|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
44-340 |
1.93e-28 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 118.86 E-value: 1.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 44 RFLNVAFDGTGDCLIAGDHQGNIYVFDL-HGNRFNLVQRTAQACTALAFNLRRKSeFLVALADYSIKCFDTVTKELVSWM 122
Cdd:COG2319 80 AVLSVAFSPDGRLLASASADGTVRLWDLaTGLLLRTLTGHTGAVRSVAFSPDGKT-LASGSADGTVRLWDLATGKLLRTL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 123 RGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLF 201
Cdd:COG2319 159 TGHSGAVTSVAFSPDGKLLASGSDDgTVRLWDLATGKLLRTLTGHTG-AVRSVAFSPDGKLLASGSADGTVRLWDLATGK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 202 CKYQLPAPPES-SSIlykvfAVTRDGRILAAGGKSNHLHLWCLEARQLFRIIQMPTkvRAIRHLEFLPDSfdagsnQVLG 280
Cdd:COG2319 238 LLRTLTGHSGSvRSV-----AFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHS--GGVNSVAFSPDG------KLLA 304
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 281 VLSQDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYIASIMENGSLNIYSVQALTQ 340
Cdd:COG2319 305 SGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
39-334 |
1.69e-26 |
|
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: 110.50 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 39 HPKVLRFlnVAFDGTGDCLIAGDHQGNIYVFDLHGNRFNLVQR----TAQACTALAFNLRrkseFLVALADYSIKCFDTV 114
Cdd:cd00200 8 HTGGVTC--VAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKghtgPVRDVAASADGTY----LASGSSDKTIRLWDLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 115 TKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 193
Cdd:cd00200 82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDkTIKVWDVETGKCLTTLRGHTD-WVNSVAFSPDGTFVASSSQDGTIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 194 AWECDTLFCKYQLPAPPESssilykVFAVT--RDGRILAAGGKSNHLHLWCLEARQLFRiiQMPTKVRAIRHLEFLPDsf 271
Cdd:cd00200 161 LWDLRTGKCVATLTGHTGE------VNSVAfsPDGEKLLSSSSDGTIKLWDLSTGKCLG--TLRGHENGVNSVAFSPD-- 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387845401 272 dagsNQVLGVLSQDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYIASIMENGSLNIYS 334
Cdd:cd00200 231 ----GYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
684-967 |
6.21e-11 |
|
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: 66.30 E-value: 6.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 684 IVDYQTQERERIRNDELDYL---RERQTVEDMQAKVDQQRVEDEAwyqkqELLRKAEETRREMLLQEEEKMIQQRQR--- 757
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMeqeRLRQEKEEKAREVERRRKLEEA-----EKARQAEMDRQAAIYAEQERMAMERERele 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 758 ---LAAVKREL---KVKEMHLQDAARRRFLKLQQD-QQEMELRRLDDEIGRKVYMRDREiaatardlemRQLELESQKRL 830
Cdd:pfam17380 352 rirQEERKRELeriRQEEIAMEISRMRELERLQMErQQKNERVRQELEAARKVKILEEE----------RQRKIQQQKVE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 831 YEKNLTENQEALAKEMRADADAYRR---KVDLEEHMFHKLIEAGETQSQKTQKWKEAEGKEfrlrsaKKASALSDASRKW 907
Cdd:pfam17380 422 MEQIRAEQEEARQREVRRLEEERARemeRVRLEEQERQQQVERLRQQEEERKRKKLELEKE------KRDRKRAEEQRRK 495
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387845401 908 FLKQEINAavehaenpchkvtavvslRRGDLDTDTHREKMIRR--PRRKAAIYKP-RRENAEE 967
Cdd:pfam17380 496 ILEKELEE------------------RKQAMIEEERKRKLLEKemEERQKAIYEEeRRREAEE 540
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
688-916 |
6.43e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 6.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 688 QTQERERIRNDELDYL-----RERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVK 762
Cdd:COG1196 285 EAQAEEYELLAELARLeqdiaRLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 763 RELKVKEMHLQDAARRRfLKLQQDQQEMELRRLDDEIgrkvymRDREIAATARDLEMRQLELESQKRLYEKNLTENQEAL 842
Cdd:COG1196 365 EALLEAEAELAEAEEEL-EELAEELLEALRAAAELAA------QLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387845401 843 AKEMRADADAYRRKVDLEEHmfhkliEAGETQSQKTQKWKEAEGKEfrLRSAKKASALSDASRKWFLKQEINAA 916
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEE------EEALLELLAELLEEAALLEA--ALAELLEELAEAAARLLLLLEAEADY 503
|
|
| RabGAP-TBC |
pfam00566 |
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ... |
462-605 |
1.18e-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: 55.72 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 462 LQKKYPIKSRKLLRVLQRTLSALAHWsviFSDTPY---LPLLAFPFVkLFQNNQLICFEVIATLIINwcQHWFEYFPN-- 536
Cdd:pfam00566 20 FPHSFFFDNGPGQNSLRRILKAYSIY---NPDVGYcqgMNFIAAPLL-LVYLDEEDAFWCFVSLLEN--YLLRDFYTPdf 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 537 PPINILSMI-ENVLAFHDKELLQHFIDHDITSQLYAWPLLETVFSEVLTREEWLKLFDNIFSNHPSFLLM 605
Cdd:pfam00566 94 PGLKRDLYVfEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVLF 163
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
693-971 |
6.82e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 6.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 693 ERIRNDELDYLRERQTVEDMQaKVDQQRVEDE---AWYQKQELLRKAEETRRE--MLLQEEEKMIQQRQRLAAVKRELKV 767
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAEEKK-KAEEAKKAEEdknMALRKAEEAKKAEEARIEevMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 768 KEMHLQDAARRRFLKLQQDQQE-----MELRRLDDEIGrkvyMRDREIAATARDlEMRQLElESQKRLYEKNLTENQEAL 842
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEekkkaEELKKAEEENK----IKAAEEAKKAEE-DKKKAE-EAKKAEEDEKKAAEALKK 1696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 843 AKEMRADADAYRRKVDLEEHMFHKLIEAGETQSQKTQKWKEAEGKEFRlrsaKKASALSDASRKWFLKQEINAAVEHAEN 922
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK----KAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1387845401 923 PCHKVTAVVS--LRRGDLDTDTHREKMIRRPRRKAAIYKprrENAEETNPV 971
Cdd:PTZ00121 1773 IRKEKEAVIEeeLDEEDEKRRMEVDKKIKDIFDNFANII---EGGKEGNLV 1820
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
690-921 |
1.41e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 690 QERERIRNdELDYLreRQTVEDMQAKVDQQRVEdeawyqkQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKE 769
Cdd:TIGR02169 695 SELRRIEN-RLDEL--SQELSDASRKIGEIEKE-------IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 770 MHLQDaARRRFLKLQQDQQEMElRRLDDEIGRKVYMRDREIAATARDLEMRQLELES--QKRLYEKnltenqeALAKEMR 847
Cdd:TIGR02169 765 ARIEE-LEEDLHKLEEALNDLE-ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQklNRLTLEK-------EYLEKEI 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 848 ADADAYRRKVDLEEHMFHKLIEAGETQSQKT-QKWKEAEGKEFRLRSAKKA---------SALSDASRKwflKQEINAAV 917
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELeEELEELEAALRDLESRLGDlkkerdeleAQLRELERK---IEELEAQI 912
|
....
gi 1387845401 918 EHAE 921
Cdd:TIGR02169 913 EKKR 916
|
|
| TBC |
smart00164 |
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ... |
501-609 |
7.78e-05 |
|
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: 44.99 E-value: 7.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 501 AFP-FVKLFQNNQLIcFEVIATLIINWCQHWFEYFpnppinilsmienvLAFHDKELLQHFIDHDITSQLYAWPLLETVF 579
Cdd:smart00164 112 AFWcLVKLMERYGPN-FYLPDMSGLQLDLLQLDRL--------------VKEYDPDLYKHLKDLGITPSLYALRWFLTLF 176
|
90 100 110
....*....|....*....|....*....|
gi 1387845401 580 SEVLTREEWLKLFDNIFSNHPSFLLMTVVA 609
Cdd:smart00164 177 ARELPLEIVLRIWDVLFAEGSDFLFRVALA 206
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
115-153 |
7.78e-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: 7.78e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1387845401 115 TKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWD 153
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDgTIKLWD 40
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
703-906 |
1.10e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.89 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 703 LRERQTVEDmQAKVDQQRVEDEAWYQKQELLRK-AEETRRemlLQEE--EKMIQQRQRLaavKREL----KVKEMHL-QD 774
Cdd:NF041483 78 LRNAQIQAD-QLRADAERELRDARAQTQRILQEhAEHQAR---LQAElhTEAVQRRQQL---DQELaerrQTVESHVnEN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 775 AARRRFLKLQQDQQEmelRRLDDEiGRKvymrDREIAATARDLEMRQLELESQKRLYEKNLTENQEALAKEMRADADAYR 854
Cdd:NF041483 151 VAWAEQLRARTESQA---RRLLDE-SRA----EAEQALAAARAEAERLAEEARQRLGSEAESARAEAEAILRRARKDAER 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1387845401 855 rkvdleehmfhkLIEAGETQSQktqkwkEAEGKEFRLRSAkkASALSDASRK 906
Cdd:NF041483 223 ------------LLNAASTQAQ------EATDHAEQLRSS--TAAESDQARR 254
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
116-153 |
1.38e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 37.32 E-value: 1.38e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1387845401 116 KELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWD 153
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDgTVKVWD 39
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
690-966 |
1.54e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 690 QERERIRNDELDYLRE-RQTVEDMQAkvDQQRVEDEAWYQKQELLRKAEETRREML-----LQEeekmiQQRQRLAAvkr 763
Cdd:NF041483 728 QERERAREQSEELLASaRKRVEEAQA--EAQRLVEEADRRATELVSAAEQTAQQVRdsvagLQE-----QAEEEIAG--- 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 764 eLKVKEMHLQDAARRrflklqQDQQEMELRRLDDEIGRKvymRDREIAATARdlEMRQLELESQKRLYEKNLTEnQEALA 843
Cdd:NF041483 798 -LRSAAEHAAERTRT------EAQEEADRVRSDAYAERE---RASEDANRLR--REAQEETEAAKALAERTVSE-AIAEA 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 844 KEMRADADAYRRKVDLEEhmfHKLIEAGETQSQKTQkwKEAEGKEFRLRSAKKASA---LSDASRKWFLKQEinAAVEHA 920
Cdd:NF041483 865 ERLRSDASEYAQRVRTEA---SDTLASAEQDAARTR--ADAREDANRIRSDAAAQAdrlIGEATSEAERLTA--EARAEA 937
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1387845401 921 ENPCHKVTAVVSLRRGdlDTDTHREKMIRRPRRKAAiyKPRRENAE 966
Cdd:NF041483 938 ERLRDEARAEAERVRA--DAAAQAEQLIAEATGEAE--RLRAEAAE 979
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
686-848 |
2.42e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.02 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 686 DYQTQERERIRNDEL--DYLRERQTVEDMQAKVDQQRVEDE----AWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLA 759
Cdd:cd16269 157 KYRQVPRKGVKAEEVlqEFLQSKEAEAEAILQADQALTEKEkeieAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 760 AVKRELKvKEMhlqdaarrrflklqqdqqEMELRRLDDEIGRkvymrdreiaatardleMRQLELESQKRLYEKNLTENQ 839
Cdd:cd16269 237 EHLRQLK-EKM------------------EEERENLLKEQER-----------------ALESKLKEQEALLEEGFKEQA 280
|
....*....
