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Conserved domains on  [gi|1387845346|ref|NP_001350083|]
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TBC1 domain family member 31 isoform 10 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
10-235 4.39e-23

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 102.68  E-value: 4.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  10 TKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 88
Cdd:COG2319   151 TGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDgTVRLWDLATGKLLRTLTGHTG-AVRSVAFSPDGKLLASGSADGTVR 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  89 AWECDTLFCKYQLPAPPES-SSIlykvfAVTRDGRILAAGGKSNHLHLWCLEARQLFRIIQMPTkvRAIRHLEFLPDSfd 167
Cdd:COG2319   230 LWDLATGKLLRTLTGHSGSvRSV-----AFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHS--GGVNSVAFSPDG-- 300

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387845346 168 agsnQVLGVLSQDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYIASIMENGSLNIYSVQALTQ 235
Cdd:COG2319   301 ----KLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364
RabGAP-TBC super family cl46302
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
 357-500 1.57e-08

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.


The actual alignment was detected with superfamily member pfam00566:

Pssm-ID: 480642  Cd Length: 178  Bit Score: 54.95  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 357 LQKKYPIKSRKLLRVLQRTLSALAHWSVIFSDTPYLPLLAFPFVkLFQNNQLICFEVIATLIINwcQHWFEYFPN--PPI 434
Cdd:pfam00566  20 FPHSFFFDNGPGQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLL-LVYLDEEDAFWCFVSLLEN--YLLRDFYTPdfPGL 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387845346 435 NILSMI-ENVLAFHDKELLQHFIDHDITSQLYAWPLLETVFSEVLTREEWLKLFDNIFSNHPSFLLM 500
Cdd:pfam00566  97 KRDLYVfEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVLF 163
DUF5401 super family cl38662
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 585-749 7.69e-08

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


The actual alignment was detected with superfamily member pfam17380:

Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 56.29  E-value: 7.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 585 QERERIRNdELDYLRERQTVE-DMQAKVDQQRVEDEAWYQKQE------LLRKAEETRREM--LLQEEEKMIQQRQRLAA 655
Cdd:pfam17380 389 QKNERVRQ-ELEAARKVKILEeERQRKIQQQKVEMEQIRAEQEearqreVRRLEEERAREMerVRLEEQERQQQVERLRQ 467

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 656 VKRELKVKEMHLQDAARRRFLKLQQD----QQEMELRR---LDDEIGR----KNLTENQEALAKE-MRADADAYRRK-VD 722
Cdd:pfam17380 468 QEEERKRKKLELEKEKRDRKRAEEQRrkilEKELEERKqamIEEERKRklleKEMEERQKAIYEEeRRREAEEERRKqQE 547

                         170       180
                  ....*....|....*....|....*....
gi 1387845346 723 LEE--HMFHKLIEAGETQSQKTQKWKEAE 749
Cdd:pfam17380 548 MEErrRIQEQMRKATEERSRLEAMERERE 576
Nup88 super family cl25737
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 656-846 5.60e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


The actual alignment was detected with superfamily member pfam10168:

Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 40.41  E-value: 5.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 656 VKRE--LKVKEMHLQDAARR-RFLKLQQDQQEMELRRLDDEigRKNLTENQEALAKemradadayrrkvdleehmfhKLI 732
Cdd:pfam10168 543 VFREeyLKKHDLAREEIQKRvKLLKLQKEQQLQELQSLEEE--RKSLSERAEKLAE---------------------KYE 599

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 733 EAGETQSQKTQKWKEAegkefrLRSAK-KASALSDASRKwfLKQE---INAAVEHAENpCHKEEPRFQNEQdssclprTS 808
Cdd:pfam10168 600 EIKDKQEKLMRRCKKV------LQRLNsQLPVLSDAERE--MKKEletINEQLKHLAN-AIKQAKKKMNYQ-------RY 663

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1387845346 809 QLNDSSEMDPSTQISLN---RRAV-----EWDTTGQNLIKKVRNLR 846
Cdd:pfam10168 664 QIAKSQSIRKKSSLSLSekqRKTIkeilkQLGSEIDELIKQVKDIN 709
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
10-235 4.39e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 102.68  E-value: 4.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  10 TKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 88
Cdd:COG2319   151 TGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDgTVRLWDLATGKLLRTLTGHTG-AVRSVAFSPDGKLLASGSADGTVR 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  89 AWECDTLFCKYQLPAPPES-SSIlykvfAVTRDGRILAAGGKSNHLHLWCLEARQLFRIIQMPTkvRAIRHLEFLPDSfd 167
Cdd:COG2319   230 LWDLATGKLLRTLTGHSGSvRSV-----AFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHS--GGVNSVAFSPDG-- 300

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387845346 168 agsnQVLGVLSQDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYIASIMENGSLNIYSVQALTQ 235
Cdd:COG2319   301 ----KLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 10-229 1.36e-19

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 90.09  E-value: 1.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  10 TKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 88
Cdd:cd00200    82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDkTIKVWDVETGKCLTTLRGHTD-WVNSVAFSPDGTFVASSSQDGTIK 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  89 AWECDTLFCKYQLPAPPESssilykVFAVT--RDGRILAAGGKSNHLHLWCLEARQLFRiiQMPTKVRAIRHLEFLPDsf 166
Cdd:cd00200   161 LWDLRTGKCVATLTGHTGE------VNSVAfsPDGEKLLSSSSDGTIKLWDLSTGKCLG--TLRGHENGVNSVAFSPD-- 230

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387845346 167 dagsNQVLGVLSQDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYIASIMENGSLNIYS 229
Cdd:cd00200   231 ----GYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
 357-500 1.57e-08

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: 54.95  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 357 LQKKYPIKSRKLLRVLQRTLSALAHWSVIFSDTPYLPLLAFPFVkLFQNNQLICFEVIATLIINwcQHWFEYFPN--PPI 434
Cdd:pfam00566  20 FPHSFFFDNGPGQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLL-LVYLDEEDAFWCFVSLLEN--YLLRDFYTPdfPGL 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387845346 435 NILSMI-ENVLAFHDKELLQHFIDHDITSQLYAWPLLETVFSEVLTREEWLKLFDNIFSNHPSFLLM 500
Cdd:pfam00566  97 KRDLYVfEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVLF 163
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 585-749 7.69e-08

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: 56.29  E-value: 7.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 585 QERERIRNdELDYLRERQTVE-DMQAKVDQQRVEDEAWYQKQE------LLRKAEETRREM--LLQEEEKMIQQRQRLAA 655
Cdd:pfam17380 389 QKNERVRQ-ELEAARKVKILEeERQRKIQQQKVEMEQIRAEQEearqreVRRLEEERAREMerVRLEEQERQQQVERLRQ 467

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 656 VKRELKVKEMHLQDAARRRFLKLQQD----QQEMELRR---LDDEIGR----KNLTENQEALAKE-MRADADAYRRK-VD 722
Cdd:pfam17380 468 QEEERKRKKLELEKEKRDRKRAEEQRrkilEKELEERKqamIEEERKRklleKEMEERQKAIYEEeRRREAEEERRKqQE 547

                         170       180
                  ....*....|....*....|....*....
gi 1387845346 723 LEE--HMFHKLIEAGETQSQKTQKWKEAE 749
Cdd:pfam17380 548 MEErrRIQEQMRKATEERSRLEAMERERE 576
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 583-780 1.24e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 1.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 583 QTQERERIRNDELDYL-----RERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVK 657
Cdd:COG1196   285 EAQAEEYELLAELARLeqdiaRLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 658 RELKVKEMHLQDAARRRF-------------LKLQQDQQEMELRRLDDEIGRKNLTENQEALAKEMRADADAYRRKVDLE 724
Cdd:COG1196   365 EALLEAEAELAEAEEELEelaeellealraaAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1387845346 725 EHMFHKLIEAGETQSQKTQKWKEAEGKEFRLRSA---KKASALSDASRKWFLKQEINAA 780
Cdd:COG1196   445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAAlaeLLEELAEAAARLLLLLEAEADY 503
PTZ00121 PTZ00121
MAEBL; Provisional
 588-799 7.67e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 7.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  588 ERIRNDELDYLRERQTVEDMQaKVDQQRVEDE---AWYQKQELLRKAEETRRE--MLLQEEEKMIQQRQRLAAVKRELKV 662
Cdd:PTZ00121  1544 EKKKADELKKAEELKKAEEKK-KAEEAKKAEEdknMALRKAEEAKKAEEARIEevMKLYEEEKKMKAEEAKKAEEAKIKA 1622

