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Conserved domains on  [gi|2024509102|ref|XP_040530791|]
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eukaryotic translation initiation factor 3 subunit A [Gallus gallus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK12678 super family cl36163
transcription termination factor Rho; Provisional
901-1150 3.20e-15

transcription termination factor Rho; Provisional


The actual alignment was detected with superfamily member PRK12678:

Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 80.72  E-value: 3.20e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  901 RRGGETESEWRRAPVERDWRRGEARDDERPfrrgddlPRRSDDLPRRGDDLPRRGPAEEKERPSVESSEDRPPRREGDED 980
Cdd:PRK12678    58 ARGGGAAAAAATPAAPAAAARRAARAAAAA-------RQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARER 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  981 RPPRREGDEDRPLRRGLDEDRPPRRGLDDDRGSWRAADDDRGPRRGMDDDRPPRRALDDDRpprralDDDRPPRRALDDD 1060
Cdd:PRK12678   131 RERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERG------RREERGRDGDDRD 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1061 RPPRRALDDDRPPRRSLDDDRGSWRAADDDRGPRRGLDDDRPPRRALDDDRPPRRGLDDDRGSWRaaDDDRGPRRGLDDD 1140
Cdd:PRK12678   205 RRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDR--DRRGRRGGDGGNE 282
                          250
                   ....*....|
gi 2024509102 1141 RGPRRGLDDD 1150
Cdd:PRK12678   283 REPELREDDV 292
PINT smart00088
motif in proteasome subunits, Int-6, Nip-1 and TRIP-15; Also called the PCI (Proteasome, COP9, ...
427-498 4.66e-12

motif in proteasome subunits, Int-6, Nip-1 and TRIP-15; Also called the PCI (Proteasome, COP9, Initiation factor 3) domain. Unknown function.


:

Pssm-ID: 214509 [Multi-domain]  Cd Length: 88  Bit Score: 63.03  E-value: 4.66e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024509102   427 YVPHLQNNTILRLLQQVAQIYQSIEFSRLATLVPFvDAFQLERSIVDAARHCDLQVRLDHTTRTLSFGSDLN 498
Cdd:smart00088    2 LVERLQRKIRLTNLLQLSEPYSSISLSDLAKLLGL-SVPEVEKLVSKAIRDGEISAKIDQVNGIVEFEEVDP 72
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
517-769 1.26e-10

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.11  E-value: 1.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  517 EQIRNQLTAMSSALakalavikppHLLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLESL-----NIQREK 591
Cdd:COG1196    270 EELRLELEELELEL----------EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELeeeleELEEEL 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  592 EELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELdpdfimA 671
Cdd:COG1196    340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL------L 413
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  672 KQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKTAYEEQ----RVRDMELWEQQEEERITTLQLEREKALEHK 747
Cdd:COG1196    414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEalleLLAELLEEAALLEAALAELLEELAEAAARL 493
                          250       260
                   ....*....|....*....|..
gi 2024509102  748 NRLSRMLEDRDLFEARLKALRR 769
Cdd:COG1196    494 LLLLEAEADYEGFLEGVKAALL 515
SF-CC1 super family cl36939
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
1100-1227 9.50e-03

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


The actual alignment was detected with superfamily member TIGR01622:

Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 40.29  E-value: 9.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1100 DRPPRRALDDDRPPRRGLDDDRGSWRAADDDRGPRRGLDDDRGPRRGLDDDRGPWRNTDDDrlsrrdddrgpwRSSEDSR 1179
Cdd:TIGR01622    4 DRERERLRDSSSAGDRDRRRDKGRERSRDRSRDRERSRSRRRDRHRDRDYYRGRERRSRSR------------RPNRRYR 71
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2024509102 1180 PgpwrpfgkpggwREREKAREDSWGPPRDSRPPGDREWDRDKDRDDNE 1227
Cdd:TIGR01622   72 P------------REKRRRRGDSYRRRRDDRRSRREKPRARDGTPEPL 107
 
Name Accession Description Interval E-value
PRK12678 PRK12678
transcription termination factor Rho; Provisional
901-1150 3.20e-15

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 80.72  E-value: 3.20e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  901 RRGGETESEWRRAPVERDWRRGEARDDERPfrrgddlPRRSDDLPRRGDDLPRRGPAEEKERPSVESSEDRPPRREGDED 980
Cdd:PRK12678    58 ARGGGAAAAAATPAAPAAAARRAARAAAAA-------RQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARER 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  981 RPPRREGDEDRPLRRGLDEDRPPRRGLDDDRGSWRAADDDRGPRRGMDDDRPPRRALDDDRpprralDDDRPPRRALDDD 1060
Cdd:PRK12678   131 RERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERG------RREERGRDGDDRD 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1061 RPPRRALDDDRPPRRSLDDDRGSWRAADDDRGPRRGLDDDRPPRRALDDDRPPRRGLDDDRGSWRaaDDDRGPRRGLDDD 1140
Cdd:PRK12678   205 RRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDR--DRRGRRGGDGGNE 282
                          250
                   ....*....|
gi 2024509102 1141 RGPRRGLDDD 1150
Cdd:PRK12678   283 REPELREDDV 292
PINT smart00088
motif in proteasome subunits, Int-6, Nip-1 and TRIP-15; Also called the PCI (Proteasome, COP9, ...
427-498 4.66e-12

motif in proteasome subunits, Int-6, Nip-1 and TRIP-15; Also called the PCI (Proteasome, COP9, Initiation factor 3) domain. Unknown function.


Pssm-ID: 214509 [Multi-domain]  Cd Length: 88  Bit Score: 63.03  E-value: 4.66e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024509102   427 YVPHLQNNTILRLLQQVAQIYQSIEFSRLATLVPFvDAFQLERSIVDAARHCDLQVRLDHTTRTLSFGSDLN 498
Cdd:smart00088    2 LVERLQRKIRLTNLLQLSEPYSSISLSDLAKLLGL-SVPEVEKLVSKAIRDGEISAKIDQVNGIVEFEEVDP 72
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
517-769 1.26e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.11  E-value: 1.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  517 EQIRNQLTAMSSALakalavikppHLLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLESL-----NIQREK 591
Cdd:COG1196    270 EELRLELEELELEL----------EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELeeeleELEEEL 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  592 EELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELdpdfimA 671
Cdd:COG1196    340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL------L 413
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  672 KQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKTAYEEQ----RVRDMELWEQQEEERITTLQLEREKALEHK 747
Cdd:COG1196    414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEalleLLAELLEEAALLEAALAELLEELAEAAARL 493
                          250       260
                   ....*....|....*....|..
gi 2024509102  748 NRLSRMLEDRDLFEARLKALRR 769
Cdd:COG1196    494 LLLLEAEADYEGFLEGVKAALL 515
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
517-805 2.24e-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: 65.47  E-value: 2.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  517 EQIRNQLTAMSSALAKALaviKPPHLLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERleslnIQREKEELEQ 596
Cdd:TIGR02169  194 DEKRQQLERLRREREKAE---RYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEK-----LTEEISELEK 265
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  597 REAELQKVRKAEEERLRQEAKERE---KERILQEHEQIK--KKTVRERLEQIKKTELG-AKAFKDID--IEDLEELDpdf 668
Cdd:TIGR02169  266 RLEEIEQLLEELNKKIKDLGEEEQlrvKEKIGELEAEIAslERSIAEKERELEDAEERlAKLEAEIDklLAEIEELE--- 342
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  669 imaKQVEQLEKEKKELQERLKNQEKKIDYFERakRLEEIPL-IKTAYEEQRVRDMELWEQQEE---------ERITTLQL 738
Cdd:TIGR02169  343 ---REIEEERKRRDKLTEEYAELKEELEDLRA--ELEEVDKeFAETRDELKDYREKLEKLKREinelkreldRLQEELQR 417
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024509102  739 EREKALEHKNRLSRMLEDRDLFEARLKALRRTVYED--KLKQFQERLAEERRNRLEERKKQRKEERRIT 805
Cdd:TIGR02169  418 LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQewKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486
PTZ00121 PTZ00121
MAEBL; Provisional
530-782 6.88e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.01  E-value: 6.88e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  530 LAKALAVIKPPHLLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERK-ERLESLNIQREKEELEQREAElqKVRKAE 608
Cdd:PTZ00121  1539 AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAE--EAKKAE 1616
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  609 EERLRQEaKEREKERILQEHEQIKKKTVRE--RLEQIKKTELGAKAFKDIDIEDLEEldpDFIMAKQVEQLEKEKKELQE 686
Cdd:PTZ00121  1617 EAKIKAE-ELKKAEEEKKKVEQLKKKEAEEkkKAEELKKAEEENKIKAAEEAKKAEE---DKKKAEEAKKAEEDEKKAAE 1692
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  687 RLKNQEKKIDYFERAKRLEEIPL-----IKTAYEEQRVRDMELWEQQEEERITTLQLEREKalEHKNRLSRMLEDRDLFE 761
Cdd:PTZ00121  1693 ALKKEAEEAKKAEELKKKEAEEKkkaeeLKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE--EEKKKIAHLKKEEEKKA 1770
                          250       260
                   ....*....|....*....|.
gi 2024509102  762 ARLKALRRTVYEDKLKQFQER 782
Cdd:PTZ00121  1771 EEIRKEKEAVIEEELDEEDEK 1791
PCI pfam01399
PCI domain; This domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and ...
405-494 9.33e-10

PCI domain; This domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15).


Pssm-ID: 460195  Cd Length: 105  Bit Score: 57.23  E-value: 9.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  405 SRVSKVLNWVKDQAEKEPELQLYVPHLQNNTILRLLQQVAQIYQSIEFSRLATLVPfVDAFQLERSIVDAARHCDLQVRL 484
Cdd:pfam01399   16 SEFEEILADYKEELLLDDGLAEHLEDLRRKIREHNLRQLSKPYSSISLSDLAKLLG-LSVDEVEKILAKLIRDGRIRAKI 94
                           90
                   ....*....|
gi 2024509102  485 DHTTRTLSFG 494
Cdd:pfam01399   95 DQVNGIVVFS 104
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
540-802 2.18e-08

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: 59.21  E-value: 2.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  540 PHLLQEKEEQHQLAVtafLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKER 619
Cdd:pfam02463  201 KLKEQAKKALEYYQL---KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEE 277
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  620 EKERILQEhEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMAK------QVEQLEKEKKELQERLKNQEK 693
Cdd:pfam02463  278 EKEKKLQE-EELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKElkkekeEIEELEKELKELEIKREAEEE 356
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  694 KIDYFERAKRLEEIPLIKTAYEEQRVRDMELWEQQEEERITTLQLEREKALEHKNRLSRMLEDRDLFEARLKALRRTVYE 773
Cdd:pfam02463  357 EEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEE 436
                          250       260
                   ....*....|....*....|....*....
gi 2024509102  774 DKLKQFQERLAEERRNRLEERKKQRKEER 802
Cdd:pfam02463  437 ESIELKQGKLTEEKEELEKQELKLLKDEL 465
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
518-754 3.28e-06

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: 50.65  E-value: 3.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  518 QIRNqltamSSALAKALAVIK---------PPHLLQEKEEQHQ----LAVTAFLKNSRK----EHQRILARrqTIEERKE 580
Cdd:cd16269     32 QIEN-----SAAVQKALAHYEeqmeqrvqlPTETLQELLDLHAacekEALEVFMKRSFKdedqKFQKKLME--QLEEKKE 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  581 RLESLNiqrEKEELEQREAELQKVRKAEEERLRQE--AKE-------REKERILQEHEQIKKKTVR--ERLE---QIKKT 646
Cdd:cd16269    105 EFCKQN---EEASSKRCQALLQELSAPLEEKISQGsySVPggyqlylEDREKLVEKYRQVPRKGVKaeEVLQeflQSKEA 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  647 ElgAKAFKDIDiEDLEELDPDFIMAK-QVEQLEKEKKELQERLKNQEKKIDYFERakrleeipliktAYEEQrvrdMELW 725
Cdd:cd16269    182 E--AEAILQAD-QALTEKEKEIEAERaKAEAAEQERKLLEEQQRELEQKLEDQER------------SYEEH----LRQL 242
                          250       260
                   ....*....|....*....|....*....
gi 2024509102  726 EQQEEERITTLQLEREKALEHKNRLSRML 754
Cdd:cd16269    243 KEKMEEERENLLKEQERALESKLKEQEAL 271
COG4253 COG4253
Uncharacterized conserved protein, DUF2345 family [Function unknown];
878-1155 6.18e-05

Uncharacterized conserved protein, DUF2345 family [Function unknown];


Pssm-ID: 443395 [Multi-domain]  Cd Length: 900  Bit Score: 47.73  E-value: 6.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  878 GLDDPFSRKESRWGDRGESESSWRRGGETESEWRRAPVERDWRRGEARDDERPFRRGDDLPRRSDDLPRRGDDLPRRGPA 957
Cdd:COG4253    197 AFADDRLTERRASAEAASRADAAALRDLRLALRLARRAATAADDAQTTDDARLTADDSAADAGSLSGSGGDGGAAGGSLA 276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  958 EEKERPSVESSeDRPPRREGDEDRPPRREGDEDRPLRRGLDEDRPPRRGLDDDRGSWRAADDDRGPRRGMDDDRPPRRAL 1037
Cdd:COG4253    277 EATSSLRVPAA-SVSLARYQRARRAAAAAAAADARAGGADAAGGVGTGGGRRLAAGLAGAAAEEEEAVGAEARARRRRLL 355
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1038 DDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPP-------RRSLDDDRGSWRAADDDRGPRRGLDDDRPPRRALDDD 1110
Cdd:COG4253    356 RAARAAIRLLAAAALALLALGRGALAGRSPAAAAGPgivggtdRRARRRATAFVDRAAGPPPRTQRARRPLLPRPRGAGG 435
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2024509102 1111 RPPRRGLDDDRGSWRAADDDRGPRRGLDDDRGPRRGLDDDRGPWR 1155
Cdd:COG4253    436 PPPRVVSTRAGDTPSADDDDGGRRVVRDDRRVAWVGGGESWGAGG 480
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
970-1130 1.83e-04

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 45.65  E-value: 1.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  970 DRPPRREGDEDRPPRREGDEDRPLRRGLDEDRpprrglDDDRgswraadddrgPRRGMDddrppRRALDDDRPPRRALDD 1049
Cdd:TIGR01642    2 DEEPDREREKSRGRDRDRSSERPRRRSRDRSR------FRDR-----------HRRSRE-----RSYREDSRPRDRRRYD 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1050 DRPPRRALDDDRPPRRalddDRPPRRSLDDDRGSwraadddRGPRRGLddDRPPRRALDDDRPPRRGLDDDRGSWRAADD 1129
Cdd:TIGR01642   60 SRSPRSLRYSSVRRSR----DRPRRRSRSVRSIE-------QHRRRLR--DRSPSNQWRKDDKKRSLWDIKPPGYELVTA 126

                   .
gi 2024509102 1130 D 1130
Cdd:TIGR01642  127 D 127
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
559-778 3.59e-04

