|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
10-235 |
4.63e-23 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 102.68 E-value: 4.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 10 TKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 88
Cdd:COG2319 151 TGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDgTVRLWDLATGKLLRTLTGHTG-AVRSVAFSPDGKLLASGSADGTVR 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 89 AWECDTLFCKYQLPAPPES-SSIlykvfAVTRDGRILAAGGKSNHLHLWCLEARQLFRIIQMPTkvRAIRHLEFLPDSfd 167
Cdd:COG2319 230 LWDLATGKLLRTLTGHSGSvRSV-----AFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHS--GGVNSVAFSPDG-- 300
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387845399 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 |
1.42e-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: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 10 TKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 88
Cdd:cd00200 82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDkTIKVWDVETGKCLTTLRGHTD-WVNSVAFSPDGTFVASSSQDGTIK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 89 AWECDTLFCKYQLPAPPESssilykVFAVT--RDGRILAAGGKSNHLHLWCLEARQLFRiiQMPTKVRAIRHLEFLPDsf 166
Cdd:cd00200 161 LWDLRTGKCVATLTGHTGE------VNSVAfsPDGEKLLSSSSDGTIKLWDLSTGKCLG--TLRGHENGVNSVAFSPD-- 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387845399 167 dagsNQVLGVLSQDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYIASIMENGSLNIYS 229
Cdd:cd00200 231 ----GYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
583-811 |
1.28e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 583 QTQERERIRNDELDYL-----RERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVK 657
Cdd:COG1196 285 EAQAEEYELLAELARLeqdiaRLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 658 RELKVKEMHLQDAARRRfLKLQQDQQEMELRRLDDEIgrkvymRDREIAATARDLEMRQLELESQKRLYEKNLTENQEAL 737
Cdd:COG1196 365 EALLEAEAELAEAEEEL-EELAEELLEALRAAAELAA------QLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387845399 738 AKEMRADADAYRRKVDLEEHmfhkliEAGETQSQKTQKWKEAEGKEfrLRSAKKASALSDASRKWFLKQEINAA 811
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEE------EEALLELLAELLEEAALLEA--ALAELLEELAEAAARLLLLLEAEADY 503
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
579-887 |
2.15e-10 |
|
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: 64.37 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 579 IVDYQTQERERIRNDELDYL---RERQTVEDMQAKVDQQRVEDEAwyqkqELLRKAEETRREMLLQEEEKMIQQRQR--- 652
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMeqeRLRQEKEEKAREVERRRKLEEA-----EKARQAEMDRQAAIYAEQERMAMERERele 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 653 ---LAAVKREL---KVKEMHLQDAARRRFLKLQQD-QQEMELRRLDDEIGRKVYMRDREiaatardlemRQLELESQKRL 725
Cdd:pfam17380 352 rirQEERKRELeriRQEEIAMEISRMRELERLQMErQQKNERVRQELEAARKVKILEEE----------RQRKIQQQKVE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 726 YEKNLTENQEALAKEMRADADAYRR---KVDLEEHMFHKLIEAGETQSQKTQKWKEAEGKEFRLRS-------------- 788
Cdd:pfam17380 422 MEQIRAEQEEARQREVRRLEEERARemeRVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKraeeqrrkilekel 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 789 -AKKASALSDASRKWFLKQEInaavEHAENPCHKEEPRFQNEQDSsclpRTSQlndssEMDPSTQIslnrravewdttgQ 867
Cdd:pfam17380 502 eERKQAMIEEERKRKLLEKEM----EERQKAIYEEERRREAEEER----RKQQ-----EMEERRRI-------------Q 555
|
330 340
....*....|....*....|
gi 1387845399 868 NLIKKVRNLRQRLTARARHR 887
Cdd:pfam17380 556 EQMRKATEERSRLEAMERER 575
|
|
| RabGAP-TBC |
pfam00566 |
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ... |
357-500 |
1.59e-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: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 357 LQKKYPIKSRKLLRVLQRTLSALAHWSVIFSDTPYLPLLAFPFVkLFQNNQLICFEVIATLIINwcQHWFEYFPN--PPI 434
Cdd:pfam00566 20 FPHSFFFDNGPGQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLL-LVYLDEEDAFWCFVSLLEN--YLLRDFYTPdfPGL 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387845399 435 NILSMI-ENVLAFHDKELLQHFIDHDITSQLYAWPLLETVFSEVLTREEWLKLFDNIFSNHPSFLLM 500
Cdd:pfam00566 97 KRDLYVfEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVLF 163
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
585-861 |
9.34e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 9.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 585 QERERIRNdELDYLreRQTVEDMQAKVDQQRVEdeawyqkQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKE 664
Cdd:TIGR02169 695 SELRRIEN-RLDEL--SQELSDASRKIGEIEKE-------IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 665 MHLQDaARRRFLKLQQDQQEMElRRLDDEIGRKVYMRDREIAATARDLEMRQLELES--QKRLYEKnltenqeALAKEMR 742
Cdd:TIGR02169 765 ARIEE-LEEDLHKLEEALNDLE-ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQklNRLTLEK-------EYLEKEI 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 743 ADADAYRRKVDLEEHMFHKLIEAGETQSQKT-QKWKEAEGKEFRLRSAKKA---------SALSDASRKwflKQEINAAV 812
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELeEELEELEAALRDLESRLGDlkkerdeleAQLRELERK---IEELEAQI 912
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1387845399 813 EHAENPCH--KEEPRFQNEQDSSCLPRTSQLNDSSEMDPST-QISLNRRAVE 861
Cdd:TIGR02169 913 EKKRKRLSelKAKLEALEEELSEIEDPKGEDEEIPEEELSLeDVQAELQRVE 964
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
588-850 |
2.74e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 588 ERIRNDELDYLRERQTVEDMQaKVDQQRVEDE---AWYQKQELLRKAEETRRE--MLLQEEEKMIQQRQRLAAVKRELKV 662
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAEEKK-KAEEAKKAEEdknMALRKAEEAKKAEEARIEevMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 663 KEMHLQDAARRRFLKLQQDQQE-----MELRRLDDEIGRKVYMRDREIAATARDLEMRQLELESQKRLYEKNLTENQEAL 737
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEekkkaEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 738 -AKEMRADADAYRRKVD----LEEHMFHKLIEA---GETQSQKTQKWKEAEGKEFRLRSAKKASALSDASRKWFLKQEIN 809
Cdd:PTZ00121 1703 kAEELKKKEAEEKKKAEelkkAEEENKIKAEEAkkeAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1387845399 810 AAVEHAENPCHKEEPR--------FQNEQDSSClPRTSQLNDSSEMDPS 850
Cdd:PTZ00121 1783 EELDEEDEKRRMEVDKkikdifdnFANIIEGGK-EGNLVINDSKEMEDS 1830
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
10-48 |
7.10e-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: 7.10e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1387845399 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 |
1.16e-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: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 396 AFP-FVKLFQNNQLIcFEVIATLIINWCQHWFEYFpnppinilsmienvLAFHDKELLQHFIDHDITSQLYAWPLLETVF 474
Cdd:smart00164 112 AFWcLVKLMERYGPN-FYLPDMSGLQLDLLQLDRL--------------VKEYDPDLYKHLKDLGITPSLYALRWFLTLF 176
|
90 100 110
....*....|....*....|....*....|
gi 1387845399 475 SEVLTREEWLKLFDNIFSNHPSFLLMTVVA 504
Cdd:smart00164 177 ARELPLEIVLRIWDVLFAEGSDFLFRVALA 206
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
11-48 |
1.26e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 37.32 E-value: 1.26e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1387845399 11 KELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWD 48
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDgTVKVWD 39
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
598-801 |
2.74e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.74 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 598 LRERQTVEDmQAKVDQQRVEDEAWYQKQELLRK-AEETRRemlLQEE--EKMIQQRQRLaavKREL----KVKEMHL-QD 669
Cdd:NF041483 78 LRNAQIQAD-QLRADAERELRDARAQTQRILQEhAEHQAR---LQAElhTEAVQRRQQL---DQELaerrQTVESHVnEN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 670 AARRRFLKLQQDQQEmelRRLDDEiGRKvymrDREIAATARDLEMRQLELESQKRLYEKNLTENQEALAKEMRADADAYR 749
Cdd:NF041483 151 VAWAEQLRARTESQA---RRLLDE-SRA----EAEQALAAARAEAERLAEEARQRLGSEAESARAEAEAILRRARKDAER 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1387845399 750 rkvdleehmfhkLIEAGETQSQktqkwkEAEGKEFRLRSAkkASALSDASRK 801
Cdd:NF041483 223 ------------LLNAASTQAQ------EATDHAEQLRSS--TAAESDQARR 254
|
|
| COG5210 |
COG5210 |
GTPase-activating protein [General function prediction only]; |
437-553 |
3.81e-03 |
|
GTPase-activating protein [General function prediction only];
Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 40.94 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 437 LSMIENVLAFHDKELLQHFIDHDITSQLYAWPLLETVFSEVLTREEWLKLFDNIFSNHPSFLLMTVVAYNICSRTPLLSC 516
Cdd:COG5210 350 LKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKL 429
|
90 100 110
....*....|....*....|....*....|....*..