gi 1387845401 840 EALAKEMRA 848
Cdd:cd16269 281 ELLQEEIRS 289
|
|
| COG5210 |
COG5210 |
GTPase-activating protein [General function prediction only]; |
542-658 |
3.15e-03 |
|
GTPase-activating protein [General function prediction only];
Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 41.33 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 542 LSMIENVLAFHDKELLQHFIDHDITSQLYAWPLLETVFSEVLTREEWLKLFDNIFSNHPSFLLMTVVAYNICSRTPLLSC 621
Cdd:COG5210 350 LKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKL 429
|
90 100 110
....*....|....*....|....*....|....*..
gi 1387845401 622 NLKDDFEFFFHHRNNLDINVVIRQVYHLMETTPTDIH 658
Cdd:COG5210 430 DSDELLDLLLKQLFLHSGKEAWSSILKFRHGTDRDIL 466
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
44-340 |
1.93e-28 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 118.86 E-value: 1.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 44 RFLNVAFDGTGDCLIAGDHQGNIYVFDL-HGNRFNLVQRTAQACTALAFNLRRKSeFLVALADYSIKCFDTVTKELVSWM 122
Cdd:COG2319 80 AVLSVAFSPDGRLLASASADGTVRLWDLaTGLLLRTLTGHTGAVRSVAFSPDGKT-LASGSADGTVRLWDLATGKLLRTL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 123 RGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLF 201
Cdd:COG2319 159 TGHSGAVTSVAFSPDGKLLASGSDDgTVRLWDLATGKLLRTLTGHTG-AVRSVAFSPDGKLLASGSADGTVRLWDLATGK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 202 CKYQLPAPPES-SSIlykvfAVTRDGRILAAGGKSNHLHLWCLEARQLFRIIQMPTkvRAIRHLEFLPDSfdagsnQVLG 280
Cdd:COG2319 238 LLRTLTGHSGSvRSV-----AFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHS--GGVNSVAFSPDG------KLLA 304
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 281 VLSQDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYIASIMENGSLNIYSVQALTQ 340
Cdd:COG2319 305 SGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
48-336 |
3.63e-28 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 118.09 E-value: 3.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 48 VAFDGTGDCLIAGDHQGNIYVFDLH-GNRFNLVQRTAQACTALAFNlrRKSEFLV-ALADYSIKCFDTVTKELVSWMRGH 125
Cdd:COG2319 126 VAFSPDGKTLASGSADGTVRLWDLAtGKLLRTLTGHSGAVTSVAFS--PDGKLLAsGSDDGTVRLWDLATGKLLRTLTGH 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 126 ESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLFCKY 204
Cdd:COG2319 204 TGAVRSVAFSPDGKLLASGSADgTVRLWDLATGKLLRTLTGHSG-SVRSVAFSPDGRLLASGSADGTVRLWDLATGELLR 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 205 QLPAPPES-SSIlykvfAVTRDGRILAAGGKSNHLHLWCLEARQLFRIIQMPTkvRAIRHLEFLPDsfdagsNQVLGVLS 283
Cdd:COG2319 283 TLTGHSGGvNSV-----AFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHT--GAVRSVAFSPD------GKTLASGS 349
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1387845401 284 QDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYIASIMENGSLNIYSVQ 336
Cdd:COG2319 350 DDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
39-334 |
1.69e-26 |
|
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: 110.50 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 39 HPKVLRFlnVAFDGTGDCLIAGDHQGNIYVFDLHGNRFNLVQR----TAQACTALAFNLRrkseFLVALADYSIKCFDTV 114
Cdd:cd00200 8 HTGGVTC--VAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKghtgPVRDVAASADGTY----LASGSSDKTIRLWDLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 115 TKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 193
Cdd:cd00200 82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDkTIKVWDVETGKCLTTLRGHTD-WVNSVAFSPDGTFVASSSQDGTIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 194 AWECDTLFCKYQLPAPPESssilykVFAVT--RDGRILAAGGKSNHLHLWCLEARQLFRiiQMPTKVRAIRHLEFLPDsf 271
Cdd:cd00200 161 LWDLRTGKCVATLTGHTGE------VNSVAfsPDGEKLLSSSSDGTIKLWDLSTGKCLG--TLRGHENGVNSVAFSPD-- 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387845401 272 dagsNQVLGVLSQDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYIASIMENGSLNIYS 334
Cdd:cd00200 231 ----GYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
49-336 |
1.13e-21 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 98.83 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 49 AFDGTGDCLIAGDHQGNIYVFDLHGNRFNLVQRTAQACTALAFNLRRKSEFLVALADYSIKCFDTVTKELVSWMRGHESS 128
Cdd:COG2319 1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 129 VFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLFCKYQLP 207
Cdd:COG2319 81 VLSVAFSPDGRLLASASADgTVRLWDLATGLLLRTLTGHTG-AVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 208 APPES-SSIlykvfAVTRDGRILAAGGKSNHLHLWCLEARQLFRIIQMPTkvRAIRHLEFLPDSfdagsnQVLGVLSQDG 286
Cdd:COG2319 160 GHSGAvTSV-----AFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHT--GAVRSVAFSPDG------KLLASGSADG 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1387845401 287 IMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYIASIMENGSLNIYSVQ 336
Cdd:COG2319 227 TVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA 276
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
86-336 |
4.72e-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: 88.55 E-value: 4.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 86 CTALAFNlrRKSEFLV-ALADYSIKCFDTVTKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKL 163
Cdd:cd00200 12 VTCVAFS--PDGKLLAtGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDkTIRLWDLETGECVRTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 164 NIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLFCKYQLPAPPESssilYKVFAVTRDGRILAAGGKSNHLHLWCL 243
Cdd:cd00200 90 TGHTS-YVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDW----VNSVAFSPDGTFVASSSQDGTIKLWDL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 244 EARQLFRIIQMPTKvrAIRHLEFLPD--SFDAGSNqvlgvlsqDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYI 321
Cdd:cd00200 165 RTGKCVATLTGHTG--EVNSVAFSPDgeKLLSSSS--------DGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLL 234
|
250
....*....|....*
gi 1387845401 322 ASIMENGSLNIYSVQ 336
Cdd:cd00200 235 ASGSEDGTIRVWDLR 249
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
123-337 |
5.69e-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: 5.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 123 RGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIrQSVGIQKVFFLPLSNTILSCFKDNSIFAWECDTLF 201
Cdd:cd00200 6 KGHTGGVTCVAFSPDGKLLATGSGDgTIKVWDLETGELLRTLKG-HTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 202 CKYQLPAppESSSILYkvFAVTRDGRILAAGGKSNHLHLWCLEARQLfrIIQMPTKVRAIRHLEFLPDsfdagsNQVLGV 281
Cdd:cd00200 85 CVRTLTG--HTSYVSS--VAFSPDGRILSSSSRDKTIKVWDVETGKC--LTTLRGHTDWVNSVAFSPD------GTFVAS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387845401 282 LSQDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYIASIMENGSLNIYSVQA 337
Cdd:cd00200 153 SSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLST 208
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
684-967 |
6.21e-11 |
|
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: 66.30 E-value: 6.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 684 IVDYQTQERERIRNDELDYL---RERQTVEDMQAKVDQQRVEDEAwyqkqELLRKAEETRREMLLQEEEKMIQQRQR--- 757
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMeqeRLRQEKEEKAREVERRRKLEEA-----EKARQAEMDRQAAIYAEQERMAMERERele 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 758 ---LAAVKREL---KVKEMHLQDAARRRFLKLQQD-QQEMELRRLDDEIGRKVYMRDREiaatardlemRQLELESQKRL 830
Cdd:pfam17380 352 rirQEERKRELeriRQEEIAMEISRMRELERLQMErQQKNERVRQELEAARKVKILEEE----------RQRKIQQQKVE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 831 YEKNLTENQEALAKEMRADADAYRR---KVDLEEHMFHKLIEAGETQSQKTQKWKEAEGKEfrlrsaKKASALSDASRKW 907
Cdd:pfam17380 422 MEQIRAEQEEARQREVRRLEEERARemeRVRLEEQERQQQVERLRQQEEERKRKKLELEKE------KRDRKRAEEQRRK 495
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387845401 908 FLKQEINAavehaenpchkvtavvslRRGDLDTDTHREKMIRR--PRRKAAIYKP-RRENAEE 967