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 45.00  E-value: 3.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  559 KNSRKEhQRILARRQTIEERK---ERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERIlqeheqikKKT 635
Cdd:NF033838   198 KEPRDE-EKIKQAKAKVESKKaeaTRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRA--------KRG 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  636 VRERLEQIKKTELGAKAfKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQ--EKKIDYFERA-KRLEeiplIKT 712
Cdd:NF033838   269 VLGEPATPDKKENDAKS-SDSSVGEETLPSPSLKPEKKVAEAEKKVEEAKKKAKDQkeEDRRNYPTNTyKTLE----LEI 343
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024509102  713 AYEEQRVRDMELW-------EQQEEERITTLQLEREKALEHKNRLSRMLEDRDlfEARLKALRRTVYEDKLKQ 778
Cdd:NF033838   344 AESDVKVKEAELElvkeeakEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRK--KAEEEAKRKAAEEDKVKE 414
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
936-1150 3.98e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 44.90  E-value: 3.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  936 DLPRRSDDLPRRGDDLPRRGPAEEKERPSVESSEDRPPRREGDEDRPPRREGDEDRPLRRGLDEDRPPRRGLDDDRGSWR 1015
Cdd:NF033609   629 DSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 708
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1016 AADDDRGPRRGMDDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRSLDDDRGSWRAADDDRGPRR 1095
Cdd:NF033609   709 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 788
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024509102 1096 GLDDDRPPRRALDDDRPPRRGLDDDRGSWRAADDDRGPRRGLDDDRGPRRGLDDD 1150
Cdd:NF033609   789 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 843
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
926-1150 2.74e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 42.20  E-value: 2.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  926 DDERPFRRGDDLPRRSDDLPRRGDDLPRRGPAEEKERPSVESSEDRPPRREGDEDRPPRREGDEDRPLRRGLDEDRPPRR 1005
Cdd:NF033609   623 DSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 702
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1006 GLDDDRGSWRAADDDRGPRRGMDDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRSLDDDRGSWR 1085
Cdd:NF033609   703 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 782
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024509102 1086 AADDDRGPRRGLDDDRPPRRALDDDRPPRRGLDDDRGSWRAADDDRGPRRGLDDDRGPRRGLDDD 1150
Cdd:NF033609   783 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 847
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
967-1226 3.66e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 41.82  E-value: 3.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  967 SSEDRPPRREGDEDRPPRREGDEDRPLRRGLDEDRPPRRGLDDDRGSWRAADDDRGPRRGMDDDRPPRRALDDDRPPRRA 1046
Cdd:NF033609   620 SDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 699
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1047 LDDDRPPRRALDDDRPPRRALDDDRPPRRSLDDDRGSWRAADDDRGPRRGLDDDRPPRRALDDDRPPRRGLDDDRGSWRA 1126
Cdd:NF033609   700 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 779
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1127 ADDDRGPRRGLDDDRGPRRGLDDDRGPWRNTDDDRLSRRDDDrgpwrSSEDSRPgpwrpfgkpggwrEREKAREDSWGPP 1206
Cdd:NF033609   780 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD-----SDSDSDS-------------DSDSDSDSDSDSD 841
                          250       260
                   ....*....|....*....|
gi 2024509102 1207 RDSRPPGDREWDRDKDRDDN 1226
Cdd:NF033609   842 SDSDSDSDSDSDSDSESDSN 861
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
966-1181 7.32e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 41.05  E-value: 7.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  966 ESSEDRPPRREGDEDRPPRREGDEDRPLRRGLDEDRPPRRGLDDDRGSWRAADDDRGPRRGMDDDRPPRRALDDDRPPRR 1045
Cdd:NF033609   649 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 728
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1046 ALDDDRPPRRALDDDRPPRRALDDDRPPRRSLDDDRGSWRAADDDRGPRRGLDDDRPPRRALDDDRPPRRGLDDDRGSWR 1125
Cdd:NF033609   729 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 808
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024509102 1126 AADDDRGPRRGLDDDRGPRRGLDDDRGPWRNTDDDRLSRRDDDRGPWRSSE---DSRPG 1181
Cdd:NF033609   809 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDsnsDSESG 867
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
1100-1227 9.50e-03

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 40.29  E-value: 9.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1100 DRPPRRALDDDRPPRRGLDDDRGSWRAADDDRGPRRGLDDDRGPRRGLDDDRGPWRNTDDDrlsrrdddrgpwRSSEDSR 1179
Cdd:TIGR01622    4 DRERERLRDSSSAGDRDRRRDKGRERSRDRSRDRERSRSRRRDRHRDRDYYRGRERRSRSR------------RPNRRYR 71
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2024509102 1180 PgpwrpfgkpggwREREKAREDSWGPPRDSRPPGDREWDRDKDRDDNE 1227
Cdd:TIGR01622   72 P------------REKRRRRGDSYRRRRDDRRSRREKPRARDGTPEPL 107
 
Name Accession Description Interval E-value
PRK12678 PRK12678
transcription termination factor Rho; Provisional
901-1150 3.20e-15

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 80.72  E-value: 3.20e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  901 RRGGETESEWRRAPVERDWRRGEARDDERPfrrgddlPRRSDDLPRRGDDLPRRGPAEEKERPSVESSEDRPPRREGDED 980
Cdd:PRK12678    58 ARGGGAAAAAATPAAPAAAARRAARAAAAA-------RQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARER 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  981 RPPRREGDEDRPLRRGLDEDRPPRRGLDDDRGSWRAADDDRGPRRGMDDDRPPRRALDDDRpprralDDDRPPRRALDDD 1060
Cdd:PRK12678   131 RERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERG------RREERGRDGDDRD 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1061 RPPRRALDDDRPPRRSLDDDRGSWRAADDDRGPRRGLDDDRPPRRALDDDRPPRRGLDDDRGSWRaaDDDRGPRRGLDDD 1140
Cdd:PRK12678   205 RRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDR--DRRGRRGGDGGNE 282
                          250
                   ....*....|
gi 2024509102 1141 RGPRRGLDDD 1150
Cdd:PRK12678   283 REPELREDDV 292
PRK12678 PRK12678
transcription termination factor Rho; Provisional
956-1156 3.98e-13

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 74.17  E-value: 3.98e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  956 PAEEKERPSVESSEDRPPRREGDEDRPPRREGDEDRPLRRGLDEDRPPRRGLDDDRGSWRAADDDRGPRRGMDDDRPPRR 1035
Cdd:PRK12678    76 AARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATE 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1036 ALDDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRSLDDDRgswraaDDDRGPRRGLDDDRPPRRALDDDRPPRR 1115
Cdd:PRK12678   156 ARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGD------DRDRRDRREQGDRREERGRRDGGDRRGR 229
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2024509102 1116 GLDDDRGSWRAADDDRGPRRGLDDDRGPRRGLDDDRGPWRN 1156
Cdd:PRK12678   230 RRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRD 270
PRK12678 PRK12678
transcription termination factor Rho; Provisional
882-1110 1.35e-12

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 72.24  E-value: 1.35e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  882 PFSRKESRWGDRGESESSWRRGGETESEWRRAPVERDWRRGEARDDERPFRRGDDLPRRSDDLPRRGDdlPRRGPAEEKE 961
Cdd:PRK12678    73 PAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRG--AARKAGEGGE 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  962 RPSVESSEDRPPRREGDEDRPPRREGDEDRPLRRGLDEDRPPRRGLDDDRGswraaDDDRGPRRGMDDDRPPRRALDDDR 1041
Cdd:PRK12678   151 QPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGD-----DRDRRDRREQGDRREERGRRDGGD 225
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024509102 1042 PPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRSLDDDRGSWRaaDDDRGPRRGLDDDRPPRRALDDD 1110
Cdd:PRK12678   226 RRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDR--DRRGRRGGDGGNEREPELREDDV 292
PINT smart00088
motif in proteasome subunits, Int-6, Nip-1 and TRIP-15; Also called the PCI (Proteasome, COP9, ...
427-498 4.66e-12

motif in proteasome subunits, Int-6, Nip-1 and TRIP-15; Also called the PCI (Proteasome, COP9, Initiation factor 3) domain. Unknown function.


Pssm-ID: 214509 [Multi-domain]  Cd Length: 88  Bit Score: 63.03  E-value: 4.66e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024509102   427 YVPHLQNNTILRLLQQVAQIYQSIEFSRLATLVPFvDAFQLERSIVDAARHCDLQVRLDHTTRTLSFGSDLN 498
Cdd:smart00088    2 LVERLQRKIRLTNLLQLSEPYSSISLSDLAKLLGL-SVPEVEKLVSKAIRDGEISAKIDQVNGIVEFEEVDP 72
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
517-769 1.26e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.11  E-value: 1.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  517 EQIRNQLTAMSSALakalavikppHLLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLESL-----NIQREK 591
Cdd:COG1196    270 EELRLELEELELEL----------EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELeeeleELEEEL 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  592 EELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELdpdfimA 671
Cdd:COG1196    340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL------L 413
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  672 KQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKTAYEEQ----RVRDMELWEQQEEERITTLQLEREKALEHK 747
Cdd:COG1196    414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEalleLLAELLEEAALLEAALAELLEELAEAAARL 493
                          250       260
                   ....*....|....*....|..
gi 2024509102  748 NRLSRMLEDRDLFEARLKALRR 769
Cdd:COG1196    494 LLLLEAEADYEGFLEGVKAALL 515
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
575-803 1.45e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.11  E-value: 1.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  575 IEERKERLESLNIQREK--------EELEQREAELQ----KVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQ 642
Cdd:COG1196    195 LGELERQLEPLERQAEKaeryrelkEELKELEAELLllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  643 ikktelgakAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDyfERAKRLEEIplikTAYEEQRVRDM 722
Cdd:COG1196    275 ---------ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE--ELEEELAEL----EEELEELEEEL 339
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  723 ELWEQQEEERITTLQLEREKALEHKNRLSRMLEDRDLFEARLKALRRTVYEDKLKQFQERLAEERRNRLEERKKQRKEER 802
Cdd:COG1196    340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419

                   .
gi 2024509102  803 R 803
Cdd:COG1196    420 E 420
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
517-805 2.24e-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: 65.47  E-value: 2.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  517 EQIRNQLTAMSSALAKALaviKPPHLLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERleslnIQREKEELEQ 596
Cdd:TIGR02169  194 DEKRQQLERLRREREKAE---RYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEK-----LTEEISELEK 265
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  597 REAELQKVRKAEEERLRQEAKERE---KERILQEHEQIK--KKTVRERLEQIKKTELG-AKAFKDID--IEDLEELDpdf 668
Cdd:TIGR02169  266 RLEEIEQLLEELNKKIKDLGEEEQlrvKEKIGELEAEIAslERSIAEKERELEDAEERlAKLEAEIDklLAEIEELE--- 342
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  669 imaKQVEQLEKEKKELQERLKNQEKKIDYFERakRLEEIPL-IKTAYEEQRVRDMELWEQQEE---------ERITTLQL 738
Cdd:TIGR02169  343 ---REIEEERKRRDKLTEEYAELKEELEDLRA--ELEEVDKeFAETRDELKDYREKLEKLKREinelkreldRLQEELQR 417
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024509102  739 EREKALEHKNRLSRMLEDRDLFEARLKALRRTVYED--KLKQFQERLAEERRNRLEERKKQRKEERRIT 805
Cdd:TIGR02169  418 LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQewKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486
PTZ00121 PTZ00121
MAEBL; Provisional
530-782 6.88e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.01  E-value: 6.88e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  530 LAKALAVIKPPHLLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERK-ERLESLNIQREKEELEQREAElqKVRKAE 608
Cdd:PTZ00121  1539 AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAE--EAKKAE 1616
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  609 EERLRQEaKEREKERILQEHEQIKKKTVRE--RLEQIKKTELGAKAFKDIDIEDLEEldpDFIMAKQVEQLEKEKKELQE 686
Cdd:PTZ00121  1617 EAKIKAE-ELKKAEEEKKKVEQLKKKEAEEkkKAEELKKAEEENKIKAAEEAKKAEE---DKKKAEEAKKAEEDEKKAAE 1692
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  687 RLKNQEKKIDYFERAKRLEEIPL-----IKTAYEEQRVRDMELWEQQEEERITTLQLEREKalEHKNRLSRMLEDRDLFE 761
Cdd:PTZ00121  1693 ALKKEAEEAKKAEELKKKEAEEKkkaeeLKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE--EEKKKIAHLKKEEEKKA 1770
                          250       260
                   ....*....|....*....|.
gi 2024509102  762 ARLKALRRTVYEDKLKQFQER 782
Cdd:PTZ00121  1771 EEIRKEKEAVIEEELDEEDEK 1791
PCI pfam01399
PCI domain; This domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and ...
405-494 9.33e-10

PCI domain; This domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15).


Pssm-ID: 460195  Cd Length: 105  Bit Score: 57.23  E-value: 9.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  405 SRVSKVLNWVKDQAEKEPELQLYVPHLQNNTILRLLQQVAQIYQSIEFSRLATLVPfVDAFQLERSIVDAARHCDLQVRL 484
Cdd:pfam01399   16 SEFEEILADYKEELLLDDGLAEHLEDLRRKIREHNLRQLSKPYSSISLSDLAKLLG-LSVDEVEKILAKLIRDGRIRAKI 94
                           90
                   ....*....|
gi 2024509102  485 DHTTRTLSFG 494
Cdd:pfam01399   95 DQVNGIVVFS 104
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
542-800 1.27e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.03  E-value: 1.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  542 LLQEKEEQHQLA-VTAFLKNSRKEHQRILARRQTIEERKE--RLESLNIQREKEELEQRE-------AELQKVRKAEEER 611
Cdd:COG1196    231 LLKLRELEAELEeLEAELEELEAELEELEAELAELEAELEelRLELEELELELEEAQAEEyellaelARLEQDIARLEER 310
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  612 LRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDpdfimAKQVEQLEKEKKELQERLKNQ 691
Cdd:COG1196    311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE-----EALLEAEAELAEAEEELEELA 385
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  692 EKKIDYFERAKRLEEIPLIKTAYEEQRVRDMELWEQQEEERITTLQLEREKALEHKNRLSRMLEDRDLFEARLKALRRTV 771
Cdd:COG1196    386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
                          250       260
                   ....*....|....*....|....*....
gi 2024509102  772 YEDKLKQFQERLAEERRNRLEERKKQRKE 800
Cdd:COG1196    466 AELLEEAALLEAALAELLEELAEAAARLL 494
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
561-806 4.80e-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: 61.23  E-value: 4.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  561 SRKEHQRILARRQTIEErkerleslnIQREKEELEQREAELQKVRKAEEERLRQ-----EAKEREKERILQEHEQIKKK- 634
Cdd:TIGR02168  665 SAKTNSSILERRREIEE---------LEEKIEELEEKIAELEKALAELRKELEEleeelEQLRKELEELSRQISALRKDl 735
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  635 --------TVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMAKQV-EQLEKEKKELQERLKNQEKKIDYFERAKRLE 705
Cdd:TIGR02168  736 arleaeveQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEiEELEAQIEQLKEELKALREALDELRAELTLL 815
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  706 EiplIKTAYEEQRVRDMELWEQQEEERITTLQLEREKALEHKNRLSRMLEDRDLFEARLKAlRRTVYEDKLKQFQERLAE 785
Cdd:TIGR02168  816 N---EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES-ELEALLNERASLEEALAL 891
                          250       260
                   ....*....|....*....|.
gi 2024509102  786 ERRNRLEERKKQRKEERRITY 806
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSE 912
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
911-1215 7.48e-09

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 60.57  E-value: 7.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  911 RRAPVERDWRRGEARDDERPFRRGDDLPRRSDDLPRRGDDLPRRGPAEEKERPSVESSEDRPPRRegDEDRPPRREGDED 990
Cdd:PHA03307   133 DLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPST--PPAAASPRPPRRS 210
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  991 RPLRRGLDEDRPprRGLDDDRGSWRAADDDRGPRRGMDDDRPPRRALDDDRPPRRALddDRPPRRALDDDRPPRRAlddd 1070
Cdd:PHA03307   211 SPISASASSPAP--APGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITL--PTRIWEASGWNGPSSRP---- 282
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1071 rPPRRSLDDDRGSWRAADDDRGPRRGLDddrPPRRALDDDRPPRRGLDDDRGSWRAADDDRGPRRGLDDDRGPRRGldDD 1150
Cdd:PHA03307   283 -GPASSSSSPRERSPSPSPSSPGSGPAP---SSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPS--RP 356
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024509102 1151 RGPwrntdddrlsrrDDDRGPWRSSEDSRPGPWRPFGKPGGWREREKAREDSWGPPRDSRPPGDR 1215
Cdd:PHA03307   357 PPP------------ADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPA 409
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
560-804 1.62e-08

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: 59.31  E-value: 1.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  560 NSRKEHQRILARRQTIEERKERLESLniQREKEELEQREAELQKVRKAEEERLRqeAKEREKERILQEHEqikkkTVRER 639
Cdd:TIGR02169  668 FSRSEPAELQRLRERLEGLKRELSSL--QSELRRIENRLDELSQELSDASRKIG--EIEKEIEQLEQEEE-----KLKER 738
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  640 LEQIKktelgakafkdidiEDLEELDPDFIMAKQ-VEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKTAYEEQR 718
Cdd:TIGR02169  739 LEELE--------------EDLSSLEQEIENVKSeLKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLE 804
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  719 --VRDMELWEQQEEERITTLQLER---EKALEHKNRLSRMLEDR--------DLFEARLKALRRTV--YEDKLKQFQERL 783
Cdd:TIGR02169  805 eeVSRIEARLREIEQKLNRLTLEKeylEKEIQELQEQRIDLKEQiksiekeiENLNGKKEELEEELeeLEAALRDLESRL 884
                          250       260
                   ....*....|....*....|.
gi 2024509102  784 AEERRNRLEERKKQRKEERRI 804
Cdd:TIGR02169  885 GDLKKERDELEAQLRELERKI 905
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
540-802 2.18e-08