gi 1387845399 517 NLKDDFEFFFHHRNNLDINVVIRQVYHLMETTPTDIH 553
Cdd:COG5210 430 DSDELLDLLLKQLFLHSGKEAWSSILKFRHGTDRDIL 466
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
585-794 |
6.34e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.58 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 585 QERERIRNDELDYLRE-RQTVEDMQAkvDQQRVEDEAWYQKQELLRKAEETRREML-----LQEeekmiQQRQRLAAvkr 658
Cdd:NF041483 728 QERERAREQSEELLASaRKRVEEAQA--EAQRLVEEADRRATELVSAAEQTAQQVRdsvagLQE-----QAEEEIAG--- 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 659 eLKVKEMHLQDAARRrflklqQDQQEMELRRLDDEIGRKvymRDREIAATARdlEMRQLELESQKRLYEKNLTEnQEALA 738
Cdd:NF041483 798 -LRSAAEHAAERTRT------EAQEEADRVRSDAYAERE---RASEDANRLR--REAQEETEAAKALAERTVSE-AIAEA 864
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387845399 739 KEMRADADAYRRKVDLEEhmfHKLIEAGETQSQKTQkwKEAEGKEFRLRSAKKASA 794
Cdd:NF041483 865 ERLRSDASEYAQRVRTEA---SDTLASAEQDAARTR--ADAREDANRIRSDAAAQA 915
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
608-690 |
7.33e-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: 39.48 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 608 QAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKEMHLQDAARRRFLKLQQDQQEMEL 687
Cdd:cd16269 208 EAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEI 287
|
...
gi 1387845399 688 RRL 690
Cdd:cd16269 288 RSL 290
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
10-235 |
4.63e-23 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 102.68 E-value: 4.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 10 TKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 88
Cdd:COG2319 151 TGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDgTVRLWDLATGKLLRTLTGHTG-AVRSVAFSPDGKLLASGSADGTVR 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 89 AWECDTLFCKYQLPAPPES-SSIlykvfAVTRDGRILAAGGKSNHLHLWCLEARQLFRIIQMPTkvRAIRHLEFLPDSfd 167
Cdd:COG2319 230 LWDLATGKLLRTLTGHSGSvRSV-----AFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHS--GGVNSVAFSPDG-- 300
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387845399 168 agsnQVLGVLSQDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYIASIMENGSLNIYSVQALTQ 235
Cdd:COG2319 301 ----KLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
7-231 |
9.84e-23 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 101.53 E-value: 9.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 7 ETVTKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNiRQSVGIQKVFFLPLSNTILSCFKDN 85
Cdd:COG2319 106 DLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADgTVRLWDLATGKLLRTLT-GHSGAVTSVAFSPDGKLLASGSDDG 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 86 SIFAWECDTLFCKYQLPAPPESSSILykvfAVTRDGRILAAGGKSNHLHLWCLEARQLFRIIQMPTkvRAIRHLEFLPDS 165
Cdd:COG2319 185 TVRLWDLATGKLLRTLTGHTGAVRSV----AFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHS--GSVRSVAFSPDG 258
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387845399 166 fdagsnQVLGVLSQDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYIASIMENGSLNIYSVQ 231
Cdd:COG2319 259 ------RLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLA 318
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
10-231 |
1.51e-22 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 101.14 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 10 TKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 88
Cdd:COG2319 193 TGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADgTVRLWDLATGKLLRTLTGHSG-SVRSVAFSPDGRLLASGSADGTVR 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 89 AWECDTLFCKYQLPAPPES-SSIlykvfAVTRDGRILAAGGKSNHLHLWCLEARQLFRIIQMPTkvRAIRHLEFLPDsfd 167
Cdd:COG2319 272 LWDLATGELLRTLTGHSGGvNSV-----AFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHT--GAVRSVAFSPD--- 341
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387845399 168 agsNQVLGVLSQDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYIASIMENGSLNIYSVQ 231
Cdd:COG2319 342 ---GKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
10-231 |
3.47e-21 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 96.90 E-value: 3.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 10 TKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 88
Cdd:COG2319 67 AGALLATLLGHTAAVLSVAFSPDGRLLASASADgTVRLWDLATGLLLRTLTGHTG-AVRSVAFSPDGKTLASGSADGTVR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 89 AWECDTLFCKYQLPAPPES-SSIlykvfAVTRDGRILAAGGKSNHLHLWCLEARQLFRIIQMPTkvRAIRHLEFLPDSfd 167
Cdd:COG2319 146 LWDLATGKLLRTLTGHSGAvTSV-----AFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHT--GAVRSVAFSPDG-- 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387845399 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 |
1.42e-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: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 10 TKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 88
Cdd:cd00200 82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDkTIKVWDVETGKCLTTLRGHTD-WVNSVAFSPDGTFVASSSQDGTIK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 89 AWECDTLFCKYQLPAPPESssilykVFAVT--RDGRILAAGGKSNHLHLWCLEARQLFRiiQMPTKVRAIRHLEFLPDsf 166
Cdd:cd00200 161 LWDLRTGKCVATLTGHTGE------VNSVAfsPDGEKLLSSSSDGTIKLWDLSTGKCLG--TLRGHENGVNSVAFSPD-- 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387845399 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 |
5.05e-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: 5.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 18 RGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIrQSVGIQKVFFLPLSNTILSCFKDNSIFAWECDTLF 96
Cdd:cd00200 6 KGHTGGVTCVAFSPDGKLLATGSGDgTIKVWDLETGELLRTLKG-HTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 97 CKYQLPAppESSSILYkvFAVTRDGRILAAGGKSNHLHLWCLEARQLfrIIQMPTKVRAIRHLEFLPDsfdagsNQVLGV 176
Cdd:cd00200 85 CVRTLTG--HTSYVSS--VAFSPDGRILSSSSRDKTIKVWDVETGKC--LTTLRGHTDWVNSVAFSPD------GTFVAS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387845399 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 |
9.81e-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: 9.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 19 GHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLFC 97
Cdd:cd00200 49 GHTGPVRDVAASADGTYLASGSSDkTIRLWDLETGECVRTLTGHTS-YVSSVAFSPDGRILSSSSRDKTIKVWDVETGKC 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 98 KYQLPAPPESssilYKVFAVTRDGRILAAGGKSNHLHLWCLEARQLFRIIQMPTKvrAIRHLEFLPD--SFDAGSNqvlg 175
Cdd:cd00200 128 LTTLRGHTDW----VNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTG--EVNSVAFSPDgeKLLSSSS---- 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387845399 176 vlsqDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYIASIMENGSLNIYSVQ 231
Cdd:cd00200 198 ----DGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLR 249
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
18-231 |
7.39e-15 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 77.64 E-value: 7.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 18 RGHESSVFSISVHASGKYAITTSSDTAQLWDLDTFQRKRKLNIRQSVGIQKVFFLPLSNTILSCFKDNSIFAWECDTLFC 97
Cdd:COG2319 33 LGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 98 KYQLPAPPES-SSIlykvfAVTRDGRILAAGGKSNHLHLWCLEARQLFRIIQMPTkvRAIRHLEFLPDSfdagsnQVLGV 176
Cdd:COG2319 113 LRTLTGHTGAvRSV-----AFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHS--GAVTSVAFSPDG------KLLAS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1387845399 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 |
1.56e-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: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 7 ETVTKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDN 85
Cdd:cd00200 121 DVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDgTIKLWDLRTGKCVATLTGHTG-EVNSVAFSPDGEKLLSSSSDG 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 86 SIFAWECDTLFCKYQLPAPPESSSILykvfAVTRDGRILAAGGKSNHLHLWCLEARQLFRIIQMPTK-VRAIRhleFLPD 164
Cdd:cd00200 200 TIKLWDLSTGKCLGTLRGHENGVNSV----AFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNsVTSLA---WSPD 272
|
170 180
....*....|....*....|.