Cdd:pfam17380 496 ILEKELEE------------------RKQAMIEEERKRKLLEKemEERQKAIYEEeRRREAEE 540
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
688-916 |
6.43e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 6.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 688 QTQERERIRNDELDYL-----RERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVK 762
Cdd:COG1196 285 EAQAEEYELLAELARLeqdiaRLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 763 RELKVKEMHLQDAARRRfLKLQQDQQEMELRRLDDEIgrkvymRDREIAATARDLEMRQLELESQKRLYEKNLTENQEAL 842
Cdd:COG1196 365 EALLEAEAELAEAEEEL-EELAEELLEALRAAAELAA------QLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387845401 843 AKEMRADADAYRRKVDLEEHmfhkliEAGETQSQKTQKWKEAEGKEfrLRSAKKASALSDASRKWFLKQEINAA 916
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEE------EEALLELLAELLEEAALLEA--ALAELLEELAEAAARLLLLLEAEADY 503
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
688-884 |
9.29e-11 |
|
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: 65.92 E-value: 9.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 688 QTQERERIRNDELDylrERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEE----KMIQQRQRLAAVKR 763
Cdd:pfam17380 444 RAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEerkqAMIEEERKRKLLEK 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 764 ELKVKEMHLQDAARRRFLKLQQ-DQQEMELRRLDDEIGRKVYMRDREIAATARDLEMRQLELESQKRLYEKNLTENQEAL 842
Cdd:pfam17380 521 EMEERQKAIYEEERRREAEEERrKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEATTPITTI 600
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1387845401 843 AKEMRADADAYRRKvDLEEHMFHKLIEAGETQSQKTQKWKEA 884
Cdd:pfam17380 601 KPIYRPRISEYQPP-DVESHMIRFTTQSPEWATPSPATWNPE 641
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
690-885 |
1.56e-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: 65.14 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 690 QERERIRNdELDYLRERQTVE-DMQAKVDQQRVEDEAWYQKQE------LLRKAEETRREMllqeeekmiqQRQRLAAVK 762
Cdd:pfam17380 389 QKNERVRQ-ELEAARKVKILEeERQRKIQQQKVEMEQIRAEQEearqreVRRLEEERAREM----------ERVRLEEQE 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 763 RELKVKEMHLQDAARRRfLKLQQDQQEMElRRLDDEIGRKVYmrDREIAATARDLemrqLELESQKRLYEKNLTENQEAL 842
Cdd:pfam17380 458 RQQQVERLRQQEEERKR-KKLELEKEKRD-RKRAEEQRRKIL--EKELEERKQAM----IEEERKRKLLEKEMEERQKAI 529
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1387845401 843 AKE-MRADADAYRRK-VDLEE--HMFHKLIEAGETQSQKTQKWKEAE 885
Cdd:pfam17380 530 YEEeRRREAEEERRKqQEMEErrRIQEQMRKATEERSRLEAMERERE 576
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
48-156 |
1.69e-09 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 61.08 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 48 VAFDGTGDCLIAGDHQGNIYVFDLH-GNRFNLVQRTAQACTALAFNlrRKSEFLV-ALADYSIKCFDTVTKELVSWMRGH 125
Cdd:COG2319 294 VAFSPDGKLLASGSDDGTVRLWDLAtGKLLRTLTGHTGAVRSVAFS--PDGKTLAsGSDDGTVRLWDLATGELLRTLTGH 371
|
90 100 110
....*....|....*....|....*....|..
gi 1387845401 126 ESSVFSISVHASGKYAITTSSD-TAQLWDLDT 156
Cdd:COG2319 372 TGAVTSVAFSPDGRTLASGSADgTVRLWDLAT 403
|
|
| RabGAP-TBC |
pfam00566 |
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ... |
462-605 |
1.18e-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: 55.72 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 462 LQKKYPIKSRKLLRVLQRTLSALAHWsviFSDTPY---LPLLAFPFVkLFQNNQLICFEVIATLIINwcQHWFEYFPN-- 536
Cdd:pfam00566 20 FPHSFFFDNGPGQNSLRRILKAYSIY---NPDVGYcqgMNFIAAPLL-LVYLDEEDAFWCFVSLLEN--YLLRDFYTPdf 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 537 PPINILSMI-ENVLAFHDKELLQHFIDHDITSQLYAWPLLETVFSEVLTREEWLKLFDNIFSNHPSFLLM 605
Cdd:pfam00566 94 PGLKRDLYVfEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVLF 163
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
649-963 |
4.28e-08 |
|
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: 57.42 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 649 LMETTPTDIHpDSMLNVFVALTKGQYpvfnqYPKFIVDYQTQ-ERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWY 727
Cdd:pfam05483 444 LLQAREKEIH-DLEIQLTAIKTSEEH-----YLKEVEDLKTElEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKK 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 728 QKQELL--RKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKemhlQDAARRRFLKLQQDQQEMELRRLDDEIGRKVYM 805
Cdd:pfam05483 518 HQEDIIncKKQEERMLKQIENLEEKEMNLRDELESVREEFIQK----GDEVKCKLDKSEENARSIEYEVLKKEKQMKILE 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 806 RD-----REIAATARDLEMRQLElesQKRLYEKNLTENQEALAKEMRADadayrrKVDLE-EHMFHKLIEAGETQSQKTQ 879
Cdd:pfam05483 594 NKcnnlkKQIENKNKNIEELHQE---NKALKKKGSAENKQLNAYEIKVN------KLELElASAKQKFEEIIDNYQKEIE 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 880 KWKEAEgkEFRLRSAKKASALSDASRKwfLKQEINAAVEhaenpcHKVTAVVSLrrgdLDTDTHR-EKMIRRPRRKAAIY 958
Cdd:pfam05483 665 DKKISE--EKLLEEVEKAKAIADEAVK--LQKEIDKRCQ------HKIAEMVAL----MEKHKHQyDKIIEERDSELGLY 730
|
....*
gi 1387845401 959 KPRRE 963
Cdd:pfam05483 731 KNKEQ 735
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
693-971 |
6.82e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 6.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 693 ERIRNDELDYLRERQTVEDMQaKVDQQRVEDE---AWYQKQELLRKAEETRRE--MLLQEEEKMIQQRQRLAAVKRELKV 767
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAEEKK-KAEEAKKAEEdknMALRKAEEAKKAEEARIEevMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 768 KEMHLQDAARRRFLKLQQDQQE-----MELRRLDDEIGrkvyMRDREIAATARDlEMRQLElESQKRLYEKNLTENQEAL 842
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEekkkaEELKKAEEENK----IKAAEEAKKAEE-DKKKAE-EAKKAEEDEKKAAEALKK 1696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 843 AKEMRADADAYRRKVDLEEHMFHKLIEAGETQSQKTQKWKEAEGKEFRlrsaKKASALSDASRKWFLKQEINAAVEHAEN 922
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK----KAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1387845401 923 PCHKVTAVVS--LRRGDLDTDTHREKMIRRPRRKAAIYKprrENAEETNPV 971
Cdd:PTZ00121 1773 IRKEKEAVIEeeLDEEDEKRRMEVDKKIKDIFDNFANII---EGGKEGNLV 1820
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
685-863 |
7.15e-08 |
|
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: 56.11 E-value: 7.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 685 VDYQTQERE---RIRNDELDylRERQTVEDMQakVDQQRVEDEAWYQKQellRKAEETRRemllQEEEKMIQQRQRLAAV 761
Cdd:pfam15709 350 VERKRREQEeqrRLQQEQLE--RAEKMREELE--LEQQRRFEEIRLRKQ---RLEEERQR----QEEEERKQRLQLQAAQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 762 KRELKvkemhLQDAARRRFLKLQQDQQEMELRRLDDEIGRKVYMRDREIAATARDLEMRQLE-LESQKRLYEKNLTENQE 840
Cdd:pfam15709 419 ERARQ-----QQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEErLEYQRQKQEAEEKARLE 493
|
170 180
....*....|....*....|...
gi 1387845401 841 ALAKEMRADADAyrrKVDLEEHM 863
Cdd:pfam15709 494 AEERRQKEEEAA---RLALEEAM 513
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
690-921 |
1.41e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 690 QERERIRNdELDYLreRQTVEDMQAKVDQQRVEdeawyqkQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKE 769
Cdd:TIGR02169 695 SELRRIEN-RLDEL--SQELSDASRKIGEIEKE-------IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 770 MHLQDaARRRFLKLQQDQQEMElRRLDDEIGRKVYMRDREIAATARDLEMRQLELES--QKRLYEKnltenqeALAKEMR 847
Cdd:TIGR02169 765 ARIEE-LEEDLHKLEEALNDLE-ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQklNRLTLEK-------EYLEKEI 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 848 ADADAYRRKVDLEEHMFHKLIEAGETQSQKT-QKWKEAEGKEFRLRSAKKA---------SALSDASRKwflKQEINAAV 917
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELeEELEELEAALRDLESRLGDlkkerdeleAQLRELERK---IEELEAQI 912
|
....