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: 59.21  E-value: 2.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  540 PHLLQEKEEQHQLAVtafLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKER 619
Cdd:pfam02463  201 KLKEQAKKALEYYQL---KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEE 277
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  620 EKERILQEhEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMAK------QVEQLEKEKKELQERLKNQEK 693
Cdd:pfam02463  278 EKEKKLQE-EELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKElkkekeEIEELEKELKELEIKREAEEE 356
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  694 KIDYFERAKRLEEIPLIKTAYEEQRVRDMELWEQQEEERITTLQLEREKALEHKNRLSRMLEDRDLFEARLKALRRTVYE 773
Cdd:pfam02463  357 EEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEE 436
                          250       260
                   ....*....|....*....|....*....
gi 2024509102  774 DKLKQFQERLAEERRNRLEERKKQRKEER 802
Cdd:pfam02463  437 ESIELKQGKLTEEKEELEKQELKLLKDEL 465
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
519-770 2.64e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.54  E-value: 2.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  519 IRNQLTAMSSALAKALAVIKPPHLLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLeslniqrekEELEQRE 598
Cdd:PRK03918   212 ISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI---------EELEEKV 282
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  599 AELQKVRKAEEERLRQeakEREKERILQEHEQIKKK--TVRERLEQIKKTelgakafkdidIEDLEEldpdfiMAKQVEQ 676
Cdd:PRK03918   283 KELKELKEKAEEYIKL---SEFYEEYLDELREIEKRlsRLEEEINGIEER-----------IKELEE------KEERLEE 342
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  677 LEKEKKELQERLKNQEKKIDYFERAKRL-EEIPLIKTAYEEQRVRDMELWEQQEEERITTLQLEREKALEHKNRLSRMLE 755
Cdd:PRK03918   343 LKKKLKELEKRLEELEERHELYEEAKAKkEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIK 422
                          250
                   ....*....|....*
gi 2024509102  756 DRDLFEARLKALRRT 770
Cdd:PRK03918   423 ELKKAIEELKKAKGK 437
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
880-1123 3.42e-08

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 58.26  E-value: 3.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  880 DDPFSRKESRWGDRGESESSWRRGGETESEWRRAPVERDWRRGEARDDERPFRRGDDLPRRS---DDLPRRGDDLPRRGP 956
Cdd:PHA03307   192 EPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENecpLPRPAPITLPTRIWE 271
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  957 AEEKERPSVESSEDRPPRREGDEDRPPRREGDEDRPL---RRGLDEDRPPRRGLDDDRGSWRAADDDRGPRRGMDDDRPP 1033
Cdd:PHA03307   272 ASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPApssPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSP 351
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1034 RRAldddrPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRsldddRGSWRAADDDRGprrgldDDRPPRRalDDDRPP 1113
Cdd:PHA03307   352 SPS-----RPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRR-----RARAAVAGRARR------RDATGRF--PAGRPR 413
                          250
                   ....*....|
gi 2024509102 1114 RRGLDDDRGS 1123
Cdd:PHA03307   414 PSPLDAGAAS 423
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
576-804 4.87e-08

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: 58.06  E-value: 4.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  576 EERKERLESLNIQREKEELEQREAELQKVRKAEEERL-------RQEAKEREKERILQEHEQIKKKTVRERLEQIKKTEL 648
Cdd:pfam02463  153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIidleelkLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  649 GA-KAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKTayEEQRVRDMELWEQ 727
Cdd:pfam02463  233 KLnEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEE--LKSELLKLERRKV 310
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024509102  728 QEEERITTLQLEREKALEHKNRLSRMLEDRDLFEARLKALRRTVYEDKLKQFQERLAEERRNRLEERKKQRKEERRI 804
Cdd:pfam02463  311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLS 387
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
542-803 8.08e-08

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: 57.29  E-value: 8.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  542 LLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKERE- 620
Cdd:pfam02463  229 LDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERr 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  621 ---KERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDpdfIMAKQVEQLEKEKKELQERLKNQEKKIDY 697
Cdd:pfam02463  309 kvdDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEE---EEEELEKLQEKLEQLEEELLAKKKLESER 385
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  698 FERAKRLEEIPLIKTAYEEQRVRDM-----------------ELWEQQEEERITTLQLEREKALEHKNRLSRMLEDRDLF 760
Cdd:pfam02463  386 LSSAAKLKEEELELKSEEEKEAQLLlelarqledllkeekkeELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL 465
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2024509102  761 EARLKALRRTVYEDKLKQFQERLAEERRNRLEERKKQRKEERR 803
Cdd:pfam02463  466 ELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSG 508
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
424-811 9.02e-08

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: 56.90  E-value: 9.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  424 LQLYVPHLQNNTILRLLQQVAQIYQSIEFSRLATLVPFVDAFQLERS-IVDAARHCDLQVRLDHTTRTLSFGSDLNYSTR 502
Cdd:pfam02463  580 LRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEgILKDTELTKLKESAKAKESGLRKGVSLEEGLA 659
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  503 EDAPLGPQLQSMPSEQIRNQLTAMSSALAKALAVIKPPHLLQEKEEQHQLAVTAFLK-------------NSRKEHQRIL 569
Cdd:pfam02463  660 EKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKleaeelladrvqeAQDKINEELK 739
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  570 ARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEE----ERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKK 645
Cdd:pfam02463  740 LLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEErektEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEE 819
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  646 TELGAKAFKDIDIEDLEELDPDFIMA-KQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKTAYEEQRVRDMEL 724
Cdd:pfam02463  820 EQLLIEQEEKIKEEELEELALELKEEqKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEK 899
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  725 WEQQEEERITTLQLEREKALEHKNRLSRMLEDRDLFEARlkalRRTVYEDKLKQFQERLAEERRNRLEERKKQRKEERR- 803
Cdd:pfam02463  900 KELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPE----ELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKv 975

                   ....*....
gi 2024509102  804 -ITYYREKE 811
Cdd:pfam02463  976 nLMAIEEFE 984
PRK12704 PRK12704
phosphodiesterase; Provisional
542-683 9.54e-08

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 56.32  E-value: 9.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  542 LLQEKEEQHQLavtaflknsRKEHQR-ILARRQTIEERKERLE--SLNIQREKEELEQREAELQKVRKAEEERLRQ-EAK 617
Cdd:PRK12704    59 LLEAKEEIHKL---------RNEFEKeLRERRNELQKLEKRLLqkEENLDRKLELLEKREEELEKKEKELEQKQQElEKK 129
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024509102  618 EREKERILQEHeqikkktvRERLEQIkkTELGAKAFKDIDIEDLE-ELDPDfiMAKQVEQLEKEKKE 683
Cdd:PRK12704   130 EEELEELIEEQ--------LQELERI--SGLTAEEAKEILLEKVEeEARHE--AAVLIKEIEEEAKE 184
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
564-846 1.04e-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: 56.67  E-value: 1.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  564 EHQRILARRQTiEERKERLESLNIQREKEELEQreaELQKVRKAEE-ERLRQEAKER------EKERILQEH----EQIK 632
Cdd:pfam17380  279 QHQKAVSERQQ-QEKFEKMEQERLRQEKEEKAR---EVERRRKLEEaEKARQAEMDRqaaiyaEQERMAMERerelERIR 354
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  633 KKTVRERLEQIKKTELGAKAFKDIDIEDL--------EELDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRL 704
Cdd:pfam17380  355 QEERKRELERIRQEEIAMEISRMRELERLqmerqqknERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQ 434
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  705 EEIPLIktayEEQRVRDMELWEQQEEERITTLQLEREKALEHK-NRLSRMLEDRDlfEARLKALRRTVYEDKLKQFQERL 783
Cdd:pfam17380  435 REVRRL----EEERAREMERVRLEEQERQQQVERLRQQEEERKrKKLELEKEKRD--RKRAEEQRRKILEKELEERKQAM 508
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024509102  784 AEERRNRLEERKKQrkEERRITYYREKEEEEQRLREEQLLKEreekerIEREKREQEQREYQE 846
Cdd:pfam17380  509 IEEERKRKLLEKEM--EERQKAIYEEERRREAEEERRKQQEM------EERRRIQEQMRKATE 563
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
517-759 1.67e-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: 55.90  E-value: 1.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  517 EQIRNQLTAMSSALAKALAVIKPPHLLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEE--RKERLESLNIQREKEEl 594
Cdd:pfam17380  363 ERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEqiRAEQEEARQREVRRLE- 441
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  595 EQREAELQKVRKAEEER------LRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELdpdf 668
Cdd:pfam17380  442 EERAREMERVRLEEQERqqqverLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKL---- 517
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  669 imakqveqLEKEKKELQERLKNQEKKidyferakrleeipliKTAYEEQRvrdmelwEQQEEERITTLQLEREKALEHKN 748
Cdd:pfam17380  518 --------LEKEMEERQKAIYEEERR----------------REAEEERR-------KQQEMEERRRIQEQMRKATEERS 566
                          250
                   ....*....|.
gi 2024509102  749 RLSRMLEDRDL 759
Cdd:pfam17380  567 RLEAMEREREM 577
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
545-784 2.61e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.46  E-value: 2.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  545 EKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLESLNIQREKE------ELEQREAELQKVRKA----EEERLRQ 614
Cdd:PRK03918   161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREineissELPELREELEKLEKEvkelEELKEEI 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  615 EAKEREKERILQEHEQIKKKtVRERLEQIKKTELGAKAFKDIdIEDLEELDPDfimAKQVEQLEKEKKELQERLKNQEKK 694
Cdd:PRK03918   241 EELEKELESLEGSKRKLEEK-IRELEERIEELKKEIEELEEK-VKELKELKEK---AEEYIKLSEFYEEYLDELREIEKR 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  695 IDYFER-----AKRLEEIPLIKTAYEEQRVRDMELWEQQEEERITTLQLEREKAL-EHKNRLSRMLEDRDL--FEARLKA 766
Cdd:PRK03918   316 LSRLEEeingiEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKkEELERLKKRLTGLTPekLEKELEE 395
                          250       260
                   ....*....|....*....|
gi 2024509102  767 L--RRTVYEDKLKQFQERLA 784
Cdd:PRK03918   396 LekAKEEIEEEISKITARIG 415
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
569-690 2.76e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 2.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  569 LARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTEL 648
Cdd:COG1196    662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2024509102  649 gakafKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKN 690
Cdd:COG1196    742 -----LEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
PTZ00121 PTZ00121
MAEBL; Provisional
558-803 4.27e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.76  E-value: 4.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  558 LKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQK---VRKAEEERLRQEAKEREKER---ILQEHEQI 631
Cdd:PTZ00121  1084 KEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKaeeARKAEDARKAEEARKAEDAKrveIARKAEDA 1163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  632 KKKTVRERLEQIKKTELGAKAfkdIDIEDLEELDP--DFIMAKQVEQLEKEKKELQERLKNQEKKIdyfERAKRLEEIPl 709
Cdd:PTZ00121  1164 RKAEEARKAEDAKKAEAARKA---EEVRKAEELRKaeDARKAEAARKAEEERKAEEARKAEDAKKA---EAVKKAEEAK- 1236
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  710 iKTAYEEQR---VRDMELWEQQEEERITTLQLERE--KALEHK--NRLSRMLEDRDLFEARLKALRRTVYEDKLKQFQER 782
Cdd:PTZ00121  1237 -KDAEEAKKaeeERNNEEIRKFEEARMAHFARRQAaiKAEEARkaDELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAK 1315
                          250       260
                   ....*....|....*....|.
gi 2024509102  783 LAEERRNRLEERKKQRKEERR 803
Cdd:PTZ00121  1316 KADEAKKKAEEAKKKADAAKK 1336
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
542-784 6.95e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.15  E-value: 6.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  542 LLQEKEEQHQLAVtafLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQK-VRKAEEERLRQEAKERE 620
Cdd:COG4913    244 LEDAREQIELLEP---IRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAeLARLEAELERLEARLDA 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  621 KERILQEHEQIKKKTVRERLEQIKktelgakafkdidiedleeldpdfimaKQVEQLEKEKKELQERLKNQEkkidyfER 700
Cdd:COG4913    321 LREELDELEAQIRGNGGDRLEQLE---------------------------REIERLERELEERERRRARLE------AL 367
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  701 AKRLE-EIPLIKTAYEEQRVRDMELWEQQEEERittlQLEREKALEHKNRLSRMLEDRDLFEARLKAL--RRTVYEDKLK 777
Cdd:COG4913    368 LAALGlPLPASAEEFAALRAEAAALLEALEEEL----EALEEALAEAEAALRDLRRELRELEAEIASLerRKSNIPARLL 443

                   ....*..
gi 2024509102  778 QFQERLA 784
Cdd:COG4913    444 ALRDALA 450
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
908-1127 9.23e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 53.64  E-value: 9.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  908 SEWRRAPVERDWRRGEARDDERPFRRGDDLPRRSDDLPRRGDDLPRRGPAEEKERPSVESSEDRPPRREGDEDR--PPRR 985
Cdd:PHA03307   759 SNPSLVPAKLAEALALLEPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAASRTASKRKSRSHTPDGGSESsgPARP 838
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  986 EGDEDRPlrrgldedrPPRRGLDDDRGSWRAADDDRGPRRGMDDDRPPRRALDDDRPPRRALDDDRPPRRA-LDDDRPPR 1064
Cdd:PHA03307   839 PGAAARP---------PPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAAAPPAGApAPRPRPAP 909
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024509102 1065 RALDDDRPPRRSldDDRGSWRaadddRGPRRGLDDDRPPRRALDDDRPPR---RGLDDDR--GSWRAA 1127
Cdd:PHA03307   910 RVKLGPMPPGGP--DPRGGFR-----RVPPGDLHTPAPSAAALAAYCPPEvvaELVDHPLfpEPWRPA 970
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
588-717 9.93e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 52.89  E-value: 9.93e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  588 QREKEElEQREAELQKVRKAEEERLRQEAKEREKERilQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPD 667
Cdd:PRK09510    80 QRKKKE-QQQAEELQQKQAAEQERLKQLEKERLAAQ--EQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRA 156
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2024509102  668 FIMAKQVEQlEKEKKELQERLKNQEKkidyfERAKRLEEIPLIKTAYEEQ 717
Cdd:PRK09510   157 AAAAKKAAA-EAKKKAEAEAAKKAAA-----EAKKKAEAEAAAKAAAEAK 200
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
479-758 1.19e-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: 53.19  E-value: 1.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  479 DLQVRLDHTTrtlsfgSDLNYSTREDAPLGPQLQSmpsEQIRN-QLTAMSSALA---KALAVIKPPHLLQEKEEQHQLav 554
Cdd:pfam05483  454 DLEIQLTAIK------TSEEHYLKEVEDLKTELEK---EKLKNiELTAHCDKLLlenKELTQEASDMTLELKKHQEDI-- 522
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  555 taflKNSRKEHQRILARRQTIEERKERLESlNIQREKEELEQREAELQ-KVRKAEEERLRQEAKEREKERILQEHEQI-- 631
Cdd:pfam05483  523 ----INCKKQEERMLKQIENLEEKEMNLRD-ELESVREEFIQKGDEVKcKLDKSEENARSIEYEVLKKEKQMKILENKcn 597
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  632 -KKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMAKQVE-QLEKEKKELQERLKNQEKKIDyferAKRLEEIPL 709
Cdd:pfam05483  598 nLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLElELASAKQKFEEIIDNYQKEIE----DKKISEEKL 673
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024509102  710 IKTAYEEQRVRDMELWEQQEEERITTLQLEREKAL--EHKNRLSRMLEDRD 758
Cdd:pfam05483  674 LEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALmeKHKHQYDKIIEERD 724
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
564-745 1.21e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 51.08  E-value: 1.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  564 EHQRILARRQTIEERKERLESL--NIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLE 641
Cdd:COG1579      4 EDLRALLDLQELDSELDRLEHRlkELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  642 QIKKtelgAKAFKDIdiedLEELDpdfIMAKQVEQLEKEKKELQERLKNQEKKIDyfERAKRLEEipLIKTAYEEQRVRD 721
Cdd:COG1579     84 NVRN----NKEYEAL----QKEIE---SLKRRISDLEDEILELMERIEELEEELA--ELEAELAE--LEAELEEKKAELD 148
                          170       180
                   ....*....|....*....|....
gi 2024509102  722 MELWEQQEEerITTLQLEREKALE 745
Cdd:COG1579    149 EELAELEAE--LEELEAEREELAA 170
PRK12704 PRK12704
phosphodiesterase; Provisional
572-707 1.45e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 52.47  E-value: 1.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  572 RQTIEERKERLEslNIQREKEeLEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQikkkTVRERLEQIKKTElgak 651
Cdd:PRK12704    41 KRILEEAKKEAE--AIKKEAL-LEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEE----NLDRKLELLEKRE---- 109
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024509102  652 afkdidiedlEELDpdfimaKQVEQLEKEKKELQERLKNQEKKIDyfERAKRLEEI 707
Cdd:PRK12704   110 ----------EELE------KKEKELEQKQQELEKKEEELEELIE--EQLQELERI 147
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
517-805 1.72e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 1.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  517 EQIRNQLTAMSSALAKALAVIKPPHLLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQ 596
Cdd:COG1196    354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  597 REAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVR-ERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMAKQVE 675
Cdd:COG1196    434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALlEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  676 QLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIK---TAYEEQRVRDMELWEQQEEERITTLQLEREK---ALEHKNR 749
Cdd:COG1196    514 LLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQnivVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRaraALAAALA 593
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024509102  750 LSRMLEDRDLFEARLKALRRTVYEDKLKQFQERLAEERRNRLEERKKQRKEERRIT 805
Cdd:COG1196    594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
PTZ00121 PTZ00121
MAEBL; Provisional
546-803 1.91e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 1.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  546 KEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERIL 625
Cdd:PTZ00121  1256 KFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK 1335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  626 QEHE------QIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDYFE 699
Cdd:PTZ00121  1336 KKAEeakkaaEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAA 1415
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  700 RAKRLEEiplIKTAYEEQRVRDMELWEQQEEERITTLQLEREKALEHKNRLSRMLEDRDLFEARLKALRRTVYEDKLKQF 779
Cdd:PTZ00121  1416 AKKKADE---AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKA 1492
                          250       260
                   ....*....|....*....|....
gi 2024509102  780 QERLAEERRNRLEERKKQRKEERR 803
Cdd:PTZ00121  1493 EEAKKKADEAKKAAEAKKKADEAK 1516
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
542-802 2.72e-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: 51.99  E-value: 2.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  542 LLQEKEEQHQLAVTAFLKNS---------RKEHQRILARRQT----IEERKERLESLniqreKEELEQREAELQKVRKAE 608
Cdd:TIGR02169  693 LQSELRRIENRLDELSQELSdasrkigeiEKEIEQLEQEEEKlkerLEELEEDLSSL-----EQEIENVKSELKELEARI 767
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  609 EERLRQEAKEREKE-----RILQEHEQIKKKTVRERLEQIKKTElgaKAFKDIDiEDLEELDPDfimakqVEQLEKEKKE 683
Cdd:TIGR02169  768 EELEEDLHKLEEALndleaRLSHSRIPEIQAELSKLEEEVSRIE---ARLREIE-QKLNRLTLE------KEYLEKEIQE 837
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  684 LQERLKNQEKKIDyfERAKRLEEIPLIKTAYEEQrVRDMELWEQQEEERITTLQLEREKALEHKNRLSRMLED--RDLFE 761
Cdd:TIGR02169  838 LQEQRIDLKEQIK--SIEKEIENLNGKKEELEEE-LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEleAQIEK 914
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024509102  762 ARLKALRRTV-----------YEDKLKQFQERLAEERRNRLEERKKQRKEER 802
Cdd:TIGR02169  915 KRKRLSELKAklealeeelseIEDPKGEDEEIPEEELSLEDVQAELQRVEEE 966
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
518-754 3.28e-06