gi 1387845399 165 SfdagsnQVLGVLSQDGIMRF 185
Cdd:cd00200 273 G------KRLASGSADGTIRI 287
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
583-811 |
1.28e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 583 QTQERERIRNDELDYL-----RERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVK 657
Cdd:COG1196 285 EAQAEEYELLAELARLeqdiaRLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 658 RELKVKEMHLQDAARRRfLKLQQDQQEMELRRLDDEIgrkvymRDREIAATARDLEMRQLELESQKRLYEKNLTENQEAL 737
Cdd:COG1196 365 EALLEAEAELAEAEEEL-EELAEELLEALRAAAELAA------QLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387845399 738 AKEMRADADAYRRKVDLEEHmfhkliEAGETQSQKTQKWKEAEGKEfrLRSAKKASALSDASRKWFLKQEINAA 811
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEE------EEALLELLAELLEEAALLEA--ALAELLEELAEAAARLLLLLEAEADY 503
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
579-887 |
2.15e-10 |
|
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: 64.37 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 579 IVDYQTQERERIRNDELDYL---RERQTVEDMQAKVDQQRVEDEAwyqkqELLRKAEETRREMLLQEEEKMIQQRQR--- 652
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMeqeRLRQEKEEKAREVERRRKLEEA-----EKARQAEMDRQAAIYAEQERMAMERERele 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 653 ---LAAVKREL---KVKEMHLQDAARRRFLKLQQD-QQEMELRRLDDEIGRKVYMRDREiaatardlemRQLELESQKRL 725
Cdd:pfam17380 352 rirQEERKRELeriRQEEIAMEISRMRELERLQMErQQKNERVRQELEAARKVKILEEE----------RQRKIQQQKVE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 726 YEKNLTENQEALAKEMRADADAYRR---KVDLEEHMFHKLIEAGETQSQKTQKWKEAEGKEFRLRS-------------- 788
Cdd:pfam17380 422 MEQIRAEQEEARQREVRRLEEERARemeRVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKraeeqrrkilekel 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 789 -AKKASALSDASRKWFLKQEInaavEHAENPCHKEEPRFQNEQDSsclpRTSQlndssEMDPSTQIslnrravewdttgQ 867
Cdd:pfam17380 502 eERKQAMIEEERKRKLLEKEM----EERQKAIYEEERRREAEEER----RKQQ-----EMEERRRI-------------Q 555
|
330 340
....*....|....*....|
gi 1387845399 868 NLIKKVRNLRQRLTARARHR 887
Cdd:pfam17380 556 EQMRKATEERSRLEAMERER 575
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
583-779 |
3.56e-10 |
|
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: 63.99 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 583 QTQERERIRNDELDylrERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEE----KMIQQRQRLAAVKR 658
Cdd:pfam17380 444 RAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEerkqAMIEEERKRKLLEK 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 659 ELKVKEMHLQDAARRRFLKLQQ-DQQEMELRRLDDEIGRKVYMRDREIAATARDLEMRQLELESQKRLYEKNLTENQEAL 737
Cdd:pfam17380 521 EMEERQKAIYEEERRREAEEERrKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEATTPITTI 600
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1387845399 738 AKEMRADADAYRRKvDLEEHMFHKLIEAGETQSQKTQKWKEA 779
Cdd:pfam17380 601 KPIYRPRISEYQPP-DVESHMIRFTTQSPEWATPSPATWNPE 641
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
585-780 |
1.00e-09 |
|
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: 62.45 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 585 QERERIRNdELDYLRERQTVE-DMQAKVDQQRVEDEAWYQKQE------LLRKAEETRREMllqeeekmiqQRQRLAAVK 657
Cdd:pfam17380 389 QKNERVRQ-ELEAARKVKILEeERQRKIQQQKVEMEQIRAEQEearqreVRRLEEERAREM----------ERVRLEEQE 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 658 RELKVKEMHLQDAARRRfLKLQQDQQEMElRRLDDEIGRKVYmrDREIAATARDLemrqLELESQKRLYEKNLTENQEAL 737
Cdd:pfam17380 458 RQQQVERLRQQEEERKR-KKLELEKEKRD-RKRAEEQRRKIL--EKELEERKQAM----IEEERKRKLLEKEMEERQKAI 529
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1387845399 738 AKE-MRADADAYRRK-VDLEE--HMFHKLIEAGETQSQKTQKWKEAE 780
Cdd:pfam17380 530 YEEeRRREAEEERRKqQEMEErrRIQEQMRKATEERSRLEAMERERE 576
|
|
| RabGAP-TBC |
pfam00566 |
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ... |
357-500 |
1.59e-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: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 357 LQKKYPIKSRKLLRVLQRTLSALAHWSVIFSDTPYLPLLAFPFVkLFQNNQLICFEVIATLIINwcQHWFEYFPN--PPI 434
Cdd:pfam00566 20 FPHSFFFDNGPGQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLL-LVYLDEEDAFWCFVSLLEN--YLLRDFYTPdfPGL 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387845399 435 NILSMI-ENVLAFHDKELLQHFIDHDITSQLYAWPLLETVFSEVLTREEWLKLFDNIFSNHPSFLLM 500
Cdd:pfam00566 97 KRDLYVfEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVLF 163
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
585-861 |
9.34e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 9.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 585 QERERIRNdELDYLreRQTVEDMQAKVDQQRVEdeawyqkQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKE 664
Cdd:TIGR02169 695 SELRRIEN-RLDEL--SQELSDASRKIGEIEKE-------IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 665 MHLQDaARRRFLKLQQDQQEMElRRLDDEIGRKVYMRDREIAATARDLEMRQLELES--QKRLYEKnltenqeALAKEMR 742
Cdd:TIGR02169 765 ARIEE-LEEDLHKLEEALNDLE-ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQklNRLTLEK-------EYLEKEI 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 743 ADADAYRRKVDLEEHMFHKLIEAGETQSQKT-QKWKEAEGKEFRLRSAKKA---------SALSDASRKwflKQEINAAV 812
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELeEELEELEAALRDLESRLGDlkkerdeleAQLRELERK---IEELEAQI 912
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1387845399 813 EHAENPCH--KEEPRFQNEQDSSCLPRTSQLNDSSEMDPST-QISLNRRAVE 861
Cdd:TIGR02169 913 EKKRKRLSelKAKLEALEEELSEIEDPKGEDEEIPEEELSLeDVQAELQRVE 964
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
588-850 |
2.74e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 588 ERIRNDELDYLRERQTVEDMQaKVDQQRVEDE---AWYQKQELLRKAEETRRE--MLLQEEEKMIQQRQRLAAVKRELKV 662
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAEEKK-KAEEAKKAEEdknMALRKAEEAKKAEEARIEevMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 663 KEMHLQDAARRRFLKLQQDQQE-----MELRRLDDEIGRKVYMRDREIAATARDLEMRQLELESQKRLYEKNLTENQEAL 737
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEekkkaEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 738 -AKEMRADADAYRRKVD----LEEHMFHKLIEA---GETQSQKTQKWKEAEGKEFRLRSAKKASALSDASRKWFLKQEIN 809
Cdd:PTZ00121 1703 kAEELKKKEAEEKKKAEelkkAEEENKIKAEEAkkeAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1387845399 810 AAVEHAENPCHKEEPR--------FQNEQDSSClPRTSQLNDSSEMDPS 850
Cdd:PTZ00121 1783 EELDEEDEKRRMEVDKkikdifdnFANIIEGGK-EGNLVINDSKEMEDS 1830
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
580-758 |
4.85e-07 |
|
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: 53.42 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 580 VDYQTQERE---RIRNDELDylRERQTVEDMQakVDQQRVEDEAWYQKQellRKAEETRRemllQEEEKMIQQRQRLAAV 656
Cdd:pfam15709 350 VERKRREQEeqrRLQQEQLE--RAEKMREELE--LEQQRRFEEIRLRKQ---RLEEERQR----QEEEERKQRLQLQAAQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 657 KRELKvkemhLQDAARRRFLKLQQDQQEMELRRLDDEIGRKVYMRDREIAATARDLEMRQLE-LESQKRLYEKNLTENQE 735
Cdd:pfam15709 419 ERARQ-----QQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEErLEYQRQKQEAEEKARLE 493
|
170 180
....*....|....*....|...
gi 1387845399 736 ALAKEMRADADAyrrKVDLEEHM 758
Cdd:pfam15709 494 AEERRQKEEEAA---RLALEEAM 513
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
591-831 |
5.68e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 591 RNDELDYLRERQTVEDMQAKVDQQRVEDEawyQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKEMHLQDA 670
Cdd:PTZ00121 1183 KAEEVRKAEELRKAEDARKAEAARKAEEE---RKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEE 1259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 671 ARRRFLKLQQDQQEMELRRLDDEIGRKVYMRDREIAATARdlEMRQLElESQKRLYEKNLTENQEALAKEMRADADAYRR 750
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAE--EKKKAD-EAKKKAEEAKKADEAKKKAEEAKKKADAAKK 1336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 751 KvdleehmfhklieAGETQSQKTQKWKEAEGKEFRLRSAKKaSALSDASRKWFLKQEINAAVEHAENPCHKEEPRFQNEQ 830
Cdd:PTZ00121 1337 K-------------AEEAKKAAEAAKAEAEAAADEAEAAEE-KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE 1402
|
.