gi 1387845401 918 EHAE 921
Cdd:TIGR02169 913 EKKR 916
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
704-928 |
2.09e-07 |
|
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: 54.27 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 704 RERQTVEDMQAKV-------DQQRVEDEAWyqkqELLRKAEETRREMLLQEEEKMIQQ--RQRLAAV------------- 761
Cdd:pfam15558 5 RDRKIAALMLARHkeeqrmrELQQQAALAW----EELRRRDQKRQETLERERRLLLQQsqEQWQAEKeqrkarlgreerr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 762 KRELKVKEMHLQDAARRRFLKLQ--QDQQEMELRRLDDEIgRKVY--------------MRDREIAATARDLEM----RQ 821
Cdd:pfam15558 81 RADRREKQVIEKESRWREQAEDQenQRQEKLERARQEAEQ-RKQCqeqrlkekeeelqaLREQNSLQLQERLEEachkRQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 822 L-ELESQKRLYEKNLTE--NQEALAKEM--RADADAYRRKVDLE------EHMFHKLIEAgETQSQKTQKWKEAEgkefR 890
Cdd:pfam15558 160 LkEREEQKKVQENNLSEllNHQARKVLVdcQAKAEELLRRLSLEqslqrsQENYEQLVEE-RHRELREKAQKEEE----Q 234
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1387845401 891 LRSAKKASALSDASRKWFLK---QEINAAVEHAENPCHKVT 928
Cdd:pfam15558 235 FQRAKWRAEEKEEERQEHKEalaELADRKIQQARQVAHKTV 275
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
686-861 |
4.45e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 686 DYQTQERERIRNDELDYLRERQTVEDMQAKVD--QQRVED-EAWYQKQELLRKAEETRREMLLQEEEKMIQQR-----QR 757
Cdd:COG4913 260 LAERYAAARERLAELEYLRAALRLWFAQRRLEllEAELEElRAELARLEAELERLEARLDALREELDELEAQIrgnggDR 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 758 LAAVKRELKVKEMHLQDAARRRfLKLQQDQQEMELrrlddeigrkvymrdrEIAATARDLEMRQLELESQKRLYEKNLTE 837
Cdd:COG4913 340 LEQLEREIERLERELEERERRR-ARLEALLAALGL----------------PLPASAEEFAALRAEAAALLEALEEELEA 402
|
170 180
....*....|....*....|....
gi 1387845401 838 NQEALAKEMRADADAYRRKVDLEE 861
Cdd:COG4913 403 LEEALAEAEAALRDLRRELRELEA 426
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
684-897 |
7.71e-07 |
|
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: 52.23 E-value: 7.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 684 IVDYQTQERERIRNDELDYLRErqtvEDMQAKVDQQRVEDEawYQKQELLRKAE------------ETRREMLLQEEEKM 751
Cdd:pfam13868 23 ERDAQIAEKKRIKAEEKEEERR----LDEMMEEERERALEE--EEEKEEERKEErkryrqeleeqiEEREQKRQEEYEEK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 752 IQQRQRLAAVKRELKVKEMHLQDAARRRFLKLQQDQQEM--ELRRLDDEIGRKVYMRDREIAATARDLEMRQLELESQKR 829
Cdd:pfam13868 97 LQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFneEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAERE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387845401 830 LYEKNLTENQEALAKEMradADAYRRKVDLEEHMFHKLIEAGETQSQKTQKwKEAEGKEFRLRSAKKA 897
Cdd:pfam13868 177 EIEEEKEREIARLRAQQ---EKAQDEKAERDELRAKLYQEEQERKERQKER-EEAEKKARQRQELQQA 240
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
688-861 |
1.03e-06 |
|
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: 51.84 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 688 QTQERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQ-------RQRLAA 760
Cdd:pfam13868 133 DEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEkaerdelRAKLYQ 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 761 VKRELKVKEMHLQDAARRRFLKL-----QQDQQEMELRRLDDEIGRKVYMRDREIAATARDLEMRQLELE--SQKRLYEK 833
Cdd:pfam13868 213 EEQERKERQKEREEAEKKARQRQelqqaREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEkrRMKRLEHR 292
|
170 180
....*....|....*....|....*...
gi 1387845401 834 NLTENQEALAKEMRADAdayrRKVDLEE 861
Cdd:pfam13868 293 RELEKQIEEREEQRAAE----REEELEE 316
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
690-794 |
1.58e-06 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 48.88 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 690 QERERIRNDEldylRERQTVEDMQAKVDQQRVEDEAWYQKQE---------LLRKAEETRREMLLQE-EEKMIQQRQRLA 759
Cdd:pfam05672 30 EEQERLEKEE----EERLRKEELRRRAEEERARREEEARRLEeerrreeeeRQRKAEEEAEEREQREqEEQERLQKQKEE 105
|
90 100 110
....*....|....*....|....*....|....*...
gi 1387845401 760 AvkrELKVKEmhlqDAARRRF---LKLQQDQQEMELRR 794
Cdd:pfam05672 106 A---EAKARE----EAERQRQereKIMQQEEQERLERK 136
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
696-921 |
5.12e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 696 RNDELDYLRERQTVEDMQAKVDQQRVEDEawyQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKEMHLQDA 775
Cdd:PTZ00121 1183 KAEEVRKAEELRKAEDARKAEAARKAEEE---RKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEE 1259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 776 ARRRFLKLQQDQQEMELRRLDDEIGRKVYMRDREIAATARdlEMRQLElESQKRLYEKNLTENQEALAKEMRADADAYRR 855
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAE--EKKKAD-EAKKKAEEAKKADEAKKKAEEAKKKADAAKK 1336
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387845401 856 KvdleehmfhklieAGETQSQKTQKWKEAEGKEFRLRSAKKaSALSDASRKWFLKQEINAAVEHAE 921
Cdd:PTZ00121 1337 K-------------AEEAKKAAEAAKAEAEAAADEAEAAEE-KAEAAEKKKEEAKKKADAAKKKAE 1388
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
691-828 |
5.19e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 50.34 E-value: 5.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 691 ERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMllQEEEKmiqqrQRLAAVKRELKVKEM 770
Cdd:pfam15709 387 EEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKK--QQEEA-----ERAEAEKQRQKELEM 459
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387845401 771 HLQDAARR--------RFLKLQQDQQEMELRRLDDEIGRKvymRDREIAATARDLEMRQLELESQK 828
Cdd:pfam15709 460 QLAEEQKRlmemaeeeRLEYQRQKQEAEEKARLEAEERRQ---KEEEAARLALEEAMKQAQEQARQ 522
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
722-846 |
5.65e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.16 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 722 EDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLaavKRELKVKEMHLQDAARRrflkLQqdQQEMELRRLDDEIGR 801
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEF---EKELRERRNELQKLEKR----LL--QKEENLDRKLELLEK 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1387845401 802 kvymRDREIAATARDLEMRQLELESQKRLYEKNLTENQEAL----------AKEM 846
Cdd:PRK12704 108 ----REEELEKKEKELEQKQQELEKKEEELEELIEEQLQELerisgltaeeAKEI 158
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
706-861 |
7.58e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.56 E-value: 7.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 706 RQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQ----RLAavKRELKVKEMHLQDAARRRFL 781
Cdd:pfam15709 335 RDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRfeeiRLR--KQRLEEERQRQEEEERKQRL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 782 KLQQDQ-----QEMELRRLDDEIGRKvymRDREIAATARDLEMRQLELESQ-----KRLYEKNLTENQEALAKEMRADAd 851
Cdd:pfam15709 413 QLQAAQerarqQQEEFRRKLQELQRK---KQQEEAERAEAEKQRQKELEMQlaeeqKRLMEMAEEERLEYQRQKQEAEE- 488
|
170
....*....|
gi 1387845401 852 ayRRKVDLEE 861
Cdd:pfam15709 489 --KARLEAEE 496
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
686-921 |
9.02e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 9.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 686 DYQTQERERIRNDELdYLRERQTVEDMQaKVDQQRVEDEAwyQKQELLRKAEETRR--EMLLQEEEKMIQQRQRLAAVKR 763
Cdd:PTZ00121 1078 DFDFDAKEDNRADEA-TEEAFGKAEEAK-KTETGKAEEAR--KAEEAKKKAEDARKaeEARKAEDARKAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 764 ELKVKEMhlQDAARRRFLKLQQDQQEMELRRLDDEIGRKVYMRD----REIAATARDLEMRQLElesQKRLYEKNLTENQ 839
Cdd:PTZ00121 1154 VEIARKA--EDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKaedaRKAEAARKAEEERKAE---EARKAEDAKKAEA 1228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 840 EALAKEMRADADAYRR----KVDLEEHMFHKLIEAGETQSQKTQKWKEAEGKEfRLRSAKKASAlSDASRKWFLKQEINA 915
Cdd:PTZ00121 1229 VKKAEEAKKDAEEAKKaeeeRNNEEIRKFEEARMAHFARRQAAIKAEEARKAD-ELKKAEEKKK-ADEAKKAEEKKKADE 1306
|
....*.