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: 50.65  E-value: 3.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  518 QIRNqltamSSALAKALAVIK---------PPHLLQEKEEQHQ----LAVTAFLKNSRK----EHQRILARrqTIEERKE 580
Cdd:cd16269     32 QIEN-----SAAVQKALAHYEeqmeqrvqlPTETLQELLDLHAacekEALEVFMKRSFKdedqKFQKKLME--QLEEKKE 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  581 RLESLNiqrEKEELEQREAELQKVRKAEEERLRQE--AKE-------REKERILQEHEQIKKKTVR--ERLE---QIKKT 646
Cdd:cd16269    105 EFCKQN---EEASSKRCQALLQELSAPLEEKISQGsySVPggyqlylEDREKLVEKYRQVPRKGVKaeEVLQeflQSKEA 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  647 ElgAKAFKDIDiEDLEELDPDFIMAK-QVEQLEKEKKELQERLKNQEKKIDYFERakrleeipliktAYEEQrvrdMELW 725
Cdd:cd16269    182 E--AEAILQAD-QALTEKEKEIEAERaKAEAAEQERKLLEEQQRELEQKLEDQER------------SYEEH----LRQL 242
                          250       260
                   ....*....|....*....|....*....
gi 2024509102  726 EQQEEERITTLQLEREKALEHKNRLSRML 754
Cdd:cd16269    243 KEKMEEERENLLKEQERALESKLKEQEAL 271
PRK12678 PRK12678
transcription termination factor Rho; Provisional
1016-1226 3.31e-06

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 51.44  E-value: 3.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1016 AADDDRGPRRGMDDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRsldDDRGSWRAADDDRGPRR 1095
Cdd:PRK12678    69 TPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQAR---ERRERGEAARRGAARKA 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1096 GLDDDRPPRRALDDDRPPRRGLDDDRgswRAADDDRGPRRglDDDRGPRRGLDDDRGPWRNTDDDRLSRRDDDRGPWRSS 1175
Cdd:PRK12678   146 GEGGEQPATEARADAAERTEEEERDE---RRRRGDREDRQ--AEAERGERGRREERGRDGDDRDRRDRREQGDRREERGR 220
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024509102 1176 EDSRPGPWRPFGKPGGWREREKAREDSWGPPRDSRPP-GDREWDRDKDRDDN 1226
Cdd:PRK12678   221 RDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGrGGRRGRRFRDRDRR 272
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
573-784 3.59e-06

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


Pssm-ID: 462861 [Multi-domain]  Cd Length: 302  Bit Score: 50.34  E-value: 3.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  573 QTIEERKERLESLNIQREKEE-LEQREAELQKVRKAEEERL-----RQEAKEREKERILQEHEqiKKKTVRERLE----- 641
Cdd:pfam09728    1 KAARELMQLLNKLDSPEEKLAaLCKKYAELLEEMKRLQKDLkklkkKQDQLQKEKDQLQSELS--KAILAKSKLEklcre 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  642 ---QIKKTELGAKAFKDIDIEDLEELDPDF------IMAKQVEQLEKEKK------ELQERLKN----QEKKIDYFERak 702
Cdd:pfam09728   79 lqkQNKKLKEESKKLAKEEEEKRKELSEKFqstlkdIQDKMEEKSEKNNKlreeneELREKLKSlieqYELRELHFEK-- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  703 rleeipLIKTAYEEQRVRDMELWEQQEEERITTLQLEREKALEHKNRLSRMLEDrdlfEARLKAlRRTVYEDKLKQFQER 782
Cdd:pfam09728  157 ------LLKTKELEVQLAEAKLQQATEEEEKKAQEKEVAKARELKAQVQTLSET----EKELRE-QLNLYVEKFEEFQDT 225

                   ..
gi 2024509102  783 LA 784
Cdd:pfam09728  226 LN 227
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
562-801 4.49e-06

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: 51.51  E-value: 4.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  562 RKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQE-------------------------A 616
Cdd:pfam02463  171 KKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEyllyldylklneeridllqellrdeQ 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  617 KEREKERILQEHEQIKKKTVRERLEQIKK-----TELGAKAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQ 691
Cdd:pfam02463  251 EEIESSKQEIEKEEEKLAQVLKENKEEEKekklqEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  692 EKKIDYFERAKRLEEIPLIKTAYEEQRVRDM----ELWEQQEEERITTLQLEREKALEHKNRLSRMLEDRDLFEAR---L 764
Cdd:pfam02463  331 KKEKEEIEELEKELKELEIKREAEEEEEEELeklqEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEaqlL 410
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2024509102  765 KALRRTVYEDKLKQFQERLAEERRNRLEERKKQRKEE 801
Cdd:pfam02463  411 LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLT 447
PRK12678 PRK12678
transcription termination factor Rho; Provisional
984-1224 5.33e-06

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 51.06  E-value: 5.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  984 RREGDEDRPLRRGLDEDRPPRRGLDDDRGSWRAADDDRGPRRGMDDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPP 1063
Cdd:PRK12678    58 ARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAA 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1064 RRaldddRPPRRSLDDDRGSWRAADDDRGPRRglDDDRPPRRALDDDRPPRRGLDDDRGSWRAADDDRGPRRGLDDDRGP 1143
Cdd:PRK12678   138 RR-----GAARKAGEGGEQPATEARADAAERT--EEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRRE 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1144 RRGLDDDRGPWRNTDDDRLSRRDDDRGPWRSSEDSRPGPWRPFGKPGGWREREKAREDswgppRDSRppGDREWDRDKDR 1223
Cdd:PRK12678   211 QGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRD-----RDRR--GRRGGDGGNER 283

                   .
gi 2024509102 1224 D 1224
Cdd:PRK12678   284 E 284
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
542-780 5.98e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 5.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  542 LLQEKEEQHQLAVTAfLKNSRKEHQRILARRQTIEERKERLEsLNIQREKEELEQREAELQKVRK--AEEERLRQEAKER 619
Cdd:TIGR02168  296 EISRLEQQKQILRER-LANLERQLEELEAQLEELESKLDELA-EELAELEEKLEELKEELESLEAelEELEAELEELESR 373
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  620 EKEriLQEHEQIKKKTVRERLEQIKKTElgakafkdidiEDLEELDpdfimaKQVEQLEKEKKELQERLKNQEKKIDYFE 699
Cdd:TIGR02168  374 LEE--LEEQLETLRSKVAQLELQIASLN-----------NEIERLE------ARLERLEDRRERLQQEIEELLKKLEEAE 434
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  700 RAKRLEEIPLIKTAYEE--QRVRDMELWEQQEEERITTLQLEREKALEHKNRLSRMLEDRDLFEARLKALRRTVYEDKLK 777
Cdd:TIGR02168  435 LKELQAELEELEEELEElqEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514

                   ...
gi 2024509102  778 QFQ 780
Cdd:TIGR02168  515 QSG 517
PHA03321 PHA03321
tegument protein VP11/12; Provisional
950-1212 6.15e-06

tegument protein VP11/12; Provisional


Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 50.73  E-value: 6.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  950 DLPRRG-PAEEKERPSVESSEDRPP----RREGDEDRPPRREGDEDRPlrrglDEDRPPRRGLDDDRGswRAADDDRGPR 1024
Cdd:PHA03321   407 ELFRTGvPSEHYEASLRLLSSRQPPgapaPRRDNDPPPPPRARPGSTP-----ACARRARAQRARDAG--PEYVDPLGAL 479
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1025 RGMDD--DRPPRRAldddRPPRRAL----DDDRPPRRALDDDRPPRRALDDDRPPRRSLDDDRGSWRAADDDRGPRR--- 1095
Cdd:PHA03321   480 RRLPAgaAPPPEPA----AAPSPATyytrMGGGPPRLPPRNRATETLRPDWGPPAAAPPEQMEDPYLEPDDDRFDRRdga 555
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1096 -GLDDDRPPRRALDDDRPPRRGLDDDRGswRAADDDRGPRRGLDDDRGPRRGLD---DDRGPWrntdddrlsrrdddrGP 1171
Cdd:PHA03321   556 aAAATSHPREAPAPDDDPIYEGVSDSEE--PVYEEIPTPRVYQNPLPRPMEGAGeppDLDAPT---------------SP 618
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2024509102 1172 WRSSEDSRPGpWR--PFGKPggwreREKAREDSWGPPRDSRPP 1212
Cdd:PHA03321   619 WVEEENPIYG-WGdsPLFSP-----PPAARFPPPDPALSPEPP 655
PTZ00121 PTZ00121
MAEBL; Provisional
543-1039 6.32e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 6.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  543 LQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREA-----ELQKvrKAEEERLRQEAK 617
Cdd:PTZ00121  1320 AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkkadAAKK--KAEEKKKADEAK 1397
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  618 EREKERILQEHEQIKKKTVRERLEQIKKtelgakafKDIDIEDLEELDPDFIMAKQVEQLEK---EKKELQERLKNQEKK 694
Cdd:PTZ00121  1398 KKAEEDKKKADELKKAAAAKKKADEAKK--------KAEEKKKADEAKKKAEEAKKADEAKKkaeEAKKAEEAKKKAEEA 1469
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  695 IDYFERAKRLEE---IPLIKTAYEEQRVRDMELwEQQEEERITTLQLEREKALEHKNRLSRMLEDRDLFEARLKALRRTV 771
Cdd:PTZ00121  1470 KKADEAKKKAEEakkADEAKKKAEEAKKKADEA-KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA 1548
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  772 yeDKLKQFQErlAEERRNRLEERKKQRKEERRITYYREKEEEEQRLREEQLLKEREEKERIEREKREQEQREYQ----ER 847
Cdd:PTZ00121  1549 --DELKKAEE--LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkikaEE 1624
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  848 VKKLEELEKKKRQREMEIEERERRREEERRGLDDPFSRKESRWGDRGESESSWRRGGETESEWRRAPVERDWRRGEARDD 927
Cdd:PTZ00121  1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA 1704
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  928 ERPFRRGDDLPRRSDDLprRGDDLPRRGPAEEKERpsvESSEDrppRREGDEDRppRREGDEDRPLRRGLDEDRPPRRGL 1007
Cdd:PTZ00121  1705 EELKKKEAEEKKKAEEL--KKAEEENKIKAEEAKK---EAEED---KKKAEEAK--KDEEEKKKIAHLKKEEEKKAEEIR 1774
                          490       500       510
                   ....*....|....*....|....*....|..
gi 2024509102 1008 DDDRGSWRAADDDRGPRRGMDDDRPPRRALDD 1039
Cdd:PTZ00121  1775 KEKEAVIEEELDEEDEKRRMEVDKKIKDIFDN 1806
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
924-1307 8.02e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.55  E-value: 8.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  924 ARDDERPFRRGDDLPRRSDDLPRRGDDLPRRGPAEEKERPSVESSEDrPPRREGDEDRPPRREGDEDRPLRRgldEDRPP 1003
Cdd:PHA03307    14 AAEGGEFFPRPPATPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAA-ACDRFEPPTGPPPGPGTEAPANES---RSTPT 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1004 RRGLDDDRGSWRAADDDRGPRRGMDDdrPPRRALDDDRPPRRALDDDRPPRRALD--DDRPPRRALDDDRPPRRSLDDDR 1081
Cdd:PHA03307    90 WSLSTLAPASPAREGSPTPPGPSSPD--PPPPTPPPASPPPSPAPDLSEMLRPVGspGPPPAASPPAAGASPAAVASDAA 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1082 GSWRAAD------------DDRGPRRGLDDDRPPRRALDDDRPPRRGLDDDRGSWRAADDDRGPRRGLDDDRGPRRGLDD 1149
Cdd:PHA03307   168 SSRQAALplsspeetarapSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGC 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1150 DRGPWRNTDDDRLSRRDDDRGPWRSS----EDSRPGPWRPFGKPGGwREREKAREDSWGPPRDSRPPGDREWDRDKDRDD 1225
Cdd:PHA03307   248 GWGPENECPLPRPAPITLPTRIWEASgwngPSSRPGPASSSSSPRE-RSPSPSPSSPGSGPAPSSPRASSSSSSSRESSS 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1226 NEkdrefdrerdfdrDDRFRRPRDDAGWRRGPAEETSswRDSSRREEWDRGGrdmrdrraddrePPLRRGPPLRSDREEP 1305
Cdd:PHA03307   327 SS-------------TSSSSESSRGAAVSPGPSPSRS--PSPSRPPPPADPS------------SPRKRPRPSRAPSSPA 379

                   ..
gi 2024509102 1306 SS 1307
Cdd:PHA03307   380 AS 381
PTZ00121 PTZ00121
MAEBL; Provisional
503-745 8.28e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.52  E-value: 8.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  503 EDAPLGPQLQSMPSEQIRNQLTAMSSA--LAKALAVIKPPHLLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKE 580
Cdd:PTZ00121  1596 EVMKLYEEEKKMKAEEAKKAEEAKIKAeeLKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK 1675
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  581 RLESLNIQRE----------KEELEQREAELQKVRKAEEERLRQEAKEREKERILQEhEQIKKKTVRER--LEQIKKTEL 648
Cdd:PTZ00121  1676 KAEEAKKAEEdekkaaealkKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA-EEAKKEAEEDKkkAEEAKKDEE 1754
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  649 GAKAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKTAYEEQRvRDMELWEQQ 728
Cdd:PTZ00121  1755 EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDS-KEMEDSAIK 1833
                          250
                   ....*....|....*..
gi 2024509102  729 EEERITTLQLEREKALE 745
Cdd:PTZ00121  1834 EVADSKNMQLEEADAFE 1850
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
517-784 9.05e-06

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: 50.36  E-value: 9.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  517 EQIRNQLTAMSSALAKALAVIKPPHLLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLEslniqrekEELEQ 596
Cdd:pfam02463  299 KSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQ--------EKLEQ 370
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  597 REAELQKVRKAEEERLRQEAKEREKErILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMAKQVEQ 676
Cdd:pfam02463  371 LEEELLAKKKLESERLSSAAKLKEEE-LELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEE 449
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  677 LEKEKKELQERLKNQEkkidyferakrleeipliktayEEQRVRDMELWEQQEEERITTLQLEREKALEHKNRLSRMLED 756
Cdd:pfam02463  450 KEELEKQELKLLKDEL----------------------ELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARS 507
                          250       260
                   ....*....|....*....|....*...
gi 2024509102  757 RdlfEARLKALRRTVYEDKLKQFQERLA 784
Cdd:pfam02463  508 G---LKVLLALIKDGVGGRIISAHGRLG 532
PTZ00121 PTZ00121
MAEBL; Provisional
563-803 9.64e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.52  E-value: 9.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  563 KEHQRILARRQTIEERK----ERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERI--LQEHEQIKKKTV 636
Cdd:PTZ00121  1197 EDARKAEAARKAEEERKaeeaRKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMahFARRQAAIKAEE 1276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  637 RERLEQIKKTELGAKA---FKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKKIdyfERAKRLEEiplIKTA 713
Cdd:PTZ00121  1277 ARKADELKKAEEKKKAdeaKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKA---EEAKKAAE---AAKA 1350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  714 YEEQRVRDMELWEQQEEERITTLQLEREKALEHKNRLSrmlEDRDLFEARLKAlrrtvYEDKLKQFQERLAEERRNRLEE 793
Cdd:PTZ00121  1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE---EKKKADEAKKKA-----EEDKKKADELKKAAAAKKKADE 1422
                          250
                   ....*....|
gi 2024509102  794 RKKQRKEERR 803
Cdd:PTZ00121  1423 AKKKAEEKKK 1432
PRK12678 PRK12678
transcription termination factor Rho; Provisional
874-1040 1.12e-05