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  663 KEMHLQDAARRRFLKLQQDQQEmELRRLDDEigRKNLTENQEALAKEMRADADAYRRKVDL--EEHMFHKLIEAGETQSQ 740
Cdd:PTZ00121  1623 EELKKAEEEKKKVEQLKKKEAE-EKKKAEEL--KKAEEENKIKAAEEAKKAEEDKKKAEEAkkAEEDEKKAAEALKKEAE 1699

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1387845346  741 KTQKWKEAEGKEfrLRSAKKASALSDASRKWFLKQEiNAAVEHAENPCHKEEPRFQNEQ 799
Cdd:PTZ00121  1700 EAKKAEELKKKE--AEEKKKAEELKKAEEENKIKAE-EAKKEAEEDKKKAEEAKKDEEE 1755
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 585-830 8.03e-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: 49.68  E-value: 8.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  585 QERERIRN--DELDYLRERQTVEDMQAKVDQQRVEDEAWYQK----------QELLRKAEETRREMllQEEEKMIQQRQR 652
Cdd:TIGR02169  695 SELRRIENrlDELSQELSDASRKIGEIEKEIEQLEQEEEKLKerleeleedlSSLEQEIENVKSEL--KELEARIEELEE 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  653 -LAAVKRELKVKEMHLQDA------ARRRFLKLQQDQQEMELRRLDDEIGRKNLtenQEALAKEMRADADAYRRKVDLEE 725
Cdd:TIGR02169  773 dLHKLEEALNDLEARLSHSripeiqAELSKLEEEVSRIEARLREIEQKLNRLTL---EKEYLEKEIQELQEQRIDLKEQI 849

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  726 HMFHKLIEAGETQSQKT-QKWKEAEGKEFRLRSAKKA---------SALSDASRKwflKQEINAAVEHAENPCH--KEEP 793
Cdd:TIGR02169  850 KSIEKEIENLNGKKEELeEELEELEAALRDLESRLGDlkkerdeleAQLRELERK---IEELEAQIEKKRKRLSelKAKL 926

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1387845346  794 RFQNEQDSSCLPRTSQLNDSSEMDPST-QISLNRRAVE 830
Cdd:TIGR02169  927 EALEEELSEIEDPKGEDEEIPEEELSLeDVQAELQRVE 964
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 10-48 6.85e-05

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 40.76  E-value: 6.85e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1387845346   10 TKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWD 48
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDgTIKLWD 40
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 396-504 1.07e-04

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: 44.22  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  396 AFP-FVKLFQNNQLIcFEVIATLIINWCQHWFEYFpnppinilsmienvLAFHDKELLQHFIDHDITSQLYAWPLLETVF 474
Cdd:smart00164 112 AFWcLVKLMERYGPN-FYLPDMSGLQLDLLQLDRL--------------VKEYDPDLYKHLKDLGITPSLYALRWFLTLF 176

                           90       100       110
                   ....*....|....*....|....*....|
gi 1387845346  475 SEVLTREEWLKLFDNIFSNHPSFLLMTVVA 504
Cdd:smart00164 177 ARELPLEIVLRIWDVLFAEGSDFLFRVALA 206
WD40 pfam00400
WD domain, G-beta repeat;
11-48 1.22e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 37.32  E-value: 1.22e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1387845346  11 KELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWD 48
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDgTVKVWD 39
COG5210 COG5210
GTPase-activating protein [General function prediction only];
437-553 3.62e-03

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 40.94  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 437 LSMIENVLAFHDKELLQHFIDHDITSQLYAWPLLETVFSEVLTREEWLKLFDNIFSNHPSFLLMTVVAYNICSRTPLLSC 516
Cdd:COG5210   350 LKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKL 429

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1387845346 517 NLKDDFEFFFHHRNNLDINVVIRQVYHLMETTPTDIH 553
Cdd:COG5210   430 DSDELLDLLLKQLFLHSGKEAWSSILKFRHGTDRDIL 466
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 608-690 5.40e-03

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.87  E-value: 5.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 608 QAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKEMHLQDAARRRFLKLQQDQQEMEL 687
Cdd:cd16269   208 EAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEI 287


                  ...
gi 1387845346 688 RRL 690
Cdd:cd16269   288 RSL 290
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 656-846 5.60e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 40.41  E-value: 5.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 656 VKRE--LKVKEMHLQDAARR-RFLKLQQDQQEMELRRLDDEigRKNLTENQEALAKemradadayrrkvdleehmfhKLI 732
Cdd:pfam10168 543 VFREeyLKKHDLAREEIQKRvKLLKLQKEQQLQELQSLEEE--RKSLSERAEKLAE---------------------KYE 599

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 733 EAGETQSQKTQKWKEAegkefrLRSAK-KASALSDASRKwfLKQE---INAAVEHAENpCHKEEPRFQNEQdssclprTS 808
Cdd:pfam10168 600 EIKDKQEKLMRRCKKV------LQRLNsQLPVLSDAERE--MKKEletINEQLKHLAN-AIKQAKKKMNYQ-------RY 663

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1387845346 809 QLNDSSEMDPSTQISLN---RRAV-----EWDTTGQNLIKKVRNLR 846
Cdd:pfam10168 664 QIAKSQSIRKKSSLSLSekqRKTIkeilkQLGSEIDELIKQVKDIN 709
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
10-235 4.39e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 102.68  E-value: 4.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  10 TKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 88
Cdd:COG2319   151 TGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDgTVRLWDLATGKLLRTLTGHTG-AVRSVAFSPDGKLLASGSADGTVR 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  89 AWECDTLFCKYQLPAPPES-SSIlykvfAVTRDGRILAAGGKSNHLHLWCLEARQLFRIIQMPTkvRAIRHLEFLPDSfd 167
Cdd:COG2319   230 LWDLATGKLLRTLTGHSGSvRSV-----AFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHS--GGVNSVAFSPDG-- 300

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387845346 168 agsnQVLGVLSQDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYIASIMENGSLNIYSVQALTQ 235
Cdd:COG2319   301 ----KLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364
WD40 COG2319
WD40 repeat [General function prediction only];
7-231 9.33e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 101.53  E-value: 9.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346   7 ETVTKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNiRQSVGIQKVFFLPLSNTILSCFKDN 85
Cdd:COG2319   106 DLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADgTVRLWDLATGKLLRTLT-GHSGAVTSVAFSPDGKLLASGSDDG 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  86 SIFAWECDTLFCKYQLPAPPESSSILykvfAVTRDGRILAAGGKSNHLHLWCLEARQLFRIIQMPTkvRAIRHLEFLPDS 165
Cdd:COG2319   185 TVRLWDLATGKLLRTLTGHTGAVRSV----AFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHS--GSVRSVAFSPDG 258

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387845346 166 fdagsnQVLGVLSQDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYIASIMENGSLNIYSVQ 231
Cdd:COG2319   259 ------RLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLA 318
WD40 COG2319
WD40 repeat [General function prediction only];
10-231 1.44e-22

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 101.14  E-value: 1.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  10 TKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 88
Cdd:COG2319   193 TGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADgTVRLWDLATGKLLRTLTGHSG-SVRSVAFSPDGRLLASGSADGTVR 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  89 AWECDTLFCKYQLPAPPES-SSIlykvfAVTRDGRILAAGGKSNHLHLWCLEARQLFRIIQMPTkvRAIRHLEFLPDsfd 167
Cdd:COG2319   272 LWDLATGELLRTLTGHSGGvNSV-----AFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHT--GAVRSVAFSPD--- 341

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387845346 168 agsNQVLGVLSQDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYIASIMENGSLNIYSVQ 231
Cdd:COG2319   342 ---GKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
10-231 3.29e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 96.90  E-value: 3.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  10 TKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 88
Cdd:COG2319    67 AGALLATLLGHTAAVLSVAFSPDGRLLASASADgTVRLWDLATGLLLRTLTGHTG-AVRSVAFSPDGKTLASGSADGTVR 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  89 AWECDTLFCKYQLPAPPES-SSIlykvfAVTRDGRILAAGGKSNHLHLWCLEARQLFRIIQMPTkvRAIRHLEFLPDSfd 167
Cdd:COG2319   146 LWDLATGKLLRTLTGHSGAvTSV-----AFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHT--GAVRSVAFSPDG-- 216