gi 1387845401 916 AVEHAE 921
Cdd:PTZ00121 1307 AKKKAE 1312
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
691-921 |
1.31e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 691 ERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKEM 770
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 771 HLQDAARRRFLKLQQDQQEMELRRLDDEIGRKvymRDREIAATARDLEMRQLELESQKRLYEKNLTENQEALAKEMRADA 850
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEE---ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387845401 851 DAYRRKVDLEEHMFHKLIEAGETQSQKTQKWKEAEGkefRLRSAKKASALSDASRKWFLKQEINAAVEHAE 921
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEE---LEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
688-888 |
1.91e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 688 QTQERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRR---EMLLQEEEKMiQQRQRLAAVKRE 764
Cdd:PTZ00121 1676 KAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKikaEEAKKEAEED-KKKAEEAKKDEE 1754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 765 LKVKEMHLQDAARRRFLKLQQDQQEMELRRLDDEIGRKVYMRDREIAATARDLEMRQlELESQKRLYEKNLTENQEALAK 844
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANII-EGGKEGNLVINDSKEMEDSAIK 1833
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1387845401 845 EMRADADAYRRKVD-LEEHMFHKLIEAGETQSQKTQKWKEAEGKE 888
Cdd:PTZ00121 1834 EVADSKNMQLEEADaFEKHKFNKNNENGEDGNKEADFNKEKDLKE 1878
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
702-921 |
2.40e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.88 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 702 YLRERQTVEDMQAKvdQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAvkrelkvkemhlQDAARRRfl 781
Cdd:PRK09510 64 YNRQQQQQKSAKRA--EEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQA------------EEAAKQA-- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 782 KLQQDQQEMELRrlddeigrkvymRDREIAATARDLEMRQLELESQKRLYEKnltENQEALAKEMRADADAyrrKVDLEE 861
Cdd:PRK09510 128 ALKQKQAEEAAA------------KAAAAAKAKAEAEAKRAAAAAKKAAAEA---KKKAEAEAAKKAAAEA---KKKAEA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387845401 862 HMFHKLIEAGETQSQKTQKWK---------EAEGKEFRLRSAKKASALSDASRKWFLKQEINAAVEHAE 921
Cdd:PRK09510 190 EAAAKAAAEAKKKAEAEAKKKaaaeakkkaAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
693-906 |
4.49e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 693 ERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKEMHL 772
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 773 QDAARRRFLKLQQD--QQEMELRRLDDEIGRKVYMRDREIAATARDLEMRQLELESQKRLYEKNLTENQEALAKEMRaDA 850
Cdd:PTZ00121 1368 AAEKKKEEAKKKADaaKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAK-KA 1446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387845401 851 DAYRRKVdlEEhmfHKLIEAGETQSQKTQKWKEAEGKEFRLRSAKKASALSDASRK 906
Cdd:PTZ00121 1447 DEAKKKA--EE---AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKK 1497
|
|
| TBC |
smart00164 |
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ... |
501-609 |
7.78e-05 |
|
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: 44.99 E-value: 7.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 501 AFP-FVKLFQNNQLIcFEVIATLIINWCQHWFEYFpnppinilsmienvLAFHDKELLQHFIDHDITSQLYAWPLLETVF 579
Cdd:smart00164 112 AFWcLVKLMERYGPN-FYLPDMSGLQLDLLQLDRL--------------VKEYDPDLYKHLKDLGITPSLYALRWFLTLF 176
|
90 100 110
....*....|....*....|....*....|
gi 1387845401 580 SEVLTREEWLKLFDNIFSNHPSFLLMTVVA 609
Cdd:smart00164 177 ARELPLEIVLRIWDVLFAEGSDFLFRVALA 206
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
115-153 |
7.78e-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: 7.78e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1387845401 115 TKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWD 153
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDgTIKLWD 40
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
696-861 |
7.81e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 7.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 696 RNDELDYLRERqtVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREmllQEEEKMIQQRQRLAAVKRELKVKEMHLQDA 775
Cdd:TIGR02168 675 RRREIEELEEK--IEELEEKIAELEKALAELRKELEELEEELEQLRK---ELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 776 ARRRFLKLQQDQQEMELRRLDDEIGRKVYMRDREIAATARDLEMRQLELESQKRLYEK----------NLTENQEALAKE 845
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeltllneEAANLRERLESL 829
|
170
....*....|....*.
gi 1387845401 846 MRADADAYRRKVDLEE 861
Cdd:TIGR02168 830 ERRIAATERRLEDLEE 845
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
697-851 |
1.00e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 697 NDELDYLRERQTvedmQAKVDQQRVEDEAWYQKQELLRKAEE--TRREMLLQEEEKMIQQRQRLAAVKRELKVKEMHLQD 774
Cdd:COG4372 44 QEELEQLREELE----QAREELEQLEEELEQARSELEQLEEEleELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387845401 775 AARRRFlKLQQDQQEMELRRldDEIGRKVYMRDREIAATARDLEMRQLELESQKRLYEKNLTENQEALAKEMRADAD 851
Cdd:COG4372 120 LQKERQ-DLEQQRKQLEAQI--AELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEAN 193
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
690-922 |
1.12e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 690 QERERIRNDELdylrerQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRR------------------EMLLQEEEKM 751
Cdd:PTZ00121 1615 AEEAKIKAEEL------KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikaaeeakkaeedkkkaeEAKKAEEDEK 1688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 752 IQQRQRLAAVKRELKVKEMHLQDAARRRflKLQQDQQEMELRRLDDEIGRKVYMRDREIAATARDLEMRQLELESQKRLY 831
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAEEKK--KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEE 1766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 832 EKNLTE---NQEALAKEMRADADAYR-----RKVDLEEHMFHKLIEAGETQSQKTQKWKEAEGKEFRLRSAKKASALSDA 903
Cdd:PTZ00121 1767 EKKAEEirkEKEAVIEEELDEEDEKRrmevdKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEA 1846
|
250
....*....|....*....
gi 1387845401 904 srKWFLKQEINAAVEHAEN 922
Cdd:PTZ00121 1847 --DAFEKHKFNKNNENGED 1863
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
692-903 |
1.57e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 692 RERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREmllQEEEKMIQQRQRLAAVKRelkvkemh 771
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKA---AAAKKKADEAKKKAEEKK-------- 1431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 772 lqdaarrrflKLQQDQQEMELRRLDDEIGRKVYMRDREIAATARDLEMRQLElESQKRLYEKNLTENQEALAKEMRADAD 851
Cdd:PTZ00121 1432 ----------KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD-EAKKKAEEAKKADEAKKKAEEAKKKAD 1500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1387845401 852 AYRRKVDlEEHMFHKLIEAGETQSQKTQKWKEAEGKEFRLRSA---KKASALSDA 903
Cdd:PTZ00121 1501 EAKKAAE-AKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAeekKKADELKKA 1554
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
707-906 |
1.93e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 44.84 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 707 QTVEDMQAK-VDQQRVEDEAWYQKQELL--RKAEETRREMLLQEEEKMIQQR----QRLAAVKRELKVKEMHLQDAARRR 779
Cdd:TIGR02794 33 GGAEIIQAVlVDPGAVAQQANRIQQQKKpaAKKEQERQKKLEQQAEEAEKQRaaeqARQKELEQRAAAEKAAKQAEQAAK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 780 FLKLQQDQQEMELRRLDDEIGRKvymrdREIAATARDLEM--RQLELESQKRLYEKNLTENQEALAK---EMRADADAyR 854
Cdd:TIGR02794 113 QAEEKQKQAEEAKAKQAAEAKAK-----AEAEAERKAKEEaaKQAEEEAKAKAAAEAKKKAEEAKKKaeaEAKAKAEA-E 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1387845401 855 RKVDLEehmfhkliEAGETQSQKTQKwKEAEGKEfRLRSAKKASALSDASRK 906
Cdd:TIGR02794 187 AKAKAE--------EAKAKAEAAKAK-AAAEAAA-KAEAEAAAAAAAEAERK 228
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
690-923 |
1.93e-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: 45.60 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 690 QERERIRNDELDYLRErqtveDMQAKVDQQRVE----DEAWYQKQELLRKAEETRR-------EMLLQEEEKMIQQRQRL 758
Cdd:pfam12128 282 QETSAELNQLLRTLDD-----QWKEKRDELNGElsaaDAAVAKDRSELEALEDQHGafldadiETAAADQEQLPSWQSEL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 759 AAVKRELKVKEMHLQDAAR---RRFLKLQQDQQEmELRRLDDEIGRKVYMRDREIAATARDLEMRQLELESQKRLYEKNL 835
Cdd:pfam12128 357 ENLEERLKALTGKHQDVTAkynRRRSKIKEQNNR-DIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEF 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 836 TENQEALAK-----EMRADADAYRRKVDLEEHMFHKLIE-AGETQSQKTQKWKEAEGKEFRLRSAK-KAS-ALSDASRKW 907
Cdd:pfam12128 436 NEEEYRLKSrlgelKLRLNQATATPELLLQLENFDERIErAREEQEAANAEVERLQSELRQARKRRdQASeALRQASRRL 515
|
250
....*....|....*.
gi 1387845401 908 FLKQEINAAVEHAENP 923
Cdd:pfam12128 516 EERQSALDELELQLFP 531
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
692-862 |
2.56e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 692 RERIRNDELDYL--------RERQTVEDMQAKVDQQRVEDEAwyQKQELLRKAEETRREMLLQEEEKMIQQrQRLAAVKR 763
Cdd:TIGR02168 219 KAELRELELALLvlrleelrEELEELQEELKEAEEELEELTA--ELQELEEKLEELRLEVSELEEEIEELQ-KELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 764 ELKVKEMHLQDA-ARRRFLKLQQDQQEMELRRLD---DEIGRKVYMRDREIAATARDLEMRQLELESQKRLYeknltENQ 839
Cdd:TIGR02168 296 EISRLEQQKQILrERLANLERQLEELEAQLEELEsklDELAEELAELEEKLEELKEELESLEAELEELEAEL-----EEL 370
|
170 180
....*....|....*....|...