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 49.90  E-value: 1.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  874 EerrglddpfsrkesrwGDRGESESSWRRGGETESEWRRAPVERDWRRGEARDDERPFRRGDDLPRRSDDLPRRGDDLPR 953
Cdd:PRK12678   142 A----------------RKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDR 205
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  954 RGPAEEKERPSVESSEDRPPRREGDEDRP--PRREGDEDRPLRRGLDEDRPPRRGLDDDRGSWRaaDDDRGPRRGMDDDR 1031
Cdd:PRK12678   206 RDRREQGDRREERGRRDGGDRRGRRRRRDrrDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDR--DRRGRRGGDGGNER 283

                   ....*....
gi 2024509102 1032 PPRRALDDD 1040
Cdd:PRK12678   284 EPELREDDV 292
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
566-685 1.19e-05

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: 48.73  E-value: 1.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  566 QRILARRQTIEE---RKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEH-EQIKKKTVRERLE 641
Cdd:cd16269    173 QEFLQSKEAEAEailQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHlRQLKEKMEEEREN 252
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2024509102  642 QIKKTELgAKAFKDIDIEDLEELDpdfiMAKQVEQLEKEKKELQ 685
Cdd:cd16269    253 LLKEQER-ALESKLKEQEALLEEG----FKEQAELLQEEIRSLK 291
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
562-684 1.60e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 1.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  562 RKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIkkktvRERLE 641
Cdd:COG1196    668 RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL-----LEELL 742
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2024509102  642 QIKKTELGAKAFKDIDIEDLEELDpdfimaKQVEQLEKEKKEL 684
Cdd:COG1196    743 EEEELLEEEALEELPEPPDLEELE------RELERLEREIEAL 779
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
592-804 1.62e-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: 48.99  E-value: 1.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  592 EELEQREAELQKVRKA-EEERLRQEAKEREKERILQEHEQIKKKtVRERLEQIKKTELGAKAFKDiDIEDLEeldpdfim 670
Cdd:COG4942     20 DAAAEAEAELEQLQQEiAELEKELAALKKEEKALLKQLAALERR-IAALARRIRALEQELAALEA-ELAELE-------- 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  671 aKQVEQLEKEKKELQERLKNQekkIDYFERAKRLEEIPLIKTAYE-EQRVRDMELWEQQEEER----------ITTLQLE 739
Cdd:COG4942     90 -KEIAELRAELEAQKEELAEL---LRALYRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARreqaeelradLAELAAL 165
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024509102  740 REKALEHKNRLSRMLEDRDLFEARLKALRRTVyEDKLKQFQERLAEERRNRLEERKKQRKEERRI 804
Cdd:COG4942    166 RAELEAERAELEALLAELEEERAALEALKAER-QKLLARLEKELAELAAELAELQQEAEELEALI 229
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
543-707 3.15e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 3.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  543 LQEKEEQHQLAVTAfLKNSRKEHQRIlarRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQ-------- 614
Cdd:COG4717     83 AEEKEEEYAELQEE-LEELEEELEEL---EAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEEleerleel 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  615 EAKEREKERILQEHEQIKKKTVRERLEqikKTELGAKAFKDIdIEDLEELDpdfimaKQVEQLEKEKKELQERLKNQEKK 694
Cdd:COG4717    159 RELEEELEELEAELAELQEELEELLEQ---LSLATEEELQDL-AEELEELQ------QRLAELEEELEEAQEELEELEEE 228
                          170
                   ....*....|...
gi 2024509102  695 IDYFERAKRLEEI 707
Cdd:COG4717    229 LEQLENELEAAAL 241
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
530-701 4.29e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 47.93  E-value: 4.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  530 LAKALAVIKPPHLlQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLESLN--IQREKEELEQREAELQKVRKA 607
Cdd:COG2433    378 IEEALEELIEKEL-PEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEaeLEEKDERIERLERELSEARSE 456
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  608 EEERLRqeaKEREKERILQEHEQIKKK--TVRERLEQIKKTELGAKAFKDIDIEDleeldpDFIMAKQVEQLEKEK-KEL 684
Cdd:COG2433    457 ERREIR---KDREISRLDREIERLEREleEERERIEELKRKLERLKELWKLEHSG------ELVPVKVVEKFTKEAiRRL 527
                          170
                   ....*....|....*..
gi 2024509102  685 QERLKNQEKKIDYFERA 701
Cdd:COG2433    528 EEEYGLKEGDVVYLRDA 544
PTZ00121 PTZ00121
MAEBL; Provisional
525-803 4.32e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 4.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  525 AMSSALAKALAVIKPPHLLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLESlniQREKEELEQREAELQK- 603
Cdd:PTZ00121  1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEED---KKKADELKKAAAAKKKa 1420
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  604 --VRKAEEE-RLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKAfkdidiedlEELDPDFIMAKQVEQLEK- 679
Cdd:PTZ00121  1421 deAKKKAEEkKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA---------DEAKKKAEEAKKADEAKKk 1491
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  680 --EKKELQERLKNQEKKIDYFERAKRLEEIPLIKTAYEEQRVRDMELWEQQEEERITTlQLEREKALEHKNRLSRMLEDR 757
Cdd:PTZ00121  1492 aeEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD-ELKKAEELKKAEEKKKAEEAK 1570
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2024509102  758 DLFEARLKALRRTvyeDKLKQFQERLAEERRNRLEERKKQRKEERR 803
Cdd:PTZ00121  1571 KAEEDKNMALRKA---EEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
558-772 5.01e-05

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: 47.81  E-value: 5.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  558 LKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVR 637
Cdd:pfam05557   14 LQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLN 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  638 ERLEQIKKTELGAKAFKDidieDLEELDPDFIMAK-QVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKTAYEE 716
Cdd:pfam05557   94 EKESQLADAREVISCLKN----ELSELRRQIQRAElELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAE 169
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024509102  717 QRVRDMELWEQQEE-------------ERITTLQLEREKALEHKNRLSRMLEDRDLFEARLKALRRTVY 772
Cdd:pfam05557  170 QRIKELEFEIQSQEqdseivknskselARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLE 238
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
575-694 5.34e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 47.90  E-value: 5.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  575 IEERKErleslNIQREKEELEQ---------REAElQKVRKAEEERLRQEAKEREKERILQEHEQIKKKtVRERLEQIKK 645
Cdd:PRK00409   504 IEEAKK-----LIGEDKEKLNEliasleeleRELE-QKAEEAEALLKEAEKLKEELEEKKEKLQEEEDK-LLEEAEKEAQ 576
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2024509102  646 TELG-AKAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKK 694
Cdd:PRK00409   577 QAIKeAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKK 626
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
516-704 5.91e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 5.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  516 SEQIRNQLTAMSSALAKALAVIKPPH-LLQEKEEQHQLAVTAFLKNSRKEhQRILARRQTIEERKERLESlNIQREKEEL 594
Cdd:TIGR02168  346 LEELKEELESLEAELEELEAELEELEsRLEELEEQLETLRSKVAQLELQI-ASLNNEIERLEARLERLED-RRERLQQEI 423
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  595 EQREAELQKVRKAE-EERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKafkdidiEDLEELDPDF-IMAK 672
Cdd:TIGR02168  424 EELLKKLEEAELKElQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE-------RELAQLQARLdSLER 496
                          170       180       190
                   ....*....|....*....|....*....|..
gi 2024509102  673 QVEQLEKEKKELQERLKNQEKKIDYFERAKRL 704
Cdd:TIGR02168  497 LQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
552-769 6.17e-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: 47.07  E-value: 6.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  552 LAVTAFLKNSRKEHQRILARRQTIEERKERLESL-----NIQREKEELEQREAELQKVRKAEEERLRQEAKE----REKE 622
Cdd:COG4942     13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALkkeekALLKQLAALERRIAALARRIRALEQELAALEAElaelEKEI 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  623 RILQEHEQIKKKTVRERLEQIKKTE--------LGAKAFKDI--DIEDLEELDPDfiMAKQVEQLEKEKKELQERLKNQE 692
Cdd:COG4942     93 AELRAELEAQKEELAELLRALYRLGrqpplallLSPEDFLDAvrRLQYLKYLAPA--RREQAEELRADLAELAALRAELE 170
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024509102  693 KKidyferAKRLEEiplIKTAYEEQRVRdmelWEQQEEERITTLQLEREKALEHKNRLSRMLEDRDLFEARLKALRR 769
Cdd:COG4942    171 AE------RAELEA---LLAELEEERAA----LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
COG4253 COG4253
Uncharacterized conserved protein, DUF2345 family [Function unknown];
878-1155 6.18e-05

Uncharacterized conserved protein, DUF2345 family [Function unknown];


Pssm-ID: 443395 [Multi-domain]  Cd Length: 900  Bit Score: 47.73  E-value: 6.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  878 GLDDPFSRKESRWGDRGESESSWRRGGETESEWRRAPVERDWRRGEARDDERPFRRGDDLPRRSDDLPRRGDDLPRRGPA 957
Cdd:COG4253    197 AFADDRLTERRASAEAASRADAAALRDLRLALRLARRAATAADDAQTTDDARLTADDSAADAGSLSGSGGDGGAAGGSLA 276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  958 EEKERPSVESSeDRPPRREGDEDRPPRREGDEDRPLRRGLDEDRPPRRGLDDDRGSWRAADDDRGPRRGMDDDRPPRRAL 1037
Cdd:COG4253    277 EATSSLRVPAA-SVSLARYQRARRAAAAAAAADARAGGADAAGGVGTGGGRRLAAGLAGAAAEEEEAVGAEARARRRRLL 355
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1038 DDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPP-------RRSLDDDRGSWRAADDDRGPRRGLDDDRPPRRALDDD 1110
Cdd:COG4253    356 RAARAAIRLLAAAALALLALGRGALAGRSPAAAAGPgivggtdRRARRRATAFVDRAAGPPPRTQRARRPLLPRPRGAGG 435
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2024509102 1111 RPPRRGLDDDRGSWRAADDDRGPRRGLDDDRGPRRGLDDDRGPWR 1155
Cdd:COG4253    436 PPPRVVSTRAGDTPSADDDDGGRRVVRDDRRVAWVGGGESWGAGG 480
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
545-742 6.53e-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: 47.76  E-value: 6.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  545 EKEEQHQLAVTAFLKNSRKEHQRILARRQT-IEERKERLESLNIQreKEELEQREAELQ--------KVRKAEEERLRQE 615
Cdd:TIGR02169  818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEqIKSIEKEIENLNGK--KEELEEELEELEaalrdlesRLGDLKKERDELE 895
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  616 AKEREKERILQEHE---QIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMakqvEQLEKEKKELQERLKNQE 692
Cdd:TIGR02169  896 AQLRELERKIEELEaqiEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL----EDVQAELQRVEEEIRALE 971
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024509102  693 ----KKIDYFER-AKRLEEipliktaYEEQRvrdMELWEQQEEERITTLQLEREK 742
Cdd:TIGR02169  972 pvnmLAIQEYEEvLKRLDE-------LKEKR---AKLEEERKAILERIEEYEKKK 1016
PRK12704 PRK12704
phosphodiesterase; Provisional
597-784 7.12e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.08  E-value: 7.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  597 REAELQKVRKAEEERLRQEAKEREKERILQEHEQIKK----KTVRERLEQIKKTELgakafkdiDIEDLEEldpdfIMAK 672
Cdd:PRK12704    34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRnefeKELRERRNELQKLEK--------RLLQKEE-----NLDR 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  673 QVEQLEKEKKELQERLKNQEKKIDYFEraKRLEEiplIKTAYEEQRvrdmelweqQEEERITTLQLErekalEHKNRLSR 752
Cdd:PRK12704   101 KLELLEKREEELEKKEKELEQKQQELE--KKEEE---LEELIEEQL---------QELERISGLTAE-----EAKEILLE 161
                          170       180       190
                   ....*....|....*....|....*....|...
gi 2024509102  753 MLEDrdlfEARLKALRRT-VYEDKLKQFQERLA 784
Cdd:PRK12704   162 KVEE----EARHEAAVLIkEIEEEAKEEADKKA 190
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
558-815 7.35e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 7.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  558 LKNSRKEHQRILARRQT---IEERKERLESLNIqrekEELEQREAELQKVR------KAEEERLRQEAK---EREKERIL 625
Cdd:PRK03918   485 LEKVLKKESELIKLKELaeqLKELEEKLKKYNL----EELEKKAEEYEKLKekliklKGEIKSLKKELEkleELKKKLAE 560
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  626 QEHeqiKKKTVRERLEQIKK--TELGAKAFKDID--IEDLEELDPDFIMAKQVEqleKEKKELQERLKNQEKKIDyfera 701
Cdd:PRK03918   561 LEK---KLDELEEELAELLKelEELGFESVEELEerLKELEPFYNEYLELKDAE---KELEREEKELKKLEEELD----- 629
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  702 KRLEEIPLIKTAYEEQRVRDMELWEQQEEERITTLqleREKALEHKNRLSRMledrdlfEARLKALRRTVyeDKLKQFQE 781
Cdd:PRK03918   630 KAFEELAETEKRLEELRKELEELEKKYSEEEYEEL---REEYLELSRELAGL-------RAELEELEKRR--EEIKKTLE 697
                          250       260       270
                   ....*....|....*....|....*....|....
gi 2024509102  782 RLaeerrnrleerkKQRKEERRityyrekeeeEQ 815
Cdd:PRK03918   698 KL------------KEELEERE----------KA 709
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
517-753 1.14e-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: 46.97  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  517 EQIRNQLTAMSSALAKALAVIKpphLLQEKEEQHQLAVTAF---LKNSRKEHQRILARRQTIEERKERLEslniqREKEE 593
Cdd:TIGR02168  764 EELEERLEEAEEELAEAEAEIE---ELEAQIEQLKEELKALreaLDELRAELTLLNEEAANLRERLESLE-----RRIAA 835
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  594 LEQREAELQKVRKAEEERLRQEAKEREKERILQE--HEQIKKKtvrerLEQIKKTELGAKAFKDidieDLEELDpdfima 671
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEelESELEAL-----LNERASLEEALALLRS----ELEELS------ 900
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  672 KQVEQLEKEKKELQERLKNQEKKIDYFERAK---RLEEIPLIKTAYEEQRVrDMELWEQQEEERITTLQLEREKALEHKN 748
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQLELRLeglEVRIDNLQERLSEEYSL-TLEEAEALENKIEDDEEEARRRLKRLEN 979

                   ....*
gi 2024509102  749 RLSRM 753
Cdd:TIGR02168  980 KIKEL 984
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
575-804 1.32e-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: 46.55  E-value: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  575 IEERKERLESLNiQREKEELEQREAELQKVRKAEEERLRQ-----------------------------EAKEREKERIL 625
Cdd:TIGR04523  347 LKKELTNSESEN-SEKQRELEEKQNEIEKLKKENQSYKQEiknlesqindleskiqnqeklnqqkdeqiKKLQQEKELLE 425
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  626 QEHEQIKKKTVRERlEQIKKTElGAKAFKDIDIEDLEELDPDFimAKQVEQLEKEKKELQERLKNQEKKIDyfERAKRLE 705
Cdd:TIGR04523  426 KEIERLKETIIKNN-SEIKDLT-NQDSVKELIIKNLDNTRESL--ETQLKVLSRSINKIKQNLEQKQKELK--SKEKELK 499
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  706 EIPLIKTAYEEQRVrdmELWEQQEEERITTLQLEREKaLEHKNRLSRMLEDRDLFEARLKalrRTVYEDKLKQFQERLAE 785
Cdd:TIGR04523  500 KLNEEKKELEEKVK---DLTKKISSLKEKIEKLESEK-KEKESKISDLEDELNKDDFELK---KENLEKEIDEKNKEIEE 572
                          250
                   ....*....|....*....
gi 2024509102  786 ERRNRLEERKKQRKEERRI 804
Cdd:TIGR04523  573 LKQTQKSLKKKQEEKQELI 591
FadA pfam09403
Adhesion protein FadA; FadA (Fusobacterium adhesin A) is an adhesin which forms two alpha ...
593-704 1.32e-04

Adhesion protein FadA; FadA (Fusobacterium adhesin A) is an adhesin which forms two alpha helices that form an intra-molecular coiled-coil arrangement.