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387845346 168 agsnQVLGVLSQDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYIASIMENGSLNIYSVQ 231
Cdd:COG2319   217 ----KLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA 276
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 10-229 1.36e-19

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 90.09  E-value: 1.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  10 TKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 88
Cdd:cd00200    82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDkTIKVWDVETGKCLTTLRGHTD-WVNSVAFSPDGTFVASSSQDGTIK 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  89 AWECDTLFCKYQLPAPPESssilykVFAVT--RDGRILAAGGKSNHLHLWCLEARQLFRiiQMPTKVRAIRHLEFLPDsf 166
Cdd:cd00200   161 LWDLRTGKCVATLTGHTGE------VNSVAfsPDGEKLLSSSSDGTIKLWDLSTGKCLG--TLRGHENGVNSVAFSPD-- 230

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387845346 167 dagsNQVLGVLSQDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYIASIMENGSLNIYS 229
Cdd:cd00200   231 ----GYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 18-232 4.83e-17

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 82.38  E-value: 4.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  18 RGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIrQSVGIQKVFFLPLSNTILSCFKDNSIFAWECDTLF 96
Cdd:cd00200     6 KGHTGGVTCVAFSPDGKLLATGSGDgTIKVWDLETGELLRTLKG-HTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  97 CKYQLPAppESSSILYkvFAVTRDGRILAAGGKSNHLHLWCLEARQLfrIIQMPTKVRAIRHLEFLPDsfdagsNQVLGV 176
Cdd:cd00200    85 CVRTLTG--HTSYVSS--VAFSPDGRILSSSSRDKTIKVWDVETGKC--LTTLRGHTDWVNSVAFSPD------GTFVAS 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1387845346 177 LSQDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYIASIMENGSLNIYSVQA 232
Cdd:cd00200   153 SSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLST 208
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 19-231 9.37e-16

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 78.53  E-value: 9.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  19 GHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLFC 97
Cdd:cd00200    49 GHTGPVRDVAASADGTYLASGSSDkTIRLWDLETGECVRTLTGHTS-YVSSVAFSPDGRILSSSSRDKTIKVWDVETGKC 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  98 KYQLPAPPESssilYKVFAVTRDGRILAAGGKSNHLHLWCLEARQLFRIIQMPTKvrAIRHLEFLPD--SFDAGSNqvlg 175
Cdd:cd00200   128 LTTLRGHTDW----VNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTG--EVNSVAFSPDgeKLLSSSS---- 197

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1387845346 176 vlsqDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYIASIMENGSLNIYSVQ 231
Cdd:cd00200   198 ----DGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLR 249
WD40 COG2319
WD40 repeat [General function prediction only];
18-231 7.03e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 77.64  E-value: 7.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  18 RGHESSVFSISVHASGKYAITTSSDTAQLWDLDTFQRKRKLNIRQSVGIQKVFFLPLSNTILSCFKDNSIFAWECDTLFC 97
Cdd:COG2319    33 LGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  98 KYQLPAPPES-SSIlykvfAVTRDGRILAAGGKSNHLHLWCLEARQLFRIIQMPTkvRAIRHLEFLPDSfdagsnQVLGV 176
Cdd:COG2319   113 LRTLTGHTGAvRSV-----AFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHS--GAVTSVAFSPDG------KLLAS 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1387845346 177 LSQDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYIASIMENGSLNIYSVQ 231
Cdd:COG2319   180 GSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLA 234
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 7-185 1.49e-14

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 75.06  E-value: 1.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346   7 ETVTKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDN 85
Cdd:cd00200   121 DVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDgTIKLWDLRTGKCVATLTGHTG-EVNSVAFSPDGEKLLSSSSDG 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  86 SIFAWECDTLFCKYQLPAPPESSSILykvfAVTRDGRILAAGGKSNHLHLWCLEARQLFRIIQMPTK-VRAIRhleFLPD 164
Cdd:cd00200   200 TIKLWDLSTGKCLGTLRGHENGVNSV----AFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNsVTSLA---WSPD 272

                         170       180
                  ....*....|....*....|.
gi 1387845346 165 SfdagsnQVLGVLSQDGIMRF 185
Cdd:cd00200   273 G------KRLASGSADGTIRI 287
RabGAP-TBC pfam00566
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ...
 357-500 1.57e-08

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: 54.95  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 357 LQKKYPIKSRKLLRVLQRTLSALAHWSVIFSDTPYLPLLAFPFVkLFQNNQLICFEVIATLIINwcQHWFEYFPN--PPI 434
Cdd:pfam00566  20 FPHSFFFDNGPGQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLL-LVYLDEEDAFWCFVSLLEN--YLLRDFYTPdfPGL 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387845346 435 NILSMI-ENVLAFHDKELLQHFIDHDITSQLYAWPLLETVFSEVLTREEWLKLFDNIFSNHPSFLLM 500
Cdd:pfam00566  97 KRDLYVfEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVLF 163
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 585-749 7.69e-08

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: 56.29  E-value: 7.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 585 QERERIRNdELDYLRERQTVE-DMQAKVDQQRVEDEAWYQKQE------LLRKAEETRREM--LLQEEEKMIQQRQRLAA 655
Cdd:pfam17380 389 QKNERVRQ-ELEAARKVKILEeERQRKIQQQKVEMEQIRAEQEearqreVRRLEEERAREMerVRLEEQERQQQVERLRQ 467

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 656 VKRELKVKEMHLQDAARRRFLKLQQD----QQEMELRR---LDDEIGR----KNLTENQEALAKE-MRADADAYRRK-VD 722
Cdd:pfam17380 468 QEEERKRKKLELEKEKRDRKRAEEQRrkilEKELEERKqamIEEERKRklleKEMEERQKAIYEEeRRREAEEERRKqQE 547

                         170       180
                  ....*....|....*....|....*....
gi 1387845346 723 LEE--HMFHKLIEAGETQSQKTQKWKEAE 749
Cdd:pfam17380 548 MEErrRIQEQMRKATEERSRLEAMERERE 576
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 583-780 1.24e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 1.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 583 QTQERERIRNDELDYL-----RERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVK 657
Cdd:COG1196   285 EAQAEEYELLAELARLeqdiaRLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 658 RELKVKEMHLQDAARRRF-------------LKLQQDQQEMELRRLDDEIGRKNLTENQEALAKEMRADADAYRRKVDLE 724
Cdd:COG1196   365 EALLEAEAELAEAEEELEelaeellealraaAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1387845346 725 EHMFHKLIEAGETQSQKTQKWKEAEGKEFRLRSA---KKASALSDASRKWFLKQEINAA 780
Cdd:COG1196   445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAAlaeLLEELAEAAARLLLLLEAEADY 503
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 574-856 2.34e-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: 54.74  E-value: 2.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 574 QYPKFIVDYQTQER------ERIRNDELDYLRE---RQTVEDM----QAKVDQQRV-----EDEAWYQKQELLR-KAEET 634
Cdd:pfam17380 279 QHQKAVSERQQQEKfekmeqERLRQEKEEKAREverRRKLEEAekarQAEMDRQAAiyaeqERMAMERERELERiRQEER 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 635 RREM--LLQEEEKM----IQQRQRLAA--------VKRELK-VKEMHLQDAARRRflKLQQDQQEMELRRLDDEIGRK-N 698
Cdd:pfam17380 359 KRELerIRQEEIAMeisrMRELERLQMerqqknerVRQELEaARKVKILEEERQR--KIQQQKVEMEQIRAEQEEARQrE 436

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 699 LTENQEALAKEMradadayrRKVDLEEHMFHKLIEAGETQSQKTQKWKEAEGKEFRLRS---------------AKKASA 763
Cdd:pfam17380 437 VRRLEEERAREM--------ERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKraeeqrrkilekeleERKQAM 508

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 764 LSDASRKWFLKQEInaavEHAENPCHKEEPRFQNEQDSsclpRTSQlndssEMDPSTQIslnrravewdttgQNLIKKVR 843
Cdd:pfam17380 509 IEEERKRKLLEKEM----EERQKAIYEEERRREAEEER----RKQQ-----EMEERRRI-------------QEQMRKAT 562

