NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2217376510|ref|XP_047279088|]
View 

rab GTPase-activating protein 1 isoform X3 [Homo sapiens]

Protein Classification

RABGAP1 family PTB domain-containing protein( domain architecture ID 10100584)

RABGAP1 (RAB GTPase activating protein 1) family PTB (phosphotyrosine-binding) domain-containing protein similar to PTB domain region of Homo sapiens Rab GTPase-activating protein 1 that may act as a GTPase-activating protein of RAB6A and play a role in microtubule nucleation by centrosome

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 394-603 1.23e-69

Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.


:

Pssm-ID: 214540 [Multi-domain]  Cd Length: 216  Bit Score: 229.89  E-value: 1.23e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  394 VRNGVPEALRGEVWQLLAGCHNNDH--LVEKYRILITKESPQD----SAITRDINRTFPAHDYFKDTGGDGQDSLYKICK 467
Cdd:smart00164   1 VRKGVPPSLRGVVWKLLLNAQPMDTsaDKDLYSRLLKETAPDDksivHQIEKDLRRTFPEHSFFQDKEGPGQESLRRVLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  468 AYSVYDEEIGYCQGQSFLAAVLLLHMP-EEQAFSVLVKIMFDYGLReLFKQNFEDLHCKFYQLERLMQEYIPDLYNHFLD 546
Cdd:smart00164  81 AYALYNPEVGYCQGMNFLAAPLLLVMEdEEDAFWCLVKLMERYGPN-FYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKD 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217376510  547 ISLEAHMYASQWFLTLFTAKFPLYMVFHIIDLLLCEGISVIFNVALGLLKTSKDDLL 603
Cdd:smart00164 160 LGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
PTB_Rab6GAP cd01211
GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a ...
 1-104 1.55e-62

GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a centrosome-associated GTPase activating protein (GAP) for Rab 6. It consists of an N-terminal PTB domain and a C-terminal TBC domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


:

Pssm-ID: 269922  Cd Length: 129  Bit Score: 207.10  E-value: 1.55e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510   1 MMSILRSQCQISLDVTLSVPNVSEGIVRLLDPQTNTEIANYPIYKILFCVRGHDGTPESDCFAFTESHYNAELFRIHVFR 80
Cdd:cd01211    26 IMAILREQSAQPIKVTLSVPNSSEGSVRLYDPTSNTEIASYPIYRILFCARGPDGTSESDCFAFTWSHGETAIFQCHVFR 105

                          90       100
                  ....*....|....*....|....
gi 2217376510  81 CEIQEAVSRILYSFATAFRRSAKQ 104
Cdd:cd01211   106 CEIPEAVSKVLYSFAKAFRRVPKS 129
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
 138-268 1.30e-35

Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and 151 amino acids in length. The family is found in association with pfam00225, pfam00498. There is a single completely conserved residue W that may be functionally important.


:

Pssm-ID: 463599  Cd Length: 149  Bit Score: 131.94  E-value: 1.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 138 FSAVPKDK----DRQCFKLRQGIDKKIVIYVQQTTNKELAIERCfglllspgKDVRNSDMHLLDleSMGKSSDGKS---- 209
Cdd:pfam12473   2 YVPVPVDQrselDPGTFQLHQGLQRRIVITLTHSSGDELPWERV--------RNVRVGDVRLLD--MKGRVPDSDStpdv 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217376510 210 -------------------YVITGSWNPKSPHFQVVNEETPKDKVLFMTTAVDLVITEVQEPVRFLLETKVRVCSPNE 268
Cdd:pfam12473  72 slkllskpvvrfnadgtssYTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVSEKCAEPVRFSMDTAVQIYPRDE 149
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 656-863 3.34e-07

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.29  E-value: 3.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  656 REQQAQQEDpIERFERENRRLQEANMRLEQENDDLA---HELVTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEEE 732
Cdd:TIGR02168  260 AELQELEEK-LEELRLEVSELEEEIEELQKELYALAneiSRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  733 KRRLEEESAQLK---EMCRRELDKAESEIKKNSSIIGDYKQICSQLSER---LEKQQTANKVEIEKIRQKVDDCERCREF 806
Cdd:TIGR02168  339 LAELEEKLEELKeelESLEAELEELEAELEELESRLEELEEQLETLRSKvaqLELQIASLNNEIERLEARLERLEDRRER 418

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217376510  807 FNKEGRVKGISSTKEVLDE------DTDEEKETLKNQLREMELELAQTKLQLVEAECKIQDLE 863
Cdd:TIGR02168  419 LQQEIEELLKKLEEAELKElqaeleELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
 
Name Accession Description Interval E-value
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 394-603 1.23e-69

Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.