Pssm-ID: 430587 [Multi-domain]  Cd Length: 99  Bit Score: 42.27  E-value: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  593 ELEQREAELQKVRKAEEERL--RQEAKEREKERiLQEHEQIKKKtVRERLEQIKKTElGAKAFKDidieDLEELdpdfim 670
Cdd:pfam09403    1 RLSALEAELQKLENKEEQRFnkEKAKAEAAAAD-LAKNYELKAE-IEEKLAKLEADS-DVRFYKD----EYKEL------ 67
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2024509102  671 akqVEQLEKEKKELQERLKNQEKKIDYFERAKRL 704
Cdd:pfam09403   68 ---LKKYKDLLKELEKEIKEEEKIIDNFEALLSL 98
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
543-707 1.70e-04

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


Pssm-ID: 462861 [Multi-domain]  Cd Length: 302  Bit Score: 45.33  E-value: 1.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  543 LQEKEEQHQLAVTAFLKNSRKEhqrILARRQTIEERKERLESLNIQ-REK-----EELEQREAELQKV-RKAEEERLRQE 615
Cdd:pfam09728   93 LAKEEEEKRKELSEKFQSTLKD---IQDKMEEKSEKNNKLREENEElREKlksliEQYELRELHFEKLlKTKELEVQLAE 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  616 AK----EREKERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDpDFI----------------MAKQVE 675
Cdd:pfam09728  170 AKlqqaTEEEEKKAQEKEVAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQ-DTLnksnevfttfkkemekMSKKIK 248
                          170       180       190
                   ....*....|....*....|....*....|....
gi 2024509102  676 QLEKEKKELQERLKNQEKKIDYF--ERAKRLEEI 707
Cdd:pfam09728  249 KLEKENLTWKRKWEKSNKALLEMaeERQKLKEEL 282
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
559-784 1.74e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.19  E-value: 1.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  559 KNSRKEHQRILARRQTIEERKERLESLNIQREK------------EELEQREAELQKVrKAEEERLRQEAKEREKERILQ 626
Cdd:PRK02224   199 KEEKDLHERLNGLESELAELDEEIERYEEQREQaretrdeadevlEEHEERREELETL-EAEIEDLRETIAETEREREEL 277
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  627 EHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEEldpdfimakQVEQLEKEKKELQERLKNQ--------------- 691
Cdd:PRK02224   278 AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEA---------RREELEDRDEELRDRLEECrvaaqahneeaeslr 348
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  692 EKKIDYFERAKRLEE--------IPLIKTAYEEQRVRDMELWEQQEE--ERITTLQLEREKALEHKNRLsrmLEDRDLFE 761
Cdd:PRK02224   349 EDADDLEERAEELREeaaeleseLEEAREAVEDRREEIEELEEEIEElrERFGDAPVDLGNAEDFLEEL---REERDELR 425
                          250       260
                   ....*....|....*....|...
gi 2024509102  762 ARLKALRRTvyedkLKQFQERLA 784
Cdd:PRK02224   426 EREAELEAT-----LRTARERVE 443
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
970-1130 1.83e-04

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 45.65  E-value: 1.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  970 DRPPRREGDEDRPPRREGDEDRPLRRGLDEDRpprrglDDDRgswraadddrgPRRGMDddrppRRALDDDRPPRRALDD 1049
Cdd:TIGR01642    2 DEEPDREREKSRGRDRDRSSERPRRRSRDRSR------FRDR-----------HRRSRE-----RSYREDSRPRDRRRYD 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1050 DRPPRRALDDDRPPRRalddDRPPRRSLDDDRGSwraadddRGPRRGLddDRPPRRALDDDRPPRRGLDDDRGSWRAADD 1129
Cdd:TIGR01642   60 SRSPRSLRYSSVRRSR----DRPRRRSRSVRSIE-------QHRRRLR--DRSPSNQWRKDDKKRSLWDIKPPGYELVTA 126

                   .
gi 2024509102 1130 D 1130
Cdd:TIGR01642  127 D 127
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
542-643 1.85e-04

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: 45.88  E-value: 1.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  542 LLQEKEEQHQLAVTAflKNSRKEHQRILARRQT-IEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKERE 620
Cdd:pfam17380  497 LEKELEERKQAMIEE--ERKRKLLEKEMEERQKaIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERE 574
                           90       100
                   ....*....|....*....|...
gi 2024509102  621 KERILQEHEQIKKKTVRERLEQI 643
Cdd:pfam17380  575 REMMRQIVESEKARAEYEATTPI 597
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
571-706 1.92e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 46.00  E-value: 1.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  571 RRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQeaKEREKERiLQEHEQIKKKTVRERLEQIKKTELGA 650
Cdd:COG2433    374 RGLSIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRR--LEEQVER-LEAEVEELEAELEEKDERIERLEREL 450
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024509102  651 KAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEE 706
Cdd:COG2433    451 SEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEH 506
RNase_Y_N pfam12072
RNase Y N-terminal region;
542-683 2.32e-04

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 43.72  E-value: 2.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  542 LLQEKEEQHQL--AVTAFLKNSRKEHQRiLARRqtIEERKERLEslniqREKEELEQREAELQKVRKAEEERLRQ-EAKE 618
Cdd:pfam12072   55 LLEAKEEIHKLraEAERELKERRNELQR-QERR--LLQKEETLD-----RKDESLEKKEESLEKKEKELEAQQQQlEEKE 126
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024509102  619 REKERILQEHeqikkktvRERLEQIKKteLGAKAFKDIDIEDLE-ELDPDfiMAKQVEQLEKEKKE 683
Cdd:pfam12072  127 EELEELIEEQ--------RQELERISG--LTSEEAKEILLDEVEeELRHE--AAVMIKEIEEEAKE 180
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
563-783 2.34e-04

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: 45.58  E-value: 2.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  563 KEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEE-ERLRQEAKER----EKERILQEHEQIKKKTVR 637
Cdd:pfam10174  502 KEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEaVRTNPEINDRirllEQEVARYKEESGKAQAEV 581
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  638 ERLEQIKKTELGAKAFKDIDIEDLEELDPdfimaKQVEqlEKEKKELQERLKNQEkkidyfERAKRLEEIpliktayEEQ 717
Cdd:pfam10174  582 ERLLGILREVENEKNDKDKKIAELESLTL-----RQMK--EQNKKVANIKHGQQE------MKKKGAQLL-------EEA 641
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024509102  718 RVRDMELW----EQQEEERITTLQLEREKALEHKNRLS---RMLEDRDLFEARLKALRRTVYEDKLKQFQERL 783
Cdd:pfam10174  642 RRREDNLAdnsqQLQLEELMGALEKTRQELDATKARLSstqQSLAEKDGHLTNLRAERRKQLEEILEMKQEAL 714
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
572-681 2.86e-04

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 44.33  E-value: 2.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  572 RQTIEERKERLESlnIQREKEELEQREAELQKVRKA---EEERLRQEAKEREKERILQEHEQikkKTVRERLEQIKKTEL 648
Cdd:COG4026    134 REELLELKEKIDE--IAKEKEKLTKENEELESELEElreEYKKLREENSILEEEFDNIKSEY---SDLKSRFEELLKKRL 208
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2024509102  649 gakaFKDIDIEDL------EELDPDFIMAKQVEQLEKEK 681
Cdd:COG4026    209 ----LEVFSLEELwkelfpEELPEEDFIYFATENLKPGK 243
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
572-706 3.08e-04

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 44.86  E-value: 3.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  572 RQTIEERKERLESLNIQREKE----ELEQREAELQKVRkaEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTE 647
Cdd:COG2268    213 EIAIAQANREAEEAELEQEREietaRIAEAEAELAKKK--AEERREAETARAEAEAAYEIAEANAEREVQRQLEIAERER 290
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024509102  648 lgakafkdidiedleeldpdfimAKQVEQLEKEKKELQERlKNQEKKIDYfERAKRLEE 706
Cdd:COG2268    291 -----------------------EIELQEKEAEREEAELE-ADVRKPAEA-EKQAAEAE 324
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
572-781 3.20e-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: 3.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  572 RQTIEERKERLESlNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKK--KTVRERLEQI-----K 644
Cdd:COG5185    324 EQELEESKRETET-GIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDtiESTKESLDEIpqnqrG 402
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  645 KTELGAKAFKD---IDIEDLEELDPDFIMA-KQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKTAyEEQRVR 720
Cdd:COG5185    403 YAQEILATLEDtlkAADRQIEELQRQIEQAtSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRS-VRSKKE 481
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024509102  721 DMELWEQQEEERITTLQLEREKALEHKNR-------------LSRMLEDRDLFEARLKALRRTVYEDKLKQFQE 781
Cdd:COG5185    482 DLNEELTQIESRVSTLKATLEKLRAKLERqlegvrskldqvaESLKDFMRARGYAHILALENLIPASELIQASN 555
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
558-755 3.37e-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: 45.43  E-value: 3.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  558 LKNSRKEHQRILARRQT-IEERKERLESLNIQ-----REKEELEQREAELQK----VRKAEEERLRQEAKEREK-ERILQ 626
Cdd:TIGR02168  328 LESKLDELAEELAELEEkLEELKEELESLEAEleeleAELEELESRLEELEEqletLRSKVAQLELQIASLNNEiERLEA 407
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  627 EHEQIKKKtvRERLEQIKKTELGAKAFKDID--IEDLEELDpdfimaKQVEQLEKEKKELQERLKNQEKKIDYFERAKRL 704
Cdd:TIGR02168  408 RLERLEDR--RERLQQEIEELLKKLEEAELKelQAELEELE------EELEELQEELERLEEALEELREELEEAEQALDA 479
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024509102  705 EEIPLIKTAYEEQRVRDMELWEQQEEERITTLQLEREKALEHKNRLSRMLE 755
Cdd:TIGR02168  480 AERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIS 530
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
559-778 3.59e-04

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 45.00  E-value: 3.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  559 KNSRKEhQRILARRQTIEERK---ERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERIlqeheqikKKT 635
Cdd:NF033838   198 KEPRDE-EKIKQAKAKVESKKaeaTRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRA--------KRG 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  636 VRERLEQIKKTELGAKAfKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQ--EKKIDYFERA-KRLEeiplIKT 712
Cdd:NF033838   269 VLGEPATPDKKENDAKS-SDSSVGEETLPSPSLKPEKKVAEAEKKVEEAKKKAKDQkeEDRRNYPTNTyKTLE----LEI 343
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024509102  713 AYEEQRVRDMELW-------EQQEEERITTLQLEREKALEHKNRLSRMLEDRDlfEARLKALRRTVYEDKLKQ 778
Cdd:NF033838   344 AESDVKVKEAELElvkeeakEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRK--KAEEEAKRKAAEEDKVKE 414
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
543-759 3.62e-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: 45.01  E-value: 3.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  543 LQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLESLNiqREKEELEQREAEL--------QKVRKAEEERLRQ 614
Cdd:TIGR04523  459 LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLN--EEKKELEEKVKDLtkkisslkEKIEKLESEKKEK 536
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  615 EAKEREKERILQEHEQIKKKTV--------RERLEQIK--KTELGAKAF-KDIDIEDLEELDPDFI------------MA 671
Cdd:TIGR04523  537 ESKISDLEDELNKDDFELKKENlekeidekNKEIEELKqtQKSLKKKQEeKQELIDQKEKEKKDLIkeieekekkissLE 616
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  672 KQVEQLEKEKKELQERLKNQEKKIDYFErakrlEEIPLIKTAYEEQRVRDMELWEQQEEERI-------TTLQLEREKAL 744
Cdd:TIGR04523  617 KELEKAKKENEKLSSIIKNIKSKKNKLK-----QEVKQIKETIKEIRNKWPEIIKKIKESKTkiddiieLMKDWLKELSL 691
                          250
                   ....*....|....*
gi 2024509102  745 EHKNRLSRMLEDRDL 759
Cdd:TIGR04523  692 HYKKYITRMIRIKDL 706
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
511-738 3.72e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 3.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  511 LQSMPSEQIRNQLTAMSSALAKalaviKPPHLLQEKEEQHQLavtafLKNSRKEHQRILARRQTIEERKERLESLniQRE 590
Cdd:COG4717     43 IRAMLLERLEKEADELFKPQGR-----KPELNLKELKELEEE-----LKEAEEKEEEYAELQEELEELEEELEEL--EAE 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  591 KEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIkkktvRERLEQIKKTELGAKAFKDiDIEDLEE------L 664
Cdd:COG4717    111 LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEEL-----EERLEELRELEEELEELEA-ELAELQEeleellE 184
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024509102  665 DPDFIMAKQVEQLEKEKKELQERLKNQEKKIdyferaKRLEEIplIKTAYEEQRVRDMELWEQQEEERITTLQL 738
Cdd:COG4717    185 QLSLATEEELQDLAEELEELQQRLAELEEEL------EEAQEE--LEELEEELEQLENELEAAALEERLKEARL 250
PHA03378 PHA03378
EBNA-3B; Provisional
952-1113 3.78e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 45.06  E-value: 3.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  952 PRRGPAEEKERPSVESsedRPPRREGDEDRPPRREGDEDRPLRR---------GLDEDRPPRRGLDDDRGSW-RAADDDR 1021
Cdd:PHA03378   598 PVPHPSQTPEPPTTQS---HIPETSAPRQWPMPLRPIPMRPLRMqpitfnvlvFPTPHQPPQVEITPYKPTWtQIGHIPY 674
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1022 GPR-RGMDDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRSLDDDRGSWRAADDDRGPRRGLDDD 1100
Cdd:PHA03378   675 QPSpTGANTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRA 754
                          170
                   ....*....|...
gi 2024509102 1101 RPPRRALDDDRPP 1113
Cdd:PHA03378   755 RPPAAAPGRARPP 767
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
936-1150 3.98e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 44.90  E-value: 3.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  936 DLPRRSDDLPRRGDDLPRRGPAEEKERPSVESSEDRPPRREGDEDRPPRREGDEDRPLRRGLDEDRPPRRGLDDDRGSWR 1015
Cdd:NF033609   629 DSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 708
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1016 AADDDRGPRRGMDDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRSLDDDRGSWRAADDDRGPRR 1095
Cdd:NF033609   709 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 788
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024509102 1096 GLDDDRPPRRALDDDRPPRRGLDDDRGSWRAADDDRGPRRGLDDDRGPRRGLDDD 1150
Cdd:NF033609   789 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 843
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
562-705 4.19e-04

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 44.07  E-value: 4.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  562 RKEHQRILARRQTIEERKERLESLniQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLE 641
Cdd:TIGR02794   64 KKEQERQKKLEQQAEEAEKQRAAE--QARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAE 141
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024509102  642 QIKKTELGAKAFKDIDIEDLEEldpdfimAKQvEQLEKEKKELQERLKNQEKKidyfERAKRLE 705
Cdd:TIGR02794  142 RKAKEEAAKQAEEEAKAKAAAE-------AKK-KAEEAKKKAEAEAKAKAEAE----AKAKAEE 193
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
566-689 5.28e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.43  E-value: 5.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  566 QRILARRQTIEERKERLESL--NIQREKEELEQREAELQKVRKAEEERLRQEAKEREKErILQEHEQIKKktvreRLEQI 643
Cdd:PRK00409   523 ASLEELERELEQKAEEAEALlkEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKE-AKKEADEIIK-----ELRQL 596
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2024509102  644 KKTELGAKAFKDIdIEDLEELDPdfiMAKQVEQLEKEKKELQERLK 689
Cdd:PRK00409   597 QKGGYASVKAHEL-IEARKRLNK---ANEKKEKKKKKQKEKQEELK 638
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
968-1081 5.72e-04

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 44.14  E-value: 5.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  968 SEDRPPRREGDEDRPPRREGDEDRPLRRGLDEDRPPRRGLDDDRGSWRAADDDRGPRRGMDDDRPPRraldddRPPRRAL 1047
Cdd:TIGR01622    2 YRDRERERLRDSSSAGDRDRRRDKGRERSRDRSRDRERSRSRRRDRHRDRDYYRGRERRSRSRRPNR------RYRPREK 75
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2024509102 1048 DDDRPP-RRALDDDRPPRR--ALDDDRPPRRSLDDDR 1081
Cdd:TIGR01622   76 RRRRGDsYRRRRDDRRSRRekPRARDGTPEPLTEDER 112
PHA03247 PHA03247
large tegument protein UL36; Provisional
919-1105 5.89e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 5.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  919 WRRGE---ARDDErpfrrGDDLPRRSDDLPRRGDD--LPRRGPAEEKERPSVESSEDRPprregdeDRPPRregdEDRPL 993
Cdd:PHA03247  2536 WIRGLeelASDDA-----GDPPPPLPPAAPPAAPDrsVPPPRPAPRPSEPAVTSRARRP-------DAPPQ----SARPR 2599
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  994 RRGLDEDRPPRRGldddrGSWRAADDDRGPRRGMDDDRP----PRRALDDDRPPRRALDDDRPPRRAldddRPPRRALDD 1069
Cdd:PHA03247  2600 APVDDRGDPRGPA-----PPSPLPPDTHAPDPPPPSPSPaanePDPHPPPTVPPPERPRDDPAPGRV----SRPRRARRL 2670
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2024509102 1070 DRPPRRSLDDDRGSWRAADDDRGPRRGLDDDRPPRR 1105
Cdd:PHA03247  2671 GRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPP 2706
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
925-1051 5.92e-04