                         330
                  ....*....|...
gi 1387845346 844 NLRQRLTARARHR 856
Cdd:pfam17380 563 EERSRLEAMERER 575
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
581-744 4.35e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.77  E-value: 4.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  581 DYQTQERERIRNDELDYLRERQTVEDMQAKVD--QQRVED-EAWYQKQELLRKAEETRREMLLQEEEKMIQQR-----QR 652
Cdd:COG4913    260 LAERYAAARERLAELEYLRAALRLWFAQRRLEllEAELEElRAELARLEAELERLEARLDALREELDELEAQIrgnggDR 339

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  653 LAAVKRELKVKEMHLQDAARRRfLKLQQDQQEMELRRLDDEigrKNLTENQEAlAKEMRADADAYRRKVDLEEHMFHKLI 732
Cdd:COG4913    340 LEQLEREIERLERELEERERRR-ARLEALLAALGLPLPASA---EEFAALRAE-AAALLEALEEELEALEEALAEAEAAL 414

                          170
                   ....*....|..
gi 1387845346  733 EAGETQSQKTQK 744
Cdd:COG4913    415 RDLRRELRELEA 426
PTZ00121 PTZ00121
MAEBL; Provisional
 588-799 7.67e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 7.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  588 ERIRNDELDYLRERQTVEDMQaKVDQQRVEDE---AWYQKQELLRKAEETRRE--MLLQEEEKMIQQRQRLAAVKRELKV 662
Cdd:PTZ00121  1544 EKKKADELKKAEELKKAEEKK-KAEEAKKAEEdknMALRKAEEAKKAEEARIEevMKLYEEEKKMKAEEAKKAEEAKIKA 1622

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  663 KEMHLQDAARRRFLKLQQDQQEmELRRLDDEigRKNLTENQEALAKEMRADADAYRRKVDL--EEHMFHKLIEAGETQSQ 740
Cdd:PTZ00121  1623 EELKKAEEEKKKVEQLKKKEAE-EKKKAEEL--KKAEEENKIKAAEEAKKAEEDKKKAEEAkkAEEDEKKAAEALKKEAE 1699

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1387845346  741 KTQKWKEAEGKEfrLRSAKKASALSDASRKWFLKQEiNAAVEHAENPCHKEEPRFQNEQ 799
Cdd:PTZ00121  1700 EAKKAEELKKKE--AEEKKKAEELKKAEEENKIKAE-EAKKEAEEDKKKAEEAKKDEEE 1755
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 584-785 2.71e-06

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 50.58  E-value: 2.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 584 TQERERIRNDELDYLR---ERQTVEDMQAKVDQQRVEDEawyqkQELLRKAEETRreMLLQEEEKMIQQRQRLAAVKREL 660
Cdd:PRK09510   61 VEQYNRQQQQQKSAKRaeeQRKKKEQQQAEELQQKQAAE-----QERLKQLEKER--LAAQEQKKQAEEAAKQAALKQKQ 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 661 KVKEMHLQDAARrrflKLQQDQQEMEL----RRLDDEIGRKNLTENQEALAKEMRADADAYRRKVDLEEHMFHKLIEAGE 736
Cdd:PRK09510  134 AEEAAAKAAAAA----KAKAEAEAKRAaaaaKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKK 209

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1387845346 737 TQSQKTQKWKEAEGKEFRLRSAKKASALSDASRKWFLKQEINAAVEHAE 785
Cdd:PRK09510  210 KAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
PTZ00121 PTZ00121
MAEBL; Provisional
 583-799 3.58e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 3.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  583 QTQERERIRNDELDY-LRERQTVEDMQAKVDQQRVEDEAwYQKQELLRKAEETRREmllQEEEKMIQQRQRLAAVKR--- 658
Cdd:PTZ00121  1411 KKAAAAKKKADEAKKkAEEKKKADEAKKKAEEAKKADEA-KKKAEEAKKAEEAKKK---AEEAKKADEAKKKAEEAKkad 1486

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  659 ELKVKEMHLQDAARRRFLKLQQDQQEMELRRLDDEIGRKNLTENQEALAKEMRADADAYRRKVDLEEhmfHKLIEAGETQ 738
Cdd:PTZ00121  1487 EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK---AEELKKAEEK 1563

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387845346  739 SQKTQKWKEAEGKEFRLRSAKKASALSDASRKWFLKQEINAAVEHAENPCHKEEPRFQNEQ 799
Cdd:PTZ00121  1564 KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 580-771 4.09e-06

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: 50.34  E-value: 4.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 580 VDYQTQERE---RIRNDELDylRERQTVEDMQakVDQQRVEDEAWYQKQellRKAEETRRemllQEEEKMIQQRQRLAAV 656
Cdd:pfam15709 350 VERKRREQEeqrRLQQEQLE--RAEKMREELE--LEQQRRFEEIRLRKQ---RLEEERQR----QEEEERKQRLQLQAAQ 418

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 657 KRELKvkemhLQDAARRRFLKLQQDQQEMELRRLDDEIGRKNltENQEALAKEmradadaYRRKVDLEEHmfhkliEAGE 736
Cdd:pfam15709 419 ERARQ-----QQEEFRRKLQELQRKKQQEEAERAEAEKQRQK--ELEMQLAEE-------QKRLMEMAEE------ERLE 478

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1387845346 737 TQSQKtqkwKEAEGK-----EFRLRSAKKASALSDASRKW 771
Cdd:pfam15709 479 YQRQK----QEAEEKarleaEERRQKEEEAARLALEEAMK 514
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 585-689 4.23e-06

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 47.34  E-value: 4.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 585 QERERIRNDEldylRERQTVEDMQAKVDQQRVEDEAWYQKQE---------LLRKAEETRREMLLQE-EEKMIQQRQRLA 654
Cdd:pfam05672  30 EEQERLEKEE----EERLRKEELRRRAEEERARREEEARRLEeerrreeeeRQRKAEEEAEEREQREqEEQERLQKQKEE 105

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1387845346 655 AvkrELKVKEmhlqDAARRRF---LKLQQDQQEMELRR 689
Cdd:pfam05672 106 A---EAKARE----EAERQRQereKIMQQEEQERLERK 136
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 585-830 8.03e-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: 49.68  E-value: 8.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  585 QERERIRN--DELDYLRERQTVEDMQAKVDQQRVEDEAWYQK----------QELLRKAEETRREMllQEEEKMIQQRQR 652
Cdd:TIGR02169  695 SELRRIENrlDELSQELSDASRKIGEIEKEIEQLEQEEEKLKerleeleedlSSLEQEIENVKSEL--KELEARIEELEE 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  653 -LAAVKRELKVKEMHLQDA------ARRRFLKLQQDQQEMELRRLDDEIGRKNLtenQEALAKEMRADADAYRRKVDLEE 725
Cdd:TIGR02169  773 dLHKLEEALNDLEARLSHSripeiqAELSKLEEEVSRIEARLREIEQKLNRLTL---EKEYLEKEIQELQEQRIDLKEQI 849

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  726 HMFHKLIEAGETQSQKT-QKWKEAEGKEFRLRSAKKA---------SALSDASRKwflKQEINAAVEHAENPCH--KEEP 793
Cdd:TIGR02169  850 KSIEKEIENLNGKKEELeEELEELEAALRDLESRLGDlkkerdeleAQLRELERK---IEELEAQIEKKRKRLSelKAKL 926

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1387845346  794 RFQNEQDSSCLPRTSQLNDSSEMDPST-QISLNRRAVE 830
Cdd:TIGR02169  927 EALEEELSEIEDPKGEDEEIPEEELSLeDVQAELQRVE 964
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 586-709 8.29e-06

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: 49.18  E-value: 8.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 586 ERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRlaavkrelkvkem 665
Cdd:pfam15709 417 AQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQK------------- 483

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1387845346 666 hlQDAARRRflklqqdQQEMELRRLDDEIGRKNLTENQEALAKE 709
Cdd:pfam15709 484 --QEAEEKA-------RLEAEERRQKEEEAARLALEEAMKQAQE 518
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 583-767 1.29e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 583 QTQERERIRNDELDYLRERQTVEdMQAKVDQQRVEDEAwyQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKV 662
Cdd:COG1196   279 LELELEEAQAEEYELLAELARLE-QDIARLEERRRELE--ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 663 KEMHLQDAARRRfLKLQQDQQEMELRRLDDEIGRKNLTENQEALAKEMRADADAYRRKVDLEEHMFHKLIEAGETQSQKT 742
Cdd:COG1196   356 AEAELAEAEEAL-LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434