gi 1387845399 831 D 831
Cdd:PTZ00121 1403 D 1403
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
581-756 |
6.29e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 581 DYQTQERERIRNDELDYLRERQTVEDMQAKVD--QQRVED-EAWYQKQELLRKAEETRREMLLQEEEKMIQQR-----QR 652
Cdd:COG4913 260 LAERYAAARERLAELEYLRAALRLWFAQRRLEllEAELEElRAELARLEAELERLEARLDALREELDELEAQIrgnggDR 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 653 LAAVKRELKVKEMHLQDAARRRfLKLQQDQQEMELrrlddeigrkvymrdrEIAATARDLEMRQLELESQKRLYEKNLTE 732
Cdd:COG4913 340 LEQLEREIERLERELEERERRR-ARLEALLAALGL----------------PLPASAEEFAALRAEAAALLEALEEELEA 402
|
170 180
....*....|....*....|....
gi 1387845399 733 NQEALAKEMRADADAYRRKVDLEE 756
Cdd:COG4913 403 LEEALAEAEAALRDLRRELRELEA 426
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
544-856 |
1.54e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.03 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 544 LMETTPTDIHpDSMLNVFVALTKGQYpvfnqYPKFIVDYQTQ-ERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWY 622
Cdd:pfam05483 444 LLQAREKEIH-DLEIQLTAIKTSEEH-----YLKEVEDLKTElEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKK 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 623 QKQELL--RKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKemhlQDAARRRFLKLQQDQQEMELRRLDDEIGRKVYM 700
Cdd:pfam05483 518 HQEDIIncKKQEERMLKQIENLEEKEMNLRDELESVREEFIQK----GDEVKCKLDKSEENARSIEYEVLKKEKQMKILE 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 701 RD-----REIAATARDLEMRQLElesQKRLYEKNLTENQEALAKEMRADadayrrKVDLE-EHMFHKLIEAGETQSQKTQ 774
Cdd:pfam05483 594 NKcnnlkKQIENKNKNIEELHQE---NKALKKKGSAENKQLNAYEIKVN------KLELElASAKQKFEEIIDNYQKEIE 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 775 KWKEAEgkEFRLRSAKKASALSDASRKwfLKQEINAAVEH--AENPCHKEEPRFQ-----NEQDSSCLPRTSQLNDSSEM 847
Cdd:pfam05483 665 DKKISE--EKLLEEVEKAKAIADEAVK--LQKEIDKRCQHkiAEMVALMEKHKHQydkiiEERDSELGLYKNKEQEQSSA 740
|
....*....
gi 1387845399 848 DPSTQISLN 856
Cdd:pfam05483 741 KAALEIELS 749
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
587-830 |
2.67e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 587 RERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREmllQEEEKMIQQRQRLAAVKR---ELKVK 663
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKA---AAAKKKADEAKKKAEEKKkadEAKKK 1439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 664 --EMHLQDAARRRF---LKLQQDQQEMELRRLDDEIGRKVYMRDREIAATARDLEMRQLELESQKRLYEKNLTEN----- 733
Cdd:PTZ00121 1440 aeEAKKADEAKKKAeeaKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEakkae 1519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 734 -----QEALAKEMRADADAYRR---KVDLEEHMFHKLIEAGETQSQKTQKWKEAEGKEFRLRSAKKASALSDASRKWFLK 805
Cdd:PTZ00121 1520 eakkaDEAKKAEEAKKADEAKKaeeKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK 1599
|
250 260
....*....|....*....|....*
gi 1387845399 806 QEINAAVEHAENPCHKEEPRFQNEQ 830
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
581-830 |
3.38e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 581 DYQTQERERIRNDELdYLRERQTVEDMQaKVDQQRVEDEAwyQKQELLRKAEETRR--EMLLQEEEKMIQQRQRLAAVKR 658
Cdd:PTZ00121 1078 DFDFDAKEDNRADEA-TEEAFGKAEEAK-KTETGKAEEAR--KAEEAKKKAEDARKaeEARKAEDARKAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 659 ELKVKEMhlQDAARRRFLKLQQDQQEMELRRLDDEIGRKVYMRD----REIAATARDLEMRQLElesQKRLYEKNLTENQ 734
Cdd:PTZ00121 1154 VEIARKA--EDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKaedaRKAEAARKAEEERKAE---EARKAEDAKKAEA 1228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 735 EALAKEMRADADAYRR----KVDLEEHMFHKLIEAGETQSQKTQKWKEAEGKEfRLRSAKKASAlSDASRKWFLKQEINA 810
Cdd:PTZ00121 1229 VKKAEEAKKDAEEAKKaeeeRNNEEIRKFEEARMAHFARRQAAIKAEEARKAD-ELKKAEEKKK-ADEAKKAEEKKKADE 1306
|
250 260
....*....|....*....|
gi 1387845399 811 AVEHAENPCHKEEPRFQNEQ 830
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEE 1326
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
617-741 |
5.72e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.78 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 617 EDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLaavKRELKVKEMHLQDAARRrflkLQqdQQEMELRRLDDEIGR 696
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEF---EKELRERRNELQKLEKR----LL--QKEENLDRKLELLEK 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1387845399 697 kvymRDREIAATARDLEMRQLELESQKRLYEKNLTENQEAL----------AKEM 741
Cdd:PRK12704 108 ----REEELEKKEKELEQKQQELEKKEEELEELIEEQLQELerisgltaeeAKEI 158
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
599-790 |
8.54e-06 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 48.88 E-value: 8.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 599 RERQTVEDMQAKV-------DQQRVEDEAWyqkqELLRKAEETRREMLLQEEEKMIQQ--RQRLAAV------------- 656
Cdd:pfam15558 5 RDRKIAALMLARHkeeqrmrELQQQAALAW----EELRRRDQKRQETLERERRLLLQQsqEQWQAEKeqrkarlgreerr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 657 KRELKVKEMHLQDAARRRFLKLQ--QDQQEMELRRLDDEIgRKVY--------------MRDREIAATARDLEM----RQ 716
Cdd:pfam15558 81 RADRREKQVIEKESRWREQAEDQenQRQEKLERARQEAEQ-RKQCqeqrlkekeeelqaLREQNSLQLQERLEEachkRQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387845399 717 L-ELESQKRLYEKNLTE--NQEALAKEMRADADAyrrkvdlEEHMFHKLIEAGETQSQKT-QKWKEAEGKEFRLRSAK 790
Cdd:pfam15558 160 LkEREEQKKVQENNLSEllNHQARKVLVDCQAKA-------EELLRRLSLEQSLQRSQENyEQLVEERHRELREKAQK 230
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
583-756 |
1.20e-05 |
|
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: 48.38 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 583 QTQERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQ-------RQRLAA 655
Cdd:pfam13868 133 DEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEkaerdelRAKLYQ 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 656 VKRELKVKEMHLQDAARRRFLKL-----QQDQQEMELRRLDDEIGRKVYMRDREIAATARDLEMRQLELE--SQKRLYEK 728
Cdd:pfam13868 213 EEQERKERQKEREEAEKKARQRQelqqaREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEkrRMKRLEHR 292
|
170 180
....*....|....*....|....*...
gi 1387845399 729 NLTENQEALAKEMRADAdayrRKVDLEE 756
Cdd:pfam13868 293 RELEKQIEEREEQRAAE----REEELEE 316
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
579-792 |
1.31e-05 |
|
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: 48.38 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 579 IVDYQTQERERIRNDELDYLRErqtvEDMQAKVDQQRVEDEawYQKQELLRKAE------------ETRREMLLQEEEKM 646
Cdd:pfam13868 23 ERDAQIAEKKRIKAEEKEEERR----LDEMMEEERERALEE--EEEKEEERKEErkryrqeleeqiEEREQKRQEEYEEK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 647 IQQRQRLAAVKRELKVKEMHLQDAARRRFLKLQQDQQEM--ELRRLDDEIGRKVYMRDREIAATARDLEMRQLELESQKR 724
Cdd:pfam13868 97 LQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFneEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAERE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387845399 725 LYEKNLTENQEALAKEMradADAYRRKVDLEEHMFHKLIEAGETQSQKTQKwKEAEGKEFRLRSAKKA 792
Cdd:pfam13868 177 EIEEEKEREIARLRAQQ---EKAQDEKAERDELRAKLYQEEQERKERQKER-EEAEKKARQRQELQQA 240
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
586-816 |
1.78e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 586 ERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKEM 665
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 666 HLQDAARRRFLKLQQDQQEMELRRLDDEIGRKvymRDREIAATARDLEMRQLELESQKRLYEKNLTENQEALAKEMRADA 745
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEE---ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387845399 746 DAYRRKVDLEEHMFHKLIEAGETQSQKTQKWKEAEGkefRLRSAKKASALSDASRKWFLKQEINAAVEHAE 816
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEE---LEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
585-689 |
1.84e-05 |
|
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: 45.80 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 585 QERERIRNDEldylRERQTVEDMQAKVDQQRVEDEAWYQKQE---------LLRKAEETRREMLLQE-EEKMIQQRQRLA 654
Cdd:pfam05672 30 EEQERLEKEE----EERLRKEELRRRAEEERARREEEARRLEeerrreeeeRQRKAEEEAEEREQREqEEQERLQKQKEE 105
|
90 100 110
....*....|....*....|....*....|....*...