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 44.14  E-value: 5.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  925 RDDERPFRRGDDLPRRSDdlpRRGDDLPRRGPAEEKERPSvESSEDRPPRREGDEDRPPRREGDEDRPLRrgldedRPPR 1004
Cdd:TIGR01622    3 RDRERERLRDSSSAGDRD---RRRDKGRERSRDRSRDRER-SRSRRRDRHRDRDYYRGRERRSRSRRPNR------RYRP 72
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2024509102 1005 RGLDDDRG-SWRAADDDRGPRRgmDDDRPPRRALDDDRPPRRaldDDR 1051
Cdd:TIGR01622   73 REKRRRRGdSYRRRRDDRRSRR--EKPRARDGTPEPLTEDER---DRR 115
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
517-784 6.28e-04

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 44.07  E-value: 6.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  517 EQIRNQLTAMSSALAKALAVIKppHLLqEKEEQHQLAVTAFLKNSRKEHQRILARR----QTIEERKERLESL------- 585
Cdd:pfam06160   89 DEIEELLDDIEEDIKQILEELD--ELL-ESEEKNREEVEELKDKYRELRKTLLANRfsygPAIDELEKQLAEIeeefsqf 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  586 -----------------NIQREKEELEQR-------EAELQKVRKAEEERLRQEAKEREKERILQEHEQIKK--KTVRER 639
Cdd:pfam06160  166 eeltesgdylearevleKLEEETDALEELmedipplYEELKTELPDQLEELKEGYREMEEEGYALEHLNVDKeiQQLEEQ 245
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  640 LEQ----IKKTELGAKAFKDIDIED-LEELdpdfimakqVEQLEKEKKELQERLKNQEKKIDYFERAKR-----LEEIPL 709
Cdd:pfam06160  246 LEEnlalLENLELDEAEEALEEIEErIDQL---------YDLLEKEVDAKKYVEKNLPEIEDYLEHAEEqnkelKEELER 316
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  710 IKTAY-----EEQRVRDmelWEQQEEERITTLQLEREKALEHKNRLSRMLEDRDLFEARLKALrrtvyEDKLKQFQERLA 784
Cdd:pfam06160  317 VQQSYtlnenELERVRG---LEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEI-----EEEQEEFKESLQ 388
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
1050-1157 7.46e-04

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 43.73  E-value: 7.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1050 DRPPRRALDDDRPPRRALDDDRPPRRSLDDDRgsWRAADDDRGPRRGLDDDRPPRRALDDDRPPRrgldDDRGSWRAADD 1129
Cdd:TIGR01642    2 DEEPDREREKSRGRDRDRSSERPRRRSRDRSR--FRDRHRRSRERSYREDSRPRDRRRYDSRSPR----SLRYSSVRRSR 75
                           90       100
                   ....*....|....*....|....*....
gi 2024509102 1130 DRGPRRGLDDDRGPR-RGLDDDRGPWRNT 1157
Cdd:TIGR01642   76 DRPRRRSRSVRSIEQhRRRLRDRSPSNQW 104
PHA03321 PHA03321
tegument protein VP11/12; Provisional
902-1120 7.99e-04

tegument protein VP11/12; Provisional


Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 43.79  E-value: 7.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  902 RGGETESEWRRAPVERDWRRGEARDDE----RPFRRGDD-------LPRRSDDLPRRGDDLPR---RGPAEEKERPSVES 967
Cdd:PHA03321   449 RPGSTPACARRARAQRARDAGPEYVDPlgalRRLPAGAApppepaaAPSPATYYTRMGGGPPRlppRNRATETLRPDWGP 528
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  968 SEDRPPRREGDEDRPPRREGDEDRPLRRGLDEDRPPRRGLDDDRGSWRAADDDRGPrrgmDDDRPPRRALDDDRPPRRAL 1047
Cdd:PHA03321   529 PAAAPPEQMEDPYLEPDDDRFDRRDGAAAAATSHPREAPAPDDDPIYEGVSDSEEP----VYEEIPTPRVYQNPLPRPME 604
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024509102 1048 DDDRPPrralDDDRPPRRALDDDRPPRRSLDDDRGSWRAADDDRGPRRGLDddrPPRRALDDDRPPRRGLDDD 1120
Cdd:PHA03321   605 GAGEPP----DLDAPTSPWVEEENPIYGWGDSPLFSPPPAARFPPPDPALS---PEPPALPAHRPRPGALAPD 670
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
949-1073 8.70e-04

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 43.73  E-value: 8.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  949 DDLPRRGPAEEKERpSVESSEDRPPRREGDEDRppRREGDEDRPLRRGLDEDRPPRRGLDDDrgswRAADDDRGPRRGMD 1028
Cdd:TIGR01642    2 DEEPDREREKSRGR-DRDRSSERPRRRSRDRSR--FRDRHRRSRERSYREDSRPRDRRRYDS----RSPRSLRYSSVRRS 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2024509102 1029 DDRPPRRALDDDR--PPRRALDDDRPPRRALDDDRppRRALDDDRPP 1073
Cdd:TIGR01642   75 RDRPRRRSRSVRSieQHRRRLRDRSPSNQWRKDDK--KRSLWDIKPP 119
Nop53 pfam07767
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ...
545-659 9.55e-04

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


Pssm-ID: 462259 [Multi-domain]  Cd Length: 353  Bit Score: 43.05  E-value: 9.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  545 EKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKerleslNIQREKEELEQREAEL-QKVRKAEEERLRQEAKE-REKE 622
Cdd:pfam07767  212 LKEEEKLERVLEKIAESAATAEAREEKRKTKAQRN------KEKRRKEEEREAKEEKaLKKKLAQLERLKEIAKEiAEKE 285
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2024509102  623 RILQEHEQIKKKTVRERLEQIKKTE---LGAKAFKDIDIE 659
Cdd:pfam07767  286 KEREEKAEARKREKRKKKKEEKKLRprkLGKHKVPEPDLE 325
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
545-749 9.78e-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: 43.40  E-value: 9.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  545 EKEEQHQLAVTAFLKNSRKEH--------QRILARRQTIE-ERKERLESLNIQREKEELEQR---EAELQKVRKAEEERL 612
Cdd:pfam15709  312 EEERSEEDPSKALLEKREQEKasrdrlraERAEMRRLEVErKRREQEEQRRLQQEQLERAEKmreELELEQQRRFEEIRL 391
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  613 RQEAKEREKERilQEHEQIKK----KTVRERLEQiKKTELGAKAFKDIDIEDLEEldpdfimAKQVEQLEKEKKELQERL 688
Cdd:pfam15709  392 RKQRLEEERQR--QEEEERKQrlqlQAAQERARQ-QQEEFRRKLQELQRKKQQEE-------AERAEAEKQRQKELEMQL 461
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024509102  689 KNQEKKIDYFERAKRLEEIPLiKTAYEEQRVRDMELWEQQEEERITTLQLEREKALEHKNR 749
Cdd:pfam15709  462 AEEQKRLMEMAEEERLEYQRQ-KQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQAR 521
atpF CHL00019
ATP synthase CF0 B subunit
553-645 9.94e-04

ATP synthase CF0 B subunit


Pssm-ID: 176962 [Multi-domain]  Cd Length: 184  Bit Score: 41.77  E-value: 9.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  553 AVTAFLKNsRKehQRILarrQTIEERKERLESLNiqrekEELEQREAELQKVrKAEEERLRQEA---KEREKERILQehe 629
Cdd:CHL00019    48 VLSDLLDN-RK--QTIL---NTIRNSEERREEAI-----EKLEKARARLRQA-ELEADEIRVNGyseIEREKENLIN--- 112
                           90
                   ....*....|....*.
gi 2024509102  630 QIKKKTvrERLEQIKK 645
Cdd:CHL00019   113 QAKEDL--ERLENYKN 126
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
571-755 1.04e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.80  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  571 RRQTIEERKERLESL--NIQREKEELEQREAELQKVRKAEEERLRQE-------AKEREKERILQEHEQIKKKtvRERLE 641
Cdd:TIGR00618  213 MPDTYHERKQVLEKElkHLREALQQTQQSHAYLTQKREAQEEQLKKQqllkqlrARIEELRAQEAVLEETQER--INRAR 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  642 QIKKTELGAKAFKDIDiedleeLDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRL-----EEIPLIKTAYEE 716
Cdd:TIGR00618  291 KAAPLAAHIKAVTQIE------QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLqtlhsQEIHIRDAHEVA 364
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2024509102  717 QRVRDMELWEQQEEERITTLQLEREKALEHKNRLSRMLE 755
Cdd:TIGR00618  365 TSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELD 403
PHA03247 PHA03247
large tegument protein UL36; Provisional
920-1123 1.14e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  920 RRGEARDDERPfrrgdDLPRRSDDLPRRGDDLPRRGPAEEKERPSVESSEDRPPRregdEDRPPRREGDEDRPLRRGLDE 999
Cdd:PHA03247  2879 ARPPVRRLARP-----AVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ----PQPPPPPPPRPQPPLAPTTDP 2949
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1000 D--RPPRRGLDDDRGSWRAADDDRGPRRGMDDDRPPRRALDDDRPPRRALDDDRPPRRA------LDDDRPPRRALDDDR 1071
Cdd:PHA03247  2950 AgaGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWAsslalhEETDPPPVSLKQTLW 3029
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024509102 1072 PPRRSLDDDRGSWRAADDDRGPRRGLD-DDRPPRRALDDDRPPRRGLDDDRGS 1123
Cdd:PHA03247  3030 PPDDTEDSDADSLFDSDSERSDLEALDpLPPEPHDPFAHEPDPATPEAGARES 3082
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
517-801 1.17e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  517 EQIRNQLTAMSSALAKALAVIKPPHLLQEKEEQHQLAVTaflknsRKEHQRILARRQTIEERKERLESLniQREKEELEQ 596
Cdd:COG4717    135 EALEAELAELPERLEELEERLEELRELEEELEELEAELA------ELQEELEELLEQLSLATEEELQDL--AEELEELQQ 206
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  597 REAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMA----- 671
Cdd:COG4717    207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLvlgll 286
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  672 ---------------KQVEQLEK--EKKELQERLKNQEKKIDYFERAKRLEEIPLIKTAYEEQRVRDMELWEQQEEERIT 734
Cdd:COG4717    287 allflllarekaslgKEAEELQAlpALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE 366
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024509102  735 TLQLEREKALEHKNrlsrmLEDRDLFEARLKALRRTV-YEDKLKQFQERLAEERRNRLEERKKQRKEE 801
Cdd:COG4717    367 ELEQEIAALLAEAG-----VEDEEELRAALEQAEEYQeLKEELEELEEQLEELLGELEELLEALDEEE 429
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
518-694 1.44e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  518 QIRNQLTAMSSALAKALAVIKPPHLLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQR 597
Cdd:COG1196    654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  598 EAElqkvrkaEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKK--TELGA---KAfkdidIEDLEELDP--DFiM 670
Cdd:COG1196    734 REE-------LLEELLEEEELLEEEALEELPEPPDLEELERELERLEReiEALGPvnlLA-----IEEYEELEEryDF-L 800
                          170       180
                   ....*....|....*....|....*.
gi 2024509102  671 AKQVEQLEKEKKELQERLK--NQEKK 694
Cdd:COG1196    801 SEQREDLEEARETLEEAIEeiDRETR 826
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
544-783 1.56e-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: 43.11  E-value: 1.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  544 QEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLeSLNIQREKEELEQREAELQKVRKAEEERLrqeakEREKER 623
Cdd:TIGR00606  855 QQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVEL-STEVQSLIREIKDAKEQDSPLETFLEKDQ-----QEKEEL 928
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  624 ILQEHEQikKKTVRERLEQIKKtELGAKAFKDIDIED-LEELDPDFIMAK---------QVEQLEKEKKELQERLKNQEK 693
Cdd:TIGR00606  929 ISSKETS--NKKAQDKVNDIKE-KVKNIHGYMKDIENkIQDGKDDYLKQKetelntvnaQLEECEKHQEKINEDMRLMRQ 1005
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  694 KIDYFERAKRLEEIPLIKtayeeqRVRDMELWEQQEEERITTLQLEREKALEHKNRLSRMLEDRDLF--EARLKALRRTV 771
Cdd:TIGR00606 1006 DIDTQKIQERWLQDNLTL------RKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIkrNHVLALGRQKG 1079
                          250
                   ....*....|..
gi 2024509102  772 YEDKLKQFQERL 783
Cdd:TIGR00606 1080 YEKEIKHFKKEL 1091
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
517-783 1.94e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 1.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  517 EQIRNQLTAMSSALAKALAVikpphlLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLeslniQREKEELEQ 596
Cdd:COG4717    159 RELEEELEELEAELAELQEE------LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA-----QEELEELEE 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  597 REAEL--QKVRKAEEERLRQEA-------------------------------------------KEREKERILQEHEQI 631
Cdd:COG4717    228 ELEQLenELEAAALEERLKEARlllliaaallallglggsllsliltiagvlflvlgllallfllLAREKASLGKEAEEL 307
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  632 KKKTVRERLEQIKKTELgAKAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQE------------------- 692
Cdd:COG4717    308 QALPALEELEEEELEEL-LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEleqeiaallaeagvedeee 386
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  693 --KKIDYFERAKRL-EEIPLIKTAYEEQRVRDMELWEQQEEERITT-LQLEREKALEHKNRLSRMLEDRDLFEARLKALR 768
Cdd:COG4717    387 lrAALEQAEEYQELkEELEELEEQLEELLGELEELLEALDEEELEEeLEELEEELEELEEELEELREELAELEAELEQLE 466
                          330
                   ....*....|....*
gi 2024509102  769 RTVYEDKLKQFQERL 783
Cdd:COG4717    467 EDGELAELLQELEEL 481
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
558-755 2.11e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 2.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  558 LKNSRKEHQRILARRQTIEER----KERLESLN--IQREKEELEQREAELQkvrKAEEERLRQEAKEREKERILQEH--E 629
Cdd:COG3883     18 IQAKQKELSELQAELEAAQAEldalQAELEELNeeYNELQAELEALQAEID---KLQAEIAEAEAEIEERREELGERarA 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  630 QIKKKTVRERLEQIkkteLGAKAFKD-ID----IEDLEELDpdfimAKQVEQLEKEKKELQERLKNQEKKIDyfERAKRL 704
Cdd:COG3883     95 LYRSGGSVSYLDVL----LGSESFSDfLDrlsaLSKIADAD-----ADLLEELKADKAELEAKKAELEAKLA--ELEALK 163
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024509102  705 EEIpliktayeEQRVRDMELWEQQEEERITTLQLEREKALEHKNRLSRMLE 755
Cdd:COG3883    164 AEL--------EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
926-1150 2.74e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 42.20  E-value: 2.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  926 DDERPFRRGDDLPRRSDDLPRRGDDLPRRGPAEEKERPSVESSEDRPPRREGDEDRPPRREGDEDRPLRRGLDEDRPPRR 1005
Cdd:NF033609   623 DSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 702
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1006 GLDDDRGSWRAADDDRGPRRGMDDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRSLDDDRGSWR 1085
Cdd:NF033609   703 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 782
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024509102 1086 AADDDRGPRRGLDDDRPPRRALDDDRPPRRGLDDDRGSWRAADDDRGPRRGLDDDRGPRRGLDDD 1150
Cdd:NF033609   783 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 847
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
1040-1135 2.89e-03

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 41.83  E-value: 2.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1040 DRPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRSLDDDRGSWRAADDDRGPRRGLDDDRPPRraldddRPPRRGLDD 1119
Cdd:TIGR01622    4 DRERERLRDSSSAGDRDRRRDKGRERSRDRSRDRERSRSRRRDRHRDRDYYRGRERRSRSRRPNR------RYRPREKRR 77
                           90
                   ....*....|....*..
gi 2024509102 1120 DRG-SWRAADDDRGPRR 1135
Cdd:TIGR01622   78 RRGdSYRRRRDDRRSRR 94
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
543-784 3.18e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 41.75  E-value: 3.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  543 LQEKEEQHQLAVTAFLKNSRKEHQRILARR----QTIEERKERLESLniqreKEELEQREAELQK--VRKAEEERLRQEA 616
Cdd:PRK04778   131 LLESEEKNREEVEQLKDLYRELRKSLLANRfsfgPALDELEKQLENL-----EEEFSQFVELTESgdYVEAREILDQLEE 205
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  617 KEREKERILQEHEQIKKKTVRERLEQIKKTELGAK-------AFKDIDIE---------------DLEELDPDfIMAKQV 674
Cdd:PRK04778   206 ELAALEQIMEEIPELLKELQTELPDQLQELKAGYRelveegyHLDHLDIEkeiqdlkeqidenlaLLEELDLD-EAEEKN 284
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  675 EQLEKEKKEL-----------QERLKNQEKKIDYFERAKR-----LEEIPLIKTAY-----EEQRVRDmelWEQQEEERI 733
Cdd:PRK04778   285 EEIQERIDQLydilerevkarKYVEKNSDTLPDFLEHAKEqnkelKEEIDRVKQSYtlnesELESVRQ---LEKQLESLE 361
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024509102  734 TTLQLEREKALEHKNRLSrMLEDRdlFEARLKALrrTVYEDKLKQFQERLA 784
Cdd:PRK04778   362 KQYDEITERIAEQEIAYS-ELQEE--LEEILKQL--EEIEKEQEKLSEMLQ 407
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
543-691 3.54e-03