gi 1387845401 840 EALAKEMRADADAYRRKVDLEEH 862
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLEL 393
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
693-880 |
3.91e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 693 ERIRN--DELDYLRE-RQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREM----LLQEEEKMIQQRQRLAAVKREL 765
Cdd:COG4913 225 EAADAlvEHFDDLERaHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRaalrLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 766 KVKEmhlqdaARRRFLKLQQDQQEMELRRLDDEI----GRKVYMRDREIAATARDLEMRQLELESQKRLY---------- 831
Cdd:COG4913 305 ARLE------AELERLEARLDALREELDELEAQIrgngGDRLEQLEREIERLERELEERERRRARLEALLaalglplpas 378
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1387845401 832 EKNLTENQEAlAKEMRADADAYRRKVDLEEHMFHKLIEAGETQSQKTQK 880
Cdd:COG4913 379 AEEFAALRAE-AAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
688-803 |
5.70e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.37 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 688 QTQERERIRNDELDYLRERQTVEDMQAKvDQQRVEDEAWYQKQeLLRKAEETRREMLLQEEEKMIQQR-----QRLAAVK 762
Cdd:pfam13868 225 EEAEKKARQRQELQQAREEQIELKERRL-AEEAEREEEEFERM-LRKQAEDEEIEQEEAEKRRMKRLEhrrelEKQIEER 302
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1387845401 763 RELKVKEMhlqdAARRRFLKLQQDQQEMELRRLDDEIGRKV 803
Cdd:pfam13868 303 EEQRAAER----EEELEEGERLREEEAERRERIEEERQKKL 339
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
710-973 |
5.85e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 710 EDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLaavkrelkvkEMHL--QDAARRRfLKLQQDQ 787
Cdd:pfam01576 60 EEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDL----------EEQLdeEEAARQK-LQLEKVT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 788 QEMELRRLDDEIgrkVYMRDR--EIAATARDLEMRQLELESQ--------------KRLYEKNLTENQEALAKE--MRAD 849
Cdd:pfam01576 129 TEAKIKKLEEDI---LLLEDQnsKLSKERKLLEERISEFTSNlaeeeekakslsklKNKHEAMISDLEERLKKEekGRQE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 850 ADAYRRKVDLeehmfhkliEAGETQSQKTQkwKEAEGKEFRLRSAKKasalsdasrkwflKQEINAAVEHAENPC-HKVT 928
Cdd:pfam01576 206 LEKAKRKLEG---------ESTDLQEQIAE--LQAQIAELRAQLAKK-------------EEELQAALARLEEETaQKNN 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1387845401 929 AVVSLRR-----GDLDTDTHREKMIrrpRRKAAiyKPRRENAEETNPVNT 973
Cdd:pfam01576 262 ALKKIREleaqiSELQEDLESERAA---RNKAE--KQRRDLGEELEALKT 306
|
|
| Pinin_SDK_memA |
pfam04696 |
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ... |
728-847 |
5.98e-04 |
|
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: 40.74 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 728 QKQELLRKAEETRREMLLQE-EEKMIQQRQRLAAVKRElkvkemhlqdaaRRRFLKLQQDQQEMELRRLDDEIGRKVYMR 806
Cdd:pfam04696 22 KKEESKQKEKEERRAEIEKRlEEKAKQEKEELEERKRE------------EREELFEERRAEQIELRALEEKLELKELME 89
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1387845401 807 DREiaaTARDLEMRQLELESQKRLY--EKNLTENQEALAKEMR 847
Cdd:pfam04696 90 TWH---ENLKALANFLKTKTEPPIYylPWKLTEKTEELLEEQI 129
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
684-858 |
6.48e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 684 IVDYQTQERERIrnDELDYLRE--RQTVEDMQAKVDqqRVED--EAWYQKQELLRKAE------ETRREMLLQEEEKMIQ 753
Cdd:PRK02224 466 HVETIEEDRERV--EELEAELEdlEEEVEEVEERLE--RAEDlvEAEDRIERLEERREdleeliAERRETIEEKRERAEE 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 754 QRQRL------AAVKRELKVKEMHLQDAARRRFLKLQQDQQEmelrrLDDEIGR--KVYMRDREIAATARDLEMRQ---- 821
Cdd:PRK02224 542 LRERAaeleaeAEEKREAAAEAEEEAEEAREEVAELNSKLAE-----LKERIESleRIRTLLAAIADAEDEIERLRekre 616
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1387845401 822 ----LELESQKRLYEKN---------LTENQEALAKEMRADADAYRRKVD 858
Cdd:PRK02224 617 alaeLNDERRERLAEKRerkreleaeFDEARIEEAREDKERAEEYLEQVE 666
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
690-832 |
6.79e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 690 QERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQEL-----LRKAEETRREMLLQEEEKMIQQRQRLAAVKRE 764
Cdd:pfam13868 193 QEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQelqqaREEQIELKERRLAEEAEREEEEFERMLRKQAE 272
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387845401 765 LKVKEMHLQDAARRRFLKLQQD-QQEMELRRLDDEIGRKVYMRDREIAATARDLEMRQLELESQKRLYE 832
Cdd:pfam13868 273 DEEIEQEEAEKRRMKRLEHRRElEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
688-973 |
6.91e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.49 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 688 QTQERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQE---LLRKAEETRREMLLQEEekmiQQRQRLAAVKRE 764
Cdd:COG3064 11 EAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEeeaREAKAEAEQRAAELAAE----AAKKLAEAEKAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 765 LKVKEMHLQDAARrrflKLQQDQQEMELRRLDDEIGRKvymRDREIAATARdlEMRQLELESQKRLYEKNLTENQEALAK 844
Cdd:COG3064 87 AEAEKKAAAEKAK----AAKEAEAAAAAEKAAAAAEKE---KAEEAKRKAE--EEAKRKAEEERKAAEAEAAAKAEAEAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 845 EMRADADAYRRKVDLEEHMFHKLIEAGETQSQKTQKWKEAEGKEFRLRSAKKASALSDASRkwfLKQEINAAVEHAENPC 924
Cdd:COG3064 158 RAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLA---LAVAARAAAASREAAL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1387845401 925 HKVTAVVSLRRGDLDTDTHREKMIRRPRRKAAIYKPRRENAEETNPVNT 973
Cdd:COG3064 235 AAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAA 283
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
735-885 |
7.05e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.40 E-value: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 735 KAEETRREMLLQEEEKMIQQRQRL---AAVKRELKVKEMHLQDAARRRflkLQQDQQEMElRRLDDEIGRKVYMRDREIA 811
Cdd:pfam15709 315 RSEEDPSKALLEKREQEKASRDRLraeRAEMRRLEVERKRREQEEQRR---LQQEQLERA-EKMREELELEQQRRFEEIR 390
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387845401 812 atardLEMRQLELESQKRLYEKNLTENQEALAKE-MRADADAYRRKvdLEEHMFHKLIEAGETQSQKTQKWKEAE 885
Cdd:pfam15709 391 -----LRKQRLEEERQRQEEEERKQRLQLQAAQErARQQQEEFRRK--LQELQRKKQQEEAERAEAEKQRQKELE 458
|
|
| vATP-synt_E |
pfam01991 |
ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as ... |
713-838 |
7.69e-04 |
|
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: 41.98 E-value: 7.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 713 QAKVD--QQRVEDEAWYQKQELLRKAEE---TRREMLLQEEEkMIQQRQR----LAAVKRELKVKEMHLQDA---ARRRF 780
Cdd:pfam01991 7 EEKAEeiRAKAEEEFAIEKAELVQEAEEkidEIYEKKEKQAE-MQKKIIIsnakNEARLKVLEAREEILDEVfneAEKKL 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387845401 781 LKLQQDQQEME--LRRLDDEIGRK-------VYMR--DREIAATARDLEMRQLELESQKRLYEKNLTEN 838
Cdd:pfam01991 86 AELEEDTDEYKdlLRKLIVQALVKlgepeviVRCRkrDEELVESALDKAAEEYKAKTKKVTVEKAGDEN 154
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
724-879 |
7.90e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 724 EAWYQKQELLRKAEETR--------REMLLQEEEKMIQQRQRLAAVKREL-KVKEMHLQDAArrrFLKLQQDQQEMELRR 794
Cdd:PRK04863 493 EAWDVARELLRRLREQRhlaeqlqqLRMRLSELEQRLRQQQRAERLLAEFcKRLGKNLDDED---ELEQLQEELEARLES 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 795 LDDEIgrkvymrdREIAATARDLEMRQLELESQKRLYEKNLTE---NQEALAK--EMRADADAYRRkvDLEEHMFHKLIE 869
Cdd:PRK04863 570 LSESV--------SEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARlrEQSGEEFEDSQ--DVTEYMQQLLER 639
|
170
....*....|
gi 1387845401 870 AGETQSQKTQ 879
Cdd:PRK04863 640 ERELTVERDE 649
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
719-862 |
8.55e-04 |
|
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: 41.68 E-value: 8.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 719 QRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKEMHLQdaARRRFLKLQQdQQEMELRRLDDE 798
Cdd:pfam14988 17 QKKIEKLWNQYVQECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQ--ALRPFAKLKE-SQEREIQDLEEE 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387845401 799 IgRKVymrDREIAATARDLEMRQLELES--QKRLYEKNLTENQEALAKEMRADADAYRR--KVDLEEH 862
Cdd:pfam14988 94 K-EKV---RAETAEKDREAHLQFLKEKAllEKQLQELRILELGERATRELKRKAQALKLaaKQALSEF 157
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
689-921 |
1.01e-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: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 689 TQERERIRNDeldylRERQTvEDMQAKVDQQRVEDEAwYQKQEL--LRKAEETRREMLLQEEEKMIQQRQRLAAvkrelk 766
Cdd:COG2268 198 IRDARIAEAE-----AERET-EIAIAQANREAEEAEL-EQEREIetARIAEAEAELAKKKAEERREAETARAEA------ 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 767 vkemhlqDAArrrfLKLQQDQQEMELRRlDDEIGRkvymRDREIAATARDLEMRQLELESQKRLyeknltenqealakem 846
Cdd:COG2268 265 -------EAA----YEIAEANAEREVQR-QLEIAE----REREIELQEKEAEREEAELEADVRK---------------- 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387845401 847 RADADAYRRKVDleehmfhkliEAGETQSQKTQKWKEAEGKEfrlrsaKKASALSDASRKWFLKQEINAAVEHAE 921
Cdd:COG2268 313 PAEAEKQAAEAE----------AEAEAEAIRAKGLAEAEGKR------ALAEAWNKLGDAAILLMLIEKLPEIAE 371
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
706-969 |
1.03e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 42.72 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 706 RQTVEDMQAKV-DQQRVEDeawyQKQELLRKAEETRREMLLQEEEKMIQQRQRLAA------VKRELKVKEMHLQDAARR 778
Cdd:COG3064 2 QEALEEKAAEAaAQERLEQ----AEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAeeeareAKAEAEQRAAELAAEAAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 779 RFLKLQQDQQEMElRRLDDEigrkvymRDREIAATARDLEMRQLELESQKRLYEKnltENQEAlAKEMRADADAYRRKVD 858
Cdd:COG3064 78 KLAEAEKAAAEAE-KKAAAE-------KAKAAKEAEAAAAAEKAAAAAEKEKAEE---AKRKA-EEEAKRKAEEERKAAE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 859 LEEHMFHKLIEAGETQSQKTQKWKEAEGKEFRLRSAKKASALSDASRKWFLKQEINAAVEHAENPcHKVTAVVSLRRGDL 938
Cdd:COG3064 146 AEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAA-AADAALLALAVAAR 224
|
250 260 270
....*....|....*....|....*....|.