Pssm-ID: 214540 [Multi-domain]  Cd Length: 216  Bit Score: 229.89  E-value: 1.23e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  394 VRNGVPEALRGEVWQLLAGCHNNDH--LVEKYRILITKESPQD----SAITRDINRTFPAHDYFKDTGGDGQDSLYKICK 467
Cdd:smart00164   1 VRKGVPPSLRGVVWKLLLNAQPMDTsaDKDLYSRLLKETAPDDksivHQIEKDLRRTFPEHSFFQDKEGPGQESLRRVLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  468 AYSVYDEEIGYCQGQSFLAAVLLLHMP-EEQAFSVLVKIMFDYGLReLFKQNFEDLHCKFYQLERLMQEYIPDLYNHFLD 546
Cdd:smart00164  81 AYALYNPEVGYCQGMNFLAAPLLLVMEdEEDAFWCLVKLMERYGPN-FYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKD 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217376510  547 ISLEAHMYASQWFLTLFTAKFPLYMVFHIIDLLLCEGISVIFNVALGLLKTSKDDLL 603
Cdd:smart00164 160 LGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
 400-603 9.47e-65

Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are GTPase activator proteins of yeast Ypt6 and Ypt7, implies that these domains are GTPase activator proteins of Rab-like small GTPases.


Pssm-ID: 459855  Cd Length: 178  Bit Score: 215.20  E-value: 9.47e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 400 EALRGEVWQllagchnndhlvekyrilitkespqdSAITRDINRTFPAHDYFKDtgGDGQDSLYKICKAYSVYDEEIGYC 479
Cdd:pfam00566   1 DELRGQVWP--------------------------EQIEKDVPRTFPHSFFFDN--GPGQNSLRRILKAYSIYNPDVGYC 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 480 QGQSFLAAVLLL-HMPEEQAFSVLVKIMFDYGLRELFKQNFEDLHCKFYQLERLMQEYIPDLYNHFLDISLEAHMYASQW 558
Cdd:pfam00566  53 QGMNFIAAPLLLvYLDEEDAFWCFVSLLENYLLRDFYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQW 132

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2217376510 559 FLTLFTAKFPLYMVFHIIDLLLCEGISV-IFNVALGLLKTSKDDLL 603
Cdd:pfam00566 133 FLTLFAREFPLSTVLRIWDYFFLEGEKFvLFRVALAILKRFREELL 178
PTB_Rab6GAP cd01211
GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a ...
 1-104 1.55e-62

GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a centrosome-associated GTPase activating protein (GAP) for Rab 6. It consists of an N-terminal PTB domain and a C-terminal TBC domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269922  Cd Length: 129  Bit Score: 207.10  E-value: 1.55e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510   1 MMSILRSQCQISLDVTLSVPNVSEGIVRLLDPQTNTEIANYPIYKILFCVRGHDGTPESDCFAFTESHYNAELFRIHVFR 80
Cdd:cd01211    26 IMAILREQSAQPIKVTLSVPNSSEGSVRLYDPTSNTEIASYPIYRILFCARGPDGTSESDCFAFTWSHGETAIFQCHVFR 105

                          90       100
                  ....*....|....*....|....
gi 2217376510  81 CEIQEAVSRILYSFATAFRRSAKQ 104
Cdd:cd01211   106 CEIPEAVSKVLYSFAKAFRRVPKS 129
COG5210 COG5210
GTPase-activating protein [General function prediction only];
366-611 3.33e-49

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 181.92  E-value: 3.33e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 366 EKILETWGELL-SKWHLNLNVRPKQLSSLVRNGVPEALRGEVWQLLAG-------CHNNDHLVEKYRILITKESPQD-SA 436
Cdd:COG5210   180 LAADKLWISYLdPNPLSFLPVQLSKLRELIRKGIPNELRGDVWEFLLGigfdldkNPGLYERLLNLHREAKIPTQEIiSQ 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 437 ITRDINRTFPAHDYFKDTGGDGQDSLYKICKAYSVYDEEIGYCQGQSFLAAVLLLHMP-EEQAFSVLVKIMFDYGLRELF 515
Cdd:COG5210   260 IEKDLSRTFPDNSLFQTEISIRAENLRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVLEsEEQAFWCLVKLLKNYGLPGYF 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 516 KQNFEDLHCKFYQLERLMQEYIPDLYNHFLDISLEAHMYASQWFLTLFTAKFPLYMVFHIIDLLLCEGISVIFNVALGLL 595
Cdd:COG5210   340 LKNLSGLHRDLKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAIL 419

                         250
                  ....*....|....*.
gi 2217376510 596 KTSKDDLLLTDFEGAL 611
Cdd:COG5210   420 KLLRDKLLKLDSDELL 435
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
 138-268 1.30e-35

Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and 151 amino acids in length. The family is found in association with pfam00225, pfam00498. There is a single completely conserved residue W that may be functionally important.


Pssm-ID: 463599  Cd Length: 149  Bit Score: 131.94  E-value: 1.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 138 FSAVPKDK----DRQCFKLRQGIDKKIVIYVQQTTNKELAIERCfglllspgKDVRNSDMHLLDleSMGKSSDGKS---- 209
Cdd:pfam12473   2 YVPVPVDQrselDPGTFQLHQGLQRRIVITLTHSSGDELPWERV--------RNVRVGDVRLLD--MKGRVPDSDStpdv 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217376510 210 -------------------YVITGSWNPKSPHFQVVNEETPKDKVLFMTTAVDLVITEVQEPVRFLLETKVRVCSPNE 268
Cdd:pfam12473  72 slkllskpvvrfnadgtssYTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVSEKCAEPVRFSMDTAVQIYPRDE 149
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 1-107 3.15e-22