gi 1387845399 655 AvkrELKVKEmhlqDAARRRF---LKLQQDQQEMELRR 689
Cdd:pfam05672 106 A---EAKARE----EAERQRQereKIMQQEEQERLERK 136
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
586-723 |
1.91e-05 |
|
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: 48.41 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 586 ERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMllQEEEKmiqqrQRLAAVKRELKVKEM 665
Cdd:pfam15709 387 EEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKK--QQEEA-----ERAEAEKQRQKELEM 459
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387845399 666 HLQDAARR--------RFLKLQQDQQEMELRRLDDEIGRKvymRDREIAATARDLEMRQLELESQK 723
Cdd:pfam15709 460 QLAEEQKRlmemaeeeRLEYQRQKQEAEEKARLEAEERRQ---KEEEAARLALEEAMKQAQEQARQ 522
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
583-783 |
2.47e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 583 QTQERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRR---EMLLQEEEKMiQQRQRLAAVKRE 659
Cdd:PTZ00121 1676 KAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKikaEEAKKEAEED-KKKAEEAKKDEE 1754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 660 LKVKEMHLQDAARRRFLKLQQDQQEMELRRLDDEIGRKVYMRDREIAATARDLEMRQlELESQKRLYEKNLTENQEALAK 739
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANII-EGGKEGNLVINDSKEMEDSAIK 1833
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1387845399 740 EMRADADAYRRKVD-LEEHMFHKLIEAGETQSQKTQKWKEAEGKE 783
Cdd:PTZ00121 1834 EVADSKNMQLEEADaFEKHKFNKNNENGEDGNKEADFNKEKDLKE 1878
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
597-816 |
3.14e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.11 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 597 YLRERQTVEDMQAKvdQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAvkrelkvkemhlQDAARRRfl 676
Cdd:PRK09510 64 YNRQQQQQKSAKRA--EEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQA------------EEAAKQA-- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 677 KLQQDQQEMELRrlddeigrkvymRDREIAATARDLEMRQLELESQKRLYEKnltENQEALAKEMRADADAyrrKVDLEE 756
Cdd:PRK09510 128 ALKQKQAEEAAA------------KAAAAAKAKAEAEAKRAAAAAKKAAAEA---KKKAEAEAAKKAAAEA---KKKAEA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387845399 757 HMFHKLIEAGETQSQKTQKWK---------EAEGKEFRLRSAKKASALSDASRKWFLKQEINAAVEHAE 816
Cdd:PRK09510 190 EAAAKAAAEAKKKAEAEAKKKaaaeakkkaAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
601-756 |
3.49e-05 |
|
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: 47.25 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 601 RQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQ----RLAavKRELKVKEMHLQDAARRRFL 676
Cdd:pfam15709 335 RDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRfeeiRLR--KQRLEEERQRQEEEERKQRL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 677 KLQQDQ-----QEMELRRLDDEIGRKvymRDREIAATARDLEMRQLELESQ-----KRLYEKNLTENQEALAKEMRADAd 746
Cdd:pfam15709 413 QLQAAQerarqQQEEFRRKLQELQRK---KQQEEAERAEAEKQRQKELEMQlaeeqKRLMEMAEEERLEYQRQKQEAEE- 488
|
170
....*....|
gi 1387845399 747 ayRRKVDLEE 756
Cdd:pfam15709 489 --KARLEAEE 496
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
588-830 |
4.66e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 588 ERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRRemllQEEEKmiqqRQRLAAVKRELKVKEMHL 667
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKK----KAEEA----KKAAEAAKAEAEAAADEA 1359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 668 QDAARRrflKLQQDQQEMELRRLDDEIGRKVYMRDREIAATARDLEMRQLELESQKRLYEKNLTENQEALAKEMRaDADA 747
Cdd:PTZ00121 1360 EAAEEK---AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK-KADE 1435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 748 YRRKVdlEEhmfHKLIEAGETQSQKTQKWKEAEGKEFRLRSAKKASALSDASRKW-FLKQEINAAVEHAENPCHKEEPRF 826
Cdd:PTZ00121 1436 AKKKA--EE---AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAdEAKKKAEEAKKKADEAKKAAEAKK 1510
|
....
gi 1387845399 827 QNEQ 830
Cdd:PTZ00121 1511 KADE 1514
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
10-48 |
7.10e-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: 7.10e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1387845399 10 TKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWD 48
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDgTIKLWD 40
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
585-831 |
1.01e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 585 QERERIRNDELdylrerQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRR------------------EMLLQEEEKM 646
Cdd:PTZ00121 1615 AEEAKIKAEEL------KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikaaeeakkaeedkkkaeEAKKAEEDEK 1688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 647 IQQRQRLAAVKRELKVKEMHLQDAARRRflKLQQDQQEMELRRLDDEIGRKVYMRDREIAATARDLEMRQLELESQKRLY 726
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAEEKK--KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEE 1766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 727 EKNLTE---NQEALAKEMRADADAYR-----RKVDLEEHMFHKLIEAGETQSQKTQKWKEAEGKEFRLRSAKKASALSDA 798
Cdd:PTZ00121 1767 EKKAEEirkEKEAVIEEELDEEDEKRrmevdKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEA 1846
|
250 260 270
....*....|....*....|....*....|...
gi 1387845399 799 srKWFLKQEINAAVEHAENpcHKEEPRFQNEQD 831
Cdd:PTZ00121 1847 --DAFEKHKFNKNNENGED--GNKEADFNKEKD 1875
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
591-756 |
1.16e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 591 RNDELDYLRERqtVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREmllQEEEKMIQQRQRLAAVKRELKVKEMHLQDA 670
Cdd:TIGR02168 675 RRREIEELEEK--IEELEEKIAELEKALAELRKELEELEEELEQLRK---ELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 671 ARRRFLKLQQDQQEMELRRLDDEIGRKVYMRDREIAATARDLEMRQLELESQKRLYEK----------NLTENQEALAKE 740
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeltllneEAANLRERLESL 829
|
170
....*....|....*.
gi 1387845399 741 MRADADAYRRKVDLEE 756
Cdd:TIGR02168 830 ERRIAATERRLEDLEE 845
|
|
| TBC |
smart00164 |
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ... |
396-504 |
1.16e-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: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 396 AFP-FVKLFQNNQLIcFEVIATLIINWCQHWFEYFpnppinilsmienvLAFHDKELLQHFIDHDITSQLYAWPLLETVF 474
Cdd:smart00164 112 AFWcLVKLMERYGPN-FYLPDMSGLQLDLLQLDRL--------------VKEYDPDLYKHLKDLGITPSLYALRWFLTLF 176
|
90 100 110
....*....|....*....|....*....|
gi 1387845399 475 SEVLTREEWLKLFDNIFSNHPSFLLMTVVA 504
Cdd:smart00164 177 ARELPLEIVLRIWDVLFAEGSDFLFRVALA 206
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
585-818 |
3.57e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.44 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 585 QERERIRNDELDYLRErqtveDMQAKVDQQRVE----DEAWYQKQELLRKAEETRR-------EMLLQEEEKMIQQRQRL 653
Cdd:pfam12128 282 QETSAELNQLLRTLDD-----QWKEKRDELNGElsaaDAAVAKDRSELEALEDQHGafldadiETAAADQEQLPSWQSEL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 654 AAVKRELKVKEMHLQDAAR---RRFLKLQQDQQEmELRRLDDEIGRKVYMRDREIAATARDLEMRQLELESQKRLYEKNL 730
Cdd:pfam12128 357 ENLEERLKALTGKHQDVTAkynRRRSKIKEQNNR-DIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEF 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 731 TENQEALAK-----EMRADADAYRRKVDLEEHMFHKLIE-AGETQSQKTQKWKEAEGKEFRLRSAK-KAS-ALSDASRKW 802
Cdd:pfam12128 436 NEEEYRLKSrlgelKLRLNQATATPELLLQLENFDERIErAREEQEAANAEVERLQSELRQARKRRdQASeALRQASRRL 515
|
250
....*....|....*.