                         170       180
                  ....*....|....*....|....*
gi 1387845346 743 QKwKEAEGKEFRLRSAKKASALSDA 767
Cdd:COG1196   435 EE-EEEEEEALEEAAEEEAELEEEE 458
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 544-825 2.35e-05

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 48.18  E-value: 2.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 544 LMETTPTDIHpDSMLNVFVALTKGQYpvfnqYPKFIVDYQTQ-ERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWY 622
Cdd:pfam05483 444 LLQAREKEIH-DLEIQLTAIKTSEEH-----YLKEVEDLKTElEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKK 517

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 623 QKQELL--RKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKemhlQDAARRRFLKLQQDQQEMELRRLDDEIGRKNLT 700
Cdd:pfam05483 518 HQEDIIncKKQEERMLKQIENLEEKEMNLRDELESVREEFIQK----GDEVKCKLDKSEENARSIEYEVLKKEKQMKILE 593

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 701 ----------ENQEALAKEMRADADAYRRKVDLE-------EHMFHKLIEAGETQSQKTQK-----WKEAEGK----EFR 754
Cdd:pfam05483 594 nkcnnlkkqiENKNKNIEELHQENKALKKKGSAEnkqlnayEIKVNKLELELASAKQKFEEiidnyQKEIEDKkiseEKL 673

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387845346 755 LRSAKKASALSDASRKwfLKQEINAAVEH--AENPCHKEEPRFQ-----NEQDSSCLPRTSQLNDSSEMDPSTQISLN 825
Cdd:pfam05483 674 LEEVEKAKAIADEAVK--LQKEIDKRCQHkiAEMVALMEKHKHQydkiiEERDSELGLYKNKEQEQSSAKAALEIELS 749
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
583-787 3.12e-05

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 47.34  E-value: 3.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 583 QTQERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQE---LLRKAEETRREMLLQEEekmiQQRQRLAAVKRE 659
Cdd:COG3064    11 EAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEeeaREAKAEAEQRAAELAAE----AAKKLAEAEKAA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 660 LKVKEMHLQDAARrrflKLQQDQQEMELRRLDDEIGRKNLTENQEALAKEMRADADAYRRKVDLEEHMFHKLIEAGETQS 739
Cdd:COG3064    87 AEAEKKAAAEKAK----AAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAA 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1387845346 740 QKTQKWKEAEGKEFRLRSAKKASALSDASRKWFLKQEINAAVEHAENP 787
Cdd:COG3064   163 AAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAA 210
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 10-48 6.85e-05

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 40.76  E-value: 6.85e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1387845346   10 TKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWD 48
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDgTIKLWD 40
PTZ00121 PTZ00121
MAEBL; Provisional
 588-799 8.40e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 8.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  588 ERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKEMHL 667
Cdd:PTZ00121  1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  668 QDAARRRFLKLQQD--QQEMELRRLDDEIGRKnlTENQEALAKEMRADADAyRRKVDLEEHMFHKLIEAGETQSQKTQKW 745
Cdd:PTZ00121  1368 AAEKKKEEAKKKADaaKKKAEEKKKADEAKKK--AEEDKKKADELKKAAAA-KKKADEAKKKAEEKKKADEAKKKAEEAK 1444

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1387845346  746 KEAEGKefrlRSAKKASALSDASRKWFLKQEINAAVEHAENPCHKEEPRFQNEQ 799
Cdd:PTZ00121  1445 KADEAK----KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEE 1494
TBC smart00164
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ...
 396-504 1.07e-04

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: 44.22  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  396 AFP-FVKLFQNNQLIcFEVIATLIINWCQHWFEYFpnppinilsmienvLAFHDKELLQHFIDHDITSQLYAWPLLETVF 474
Cdd:smart00164 112 AFWcLVKLMERYGPN-FYLPDMSGLQLDLLQLDRL--------------VKEYDPDLYKHLKDLGITPSLYALRWFLTLF 176

                           90       100       110
                   ....*....|....*....|....*....|
gi 1387845346  475 SEVLTREEWLKLFDNIFSNHPSFLLMTVVA 504
Cdd:smart00164 177 ARELPLEIVLRIWDVLFAEGSDFLFRVALA 206
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 583-752 1.11e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 45.29  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 583 QTQERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQ-------RQRLAA 655
Cdd:pfam13868 133 DEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEkaerdelRAKLYQ 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 656 VKRELKVKEMHLQDAARRRFLKL-----QQDQQEMELRRLDDEIGR------KNLTENQEALAKEMRADADAYRRKVDLE 724
Cdd:pfam13868 213 EEQERKERQKEREEAEKKARQRQelqqaREEQIELKERRLAEEAEReeeefeRMLRKQAEDEEIEQEEAEKRRMKRLEHR 292

                         170       180
                  ....*....|....*....|....*...
gi 1387845346 725 EHMfHKLIEAGETQSQKTQKWKEAEGKE 752
Cdd:pfam13868 293 REL-EKQIEEREEQRAAEREEELEEGER 319
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 585-748 1.37e-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: 45.50  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 585 QERERIRNDELDYLRERQTVEDMQAKVDQQRVED--EAWYQKQELlRKAEETRREMLLQEEEKMIQQRQRLAAVKRElKV 662
Cdd:pfam17380 491 EQRRKILEKELEERKQAMIEEERKRKLLEKEMEErqKAIYEEERR-REAEEERRKQQEMEERRRIQEQMRKATEERS-RL 568

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 663 KEMHLQDAARRRFLKLQQDQQEMElrrlddeigrknLTENQEALAKEMRADADAYRRKvDLEEHMFHKLIEAGETQSQKT 742
Cdd:pfam17380 569 EAMEREREMMRQIVESEKARAEYE------------ATTPITTIKPIYRPRISEYQPP-DVESHMIRFTTQSPEWATPSP 635


                  ....*.
gi 1387845346 743 QKWKEA 748
Cdd:pfam17380 636 ATWNPE 641
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
584-785 1.64e-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: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 584 TQERERIRNDeldylRERQTvEDMQAKVDQQRVEDEAwYQKQEL--LRKAEETRREMLLQEEEKMIQQRQR--------L 653
Cdd:COG2268   198 IRDARIAEAE-----AERET-EIAIAQANREAEEAEL-EQEREIetARIAEAEAELAKKKAEERREAETARaeaeaayeI 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 654 AAVKRELKVkEMHLQDAARRRFLKLQQDQQEMELRRLDDEIgrknltenqealakEMRADADAYRRKVDleehmfhkliE 733
Cdd:COG2268   271 AEANAEREV-QRQLEIAEREREIELQEKEAEREEAELEADV--------------RKPAEAEKQAAEAE----------A 325

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1387845346 734 AGETQSQKTQKWKEAEGKEfrlrsaKKASALSDASRKWFLKQEINAAVEHAE 785
Cdd:COG2268   326 EAEAEAIRAKGLAEAEGKR------ALAEAWNKLGDAAILLMLIEKLPEIAE 371
PTZ00121 PTZ00121
MAEBL; Provisional
 585-761 2.40e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 2.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  585 QERERIRNDELdylrerQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRlaavKRELKVKE 664
Cdd:PTZ00121  1615 AEEAKIKAEEL------KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK----AEEAKKAE 1684

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  665 MHLQDAARRRFLKLQQDQQEMELRRLDDEIGRKnlTENQEALAKEMRADADAYRRKVDLEEHMFHKLIEAGETQSQKTQK 744
Cdd:PTZ00121  1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK--AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHL 1762

                          170
                   ....*....|....*..
gi 1387845346  745 WKEAEGKEFRLRSAKKA 761
Cdd:PTZ00121  1763 KKEEEKKAEEIRKEKEA 1779
PTZ00121 PTZ00121
MAEBL; Provisional
 587-815 2.68e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 2.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  587 RERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREmllQEEEKMIQQRQRLAAVKR---ELKVK 663
Cdd:PTZ00121  1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKA---AAAKKKADEAKKKAEEKKkadEAKKK 1439

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  664 --EMHLQDAARRRF---LKLQQDQQEMELRRLDDEIGRK----NLTENQEALAKEMRADADAYRRKVDlEEHMFHKLIEA 734
Cdd:PTZ00121  1440 aeEAKKADEAKKKAeeaKKAEEAKKKAEEAKKADEAKKKaeeaKKADEAKKKAEEAKKKADEAKKAAE-AKKKADEAKKA 1518