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 93.15  E-value: 3.15e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510    1 MMSILRSQCQISLDVTLSVPNVSEGIVRLLDPQTNTEIANYPIYKILFCVRGHDGtpeSDCFAFTESHYNAELFRIHVFR 80
Cdd:smart00462  29 IRKLRAAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPDD---LDVFGYIARDPGSSRFACHVFR 105

                           90       100
                   ....*....|....*....|....*....
gi 2217376510   81 CEI--QEAVSRILYSFATAFRRSAKQTPL 107
Cdd:smart00462 106 CEKaaEDIALAIGQAFQLAYELKLKARSE 134
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 656-863 3.34e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.29  E-value: 3.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  656 REQQAQQEDpIERFERENRRLQEANMRLEQENDDLA---HELVTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEEE 732
Cdd:TIGR02168  260 AELQELEEK-LEELRLEVSELEEEIEELQKELYALAneiSRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  733 KRRLEEESAQLK---EMCRRELDKAESEIKKNSSIIGDYKQICSQLSER---LEKQQTANKVEIEKIRQKVDDCERCREF 806
Cdd:TIGR02168  339 LAELEEKLEELKeelESLEAELEELEAELEELESRLEELEEQLETLRSKvaqLELQIASLNNEIERLEARLERLEDRRER 418

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217376510  807 FNKEGRVKGISSTKEVLDE------DTDEEKETLKNQLREMELELAQTKLQLVEAECKIQDLE 863
Cdd:TIGR02168  419 LQQEIEELLKKLEEAELKElqaeleELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 625-863 1.13e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 46.12  E-value: 1.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  625 EENAKKLMELACNM--KISQKKLKKYEKEYHTMREQQAQ---QEDPIERFERENR---RLQEANMRLEQENDDLAHELVT 696
Cdd:pfam02463  172 KEALKKLIEETENLaeLIIDLEELKLQELKLKEQAKKALeyyQLKEKLELEEEYLlylDYLKLNEERIDLLQELLRDEQE 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  697 SKIALRKDLDNAEEKADALNKELLMTKQ----------KLIDAEEEKRRLEEESAQLKEMCRRELDKAESEIKKNSSIIG 766
Cdd:pfam02463  252 EIESSKQEIEKEEEKLAQVLKENKEEEKekklqeeelkLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  767 DYKQICSQLS---ERLEKQQTANKVEIEKIRQKVDDCERCR-----------EFFNKEGRVKGISSTKEVLDEDTDEEKE 832
Cdd:pfam02463  332 KEKEEIEELEkelKELEIKREAEEEEEEELEKLQEKLEQLEeellakkklesERLSSAAKLKEEELELKSEEEKEAQLLL 411

                          250       260       270
                   ....*....|....*....|....*....|.
gi 2217376510  833 TLKNQLREMELELAQTKLQLVEAECKIQDLE 863
Cdd:pfam02463  412 ELARQLEDLLKEEKKEELEILEEEEESIELK 442
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
27-98 2.02e-04

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 42.35  E-value: 2.02e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217376510  27 VRLLDPQTNTEIANYPIYKILFCVRGHDGTpeSDCFAFTESHYNAELFRIHVFRCEiqEAVSRILYSFATAF 98
Cdd:pfam00640  63 LKLLNPDTQELIHDHPLVSISFCADGDPDL--MRYFAYIARDKATNKFACHVFESE--DGAQDIAQSIGQAF 130
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 656-878 3.03e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 3.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 656 REQQAQQEDPIERFERENRRLQEANMRLEQENDDLaHELVTSKIALRKDLDNAEEKADALnkellmtKQKLIDAEEEKRR 735
Cdd:COG1196   256 EELEAELAELEAELEELRLELEELELELEEAQAEE-YELLAELARLEQDIARLEERRREL-------EERLEELEEELAE 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 736 LEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEKIRQKVDDCERCREFFNKEGRVKG 815
Cdd:COG1196   328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217376510 816 ISSTKEVLDEDTDEEKETLKNQLREMELELAQTKLQLVEAECKIQDLEHHLGLALNEVQAAKK 878
Cdd:COG1196   408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
654-874 2.07e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 654 TMREQQAQQEDPIERFErenrRLQEANMRLE--QENDDLAHELVTSKialRKDLDNAEEKADALNKEllmtKQKLIDAEE 731
Cdd:PRK02224  486 DLEEEVEEVEERLERAE----DLVEAEDRIErlEERREDLEELIAER---RETIEEKRERAEELRER----AAELEAEAE 554

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 732 EKRRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQtankvEIEKIRQKVDD-CERCREffNKE 810
Cdd:PRK02224  555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAED-----EIERLREKREAlAELNDE--RRE 627

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217376510 811 gRVKGISSTKEVLDEDTDEEK-ETLKNQLREMELELAQTKLQLVEAECKIQDLEHHLGLALNEVQ 874
Cdd:PRK02224  628 -RLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELE 691
 
Name Accession Description Interval E-value
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 394-603 1.23e-69

Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.