gi 1387845401 939 DTDTHREKMIRRPRRKAAIYKPRRENAEETN 969
Cdd:COG3064 225 AAAASREAALAAVEATEEAALGGAEEAADLA 255
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
690-906 |
1.07e-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: 43.12 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 690 QERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQR-----QRLAAVKRE 764
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKleelkEELESLEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 765 LKVKEMHLQDAARRrflkLQQDQQEMELRRlddeigRKVYMRDREIAATARDLEMRQLELESQKRLYEKNLTENQEALAK 844
Cdd:TIGR02168 360 LEELEAELEELESR----LEELEEQLETLR------SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387845401 845 EMRADADAYRRKVDLEEHMFHKLIEAGETqsqktqkwKEAEGKEFRLRSAKKASALSDASRK 906
Cdd:TIGR02168 430 LEEAELKELQAELEELEEELEELQEELER--------LEEALEELREELEEAEQALDAAERE 483
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
713-967 |
1.09e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 42.72 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 713 QAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRElkvkemhLQDAARRRflKLQQDQQEMEL 792
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQ-------AEEEAREA--KAEAEQRAAEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 793 RrlddeigrkvymrdreiAATARdlemRQLELESQKRLYEKNLTENQEALAKEmrADADAYRRKVDLEEhmfhkliEAGE 872
Cdd:COG3064 72 A-----------------AEAAK----KLAEAEKAAAEAEKKAAAEKAKAAKE--AEAAAAAEKAAAAA-------EKEK 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 873 TQSQKTQKWKEAEGKEFRLRSAKKASALSDASRKWFLKQEINAAVEHAENPCHKVTAVVSLRRGDLDTDTHREKMIRRPR 952
Cdd:COG3064 122 AEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAA 201
|
250
....*....|....*
gi 1387845401 953 RKAAIYKPRRENAEE 967
Cdd:COG3064 202 ALAAAAAAAAADAAL 216
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
703-906 |
1.10e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.89 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 703 LRERQTVEDmQAKVDQQRVEDEAWYQKQELLRK-AEETRRemlLQEE--EKMIQQRQRLaavKREL----KVKEMHL-QD 774
Cdd:NF041483 78 LRNAQIQAD-QLRADAERELRDARAQTQRILQEhAEHQAR---LQAElhTEAVQRRQQL---DQELaerrQTVESHVnEN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 775 AARRRFLKLQQDQQEmelRRLDDEiGRKvymrDREIAATARDLEMRQLELESQKRLYEKNLTENQEALAKEMRADADAYR 854
Cdd:NF041483 151 VAWAEQLRARTESQA---RRLLDE-SRA----EAEQALAAARAEAERLAEEARQRLGSEAESARAEAEAILRRARKDAER 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1387845401 855 rkvdleehmfhkLIEAGETQSQktqkwkEAEGKEFRLRSAkkASALSDASRK 906
Cdd:NF041483 223 ------------LLNAASTQAQ------EATDHAEQLRSS--TAAESDQARR 254
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
697-884 |
1.16e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.21 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 697 NDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQ-----ELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELkvkEMH 771
Cdd:pfam13868 5 SDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEkeeerRLDEMMEEERERALEEEEEKEEERKEERKRYRQEL---EEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 772 LQDAARRRFLKLQQDQQEmelRRLDDEIGRKVYMRDREIA--------ATARDLEMRQLELESQKRL-YEKNLTENQEAL 842
Cdd:pfam13868 82 IEEREQKRQEEYEEKLQE---REQMDEIVERIQEEDQAEAeeklekqrQLREEIDEFNEEQAEWKELeKEEEREEDERIL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1387845401 843 --AKEMRADADAYRRKVDLEEHMFHKLIEAGETQSQKTQKWKEA 884
Cdd:pfam13868 159 eyLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAE 202
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
116-153 |
1.38e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 37.32 E-value: 1.38e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1387845401 116 KELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWD 153
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDgTVKVWD 39
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
690-966 |
1.54e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 690 QERERIRNDELDYLRE-RQTVEDMQAkvDQQRVEDEAWYQKQELLRKAEETRREML-----LQEeekmiQQRQRLAAvkr 763
Cdd:NF041483 728 QERERAREQSEELLASaRKRVEEAQA--EAQRLVEEADRRATELVSAAEQTAQQVRdsvagLQE-----QAEEEIAG--- 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 764 eLKVKEMHLQDAARRrflklqQDQQEMELRRLDDEIGRKvymRDREIAATARdlEMRQLELESQKRLYEKNLTEnQEALA 843
Cdd:NF041483 798 -LRSAAEHAAERTRT------EAQEEADRVRSDAYAERE---RASEDANRLR--REAQEETEAAKALAERTVSE-AIAEA 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 844 KEMRADADAYRRKVDLEEhmfHKLIEAGETQSQKTQkwKEAEGKEFRLRSAKKASA---LSDASRKWFLKQEinAAVEHA 920
Cdd:NF041483 865 ERLRSDASEYAQRVRTEA---SDTLASAEQDAARTR--ADAREDANRIRSDAAAQAdrlIGEATSEAERLTA--EARAEA 937
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1387845401 921 ENPCHKVTAVVSLRRGdlDTDTHREKMIRRPRRKAAiyKPRRENAE 966
Cdd:NF041483 938 ERLRDEARAEAERVRA--DAAAQAEQLIAEATGEAE--RLRAEAAE 979
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
722-909 |
1.73e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 722 EDEAWYQKQELLRKAEETRREmLLQEEEKMIQQRQRLAAVKRELKVKEMHLQDAARRRFLKLQQDQQEMELRRLDDEIgR 801
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERL-E 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 802 KVYMRDREIAATARDLEMRQLELESQKRLYEKNLTENQEALAKEMRADADAYRRkvdLEEHMFHKLIEAGETQSQKTQKW 881
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE---LQQRLAELEEELEEAQEELEELE 226
|
170 180
....*....|....*....|....*...
gi 1387845401 882 KEAEGKEFRLRSAKKASALSDASRKWFL 909
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARLLLLI 254
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
686-848 |
2.42e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.02 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 686 DYQTQERERIRNDEL--DYLRERQTVEDMQAKVDQQRVEDE----AWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLA 759
Cdd:cd16269 157 KYRQVPRKGVKAEEVlqEFLQSKEAEAEAILQADQALTEKEkeieAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 760 AVKRELKvKEMhlqdaarrrflklqqdqqEMELRRLDDEIGRkvymrdreiaatardleMRQLELESQKRLYEKNLTENQ 839
Cdd:cd16269 237 EHLRQLK-EKM------------------EEERENLLKEQER-----------------ALESKLKEQEALLEEGFKEQA 280
|
....*....
gi 1387845401 840 EALAKEMRA 848
Cdd:cd16269 281 ELLQEEIRS 289
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
736-863 |
2.42e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 39.64 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 736 AEETRRemLLQEeekmiqqRQRLAAVKRELKVKEMHLQDAARRRFLKL-------QQDQQEMELRRLDDEigRKVYMRDR 808
Cdd:pfam05672 9 AEEAAR--ILAE-------KRRQAREQREREEQERLEKEEEERLRKEElrrraeeERARREEEARRLEEE--RRREEEER 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1387845401 809 EIAATARDLEMRQLELESQKRLYEknltENQEAlakEMRADADAYRRKVDLEEHM 863
Cdd:pfam05672 78 QRKAEEEAEEREQREQEEQERLQK----QKEEA---EAKAREEAERQRQEREKIM 125
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
688-854 |
2.68e-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: 41.86 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 688 QTQERERIRNDELDYLRERQT---VEDMQAKVDQQRVEDEAWYQKqelLRKAEETR---REMLLQEEEKMIQQRQRLAAV 761
Cdd:COG3096 948 EQQRRLKQQIFALSEVVQRRPhfsYEDAVGLLGENSDLNEKLRAR---LEQAEEARreaREQLRQAQAQYSQYNQVLASL 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 762 KRELKVKEMHLQDaarrrflkLQQDQQEMELrRLDDEIGRKVYMRDREIAATARDLEMRQLELESQKRLYEKnlteNQEA 841
Cdd:COG3096 1025 KSSRDAKQQTLQE--------LEQELEELGV-QADAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEA----EMDS 1091
|
170
....*....|...