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  735 GEtqSQKTQKWKEAEGKEfRLRSAKKASALSDAsrkwflkQEINAA--VEHAENPCHKEEPRFQNEQDSSCLPRTSQLND 812
Cdd:PTZ00121  1519 EE--AKKADEAKKAEEAK-KADEAKKAEEKKKA-------DELKKAeeLKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK 1588


                   ...
gi 1387845346  813 SSE 815
Cdd:PTZ00121  1589 AEE 1591
PTZ00121 PTZ00121
MAEBL; Provisional
 591-800 3.09e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 3.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  591 RNDELDYLRERQTVEDMQAKVDQQRVEDEawyQKQELLRKAEETRR---------------------------EMLLQEE 643
Cdd:PTZ00121  1183 KAEEVRKAEELRKAEDARKAEAARKAEEE---RKAEEARKAEDAKKaeavkkaeeakkdaeeakkaeeernneEIRKFEE 1259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  644 EKMIQQRQRLAAVKRELKVKEMHLQDAARRRflKLQQDQQEMELRRLDDeiGRKNLTENQEalAKEMRADADAYRRKVDL 723
Cdd:PTZ00121  1260 ARMAHFARRQAAIKAEEARKADELKKAEEKK--KADEAKKAEEKKKADE--AKKKAEEAKK--ADEAKKKAEEAKKKADA 1333

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387845346  724 EEHmfhkliEAGETQSQKTQKWKEAEGKEFRLRSAKKaSALSDASRKWFLKQEINAAVEHAENPCHKEEPRFQNEQD 800
Cdd:PTZ00121  1334 AKK------KAEEAKKAAEAAKAEAEAAADEAEAAEE-KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEED 1403
WD40 COG2319
WD40 repeat [General function prediction only];
10-51 3.52e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 43.75  E-value: 3.52e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1387845346  10 TKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWDLDT 51
Cdd:COG2319   361 TGELLRTLTGHTGAVTSVAFSPDGRTLASGSADgTVRLWDLAT 403
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
588-779 5.11e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 5.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  588 ERIRN--DELDYLRE-RQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREM----LLQEEEKMIQQRQRLAAVKREL 660
Cdd:COG4913    225 EAADAlvEHFDDLERaHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRaalrLWFAQRRLELLEAELEELRAEL 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  661 KVKEMHL------QDAARRRFLKLQQDQQEMELRRLDD---EIGRKNLT-ENQEALAKEMRADADAYRRKVDLEEHMFHK 730
Cdd:COG4913    305 ARLEAELerlearLDALREELDELEAQIRGNGGDRLEQlerEIERLERElEERERRRARLEALLAALGLPLPASAEEFAA 384

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1387845346  731 LI-EAGETQSQKTQKWKEAEGKEFRLRSAKkaSALSDASRKwfLKQEINA 779
Cdd:COG4913    385 LRaEAAALLEALEEELEALEEALAEAEAAL--RDLRRELRE--LEAEIAS 430
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 602-780 5.24e-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: 43.30  E-value: 5.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 602 QTVEDMQAK-VDQQRVEDEAWYQKQELL--RKAEETRREMLLQEEEKMIQQRQRLAAVKRELKvkemhlQDAARrrflkl 678
Cdd:TIGR02794  33 GGAEIIQAVlVDPGAVAQQANRIQQQKKpaAKKEQERQKKLEQQAEEAEKQRAAEQARQKELE------QRAAA------ 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 679 QQDQQEMELRRLDDEIGRKNLTENQEALAKEMRADADAYRRKvdleehmfhKLIEAGETQSQKTQKWKEA-----EGKEF 753
Cdd:TIGR02794 101 EKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAER---------KAKEEAAKQAEEEAKAKAAaeakkKAEEA 171

                         170       180
                  ....*....|....*....|....*..
gi 1387845346 754 RLRSAKKASALSDASRKwfLKQEINAA 780
Cdd:TIGR02794 172 KKKAEAEAKAKAEAEAK--AKAEEAKA 196
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
 585-720 5.27e-04

ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.


Pssm-ID: 463442 [Multi-domain]  Cd Length: 264  Bit Score: 42.66  E-value: 5.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 585 QERERIR-NDELdyLRERqtvedMQAKVDQQRvedeawYQKQELLRKAEEtrremllqeeekmiqqrqrlaAVKRelkvk 663
Cdd:pfam12037  98 QKQQRAQyQDEL--ARKR-----YQDQLEAQR------RRNEELLRKQEE---------------------SVAK----- 138

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1387845346 664 emhlQDAARRRFLKLQQDQQEMELRRlddEIGRKNLTENQEALAKEMRADADAYRRK 720
Cdd:pfam12037 139 ----QEAMRIQAQRRQTEEHEAELRR---ETERAKAEAEAEARAKEERENEDLNLEQ 188
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 599-725 5.64e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 43.63  E-value: 5.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  599 RERQTVEDMQAKVDQQRVEDEawyQKQELLRKAEETRREMLLQEEEKMI---QQRQRLAAVKRELKVKEMHLQD-----A 670
Cdd:pfam01576  152 KERKLLEERISEFTSNLAEEE---EKAKSLSKLKNKHEAMISDLEERLKkeeKGRQELEKAKRKLEGESTDLQEqiaelQ 228

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387845346  671 ARRRFLKLQQDQQEMELR----RLDDEIGRKN------------LTENQEALAKEMRADADAYRRKVDLEE 725
Cdd:pfam01576  229 AQIAELRAQLAKKEEELQaalaRLEEETAQKNnalkkireleaqISELQEDLESERAARNKAEKQRRDLGE 299
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 585-733 7.65e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.60  E-value: 7.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 585 QERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAwyQKQELLRKAEETRREMLLQEEEKMIQQRQRLAA----VKREL 660
Cdd:pfam13868 193 QEKAQDEKAERDELRAKLYQEEQERKERQKEREEAE--KKARQRQELQQAREEQIELKERRLAEEAEREEEeferMLRKQ 270

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387845346 661 KVKEMHLQDAARRRFLKLQQDQQEMElRRLDDEIGRKNLTENQEALAKEMRADADAYRRKVdLEEHMFHKLIE 733
Cdd:pfam13868 271 AEDEEIEQEEAEKRRMKRLEHRRELE-KQIEEREEQRAAEREEELEEGERLREEEAERRER-IEEERQKKLKE 341
PRK02292 PRK02292
V-type ATP synthase subunit E; Provisional
 604-733 8.85e-04

V-type ATP synthase subunit E; Provisional


Pssm-ID: 235026 [Multi-domain]  Cd Length: 188  Bit Score: 41.14  E-value: 8.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 604 VEDMQ--AKVDQQRVEDEAWYQKQELLRKAEETRREML---LQEEEKMIQQ--RQRLAAVKRELKVKEMhlqdAARRRFL 676
Cdd:PRK02292    7 VEDIRdeARARASEIRAEADEEAEEIIAEAEADAEEILedrEAEAEREIEQlrEQELSSAKLEAKRERL----NARKEVL 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387845346 677 KLQQDQQEMELRRLDDeigrknltENQEALAKEMRADADA-----YRRKVDleEHMFHKLIE 733
Cdd:PRK02292   83 EDVRNQVEDEIASLDG--------DKREELTKSLLDAADAdgvrvYSRKDD--EDLVKSLLS 134
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 586-785 8.94e-04

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: 8.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 586 ERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKEM 665
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 666 HLQDAARRRFLKLQQDQQEMEL---RRLDDEIGRKNLTENQEALAKEMRADADAYRRKVDLEEHMFHKLIEAGETQSQKT 742
Cdd:COG1196   313 ELEERLEELEEELAELEEELEEleeELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1387845346 743 QKWKEAEGKEFRLRSAKKASALSDASRKWFLKQEINAAVEHAE 785
Cdd:COG1196   393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 576-708 9.48e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.89  E-value: 9.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 576 PKFIVDyqtQERERIRNDELDylrerqtVEDMQAKVDQQRVE-DEAWYQKQELLRKAEETRREMllqeEEKMIQQRQRLA 654
Cdd:PRK00409  500 PENIIE---EAKKLIGEDKEK-------LNELIASLEELERElEQKAEEAEALLKEAEKLKEEL----EEKKEKLQEEED 565