Pssm-ID: 214540 [Multi-domain]  Cd Length: 216  Bit Score: 229.89  E-value: 1.23e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  394 VRNGVPEALRGEVWQLLAGCHNNDH--LVEKYRILITKESPQD----SAITRDINRTFPAHDYFKDTGGDGQDSLYKICK 467
Cdd:smart00164   1 VRKGVPPSLRGVVWKLLLNAQPMDTsaDKDLYSRLLKETAPDDksivHQIEKDLRRTFPEHSFFQDKEGPGQESLRRVLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  468 AYSVYDEEIGYCQGQSFLAAVLLLHMP-EEQAFSVLVKIMFDYGLReLFKQNFEDLHCKFYQLERLMQEYIPDLYNHFLD 546
Cdd:smart00164  81 AYALYNPEVGYCQGMNFLAAPLLLVMEdEEDAFWCLVKLMERYGPN-FYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKD 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217376510  547 ISLEAHMYASQWFLTLFTAKFPLYMVFHIIDLLLCEGISVIFNVALGLLKTSKDDLL 603
Cdd:smart00164 160 LGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
 400-603 9.47e-65

Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are GTPase activator proteins of yeast Ypt6 and Ypt7, implies that these domains are GTPase activator proteins of Rab-like small GTPases.


Pssm-ID: 459855  Cd Length: 178  Bit Score: 215.20  E-value: 9.47e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 400 EALRGEVWQllagchnndhlvekyrilitkespqdSAITRDINRTFPAHDYFKDtgGDGQDSLYKICKAYSVYDEEIGYC 479
Cdd:pfam00566   1 DELRGQVWP--------------------------EQIEKDVPRTFPHSFFFDN--GPGQNSLRRILKAYSIYNPDVGYC 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 480 QGQSFLAAVLLL-HMPEEQAFSVLVKIMFDYGLRELFKQNFEDLHCKFYQLERLMQEYIPDLYNHFLDISLEAHMYASQW 558
Cdd:pfam00566  53 QGMNFIAAPLLLvYLDEEDAFWCFVSLLENYLLRDFYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQW 132

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2217376510 559 FLTLFTAKFPLYMVFHIIDLLLCEGISV-IFNVALGLLKTSKDDLL 603
Cdd:pfam00566 133 FLTLFAREFPLSTVLRIWDYFFLEGEKFvLFRVALAILKRFREELL 178
PTB_Rab6GAP cd01211
GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a ...
 1-104 1.55e-62

GTPase activating protein for Rab 6 Phosphotyrosine-binding (PTB) domain; GAPCenA is a centrosome-associated GTPase activating protein (GAP) for Rab 6. It consists of an N-terminal PTB domain and a C-terminal TBC domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.


Pssm-ID: 269922  Cd Length: 129  Bit Score: 207.10  E-value: 1.55e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510   1 MMSILRSQCQISLDVTLSVPNVSEGIVRLLDPQTNTEIANYPIYKILFCVRGHDGTPESDCFAFTESHYNAELFRIHVFR 80
Cdd:cd01211    26 IMAILREQSAQPIKVTLSVPNSSEGSVRLYDPTSNTEIASYPIYRILFCARGPDGTSESDCFAFTWSHGETAIFQCHVFR 105

                          90       100
                  ....*....|....*....|....
gi 2217376510  81 CEIQEAVSRILYSFATAFRRSAKQ 104
Cdd:cd01211   106 CEIPEAVSKVLYSFAKAFRRVPKS 129
COG5210 COG5210
GTPase-activating protein [General function prediction only];
366-611 3.33e-49

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 181.92  E-value: 3.33e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 366 EKILETWGELL-SKWHLNLNVRPKQLSSLVRNGVPEALRGEVWQLLAG-------CHNNDHLVEKYRILITKESPQD-SA 436
Cdd:COG5210   180 LAADKLWISYLdPNPLSFLPVQLSKLRELIRKGIPNELRGDVWEFLLGigfdldkNPGLYERLLNLHREAKIPTQEIiSQ 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 437 ITRDINRTFPAHDYFKDTGGDGQDSLYKICKAYSVYDEEIGYCQGQSFLAAVLLLHMP-EEQAFSVLVKIMFDYGLRELF 515
Cdd:COG5210   260 IEKDLSRTFPDNSLFQTEISIRAENLRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVLEsEEQAFWCLVKLLKNYGLPGYF 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 516 KQNFEDLHCKFYQLERLMQEYIPDLYNHFLDISLEAHMYASQWFLTLFTAKFPLYMVFHIIDLLLCEGISVIFNVALGLL 595
Cdd:COG5210   340 LKNLSGLHRDLKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAIL 419

                         250
                  ....*....|....*.
gi 2217376510 596 KTSKDDLLLTDFEGAL 611
Cdd:COG5210   420 KLLRDKLLKLDSDELL 435
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
 138-268 1.30e-35

Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and 151 amino acids in length. The family is found in association with pfam00225, pfam00498. There is a single completely conserved residue W that may be functionally important.