gi 1387845399 803 FLKQEINAAVEHAENP 818
Cdd:pfam12128 516 EERQSALDELELQLFP 531
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
10-51 |
3.68e-04 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 43.75 E-value: 3.68e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1387845399 10 TKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWDLDT 51
Cdd:COG2319 361 TGELLRTLTGHTGAVTSVAFSPDGRTLASGSADgTVRLWDLAT 403
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
602-801 |
3.92e-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: 43.68 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 602 QTVEDMQAK-VDQQRVEDEAWYQKQELL--RKAEETRREMLLQEEEKMIQQR----QRLAAVKRELKVKEMHLQDAARRR 674
Cdd:TIGR02794 33 GGAEIIQAVlVDPGAVAQQANRIQQQKKpaAKKEQERQKKLEQQAEEAEKQRaaeqARQKELEQRAAAEKAAKQAEQAAK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 675 FLKLQQDQQEMELRRLDDEIGRKvymrdREIAATARDLEM--RQLELESQKRLYEKNLTENQEALAK---EMRADADAyR 749
Cdd:TIGR02794 113 QAEEKQKQAEEAKAKQAAEAKAK-----AEAEAERKAKEEaaKQAEEEAKAKAAAEAKKKAEEAKKKaeaEAKAKAEA-E 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1387845399 750 RKVDLEehmfhkliEAGETQSQKTQKwKEAEGKEfRLRSAKKASALSDASRK 801
Cdd:TIGR02794 187 AKAKAE--------EAKAKAEAAKAK-AAAEAAA-KAEAEAAAAAAAEAERK 228
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
587-757 |
4.62e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 587 RERIRNDELDYL--------RERQTVEDMQAKVDQQRVEDEAwyQKQELLRKAEETRREMLLQEEEKMIQQrQRLAAVKR 658
Cdd:TIGR02168 219 KAELRELELALLvlrleelrEELEELQEELKEAEEELEELTA--ELQELEEKLEELRLEVSELEEEIEELQ-KELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 659 ELKVKEMHLQDA-ARRRFLKLQQDQQEMELRRLD---DEIGRKVYMRDREIAATARDLEMRQLELESQKRLYeknltENQ 734
Cdd:TIGR02168 296 EISRLEQQKQILrERLANLERQLEELEAQLEELEsklDELAEELAELEEKLEELKEELESLEAELEELEAEL-----EEL 370
|
170 180
....*....|....*....|...
gi 1387845399 735 EALAKEMRADADAYRRKVDLEEH 757
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLEL 393
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
588-775 |
5.20e-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: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 588 ERIRN--DELDYLRE-RQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREM----LLQEEEKMIQQRQRLAAVKREL 660
Cdd:COG4913 225 EAADAlvEHFDDLERaHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRaalrLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 661 KVKEmhlqdaARRRFLKLQQDQQEMELRRLDDEI----GRKVYMRDREIAATARDLEMRQLELESQKRLY---------- 726
Cdd:COG4913 305 ARLE------AELERLEARLDALREELDELEAQIrgngGDRLEQLEREIERLERELEERERRRARLEALLaalglplpas 378
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1387845399 727 EKNLTENQEAlAKEMRADADAYRRKVDLEEHMFHKLIEAGETQSQKTQK 775
Cdd:COG4913 379 AEEFAALRAE-AAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
592-746 |
5.67e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 592 NDELDYLRERQTvedmQAKVDQQRVEDEAWYQKQELLRKAEE--TRREMLLQEEEKMIQQRQRLAAVKRELKVKEMHLQD 669
Cdd:COG4372 44 QEELEQLREELE----QAREELEQLEEELEQARSELEQLEEEleELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387845399 670 AARRRFlklQQDQQEMELRRLDDEIGRKVYMRDREIAATARDLEMRQLELESQKRLYEKNLTENQEALAKEMRADAD 746
Cdd:COG4372 120 LQKERQ---DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEAN 193
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
584-816 |
1.09e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.55 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 584 TQERERIRNDeldylRERQTvEDMQAKVDQQRVEDEAwYQKQEL--LRKAEETRREMLLQEEEKMIQQRQRLAAvkrelk 661
Cdd:COG2268 198 IRDARIAEAE-----AERET-EIAIAQANREAEEAEL-EQEREIetARIAEAEAELAKKKAEERREAETARAEA------ 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 662 vkemhlqDAArrrfLKLQQDQQEMELRRlDDEIGRkvymRDREIAATARDLEMRQLELESQKRLyeknltenqealakem 741
Cdd:COG2268 265 -------EAA----YEIAEANAEREVQR-QLEIAE----REREIELQEKEAEREEAELEADVRK---------------- 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387845399 742 RADADAYRRKVDleehmfhkliEAGETQSQKTQKWKEAEGKEfrlrsaKKASALSDASRKWFLKQEINAAVEHAE 816
Cdd:COG2268 313 PAEAEKQAAEAE----------AEAEAEAIRAKGLAEAEGKR------ALAEAWNKLGDAAILLMLIEKLPEIAE 371
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
11-48 |
1.26e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 37.32 E-value: 1.26e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1387845399 11 KELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWD 48
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDgTVKVWD 39
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
579-753 |
1.27e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 579 IVDYQTQERERIrnDELDYLRE--RQTVEDMQAKVDqqRVED--EAWYQKQELLRKAE------ETRREMLLQEEEKMIQ 648
Cdd:PRK02224 466 HVETIEEDRERV--EELEAELEdlEEEVEEVEERLE--RAEDlvEAEDRIERLEERREdleeliAERRETIEEKRERAEE 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 649 QRQRL------AAVKRELKVKEMHLQDAARRRFLKLQQDQQEmelrrLDDEIGR--KVYMRDREIAATARDLEMRQ---- 716
Cdd:PRK02224 542 LRERAaeleaeAEEKREAAAEAEEEAEEAREEVAELNSKLAE-----LKERIESleRIRTLLAAIADAEDEIERLRekre 616
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1387845399 717 ----LELESQKRLYEKN---------LTENQEALAKEMRADADAYRRKVD 753
Cdd:PRK02224 617 alaeLNDERRERLAEKRerkreleaeFDEARIEEAREDKERAEEYLEQVE 666
|
|
| vATP-synt_E |
pfam01991 |
ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as ... |
608-733 |
1.33e-03 |
|
ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as well as the archaebacterial ATP synthase E subunit.
Pssm-ID: 396537 [Multi-domain] Cd Length: 199 Bit Score: 40.83 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 608 QAKVD--QQRVEDEAWYQKQELLRKAEE---TRREMLLQEEEkMIQQRQR----LAAVKRELKVKEMHLQDA---ARRRF 675
Cdd:pfam01991 7 EEKAEeiRAKAEEEFAIEKAELVQEAEEkidEIYEKKEKQAE-MQKKIIIsnakNEARLKVLEAREEILDEVfneAEKKL 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387845399 676 LKLQQDQQEME--LRRLDDEIGRK-------VYMR--DREIAATARDLEMRQLELESQKRLYEKNLTEN 733
Cdd:pfam01991 86 AELEEDTDEYKdlLRKLIVQALVKlgepeviVRCRkrDEELVESALDKAAEEYKAKTKKVTVEKAGDEN 154
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
619-774 |
1.58e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 619 EAWYQKQELLRKAEETR--------REMLLQEEEKMIQQRQRLAAVKREL-KVKEMHLQDAArrrFLKLQQDQQEMELRR 689
Cdd:PRK04863 493 EAWDVARELLRRLREQRhlaeqlqqLRMRLSELEQRLRQQQRAERLLAEFcKRLGKNLDDED---ELEQLQEELEARLES 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 690 LDDEIgrkvymrdREIAATARDLEMRQLELESQKRLYEKNLTE---NQEALAK--EMRADADAYRRkvDLEEHMFHKLIE 764
Cdd:PRK04863 570 LSESV--------SEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARlrEQSGEEFEDSQ--DVTEYMQQLLER 639
|
170
....*....|
gi 1387845399 765 AGETQSQKTQ 774
Cdd:PRK04863 640 ERELTVERDE 649
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
585-801 |
1.83e-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: 42.35 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 585 QERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQR-----QRLAAVKRE 659
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKleelkEELESLEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 660 LKVKEMHLQDAARRrflkLQQDQQEMELRRlddeigRKVYMRDREIAATARDLEMRQLELESQKRLYEKNLTENQEALAK 739
Cdd:TIGR02168 360 LEELEAELEELESR----LEELEEQLETLR------SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387845399 740 EMRADADAYRRKVDLEEHMFHKLIEAGETqsqktqkwKEAEGKEFRLRSAKKASALSDASRK 801
Cdd:TIGR02168 430 LEEAELKELQAELEELEEELEELQEELER--------LEEALEELREELEEAEQALDAAERE 483
|
|
| Pinin_SDK_memA |
pfam04696 |
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ... |
623-742 |
2.18e-03 |
|
pinin/SDK/memA/ protein conserved region; Members of this family have very varied localizations within the eukaryotic cell. pinin is known to localize at the desmosomes and is implicated in anchoring intermediate filaments to the desmosomal plaque. SDK2/3 is a dynamically localized nuclear protein thought to be involved in modulation of alternative pre-mRNA splicing. memA is a tumour marker preferentially expressed in human melanoma cell lines. A common feature of the members of this family is that they may all participate in regulating protein-protein interactions.