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1387845346 655 AVKRELKVKEMHLQDAARRRFLKLQQDQQEMElRRLDDEIGRKNLTENQEALAK 708
Cdd:PRK00409  566 KLLEEAEKEAQQAIKEAKKEADEIIKELRQLQ-KGGYASVKAHELIEARKRLNK 618
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 579-748 1.05e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.21  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 579 IVDYQTQERERIRNDELDYLRErqtvEDMQAKVDQQRVEDEawYQKQELLRKAE------------ETRREMLLQEEEKM 646
Cdd:pfam13868  23 ERDAQIAEKKRIKAEEKEEERR----LDEMMEEERERALEE--EEEKEEERKEErkryrqeleeqiEEREQKRQEEYEEK 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 647 IQQRQRLAAVKRELKVKEMHLQDAARRRFLKLQQDQQEM--ELRRLDDEIGRKNLTENQEAL--AKEMRADADAYRRKVD 722
Cdd:pfam13868  97 LQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFneEQAEWKELEKEEEREEDERILeyLKEKAEREEEREAERE 176

                         170       180
                  ....*....|....*....|....*.
gi 1387845346 723 LEEHMFHKLIEAGETQSQKTQKWKEA 748
Cdd:pfam13868 177 EIEEEKEREIARLRAQQEKAQDEKAE 202
WD40 pfam00400
WD domain, G-beta repeat;
11-48 1.22e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 37.32  E-value: 1.22e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1387845346  11 KELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWD 48
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDgTVKVWD 39
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 584-777 1.89e-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: 41.88  E-value: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  584 TQERER-----IRNDELDYLRERQTVED-MQAKVDQQRVEDEAWYQKQELLRKAEE-----------------TRREMLL 640
Cdd:TIGR00618  656 TQERVRehalsIRVLPKELLASRQLALQkMQSEKEQLTYWKEMLAQCQTLLRELEThieeydrefneienassSLGSDLA 735

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  641 QEEEKMIQQRQRLAAVKRE-LKVKEMHLQDAARRRFLKLQQDQQEMELRRlDDEIGRKNLTENQEALAK---EMRADADA 716
Cdd:TIGR00618  736 AREDALNQSLKELMHQARTvLKARTEAHFNNNEEVTAALQTGAELSHLAA-EIQFFNRLREEDTHLLKTleaEIGQEIPS 814

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  717 YRRKVDLEEHMF--------HKLIEAGETQSQKTQKWKEAEGKEFRLRSAKKASA-LSDASRKWFLKQEI 777
Cdd:TIGR00618  815 DEDILNLQCETLvqeeeqflSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAkIIQLSDKLNGINQI 884
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 585-770 2.14e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 2.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  585 QERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQR-----QRLAAVKRE 659
Cdd:TIGR02168  280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKleelkEELESLEAE 359

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  660 LKVKEMHLQDA-------------ARRRF--LKLQQDQQEMELRRLDDEI-----GRKNLTENQEALAKEM-RADADAYR 718
Cdd:TIGR02168  360 LEELEAELEELesrleeleeqletLRSKVaqLELQIASLNNEIERLEARLerledRRERLQQEIEELLKKLeEAELKELQ 439

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1387845346  719 RKVDLEEHMFHKLIEAGETqsqktqkwKEAEGKEFRLRSAKKASALSDASRK 770
Cdd:TIGR02168  440 AELEELEEELEELQEELER--------LEEALEELREELEEAEQALDAAERE 483
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
601-763 2.39e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 41.56  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 601 RQTVEDMQAKV-DQQRVEDeawyQKQELLRKAEETRREMLLQEEEKMIQQRQRLAA------VKRELKVKEMHLQDAARR 673
Cdd:COG3064     2 QEALEEKAAEAaAQERLEQ----AEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAeeeareAKAEAEQRAAELAAEAAK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 674 RFLKLQQDQQEMElRRLDDEIgRKNLTENQEALAKEmRADADAYRRKVDLEEhmfHKLIEAGETQSQKTQKWKEAEGKEF 753
Cdd:COG3064    78 KLAEAEKAAAEAE-KKAAAEK-AKAAKEAEAAAAAE-KAAAAAEKEKAEEAK---RKAEEEAKRKAEEERKAAEAEAAAK 151

                         170
                  ....*....|
gi 1387845346 754 RLRSAKKASA 763
Cdd:COG3064   152 AEAEAARAAA 161
PDCD7 pfam16021
Programmed cell death protein 7;
613-720 2.39e-03

Programmed cell death protein 7;


Pssm-ID: 464979 [Multi-domain]  Cd Length: 305  Bit Score: 40.86  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 613 QQRVEDEA-WyqkQELLRKAEETRREmlLQEEEKMIQQRQRLAAVKREL-KVKEMHLQDAARRRFLKLQQDQQEMELRRL 690
Cdd:pfam16021  28 RENVEDDSvW---SESYSRAAELKHE--LQEKLLLLEDPELLESLKRKLeRRQKKRLRRKRRKEERKEEKKEEQERRAER 102

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1387845346 691 DDEIG----RKNLTENQEALAKEMRADADAY----RRK 720
Cdd:pfam16021 103 EAKIDkwrrKQIQEVEEKKRERELKLAADAVlsevRKK 140
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 623-718 3.02e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 623 QKQELLRKAEETRREmLLQEEEKMIQQRQRLAAVKRELKVKEMHLQDAARR-RFLKLQQDQQEMELRRLDDEIG--RKNL 699
Cdd:COG4942    21 AAAEAEAELEQLQQE-IAELEKELAALKKEEKALLKQLAALERRIAALARRiRALEQELAALEAELAELEKEIAelRAEL 99

                          90
                  ....*....|....*....
gi 1387845346 700 TENQEALAKEMRAdadAYR 718
Cdd:COG4942   100 EAQKEELAELLRA---LYR 115
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 599-741 3.05e-03

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


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 40.79  E-value: 3.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 599 RERQTVEDMQAKV-------DQQRVEDEAWyqkqELLRKAEETRREMLLQEEEKMIQQ--RQRLAAV------------- 656
Cdd:pfam15558   5 RDRKIAALMLARHkeeqrmrELQQQAALAW----EELRRRDQKRQETLERERRLLLQQsqEQWQAEKeqrkarlgreerr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 657 KRELKVKEMHLQDAARRRFLKLQ--QDQQEMELRRLDDEIgRKnltENQEALAKEMRADADAYRRKVDLEEHmfHKLIEA 734
Cdd:pfam15558  81 RADRREKQVIEKESRWREQAEDQenQRQEKLERARQEAEQ-RK---QCQEQRLKEKEEELQALREQNSLQLQ--ERLEEA 154


                  ....*..
gi 1387845346 735 GETQSQK 741
Cdd:pfam15558 155 CHKRQLK 161
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
585-782 3.58e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 40.79  E-value: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 585 QERERIRNDELDYLRERQTVEDmQAKVDQQRVEDEAwyQKQELLRKAEETRREM---LLQEEEKMIQQRQRLAAVKRELK 661
Cdd:COG3064    39 AEEERLAELEAKRQAEEEAREA-KAEAEQRAAELAA--EAAKKLAEAEKAAAEAekkAAAEKAKAAKEAEAAAAAEKAAA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 662 VKEMHLQDAARRRFLKLQQDQQEMELRRLDDEIGRKNLTENQEALAKEMRADADAYRRKVDLEEHMFHKLIEAGETQSQK 741
Cdd:COG3064   116 AAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADT 195

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1387845346 742 TQKWKEAEGKEFRLRSAKKASALSDASRKWFLKQEINAAVE 782
Cdd:COG3064   196 AAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAA 236
COG5210 COG5210
GTPase-activating protein [General function prediction only];
437-553 3.62e-03

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 40.94  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 437 LSMIENVLAFHDKELLQHFIDHDITSQLYAWPLLETVFSEVLTREEWLKLFDNIFSNHPSFLLMTVVAYNICSRTPLLSC 516
Cdd:COG5210   350 LKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKL 429

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1387845346 517 NLKDDFEFFFHHRNNLDINVVIRQVYHLMETTPTDIH 553
Cdd:COG5210   430 DSDELLDLLLKQLFLHSGKEAWSSILKFRHGTDRDIL 466
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
608-782 3.93e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 40.79  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 608 QAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRElkvkemhLQDAARRRFLKLQQDQQEM-- 685
Cdd:COG3064     1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQ-------AEEEAREAKAEAEQRAAELaa 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 686 ELRRLDDEIGRKNLTENQEALAKEMRADADAyRRKVDLEEhmfhKLIEAGETQSQKTQKWKEAEGKEFRLRSAKKASALS 765
Cdd:COG3064    74 EAAKKLAEAEKAAAEAEKKAAAEKAKAAKEA-EAAAAAEK----AAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEA 148