Pssm-ID: 463599  Cd Length: 149  Bit Score: 131.94  E-value: 1.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 138 FSAVPKDK----DRQCFKLRQGIDKKIVIYVQQTTNKELAIERCfglllspgKDVRNSDMHLLDleSMGKSSDGKS---- 209
Cdd:pfam12473   2 YVPVPVDQrselDPGTFQLHQGLQRRIVITLTHSSGDELPWERV--------RNVRVGDVRLLD--MKGRVPDSDStpdv 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217376510 210 -------------------YVITGSWNPKSPHFQVVNEETPKDKVLFMTTAVDLVITEVQEPVRFLLETKVRVCSPNE 268
Cdd:pfam12473  72 slkllskpvvrfnadgtssYTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVSEKCAEPVRFSMDTAVQIYPRDE 149
PTB smart00462
Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain ...
 1-107 3.15e-22

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.


Pssm-ID: 214675  Cd Length: 134  Bit Score: 93.15  E-value: 3.15e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510    1 MMSILRSQCQISLDVTLSVPNVSEGIVRLLDPQTNTEIANYPIYKILFCVRGHDGtpeSDCFAFTESHYNAELFRIHVFR 80
Cdd:smart00462  29 IRKLRAAQGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPDD---LDVFGYIARDPGSSRFACHVFR 105

                           90       100
                   ....*....|....*....|....*....
gi 2217376510   81 CEI--QEAVSRILYSFATAFRRSAKQTPL 107
Cdd:smart00462 106 CEKaaEDIALAIGQAFQLAYELKLKARSE 134
PTB cd00934
Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are ...
 5-98 9.70e-14

Phosphotyrosine-binding (PTB) PH-like fold; PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to bind peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains.


Pssm-ID: 269911  Cd Length: 120  Bit Score: 68.69  E-value: 9.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510   5 LRSQCQISLDVTLsvpNVSEGIVRLLDPQTNTEIANYPIYKILFCVRGHDgtpESDCFAFTESHYNAELFRIHVFRCEIQ 84
Cdd:cd00934    33 LKSSKRKPGPVLL---EVSSKGVKLLDLDTKELLLRHPLHRISYCGRDPD---NPNVFAFIAGEEGGSGFRCHVFQCEDE 106

                          90
                  ....*....|....
gi 2217376510  85 EAVSRILYSFATAF 98
Cdd:cd00934   107 EEAEEILQAIGQAF 120
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 656-863 3.34e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.29  E-value: 3.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  656 REQQAQQEDpIERFERENRRLQEANMRLEQENDDLA---HELVTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEEE 732
Cdd:TIGR02168  260 AELQELEEK-LEELRLEVSELEEEIEELQKELYALAneiSRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  733 KRRLEEESAQLK---EMCRRELDKAESEIKKNSSIIGDYKQICSQLSER---LEKQQTANKVEIEKIRQKVDDCERCREF 806
Cdd:TIGR02168  339 LAELEEKLEELKeelESLEAELEELEAELEELESRLEELEEQLETLRSKvaqLELQIASLNNEIERLEARLERLEDRRER 418

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217376510  807 FNKEGRVKGISSTKEVLDE------DTDEEKETLKNQLREMELELAQTKLQLVEAECKIQDLE 863
Cdd:TIGR02168  419 LQQEIEELLKKLEEAELKElqaeleELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 666-878 3.57e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.29  E-value: 3.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  666 IERFERENRRLQEANMRLEQENDDLAHELVTSKIA---LRKDLDNAEEKADALNKELLMTKQKLIDAEEEKRRLEEESAQ 742
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAELQELEEKleeLRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  743 LKemcrRELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQtankVEIEKIRQKVDdcERCREFFNKEGRVkgisstkev 822
Cdd:TIGR02168  314 LE----RQLEELEAQLEELESKLDELAEELAELEEKLEELK----EELESLEAELE--ELEAELEELESRL--------- 374

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217376510  823 ldEDTDEEKETLKNQLREMELELAQTKLQLVEAECKIQDLEHHLGLALNEVQAAKK 878
Cdd:TIGR02168  375 --EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 670-877 1.06e-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: 46.20  E-value: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  670 ERENRRLQEANMRLEQENDDLAHELvtskIALRKDLDNAEEKADALNKELLMTKQKLIDAEEEKRRLEEESAQLKEMCRR 749
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKAL----AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  750 ------ELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEKIRQKVDDCERC-----REFFNKEGRVKGISS 818
Cdd:TIGR02168  752 lskeltELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEltllnEEAANLRERLESLER 831

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217376510  819 TKevldEDTDEEKETLKNQLREMELELAQTKLQLVEAECKIQDLEHHLGLALNEVQAAK 877
Cdd:TIGR02168  832 RI----AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 625-863 1.13e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 46.12  E-value: 1.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  625 EENAKKLMELACNM--KISQKKLKKYEKEYHTMREQQAQ---QEDPIERFERENR---RLQEANMRLEQENDDLAHELVT 696
Cdd:pfam02463  172 KEALKKLIEETENLaeLIIDLEELKLQELKLKEQAKKALeyyQLKEKLELEEEYLlylDYLKLNEERIDLLQELLRDEQE 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  697 SKIALRKDLDNAEEKADALNKELLMTKQ----------KLIDAEEEKRRLEEESAQLKEMCRRELDKAESEIKKNSSIIG 766
Cdd:pfam02463  252 EIESSKQEIEKEEEKLAQVLKENKEEEKekklqeeelkLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  767 DYKQICSQLS---ERLEKQQTANKVEIEKIRQKVDDCERCR-----------EFFNKEGRVKGISSTKEVLDEDTDEEKE 832
Cdd:pfam02463  332 KEKEEIEELEkelKELEIKREAEEEEEEELEKLQEKLEQLEeellakkklesERLSSAAKLKEEELELKSEEEKEAQLLL 411