Pssm-ID: 461396 [Multi-domain] Cd Length: 130 Bit Score: 39.20 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 623 QKQELLRKAEETRREMLLQE-EEKMIQQRQRLAAVKRElkvkemhlqdaaRRRFLKLQQDQQEMELRRLDDEIGRKVYMR 701
Cdd:pfam04696 22 KKEESKQKEKEERRAEIEKRlEEKAKQEKEELEERKRE------------EREELFEERRAEQIELRALEEKLELKELME 89
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1387845399 702 DREiaaTARDLEMRQLELESQKRLY--EKNLTENQEALAKEMR 742
Cdd:pfam04696 90 TWH---ENLKALANFLKTKTEPPIYylPWKLTEKTEELLEEQI 129
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
598-801 |
2.74e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.74 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 598 LRERQTVEDmQAKVDQQRVEDEAWYQKQELLRK-AEETRRemlLQEE--EKMIQQRQRLaavKREL----KVKEMHL-QD 669
Cdd:NF041483 78 LRNAQIQAD-QLRADAERELRDARAQTQRILQEhAEHQAR---LQAElhTEAVQRRQQL---DQELaerrQTVESHVnEN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 670 AARRRFLKLQQDQQEmelRRLDDEiGRKvymrDREIAATARDLEMRQLELESQKRLYEKNLTENQEALAKEMRADADAYR 749
Cdd:NF041483 151 VAWAEQLRARTESQA---RRLLDE-SRA----EAEQALAAARAEAERLAEEARQRLGSEAESARAEAEAILRRARKDAER 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1387845399 750 rkvdleehmfhkLIEAGETQSQktqkwkEAEGKEFRLRSAkkASALSDASRK 801
Cdd:NF041483 223 ------------LLNAASTQAQ------EATDHAEQLRSS--TAAESDQARR 254
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
630-780 |
2.90e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.09 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 630 KAEETRREMLLQEEEKMIQQRQRL---AAVKRELKVKEMHLQDAARRRflkLQQDQQEMElRRLDDEIGRKVYMRDREIA 706
Cdd:pfam15709 315 RSEEDPSKALLEKREQEKASRDRLraeRAEMRRLEVERKRREQEEQRR---LQQEQLERA-EKMREELELEQQRRFEEIR 390
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387845399 707 atardLEMRQLELESQKRLYEKNLTENQEALAKE-MRADADAYRRKvdLEEHMFHKLIEAGETQSQKTQKWKEAE 780
Cdd:pfam15709 391 -----LRKQRLEEERQRQEEEERKQRLQLQAAQErARQQQEEFRRK--LQELQRKKQQEEAERAEAEKQRQKELE 458
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
585-727 |
3.40e-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: 40.67 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 585 QERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQEL-----LRKAEETRREMLLQEEEKMIQQRQRLAAVKRE 659
Cdd:pfam13868 193 QEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQelqqaREEQIELKERRLAEEAEREEEEFERMLRKQAE 272
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387845399 660 LKVKEMHLQDAARRRFLKLQQD-QQEMELRRLDDEIGRKVYMRDREIAATARDLEMRQLELESQKRLYE 727
Cdd:pfam13868 273 DEEIEQEEAEKRRMKRLEHRRElEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
568-882 |
3.71e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.22 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 568 QYPVFNQYPKFIVDYQTQERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAwyQKQELLRKAE---------ETRREM 638
Cdd:COG5022 783 LRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRET--EEVEFSLKAEvliqkfgrsLKAKKR 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 639 --LLQEEEKMIQQRQRLAAVKRELKVKEmhlQDAARRRFLKLQQDQQEMELRRL----DDEIGRKVYMRDREIAATARDL 712
Cdd:COG5022 861 fsLLKKETIYLQSAQRVELAERQLQELK---IDVKSISSLKLVNLELESEIIELkkslSSDLIENLEFKTELIARLKKLL 937
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 713 EMRQLELESQKRLYEKNLTENQEALAKEMRADADAYRRKVDLEEhmfhKLIEAGETQSQKTQKWKeAEGKEFRlrsaKKA 792
Cdd:COG5022 938 NNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKST----ILVREGNKANSELKNFK-KELAELS----KQY 1008
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 793 SALSDASRKWFLKQEINAAVEHAENPCHKEEPRFQNEQDSSCLPRTSQLNDSSEMDPSTQISLNRRAVEWDTTGQNLIKK 872
Cdd:COG5022 1009 GALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLES 1088
|
330
....*....|
gi 1387845399 873 VRNLRQRLTA 882
Cdd:COG5022 1089 TENLLKTINV 1098
|
|
| COG5210 |
COG5210 |
GTPase-activating protein [General function prediction only]; |
437-553 |
3.81e-03 |
|
GTPase-activating protein [General function prediction only];
Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 40.94 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 437 LSMIENVLAFHDKELLQHFIDHDITSQLYAWPLLETVFSEVLTREEWLKLFDNIFSNHPSFLLMTVVAYNICSRTPLLSC 516
Cdd:COG5210 350 LKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKL 429
|
90 100 110
....*....|....*....|....*....|....*..
gi 1387845399 517 NLKDDFEFFFHHRNNLDINVVIRQVYHLMETTPTDIH 553
Cdd:COG5210 430 DSDELLDLLLKQLFLHSGKEAWSSILKFRHGTDRDIL 466
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
617-804 |
3.84e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 617 EDEAWYQKQELLRKAEETRREmLLQEEEKMIQQRQRLAAVKRELKVKEMHLQDAARRRFLKLQQDQQEMELRRLDDEIgR 696
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERL-E 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 697 KVYMRDREIAATARDLEMRQLELESQKRLYEKNLTENQEALAKEMRADADAYRRkvdLEEHMFHKLIEAGETQSQKTQKW 776
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE---LQQRLAELEEELEEAQEELEELE 226
|
170 180
....*....|....*....|....*...
gi 1387845399 777 KEAEGKEFRLRSAKKASALSDASRKWFL 804
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARLLLLI 254
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
577-727 |
3.92e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 577 KFIVDYQTQERERIRNDELdyLRERQTVEDMQAKVDQQRVEDEAWYQKQEL-LRKAEET---RREMLLQEEEKMIQQRQR 652
Cdd:PRK12704 41 KRILEEAKKEAEAIKKEAL--LEAKEEIHKLRNEFEKELRERRNELQKLEKrLLQKEENldrKLELLEKREEELEKKEKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 653 LAAVKRELKVKEMHLQDAARRRFLKLQQ-------DQQEMELRRLDDEIgrkvymrDREIAATARDLEMrQLELESQKRL 725
Cdd:PRK12704 119 LEQKQQELEKKEEELEELIEEQLQELERisgltaeEAKEILLEKVEEEA-------RHEAAVLIKEIEE-EAKEEADKKA 190
|
..
gi 1387845399 726 YE 727
Cdd:PRK12704 191 KE 192
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
583-698 |
4.19e-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: 40.29 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 583 QTQERERIRNDELDYLRERQTVEDMQAKvDQQRVEDEAWYQKQeLLRKAEETRREMLLQEEEKMIQQR-----QRLAAVK 657
Cdd:pfam13868 225 EEAEKKARQRQELQQAREEQIELKERRL-AEEAEREEEEFERM-LRKQAEDEEIEQEEAEKRRMKRLEhrrelEKQIEER 302
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1387845399 658 RELKVKEMhlqdAARRRFLKLQQDQQEMELRRLDDEIGRKV 698
Cdd:pfam13868 303 EEQRAAER----EEELEEGERLREEEAERRERIEEERQKKL 339
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
583-749 |
4.44e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 583 QTQERERIRNDELDYLRERQT---VEDMQAKVDQQRVEDEAWYQKqelLRKAEETR---REMLLQEEEKMIQQRQRLAAV 656
Cdd:COG3096 948 EQQRRLKQQIFALSEVVQRRPhfsYEDAVGLLGENSDLNEKLRAR---LEQAEEARreaREQLRQAQAQYSQYNQVLASL 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 657 KRELKVKEMHLQDaarrrflkLQQDQQEMELrRLDDEIGRKVYMRDREIAATARDLEMRQLELESQKRLYEKnlteNQEA 736
Cdd:COG3096 1025 KSSRDAKQQTLQE--------LEQELEELGV-QADAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEA----EMDS 1091
|
170
....*....|...