                         170
                  ....*....|....*..
gi 1387845346 766 DASRKWFLKQEINAAVE 782
Cdd:COG3064   149 AAKAEAEAARAAAAAAA 165
PRK12705 PRK12705
hypothetical protein; Provisional
 587-734 4.25e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 40.46  E-value: 4.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 587 RERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAvkRELKVKEMH 666
Cdd:PRK12705   27 KRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDA--RAEKLDNLE 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387845346 667 LQDAARRRFLKLQQDQQEMELRRLDDEIGRK-NLTENQ--EALAKEMRADAD---AYRRKVDLEEHMFHKLIEA 734
Cdd:PRK12705  105 NQLEEREKALSARELELEELEKQLDNELYRVaGLTPEQarKLLLKLLDAELEeekAQRVKKIEEEADLEAERKA 178
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 608-690 5.40e-03

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.87  E-value: 5.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 608 QAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKEMHLQDAARRRFLKLQQDQQEMEL 687
Cdd:cd16269   208 EAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEI 287


                  ...
gi 1387845346 688 RRL 690
Cdd:cd16269   288 RSL 290
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 656-846 5.60e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 40.41  E-value: 5.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 656 VKRE--LKVKEMHLQDAARR-RFLKLQQDQQEMELRRLDDEigRKNLTENQEALAKemradadayrrkvdleehmfhKLI 732
Cdd:pfam10168 543 VFREeyLKKHDLAREEIQKRvKLLKLQKEQQLQELQSLEEE--RKSLSERAEKLAE---------------------KYE 599

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 733 EAGETQSQKTQKWKEAegkefrLRSAK-KASALSDASRKwfLKQE---INAAVEHAENpCHKEEPRFQNEQdssclprTS 808
Cdd:pfam10168 600 EIKDKQEKLMRRCKKV------LQRLNsQLPVLSDAERE--MKKEletINEQLKHLAN-AIKQAKKKMNYQ-------RY 663

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1387845346 809 QLNDSSEMDPSTQISLN---RRAV-----EWDTTGQNLIKKVRNLR 846
Cdd:pfam10168 664 QIAKSQSIRKKSSLSLSekqRKTIkeilkQLGSEIDELIKQVKDIN 709
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 670-770 5.79e-03

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 38.10  E-value: 5.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 670 AARRRFLKLQQDQQEMElRRLDDEIGRKNLTENQEALAKE-MRADADAYRRKVDLEEHMFHKLIEAGETQSQKTQKWKEA 748
Cdd:pfam05672  17 AEKRRQAREQREREEQE-RLEKEEEERLRKEELRRRAEEErARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEE 95

                          90       100
                  ....*....|....*....|..
gi 1387845346 749 EGKEFRLRSAKKASALSDASRK 770
Cdd:pfam05672  96 QERLQKQKEEAEAKAREEAERQ 117
mukB PRK04863
chromosome partition protein MukB;
619-757 6.33e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.33  E-value: 6.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346  619 EAWYQKQELLRKAEETRREmllqeeekmIQQRQRLaavkrelkvkEMHLQDAARRrfLKLQQDQQemelRRLDDEIGRKN 698
Cdd:PRK04863   493 EAWDVARELLRRLREQRHL---------AEQLQQL----------RMRLSELEQR--LRQQQRAE----RLLAEFCKRLG 547

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1387845346  699 LTENQEALAKEMRADADAyrRKVDLEEhmfhKLIEAGETQSQKTQKWKEAEGKEFRLRS 757
Cdd:PRK04863   548 KNLDDEDELEQLQEELEA--RLESLSE----SVSEARERRMALRQQLEQLQARIQRLAA 600
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
579-720 8.22e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 8.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 579 IVDYQTQERERIrnDELDYLRE--RQTVEDMQAKVDqqRVED--EAWYQKQELLRKAE------ETRREMLLQEEEKMIQ 648
Cdd:PRK02224  466 HVETIEEDRERV--EELEAELEdlEEEVEEVEERLE--RAEDlvEAEDRIERLEERREdleeliAERRETIEEKRERAEE 541

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387845346 649 QRQRL------AAVKRELKVKEMHLQDAARRRFLKLQQDQQEmelrrLDDEIGRKNLTENQEALAKEMRADADAYRRK 720
Cdd:PRK02224  542 LRERAaeleaeAEEKREAAAEAEEEAEEAREEVAELNSKLAE-----LKERIESLERIRTLLAAIADAEDEIERLREK 614
Nop53 pfam07767
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ...
 609-731 8.32e-03

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


Pssm-ID: 462259 [Multi-domain]  Cd Length: 353  Bit Score: 39.20  E-value: 8.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 609 AKVDQQRVEDEAwyQKQELLRKAEETRREMLLQEEEKMIQQrQRLAAVKRELKVKEmhlqdAARRRFLKlQQDQQEMELR 688
Cdd:pfam07767 205 VEAEKKRLKEEE--KLERVLEKIAESAATAEAREEKRKTKA-QRNKEKRRKEEERE-----AKEEKALK-KKLAQLERLK 275

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1387845346 689 RLDDEIGRKnltENQEALAKEMRADADAyRRKVDLEEHMFHKL 731
Cdd:pfam07767 276 EIAKEIAEK---EKEREEKAEARKREKR-KKKKEEKKLRPRKL 314
PRK12704 PRK12704
phosphodiesterase; Provisional
 577-720 8.71e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 8.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 577 KFIVDYQTQERERIRNDELdyLRERQTVEDMQAKVDQQRVEDEAWYQKQEL-LRKAEET---RREMLLQEEEKMIQQRQR 652
Cdd:PRK12704   41 KRILEEAKKEAEAIKKEAL--LEAKEEIHKLRNEFEKELRERRNELQKLEKrLLQKEENldrKLELLEKREEELEKKEKE 118

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387845346 653 LAAVKRELKVKEMHLQDaarrrflKLQQDQQEME-LRRLDDEIGRKNLTENQEalaKEMRADADAYRRK 720
Cdd:PRK12704  119 LEQKQQELEKKEEELEE-------LIEEQLQELErISGLTAEEAKEILLEKVE---EEARHEAAVLIKE 177
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 624-854 9.05e-03

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 39.49  E-value: 9.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 624 KQELLR-KAEETRREM--LLQEEEKMIQQRQRLAAVKR------ELKVKEMHLQDAARRRFLK-LQQDQQEMELRRLDDE 693
Cdd:pfam07888  28 RAELLQnRLEECLQERaeLLQAQEAANRQREKEKERYKrdreqwERQRRELESRVAELKEELRqSREKHEELEEKYKELS 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 694 IGRKNLTENQEALakeMRADADAYRRKVDLEEHMfhklieagETQSQKTQKwKEAEGKEFRLRsAKKASAL---SDASRK 770
Cdd:pfam07888 108 ASSEELSEEKDAL---LAQRAAHEARIRELEEDI--------KTLTQRVLE-RETELERMKER-AKKAGAQrkeEEAERK 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 771 wflkqEINAAVEHAENPCHKEEPRFQN------EQDSSCLprtsQLNDSSEMDPSTQISLNRRAVEwdttGQNLIKKVRN 844
Cdd:pfam07888 175 -----QLQAKLQQTEEELRSLSKEFQElrnslaQRDTQVL----QLQDTITTLTQKLTTAHRKEAE----NEALLEELRS 241

                         250
                  ....*....|
gi 1387845346 845 LRQRLTARAR 854
Cdd:pfam07888 242 LQERLNASER 251
PRK12704 PRK12704
phosphodiesterase; Provisional
 617-720 9.74e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.38  E-value: 9.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845346 617 EDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLaavKRELKVKEMHLQDAARRrflkLQQ-----DQQEMELRRLD 691
Cdd:PRK12704   37 EEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEF---EKELRERRNELQKLEKR----LLQkeenlDRKLELLEKRE 109

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1387845346 692 DEI--GRKNLTENQEALaKEMRADADAYRRK 720
Cdd:PRK12704  110 EELekKEKELEQKQQEL-EKKEEELEELIEE 139
 
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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