                          250       260       270
                   ....*....|....*....|....*....|.
gi 2217376510  833 TLKNQLREMELELAQTKLQLVEAECKIQDLE 863
Cdd:pfam02463  412 ELARQLEDLLKEEKKEELEILEEEEESIELK 442
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 653-874 1.97e-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: 1.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  653 HTMREQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELVTSKIALRK---DLDNAEEKADALNKELlmtKQKLIDA 729
Cdd:TIGR02168  722 EELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEaeeELAEAEAEIEELEAQI---EQLKEEL 798

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  730 EEEKRRLEEESAQLKEMcRRELDKAESEIKKNSSIIGDykqiCSQLSERLEKQQTANKVEIEKIRQKVDDCERCREFFNK 809
Cdd:TIGR02168  799 KALREALDELRAELTLL-NEEAANLRERLESLERRIAA----TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217376510  810 EgrVKGISSTKEVLDEDTD---EEKETLKNQLREMELELAQTKLQLVEAECKIQDLEHHLGLALNEVQ 874
Cdd:TIGR02168  874 E--LEALLNERASLEEALAllrSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
PID pfam00640
Phosphotyrosine interaction domain (PTB/PID);
27-98 2.02e-04

Phosphotyrosine interaction domain (PTB/PID);


Pssm-ID: 395515  Cd Length: 133  Bit Score: 42.35  E-value: 2.02e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217376510  27 VRLLDPQTNTEIANYPIYKILFCVRGHDGTpeSDCFAFTESHYNAELFRIHVFRCEiqEAVSRILYSFATAF 98
Cdd:pfam00640  63 LKLLNPDTQELIHDHPLVSISFCADGDPDL--MRYFAYIARDKATNKFACHVFESE--DGAQDIAQSIGQAF 130
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 656-878 3.03e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 3.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 656 REQQAQQEDPIERFERENRRLQEANMRLEQENDDLaHELVTSKIALRKDLDNAEEKADALnkellmtKQKLIDAEEEKRR 735
Cdd:COG1196   256 EELEAELAELEAELEELRLELEELELELEEAQAEE-YELLAELARLEQDIARLEERRREL-------EERLEELEEELAE 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 736 LEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTANKVEIEKIRQKVDDCERCREFFNKEGRVKG 815
Cdd:COG1196   328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217376510 816 ISSTKEVLDEDTDEEKETLKNQLREMELELAQTKLQLVEAECKIQDLEHHLGLALNEVQAAKK 878
Cdd:COG1196   408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 655-877 4.00e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 44.34  E-value: 4.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  655 MREQQAQQEDPIERFERENRRLQEANMRLEqendDLAHELVTSKiALRKD-LDNAEEKADALNKELLM-------TKQKL 726
Cdd:pfam15921  119 LQEMQMERDAMADIRRRESQSQEDLRNQLQ----NTVHELEAAK-CLKEDmLEDSNTQIEQLRKMMLShegvlqeIRSIL 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  727 IDAEEEKRRLEEESAQLKEMCRRELDKAESEI-KKNSSIIGDYKQICSQLSERLE--KQQTANKVEI------EKIRQKV 797
Cdd:pfam15921  194 VDFEEASGKKIYEHDSMSTMHFRSLGSAISKIlRELDTEISYLKGRIFPVEDQLEalKSESQNKIELllqqhqDRIEQLI 273

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  798 DDCE-----RCREFFNKEGRVKGISSTKEVLDEDTDEEKETLKNQLREMELELAQTKLQLVEA----ECKIQDLEHHLGL 868
Cdd:pfam15921  274 SEHEveitgLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAkrmyEDKIEELEKQLVL 353


                   ....*....
gi 2217376510  869 ALNEVQAAK 877
Cdd:pfam15921  354 ANSELTEAR 362
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 679-879 1.32e-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: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 679 ANMRLEQENDDLAhELVTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEeekrrleeesAQLKEMcRRELDKAESEI 758
Cdd:COG3883    14 ADPQIQAKQKELS-ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ----------AEIDKL-QAEIAEAEAEI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 759 KKNSSIIGD-----YKQICSQ------LS-----------ERLEKQQTANKVEIEKIRQKVDDCErcreffNKEGRVKGI 816
Cdd:COG3883    82 EERREELGEraralYRSGGSVsyldvlLGsesfsdfldrlSALSKIADADADLLEELKADKAELE------AKKAELEAK 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217376510 817 SSTKEVLDEDTDEEKETLKNQLREMELELAQTKLQLVEAECKIQDLEHHLGLALNEVQAAKKT 879
Cdd:COG3883   156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 656-863 1.51e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.36  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  656 REQQAQQEDPIERFERENRRLQEANMRLEQENDDLAhELVTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAeeekrr 735
Cdd:TIGR02169  719 GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE-NVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS------ 791