gi 1387845401 842 LAKEMRADADAYR 854
Cdd:COG3096 1092 LQKRLRKAERDYK 1104
|
|
| COG5210 |
COG5210 |
GTPase-activating protein [General function prediction only]; |
542-658 |
3.15e-03 |
|
GTPase-activating protein [General function prediction only];
Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 41.33 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 542 LSMIENVLAFHDKELLQHFIDHDITSQLYAWPLLETVFSEVLTREEWLKLFDNIFSNHPSFLLMTVVAYNICSRTPLLSC 621
Cdd:COG5210 350 LKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKL 429
|
90 100 110
....*....|....*....|....*....|....*..
gi 1387845401 622 NLKDDFEFFFHHRNNLDINVVIRQVYHLMETTPTDIH 658
Cdd:COG5210 430 DSDELLDLLLKQLFLHSGKEAWSSILKFRHGTDRDIL 466
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
744-854 |
3.16e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 744 LLQEEEKMIQQRQRLAAVKRELKVKEMHLQDAARrrflklQQDQQEMELRRLDDEIGRKVyMRDREIAATARDLEMRQLE 823
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKK------EEKALLKQLAALERRIAALA-RRIRALEQELAALEAELAE 87
|
90 100 110
....*....|....*....|....*....|.
gi 1387845401 824 LESQKRLYEKNLTENQEALAKEMRAdadAYR 854
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRA---LYR 115
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
691-844 |
3.40e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 691 ERERIRNDELDYLRERQTVEDmQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKEm 770
Cdd:COG4717 312 ALEELEEEELEELLAALGLPP-DLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRA- 389
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387845401 771 HLQDAARRRFLKLQQDQQEMELRRLDDEIGRKVYMRDREiaatarDLEMRQLELESQKRLYEKNLTENQEALAK 844
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE------ELEEELEELEEELEELEEELEELREELAE 457
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
682-832 |
4.05e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 682 KFIVDYQTQERERIRNDELdyLRERQTVEDMQAKVDQQRVEDEAWYQKQEL-LRKAEET---RREMLLQEEEKMIQQRQR 757
Cdd:PRK12704 41 KRILEEAKKEAEAIKKEAL--LEAKEEIHKLRNEFEKELRERRNELQKLEKrLLQKEENldrKLELLEKREEELEKKEKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 758 LAAVKRELKVKEMHLQDAARRRFLKLQQ-------DQQEMELRRLDDEIgrkvymrDREIAATARDLEMrQLELESQKRL 830
Cdd:PRK12704 119 LEQKQQELEKKEEELEELIEEQLQELERisgltaeEAKEILLEKVEEEA-------RHEAAVLIKEIEE-EAKEEADKKA 190
|
..
gi 1387845401 831 YE 832
Cdd:PRK12704 191 KE 192
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
713-795 |
4.18e-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: 40.25 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 713 QAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKEMHLQDAARRRFLKLQQDQQEMEL 792
Cdd:cd16269 208 EAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEI 287
|
...
gi 1387845401 793 RRL 795
Cdd:cd16269 288 RSL 290
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
688-907 |
5.23e-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: 40.13 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 688 QTQERERIRNDELDYLRER-----QTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLlqeeEKMIQQRQRLAAVK 762
Cdd:COG4942 45 ALKKEEKALLKQLAALERRiaalaRRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL----AELLRALYRLGRQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 763 R-ELKVKEMHLQDAARR-RFLK--LQQDQQEME-LRRLDDEIGRKVymrdREIAATARDLEMRQLELESQKRLYEKNLTE 837
Cdd:COG4942 121 PlALLLSPEDFLDAVRRlQYLKylAPARREQAEeLRADLAELAALR----AELEAERAELEALLAELEEERAALEALKAE 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 838 NQEALAKeMRADADAYRRKVDleehmfhkliEAGETQSQKTQKWKEAEGKEFRLRSAKKASALSDASRKW 907
Cdd:COG4942 197 RQKLLAR-LEKELAELAAELA----------ELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
705-913 |
5.87e-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: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 705 ERQTVEDMQAKvDQQRV---EDEAWYQKQELLRKaeETRREMLLQEEEKMIQQRQRLAAVKRELKVKEMHLQDAARRRFL 781
Cdd:pfam07888 116 EKDALLAQRAA-HEARIrelEEDIKTLTQRVLER--ETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 782 KLQ-----QDQQEMELRRLDDEIGRkvyMRDREIAATARDLEMRQL--ELES-QKRLyekNLTENQEALAKEMRADADAY 853
Cdd:pfam07888 193 EFQelrnsLAQRDTQVLQLQDTITT---LTQKLTTAHRKEAENEALleELRSlQERL---NASERKVEGLGEELSSMAAQ 266
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387845401 854 RRKVDLEEHmfHKLIEAGETQSQKTQ---KWKEAEGKEFRLRSAKKASALSDASRKWFLKQEI 913
Cdd:pfam07888 267 RDRTQAELH--QARLQAAQLTLQLADaslALREGRARWAQERETLQQSAEADKDRIEKLSAEL 327
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
704-858 |
6.38e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 704 RERQTVEDMQAKVDQQRVEDEAwyQKQELlrKAEETRREMLLQEEEKMIQQ-RQRLAAVK--RELKV--KEMHlqdaarr 778
Cdd:COG1579 31 AELAELEDELAALEARLEAAKT--ELEDL--EKEIKRLELEIEEVEARIKKyEEQLGNVRnnKEYEAlqKEIE------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 779 rFLKLQQDQQEMELRRLDDEIGRKvymrDREIAATARDLEMRQLELESQKRLYEKNLTENQEALAkEMRADADAYRRKVD 858
Cdd:COG1579 100 -SLKRRISDLEDEILELMERIEEL----EEELAELEAELAELEAELEEKKAELDEELAELEAELE-ELEAEREELAAKIP 173
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
688-967 |
8.77e-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: 8.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 688 QTQERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREmLLQEEEKMIQQRQRLAAVKRELKV 767
Cdd:COG3064 25 KRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKL-AEAEKAAAEAEKKAAAEKAKAAKE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 768 KEmhlQDAARRRFLKLQQDQQEMELRRLDDEIGRKVYMRDREIAATARDLEmrqlELESQKRLYEKNLTENQEALAKEMR 847
Cdd:COG3064 104 AE---AAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAK----AEAEAARAAAAAAAAAAAAAARAAA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 848 ADADAYRRKVDLEEHMFHKLIEAGETQSQKTQKWKEAEGKEFRLRSAKKASALSDASRKWFLKQEINAAVEHAENPCHKV 927
Cdd:COG3064 177 GAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAA 256
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1387845401 928 TAVVSLRRGDLDTDTHREKMIRRPRRKAAIYKPRRENAEE 967
Cdd:COG3064 257 VGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLV 296
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
649-924 |
8.87e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.95 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 649 LMETTPTDIHPDSMLNVF----------VALTKgQYPVFNQYPKFIVDYQTqERERIRNDELDYLRE-RQTVEDMQAKVD 717
Cdd:TIGR00618 169 LMNLFPLDQYTQLALMEFakkkslhgkaELLTL-RSQLLTLCTPCMPDTYH-ERKQVLEKELKHLREaLQQTQQSHAYLT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 718 QQRVEDEAWYQKQELLRKA--------------EETRREM--------LLQEEEKMIQQRQRLAAVKRELKVKEMHLQDA 775
Cdd:TIGR00618 247 QKREAQEEQLKKQQLLKQLrarieelraqeavlEETQERInrarkaapLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 776 ARRRFLKLQQDQQEMELRRLDDEIGRK--VYMRDREIAATARDLEMRQLELESQKRLYEKNLT--ENQEALAKEMRADAD 851
Cdd:TIGR00618 327 LMKRAAHVKQQSSIEEQRRLLQTLHSQeiHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTtlTQKLQSLCKELDILQ 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 852 AYRRKVDLEEHMF-----HKLIEAGETQSQK-------------TQKWKEAEGKEFRLRSAKKASALSDASRKWFLKQE- 912
Cdd:TIGR00618 407 REQATIDTRTSAFrdlqgQLAHAKKQQELQQryaelcaaaitctAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQEt 486
|
330
....*....|....*...
gi 1387845401 913 ------INAAVEHAENPC 924
Cdd:TIGR00618 487 rkkavvLARLLELQEEPC 504
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
724-850 |
9.97e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 38.53 E-value: 9.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845401 724 EAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRE--LKVKEmhlQDAARRRFLKLQQDQQEMELRRLDDEIgR 801
Cdd:pfam13904 58 ENWLAAKQRQRQKELQAQKEEREKEEQEAELRKRLAKEKYQewLQRKA---RQQTKKREESHKQKAAESASKSLAKPE-R 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1387845401 802 KVymrdreIAATARDL----EMRQLELESQKRLYEKNLTENQEALAKEMRADA 850
Cdd:pfam13904 134 KV------SQEEAKEVlqewERKKLEQQQRKREEEQREQLKKEEEEQERKQLA 180
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