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


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 41.28  E-value: 3.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  543 LQEKEEQHQLAVtaflkNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKE 622
Cdd:pfam09787   77 LQELEAQQQEEA-----ESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKL 151
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024509102  623 RilqehEQIKKKT--------VRERLEQIKKTELGAKAFkdidiedLEELDPDF-IMAKQVEQLEKEKKELQERLKNQ 691
Cdd:pfam09787  152 R-----NQLTSKSqssssqseLENRLHQLTETLIQKQTM-------LEALSTEKnSLVLQLERMEQQIKELQGEGSNG 217
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
570-645 3.65e-03

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


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 41.12  E-value: 3.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  570 ARRQTIEERKERLESLniQREKEELEQREAELQKVRKAEEERLRQEAK------EREKERILQEHEQIKKKTVRERLEQI 643
Cdd:pfam02841  201 AKEKAIEAERAKAEAA--EAEQELLREKQKEEEQMMEAQERSYQEHVKqliekmEAEREQLLAEQERMLEHKLQEQEELL 278

                   ..
gi 2024509102  644 KK 645
Cdd:pfam02841  279 KE 280
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
967-1226 3.66e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 41.82  E-value: 3.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  967 SSEDRPPRREGDEDRPPRREGDEDRPLRRGLDEDRPPRRGLDDDRGSWRAADDDRGPRRGMDDDRPPRRALDDDRPPRRA 1046
Cdd:NF033609   620 SDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 699
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1047 LDDDRPPRRALDDDRPPRRALDDDRPPRRSLDDDRGSWRAADDDRGPRRGLDDDRPPRRALDDDRPPRRGLDDDRGSWRA 1126
Cdd:NF033609   700 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 779
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1127 ADDDRGPRRGLDDDRGPRRGLDDDRGPWRNTDDDRLSRRDDDrgpwrSSEDSRPgpwrpfgkpggwrEREKAREDSWGPP 1206
Cdd:NF033609   780 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD-----SDSDSDS-------------DSDSDSDSDSDSD 841
                          250       260
                   ....*....|....*....|
gi 2024509102 1207 RDSRPPGDREWDRDKDRDDN 1226
Cdd:NF033609   842 SDSDSDSDSDSDSDSESDSN 861
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
608-776 4.08e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.38  E-value: 4.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  608 EEERLRQEAKEREKERILQEHEQIKKKTVRERleqikktelgakafkdidIEDLEEldpdfimakQVEQLEKEKKELQER 687
Cdd:COG2433    383 EELIEKELPEEEPEAEREKEHEERELTEEEEE------------------IRRLEE---------QVERLEAEVEELEAE 435
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  688 LKNQEKKIDYFERakrleEIPLIKTAYEEQRVRDMELweQQEEERITTLQLEREKALEHKNRLSRMLEdrdlfeaRLKAL 767
Cdd:COG2433    436 LEEKDERIERLER-----ELSEARSEERREIRKDREI--SRLDREIERLERELEEERERIEELKRKLE-------RLKEL 501

                   ....*....
gi 2024509102  768 RRTVYEDKL 776
Cdd:COG2433    502 WKLEHSGEL 510
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
958-1090 4.20e-03

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 41.42  E-value: 4.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  958 EEKERPSVESSEDRppRREGDEDRPPRREGDEDRplRRGLDEDRPPRRGLDDDRGSWRAADDDRGPRRGMDDDRPPRRal 1037
Cdd:TIGR01642    2 DEEPDREREKSRGR--DRDRSSERPRRRSRDRSR--FRDRHRRSRERSYREDSRPRDRRRYDSRSPRSLRYSSVRRSR-- 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024509102 1038 ddDRPPRRALDDDRPPR-RALDDDRPPRRALDDDRPPRRSLDDDRGSWRAADDD 1090
Cdd:TIGR01642   76 --DRPRRRSRSVRSIEQhRRRLRDRSPSNQWRKDDKKRSLWDIKPPGYELVTAD 127
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
572-693 4.55e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 41.36  E-value: 4.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  572 RQTIEERKERLESLnIQREKEELEQREAELqkvrkaeeERLRQ--EAKEREKERILQEHEQIKkkTVRERLEQI-KKTEL 648
Cdd:PRK04778   305 RKYVEKNSDTLPDF-LEHAKEQNKELKEEI--------DRVKQsyTLNESELESVRQLEKQLE--SLEKQYDEItERIAE 373
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2024509102  649 GAKAFKDIdIEDLEELDpdfimaKQVEQLEKEKKELQERLKNQEK 693
Cdd:PRK04778   374 QEIAYSEL-QEELEEIL------KQLEEIEKEQEKLSEMLQGLRK 411
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
572-635 4.73e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 41.47  E-value: 4.73e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024509102  572 RQTIEERKERLEslniqREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKT 635
Cdd:PRK05035   452 KARFEARQARLE-----REKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKA 510
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
562-758 5.20e-03

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 41.36  E-value: 5.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  562 RKEHQRILARRQTIEERKERLESLNIQREKEELEQREaelqkvRKAEEERLRQEAKEREKERILQEHEQI---KKKTVRE 638
Cdd:PTZ00440   794 NKISNDINILKENKKNNQDLLNSYNILIQKLEAHTEK------NDEELKQLLQKFPTEDENLNLKELEKEfneNNQIVDN 867
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  639 RLEQIKKTELGAKAFKDIDIEdleeLDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKTAYEEQR 718
Cdd:PTZ00440   868 IIKDIENMNKNINIIKTLNIA----INRSNSNKQLVEHLLNNKIDLKNKLEQHMKIINTDNIIQKNEKLNLLNNLNKEKE 943
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2024509102  719 vrdmELWEQQEEERITTLQLEREKALEHKNRLSRMLEDRD 758
Cdd:PTZ00440   944 ----KIEKQLSDTKINNLKMQIEKTLEYYDKSKENINGND 979
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
588-766 5.28e-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: 40.60  E-value: 5.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  588 QREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKtelgakafkdidiedleeldpd 667
Cdd:TIGR02794   46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKA---------------------- 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  668 fimAKQVEQLEKEKKELQ---ERLKNQEKKidyfERAKRLEEIPLIKTAYEEQRvrdmelweQQEEERITTLQLERE-KA 743
Cdd:TIGR02794  104 ---AKQAEQAAKQAEEKQkqaEEAKAKQAA----EAKAKAEAEAERKAKEEAAK--------QAEEEAKAKAAAEAKkKA 168
                          170       180
                   ....*....|....*....|...
gi 2024509102  744 LEHKNRLSRMLEDRDLFEARLKA 766
Cdd:TIGR02794  169 EEAKKKAEAEAKAKAEAEAKAKA 191
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
572-691 5.38e-03

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


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 38.57  E-value: 5.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  572 RQTIEERKERleslnIQREKEELEQREAELQKVRKAEEERLrQEAKErEKERILQEHEQIKKKTVRERLEQIKktelgak 651
Cdd:cd06503     25 LKALDEREEK-----IAESLEEAEKAKEEAEELLAEYEEKL-AEARA-EAQEIIEEARKEAEKIKEEILAEAK------- 90
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2024509102  652 afkdidiEDLEEldpdfIMAKQVEQLEKEKKELQERLKNQ 691
Cdd:cd06503     91 -------EEAER-----ILEQAKAEIEQEKEKALAELRKE 118
PRK12705 PRK12705
hypothetical protein; Provisional
544-690 5.52e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 40.85  E-value: 5.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  544 QEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEERKERLESLNIQREKEEL----EQREAELQKVRKAEEERLRQEAKER 619
Cdd:PRK12705    36 ERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLvqkeEQLDARAEKLDNLENQLEEREKALS 115
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024509102  620 EKERILQEheqiKKKTVRERLEQIkkTELGAKAFKDIDIEDLE-ELDPDfiMAKQVEQLEKEKKELQERLKN 690
Cdd:PRK12705   116 ARELELEE----LEKQLDNELYRV--AGLTPEQARKLLLKLLDaELEEE--KAQRVKKIEEEADLEAERKAQ 179
PRK12678 PRK12678
transcription termination factor Rho; Provisional
1032-1227 6.29e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 41.04  E-value: 6.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1032 PPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRALDDDRPPRRSLDDDRGSWRAADDDRGPRRgldDDRPPRRALDDDR 1111
Cdd:PRK12678    65 AAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQAR---ERRERGEAARRGA 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1112 PPRRGLDDDRGSWRAADDDRGPRRGLDDDRGPRRGLDDDRGpwrntdddrlsrrdddrgpwRSSEDSRPGPWRPFGKPGG 1191
Cdd:PRK12678   142 ARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQ--------------------AEAERGERGRREERGRDGD 201
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2024509102 1192 WREREKAREDSWGPPRDSRPPGDREWDRDKDRDDNE 1227
Cdd:PRK12678   202 DRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRD 237
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
966-1181 7.32e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 41.05  E-value: 7.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  966 ESSEDRPPRREGDEDRPPRREGDEDRPLRRGLDEDRPPRRGLDDDRGSWRAADDDRGPRRGMDDDRPPRRALDDDRPPRR 1045
Cdd:NF033609   649 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 728
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1046 ALDDDRPPRRALDDDRPPRRALDDDRPPRRSLDDDRGSWRAADDDRGPRRGLDDDRPPRRALDDDRPPRRGLDDDRGSWR 1125
Cdd:NF033609   729 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 808
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024509102 1126 AADDDRGPRRGLDDDRGPRRGLDDDRGPWRNTDDDRLSRRDDDRGPWRSSE---DSRPG 1181
Cdd:NF033609   809 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDsnsDSESG 867
F-BAR_PSTPIP cd07647
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
559-751 7.33e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Vetebrates contain two Proline-Serine-Threonine Phosphatase-Interacting Proteins (PSTPIPs), PSTPIP1 and PSTPIP2. PSTPIPs are mainly expressed in hematopoietic cells and are involved in the regulation of cell adhesion and motility. Mutations in PSTPIPs have been shown to cause autoinflammatory disorders. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain, while PSTPIP2 contains only the N-terminal F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153331 [Multi-domain]  Cd Length: 239  Bit Score: 39.77  E-value: 7.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  559 KNSRKEHQRILARRQTIEER--KERLESLNIQREKEELEQREAELQKVRKAEEE----------RLRQEAKEREKERILQ 626
Cdd:cd07647     18 KKMCKELEDFLKQRAKAEEDygKALLKLSKSAGPGDEIGTLKSSWDSLRKETENvanahiqlaqSLREEAEKLEEFREKQ 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  627 E-----HEQIKKKTVRERLEQIKKTeLGAKAFKDIDIEDLEELDPDF----IMAKQVEQLEKEKKELQERLKNQEKKIDY 697
Cdd:cd07647     98 KeerkkTEDIMKRSQKNKKELYKKT-MKAKKSYEQKCREKDKAEQAYekssSGAQPKEAEKLKKKAAQCKTSAEEADSAY 176
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024509102  698 FERAKRLEEiplIKTAYEEQRVRDMELWEQQEEERITTLqleREKALEHKNRLS 751
Cdd:cd07647    177 KSSIGCLED---ARVEWESEHATACQVFQNMEEERIKFL---RNALWVHCNLGS 224
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
543-652 8.82e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.17  E-value: 8.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  543 LQEKEEQHQLavtaflKNSRKEHQRILARrqtiEERKERLEslniQREKEELEQREAELQKVRKAEEERLRQEAKEREKE 622
Cdd:PRK09510    92 LQQKQAAEQE------RLKQLEKERLAAQ----EQKKQAEE----AAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAA 157
                           90       100       110
                   ....*....|....*....|....*....|
gi 2024509102  623 RILQEHEQIKKKtvRERLEQIKKTELGAKA 652
Cdd:PRK09510   158 AAAKKAAAEAKK--KAEAEAAKKAAAEAKK 185
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
499-756 9.46e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 9.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  499 YSTREDAPLGPQLQSMPSEQIRNQLTAMSSALAKALAVIKPPHLLQEKEEQHQLAVTAFLKNSRKEHQRILARRQTIEER 578
Cdd:COG4717    292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE 371
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  579 KERLESLNIQREKEELEQREAELQKVRKAEEERlrqeakeREKERILQEHEqikkKTVRERLEQIKKTELGAKafkdidI 658
Cdd:COG4717    372 IAALLAEAGVEDEEELRAALEQAEEYQELKEEL-------EELEEQLEELL----GELEELLEALDEEELEEE------L 434
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  659 EDLEEldpdfimakQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEiplIKTAYEEQRVRdmelwEQQEEERITTLQ- 737
Cdd:COG4717    435 EELEE---------ELEELEEELEELREELAELEAELEQLEEDGELAE---LLQELEELKAE-----LRELAEEWAALKl 497
                          250       260
                   ....*....|....*....|...
gi 2024509102  738 ----LEREKALEHKNRLSRMLED 756
Cdd:COG4717    498 alelLEEAREEYREERLPPVLER 520
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
1100-1227 9.50e-03

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 40.29  E-value: 9.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102 1100 DRPPRRALDDDRPPRRGLDDDRGSWRAADDDRGPRRGLDDDRGPRRGLDDDRGPWRNTDDDrlsrrdddrgpwRSSEDSR 1179
Cdd:TIGR01622    4 DRERERLRDSSSAGDRDRRRDKGRERSRDRSRDRERSRSRRRDRHRDRDYYRGRERRSRSR------------RPNRRYR 71
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2024509102 1180 PgpwrpfgkpggwREREKAREDSWGPPRDSRPPGDREWDRDKDRDDNE 1227
Cdd:TIGR01622   72 P------------REKRRRRGDSYRRRRDDRRSRREKPRARDGTPEPL 107
PRK11637 PRK11637
AmiB activator; Provisional
541-634 9.52e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 40.06  E-value: 9.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  541 HLLQEKEEQHQlavtAFLKNSRKEHQRIlarRQTIEERKERLESLNIQREKE-----ELEQREAELQ-KVRKAEEE-RLR 613
Cdd:PRK11637   187 AELEEKQSQQK----TLLYEQQAQQQKL---EQARNERKKTLTGLESSLQKDqqqlsELRANESRLRdSIARAEREaKAR 259
                           90       100
                   ....*....|....*....|.
gi 2024509102  614 QEAKEREKERILQEHEQIKKK 634
Cdd:PRK11637   260 AEREAREAARVRDKQKQAKRK 280
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
558-697 9.60e-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: 40.39  E-value: 9.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  558 LKNSRKEHQrILARRQTIEERKERLESL-NIQREKEEL-EQREAELQKVRKAEEER-LRQEAKEREKERILQEHEQI--- 631
Cdd:TIGR04523  554 LKKENLEKE-IDEKNKEIEELKQTQKSLkKKQEEKQELiDQKEKEKKDLIKEIEEKeKKISSLEKELEKAKKENEKLssi 632
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  632 ------KKKTVRERLEQIKKTELGAKA-FKDID--IEDLEELDPDFIMA------------------------------- 671
Cdd:TIGR04523  633 ikniksKKNKLKQEVKQIKETIKEIRNkWPEIIkkIKESKTKIDDIIELmkdwlkelslhykkyitrmirikdlpkleek 712
                          170       180       190
                   ....*....|....*....|....*....|.
gi 2024509102  672 -KQVEQ----LEKEKKELQERLKNQEKKIDY 697
Cdd:TIGR04523  713 yKEIEKelkkLDEFSKELENIIKNFNKKFDD 743
COG5022 COG5022
Myosin heavy chain [General function prediction only];
562-803 9.87e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 40.45  E-value: 9.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  562 RKEHQRILARRQTIEERKERLESLniQREKEELEQREAELQKVRKAEEERlRQEAKEREKERILQEHEQIKKKTVRERLE 641
Cdd:COG5022    761 RRRYLQALKRIKKIQVIQHGFRLR--RLVDYELKWRLFIKLQPLLSLLGS-RKEYRSYLACIIKLQKTIKREKKLRETEE 837
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  642 Q---IKKTELGAKAFKDI-DIEDLEELDPDFIMAKQVEQLEKEKKELQErLKNQEKKIDY-FERAKRLEEIPLiktayee 716
Cdd:COG5022    838 VefsLKAEVLIQKFGRSLkAKKRFSLLKKETIYLQSAQRVELAERQLQE-LKIDVKSISSlKLVNLELESEII------- 909
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024509102  717 qrvrdmELWEQQEEERITTLQLErekaLEHKNRLSRMLEDRDLFEARLKALRRTVYEDKLKQFQERLAEERRNRLEERKK 796
Cdd:COG5022    910 ------ELKKSLSSDLIENLEFK----TELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKK 979

                   ....*..
gi 2024509102  797 QRKEERR 803
Cdd:COG5022    980 STILVRE 986
 
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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