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  736 leeesaQLKEMcRRELDKAESEIKKNSSIIGDYKQIcsqLSERLEKQQTANKvEIEKIRQKVDDCERCREffnkegrvkg 815
Cdd:TIGR02169  792 ------RIPEI-QAELSKLEEEVSRIEARLREIEQK---LNRLTLEKEYLEK-EIQELQEQRIDLKEQIK---------- 850

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2217376510  816 isstkevldeDTDEEKETLKNQLREMELELAQTKLQLVEAECKIQDLE 863
Cdd:TIGR02169  851 ----------SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLK 888
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 654-866 1.92e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.03  E-value: 1.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  654 TMREQQAQQEDPIERFERENRRLQEANMRleqENDDLAHELVTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEEEK 733
Cdd:pfam15921  289 SARSQANSIQSQLEIIQEQARNQNSMYMR---QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTER 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  734 RRLEEESAQLKEMCRR---ELDKAESEIkknssiigdykQICSQLSERLEKQQTANKVEIEKIRQKVDD----CERCREF 806
Cdd:pfam15921  366 DQFSQESGNLDDQLQKllaDLHKREKEL-----------SLEKEQNKRLWDRDTGNSITIDHLRRELDDrnmeVQRLEAL 434

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217376510  807 FNK---------EGRVKGISSTKEVLDEDTD--EEKETLKNQLREMELELAQTKLQLVEAECKIQDLEHHL 866
Cdd:pfam15921  435 LKAmksecqgqmERQMAAIQGKNESLEKVSSltAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASL 505
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
654-874 2.07e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 654 TMREQQAQQEDPIERFErenrRLQEANMRLE--QENDDLAHELVTSKialRKDLDNAEEKADALNKEllmtKQKLIDAEE 731
Cdd:PRK02224  486 DLEEEVEEVEERLERAE----DLVEAEDRIErlEERREDLEELIAER---RETIEEKRERAEELRER----AAELEAEAE 554

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 732 EKRRLEEESAQLKEMCRRELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQtankvEIEKIRQKVDD-CERCREffNKE 810
Cdd:PRK02224  555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAED-----EIERLREKREAlAELNDE--RRE 627

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217376510 811 gRVKGISSTKEVLDEDTDEEK-ETLKNQLREMELELAQTKLQLVEAECKIQDLEHHLGLALNEVQ 874
Cdd:PRK02224  628 -RLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELE 691
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 657-879 3.58e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 3.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  657 EQQAQQEDPIERFERENRRLQEANMRLEQENDDLAHELVTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEEEKRrl 736
Cdd:TIGR02169  248 SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA-- 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  737 eeesaQLKEmcrrELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTankvEIEKIRQKVDDCERCreffNKEGRVKGI 816
Cdd:TIGR02169  326 -----KLEA----EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE----ELEDLRAELEEVDKE----FAETRDELK 388

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217376510  817 SSTKEVldEDTDEEKETLKNQLREMELELAQTKLQLVEAECKIQDLEHhlglALNEVQAAKKT 879
Cdd:TIGR02169  389 DYREKL--EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA----KINELEEEKED 445
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 595-872 4.32e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.80  E-value: 4.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  595 LKTSKDdlLLTDFeGALKFFRVQLpkryrsEENAKKLMELACnmKISQKKLKKYEKEYHTMREQQAQQEDPIERFERENR 674
Cdd:TIGR00606  781 EESAKV--CLTDV-TIMERFQMEL------KDVERKIAQQAA--KLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNR 849

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  675 RLQEANMRLEQENDDLAHELVTSKIALRKDLDNAEEKADALnKELLMTKQKLIDAEEEKRRLEEESAQLKEMCRRELD-- 752
Cdd:TIGR00606  850 KLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQL-VELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEel 928

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  753 ---------KAESEI----KKNSSIIGDYKQICSQLSERLEKQQTANKVEIEKIRQKVDDCERCREFFNKEGRVKGISST 819
Cdd:TIGR00606  929 issketsnkKAQDKVndikEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDID 1008

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217376510  820 KEVLDEDTDEEKETL---KNQLREMELELAQ-----TKLQLVEAECKIQDLEHHLGLALNE 872
Cdd:TIGR00606 1009 TQKIQERWLQDNLTLrkrENELKEVEEELKQhlkemGQMQVLQMKQEHQKLEENIDLIKRN 1069
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 653-887 4.69e-03

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 40.98  E-value: 4.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  653 HTMREQQAQQEDPIERFERE-----------NRRLQEANMRLEQ---ENDDLAHEL------------------------ 694
Cdd:pfam12128  474 ERAREEQEAANAEVERLQSElrqarkrrdqaSEALRQASRRLEErqsALDELELQLfpqagtllhflrkeapdweqsigk 553

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  695 -VTSKIALRKDLD---NAEEKADALNKELLMTKQKLIDAEEekrrleeeSAQLKEMCRRELDKAESEIKKNSSIIGDYKQ 770
Cdd:pfam12128  554 vISPELLHRTDLDpevWDGSVGGELNLYGVKLDLKRIDVPE--------WAASEEELRERLDKAEEALQSAREKQAAAEE 625