gi 1387845399 737 LAKEMRADADAYR 749
Cdd:COG3096 1092 LQKRLRKAERDYK 1104
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
639-749 |
4.53e-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: 40.52 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 639 LLQEEEKMIQQRQRLAAVKRELKVKEMHLQDAARrrflklQQDQQEMELRRLDDEIGRKVyMRDREIAATARDLEMRQLE 718
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKK------EEKALLKQLAALERRIAALA-RRIRALEQELAALEAELAE 87
|
90 100 110
....*....|....*....|....*....|.
gi 1387845399 719 LESQKRLYEKNLTENQEALAKEMRAdadAYR 749
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRA---LYR 115
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
633-880 |
5.17e-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: 40.26 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 633 ETRREMLLQEEEKMIQQRQRLAAVKRELKVKEMHLQDAARRRFLKLQ-----QDQQEMELRRLDDEIGRkvyMRDREIAA 707
Cdd:pfam07888 149 ETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQelrnsLAQRDTQVLQLQDTITT---LTQKLTTA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 708 TARDLEMRQL--ELES-QKRLyekNLTENQEALAKEMRADADAYRRKVDLEEHmfHKLIEAGETQSQKTQ---KWKEAEG 781
Cdd:pfam07888 226 HRKEAENEALleELRSlQERL---NASERKVEGLGEELSSMAAQRDRTQAELH--QARLQAAQLTLQLADaslALREGRA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 782 KEFRLRSAKKASALSDASRkwflKQEINAAVEHAENPCHKE-------EPRFQNEQDSSCLPRTSQLNDSSEMDPSTQIs 854
Cdd:pfam07888 301 RWAQERETLQQSAEADKDR----IEKLSAELQRLEERLQEErmereklEVELGREKDCNRVQLSESRRELQELKASLRV- 375
|
250 260
....*....|....*....|....*.
gi 1387845399 855 LNRRAVEWDTTGQNLIKKVRNLRQRL 880
Cdd:pfam07888 376 AQKEKEQLQAEKQELLEYIRQLEQRL 401
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
614-757 |
5.23e-03 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 39.37 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 614 QRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKEMHLQdaARRRFLKLQQdQQEMELRRLDDE 693
Cdd:pfam14988 17 QKKIEKLWNQYVQECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQ--ALRPFAKLKE-SQEREIQDLEEE 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387845399 694 IgRKVymrDREIAATARDLEMRQLELES--QKRLYEKNLTENQEALAKEMRADADAYRR--KVDLEEH 757
Cdd:pfam14988 94 K-EKV---RAETAEKDREAHLQFLKEKAllEKQLQELRILELGERATRELKRKAQALKLaaKQALSEF 157
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
585-794 |
6.34e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.58 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 585 QERERIRNDELDYLRE-RQTVEDMQAkvDQQRVEDEAWYQKQELLRKAEETRREML-----LQEeekmiQQRQRLAAvkr 658
Cdd:NF041483 728 QERERAREQSEELLASaRKRVEEAQA--EAQRLVEEADRRATELVSAAEQTAQQVRdsvagLQE-----QAEEEIAG--- 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 659 eLKVKEMHLQDAARRrflklqQDQQEMELRRLDDEIGRKvymRDREIAATARdlEMRQLELESQKRLYEKNLTEnQEALA 738
Cdd:NF041483 798 -LRSAAEHAAERTRT------EAQEEADRVRSDAYAERE---RASEDANRLR--REAQEETEAAKALAERTVSE-AIAEA 864
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387845399 739 KEMRADADAYRRKVDLEEhmfHKLIEAGETQSQKTQkwKEAEGKEFRLRSAKKASA 794
Cdd:NF041483 865 ERLRSDASEYAQRVRTEA---SDTLASAEQDAARTR--ADAREDANRIRSDAAAQA 915
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
608-690 |
7.33e-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: 39.48 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 608 QAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKEMHLQDAARRRFLKLQQDQQEMEL 687
Cdd:cd16269 208 EAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEI 287
|
...
gi 1387845399 688 RRL 690
Cdd:cd16269 288 RSL 290
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
583-794 |
7.67e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 40.02 E-value: 7.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 583 QTQERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQE---LLRKAEETRREMLLQEEekmiQQRQRLAAVKRE 659
Cdd:COG3064 11 EAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEeeaREAKAEAEQRAAELAAE----AAKKLAEAEKAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 660 LKVKEMHLQDAARrrflKLQQDQQEMELRRLDDEIGRKvymRDREIAATARdlEMRQLELESQKRLYEKNLTENQEALAK 739
Cdd:COG3064 87 AEAEKKAAAEKAK----AAKEAEAAAAAEKAAAAAEKE---KAEEAKRKAE--EEAKRKAEEERKAAEAEAAAKAEAEAA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1387845399 740 EMRADADAYRRKVDLEEHMFHKLIEAGETQSQKTQKWKEAEGKEFRLRSAKKASA 794
Cdd:COG3064 158 RAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAA 212
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
586-739 |
7.93e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 586 ERERIRNDELDYLRERQTVEDmQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKEm 665
Cdd:COG4717 312 ALEELEEEELEELLAALGLPP-DLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRA- 389
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387845399 666 HLQDAARRRFLKLQQDQQEMELRRLDDEIGRKVYMRDREiaatarDLEMRQLELESQKRLYEKNLTENQEALAK 739
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE------ELEEELEELEEELEELEEELEELREELAE 457
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
601-818 |
7.94e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 39.64 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 601 RQTVEDMQAKV-DQQRVEDeawyQKQELLRKAEETRREMLLQEEEKMIQQRQRLAA------VKRELKVKEMHLQDAARR 673
Cdd:COG3064 2 QEALEEKAAEAaAQERLEQ----AEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAeeeareAKAEAEQRAAELAAEAAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 674 RFLKLQQDQQEMElRRLDDEigrkvymRDREIAATARDLEMRQLELESQKRLYEknltENQEALAKEMRADADAYRRKVD 753
Cdd:COG3064 78 KLAEAEKAAAEAE-KKAAAE-------KAKAAKEAEAAAAAEKAAAAAEKEKAE----EAKRKAEEEAKRKAEEERKAAE 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387845399 754 LEEHMFHKLIEAGETQSQKTQKWKEAEGKEFRLRSAKKASALSDASRKWFLKQEINAAVEHAENP 818
Cdd:COG3064 146 AEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAA 210
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
599-756 |
8.17e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 599 RERQTVEDMQAKVDQQRVEDEawyQKQELLRKAEETRREMLLQEEEKMI---QQRQRLAAVKRELKVKEMHLQDAARRrf 675
Cdd:pfam01576 152 KERKLLEERISEFTSNLAEEE---EKAKSLSKLKNKHEAMISDLEERLKkeeKGRQELEKAKRKLEGESTDLQEQIAE-- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 676 LKLQQDQQEMELRRLDDEIGRKVYMRDREiaATARDLEMRQL-ELESQkrlyeknLTENQEALAKEMRADADAYRRKVDL 754
Cdd:pfam01576 227 LQAQIAELRAQLAKKEEELQAALARLEEE--TAQKNNALKKIrELEAQ-------ISELQEDLESERAARNKAEKQRRDL 297
|
..
gi 1387845399 755 EE 756
Cdd:pfam01576 298 GE 299
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
581-743 |
8.29e-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: 39.10 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 581 DYQTQERERIRNDEL--DYLRERQTVEDMQAKVDQQRVEDE----AWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLA 654
Cdd:cd16269 157 KYRQVPRKGVKAEEVlqEFLQSKEAEAEAILQADQALTEKEkeieAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845399 655 AVKRELKVKemhlqdaarrrflklqqdqQEMELRRLDDEIGRkvymrdreiaatardleMRQLELESQKRLYEKNLTENQ 734
Cdd:cd16269 237 EHLRQLKEK-------------------MEEERENLLKEQER-----------------ALESKLKEQEALLEEGFKEQA 280
|
....*....
gi 1387845399 735 EALAKEMRA 743
Cdd:cd16269 281 ELLQEEIRS 289
|
|
| |
