ 190
Cdd:pfam04012  45 LAQTIARQKQLERRLEQQTEQAKKLEEKAQ------AALTKGNEELAREALAEKKSLEKQAEALETQLAQQRSAVEQLRK 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  191 KLEDVMAKLEEEKKKTNELEEELSAEKrrsteMEAQMEKQLSEFDTER-----EQLRAKLNREEAhTTDLKEEIDKMRKM 265
Cdd:pfam04012 119 QLAALETKIQQLKAKKNLLKARLKAAK-----AQEAVQTSLGSLSTSSatdsfERIEEKIEEREA-RADAAAELASAVDL 192


                  ....*
gi 767948853  266 IEQLK 270
Cdd:pfam04012 193 DAKLE 197
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 120-229 7.30e-03

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 38.05  E-value: 7.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  120 KMQ----ERMSAQLAA--AESRQKKLEMEKLQ-----------LQALEQEHKKLAARLEE-----ERGKNKQV------- 170
Cdd:pfam12718   1 KMNslklEAENAQERAeeLEEKVKELEQENLEkeqeikslthkNQQLEEEVEKLEEQLKEakekaEESEKLKTnnenltr 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  171 -VLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEK 229
Cdd:pfam12718  81 kIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKE 140
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 185-290 7.45e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 39.88  E-value: 7.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853  185 VIEEAQKLEdvmAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRK 264
Cdd:pfam07888  25 VVPRAELLQ---NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEE 101

                          90       100       110
                  ....*....|....*....|....*....|
gi 767948853  265 MIEQLKRGSDS----KPSLSLPRKTKDRRL 290
Cdd:pfam07888 102 KYKELSASSEElseeKDALLAQRAAHEARI 131
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 182-271 7.47e-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: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 37.95  E-value: 7.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853   182 SGKVIEEAQKLEDVMAKLEEEKKKtneLEEELsaekrrsTEMEAQMEKQLSEFDTEreqlRAKLNREEAhtTDLKEEIDK 261
Cdd:smart00935   6 VQKILQESPAGKAAQKQLEKEFKK---RQAEL-------EKLEKELQKLKEKLQKD----AATLSEAAR--EKKEKELQK 69

                           90
                   ....*....|
gi 767948853   262 MRKMIEQLKR 271
Cdd:smart00935  70 KVQEFQRKQQ 79
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
323-517 7.50e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 40.24  E-value: 7.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 323 PLTMPVKPSTGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPSAnkieengPSTGSTPDPTSSTPPLP 402
Cdd:PRK12323 402 PPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAA-------PAAAARPAAAGPRPVAA 474

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 403 SNAAPPTAQTPGI--APQNSQAPPMHSLHSPCANTSLHPglnpriQAARFRFQGNANDPDQngNTTQSPPSRdvsPTSRD 480
Cdd:PRK12323 475 AAAAAPARAAPAAapAPADDDPPPWEELPPEFASPAPAQ------PDAAPAGWVAESIPDP--ATADPDDAF---ETLAP 543

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767948853 481 NLVAKQLARntVTQALSRFTSPQAGAPSRPGVPPTGD 517
Cdd:PRK12323 544 APAAAPAPR--AAAATEPVVAPRPPRASASGLPDMFD 578
YscO-like pfam16789
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ...
 209-275 8.25e-03

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


Pssm-ID: 435583 [Multi-domain]  Cd Length: 160  Bit Score: 37.89  E-value: 8.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767948853  209 LEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRaklNREEAHTTDLKEEIDKMRKMIEQLKRGSDS 275
Cdd:pfam16789   5 LEQVLDIKKKRVEEAEKVVKDKKRALEKEKEKLA---ELEAERDKVRKHKKAKMQQLRDEMDRGTTS 68
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
120-274 8.36e-03

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 39.72  E-value: 8.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 120 KMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSgkvIEEAQKLEDVMAKL 199
Cdd:COG5059  406 IMKSIISGTFERKKLLKEEGWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHDLS---SLLSSIPEETSDRV 482

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767948853 200 EEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQ---LRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSD 274
Cdd:COG5059  483 ESEKASKLRSSASTKLNLRSSRSHSKFRDHLNGSNSSTKELslnQVDLAGSERKVSQSVGELLRETQSLNKSLSSLGD 560
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
122-270 8.84e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 8.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 122 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEErgknkqvVLMLVKECKQLSGKVIEEAQKLEDVMAKLEE 201
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRED-------ADDLEERAEELREEAAELESELEEAREAVED 381

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767948853 202 EKKKTNELEEELSAEKRRSTEMEAQMEK---QLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 270
Cdd:PRK02224 382 RREEIEELEEEIEELRERFGDAPVDLGNaedFLEELREERDELREREAELEATLRTARERVEEAEALLEAGK 453
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 137-278 8.96e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 38.88  E-value: 8.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 137 KKLEMEKLQLQALEQEHKKLAARLEEergknkqvvlmLVKECKQLsGKVIEE-AQKLEDvMAKLEEEKKKT-NELEEELS 214
Cdd:cd07596    4 QEFEEAKDYILKLEEQLKKLSKQAQR-----------LVKRRREL-GSALGEfGKALIK-LAKCEEEVGGElGEALSKLG 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767948853 215 -AEKRRSTEMEAQMEKQLSEF-DTEREQLR----AKL---NREEA--HTTDLKEEIDKMRKMIEQLKRGSDSKPS 278
Cdd:cd07596   71 kAAEELSSLSEAQANQELVKLlEPLKEYLRycqaVKEtldDRADAllTLQSLKKDLASKKAQLEKLKAAPGIKPA 145
PHA03095 PHA03095
ankyrin-like protein; Provisional
 673-833 9.79e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.62  E-value: 9.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 673 ASSCRPGASDSLLVTASGWSPSLTPLLMSggpaplagrpTLLQQAAAQGNVTLLSML-LNEEGLDINYSCEDGHSALYSA 751
Cdd:PHA03095 195 LQSFKPRARIVRELIRAGCDPAATDMLGN----------TPLHSMATGSSCKRSLVLpLLIAGISINARNRYGQTPLHYA 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 752 AKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLIS-------YDANINHAADGGQTPLYlackNGNKE 824
Cdd:PHA03095 265 AVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAknpsaetVAATLNTASVAGGDIPS----DATRL 340

                        170
                 ....*....|
gi 767948853 825 C-IKLLLEAG 833
Cdd:PHA03095 341 CvAKVVLRGA 350
NtpH COG2811
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal ...
 184-264 1.00e-02

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


Pssm-ID: 442060 [Multi-domain]  Cd Length: 108  Bit Score: 36.82  E-value: 1.00e-02
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948853 184 KVIEEA-QKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQ--LSEFDTEREQLRAKLnREEAhttdlKEEID 260
Cdd:COG2811    8 KEIKEAeEEADEIIEEAKEEREERIAEAREEAEEIIEQAEEEAEEEAQerLEEAREEAEAEAEEI-IEEG-----EKEAE 81


                 ....
gi 767948853 261 KMRK 264
Cdd:COG2811   82 ALKK 85
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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