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  771 ICSQLSERLEKQQTA----------NKVEIEKI----RQKVDDCERCREFFNK--EGRVKGISSTKEVLDEDTDEEKETL 834
Cdd:pfam12128  626 QLVQANGELEKASREetfartalknARLDLRRLfdekQSEKDKKNKALAERKDsaNERLNSLEAQLKQLDKKHQAWLEEQ 705

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217376510  835 KNQLREMELELaQTKLQLVEAECKIQDLEHHLGLALNEVQAAK-----KTWFNRTLSS 887
Cdd:pfam12128  706 KEQKREARTEK-QAYWQVVEGALDAQLALLKAAIAARRSGAKAelkalETWYKRDLAS 762
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 656-877 4.80e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 4.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 656 REQQAQQEDPIERFERENRRLQEANMRLEQENDDLAH------ELVTSKIALRKDLDNAEEKADALNKELLMTKQKLIDA 729
Cdd:COG1196   291 YELLAELARLEQDIARLEERRRELEERLEELEEELAEleeeleELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 730 EEEKR----RLEEESAQLKEMCRRELDKAESEikknssiigdykqicsqlsERLEKQQTANKVEIEKIRQkvddcercre 805
Cdd:COG1196   371 EAELAeaeeELEELAEELLEALRAAAELAAQL-------------------EELEEAEEALLERLERLEE---------- 421

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217376510 806 ffNKEGRVKGISSTKEVLDEDTDEEKETLKNQLREmELELAQTKLQLVEAECKIQDLEHHLGLALNEVQAAK 877
Cdd:COG1196   422 --ELEELEEALAELEEEEEEEEEALEEAAEEEAEL-EEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
656-814 4.94e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 4.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 656 REQQAQQEDPIERFERENRRLQEANMRLEQENDdlAHELVTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEEEKRR 735
Cdd:COG4717    94 QEELEELEEELEELEAELEELREELEKLEKLLQ--LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE 171

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217376510 736 LEEESAQLKEMCRRELDKAESEIKknsSIIGDYKQICSQLsERLEKQQTANKVEIEKIRQKVDDCERCREFFNKEGRVK 814
Cdd:COG4717   172 LAELQEELEELLEQLSLATEEELQ---DLAEELEELQQRL-AELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 666-863 5.03e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 5.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  666 IERFERENRR----LQEANMRLEqENDDLAHELVTSKIALRKDLDNAEeKADALNKELLMTKQKLIdaeeekrrleeeSA 741
Cdd:TIGR02169  165 VAEFDRKKEKaleeLEEVEENIE-RLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGYEL------------LK 230

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  742 QLKEMcRRELDKAESEIkknssiigdykqicsqlsERLEKQQTANKVEIEKIRQKVDDCERCREFFNKEgrvkgisstke 821
Cdd:TIGR02169  231 EKEAL-ERQKEAIERQL------------------ASLEEELEKLTEEISELEKRLEEIEQLLEELNKK----------- 280

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2217376510  822 vLDEDTDEEKETLKNQLREMELELAQTKLQLVEAECKIQDLE 863
Cdd:TIGR02169  281 -IKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
mukB PRK04863
chromosome partition protein MukB;
671-852 5.11e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.71  E-value: 5.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  671 RENRRLQEAnMRLEQENDDLAHELVTSKIAL--------RKDLDNAEEKADALNKELLMTKQKLIDaeeekrrleeeSAQ 742
Cdd:PRK04863   240 RENRMTLEA-IRVTQSDRDLFKHLITESTNYvaadymrhANERRVHLEEALELRRELYTSRRQLAA-----------EQY 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510  743 LKEMCRRELDkaesEIKKNSSIIG-DYkqicSQLSERLEKQQTANKVEiEKIRQKVDDCERcreffnKEGRvkgISSTKE 821
Cdd:PRK04863   308 RLVEMARELA----ELNEAESDLEqDY----QAASDHLNLVQTALRQQ-EKIERYQADLEE------LEER---LEEQNE 369

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2217376510  822 VLdEDTDEEKETLKNQLREMELELAQTKLQL 852
Cdd:PRK04863   370 VV-EEADEQQEENEARAEAAEEEVDELKSQL 399
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
666-878 8.06e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 8.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 666 IERFERENRRLQEANMRLEQE----NDDL--AHELVTSKIALRKDLDNAEEKADALNKELLMTKQKLIDAEEEKRRleee 739
Cdd:PRK03918  520 LEKKAEEYEKLKEKLIKLKGEikslKKELekLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLK---- 595

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376510 740 saQLKEMCRR--ELDKAESEIKKNSSIIGDYKQICSQLSERLEKQQTankvEIEKIRQKVDDCERC---REFFNKEGRVK 814
Cdd:PRK03918  596 --ELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEK----RLEELRKELEELEKKyseEEYEELREEYL 669

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217376510 815 GISSTKEVLDEdtdeEKETLKNQLREMELELAQTKLQLVEAECKIQDLEhHLGLALNEVQAAKK 878
Cdd:PRK03918  670 ELSRELAGLRA----ELEELEKRREEIKKTLEKLKEELEEREKAKKELE-KLEKALERVEELRE 728
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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