|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
44-340 |
2.08e-28 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 118.86 E-value: 2.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 44 RFLNVAFDGTGDCLIAGDHQGNIYVFDL-HGNRFNLVQRTAQACTALAFNLRRKSeFLVALADYSIKCFDTVTKELVSWM 122
Cdd:COG2319 80 AVLSVAFSPDGRLLASASADGTVRLWDLaTGLLLRTLTGHTGAVRSVAFSPDGKT-LASGSADGTVRLWDLATGKLLRTL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 123 RGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLF 201
Cdd:COG2319 159 TGHSGAVTSVAFSPDGKLLASGSDDgTVRLWDLATGKLLRTLTGHTG-AVRSVAFSPDGKLLASGSADGTVRLWDLATGK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 202 CKYQLPAPPES-SSIlykvfAVTRDGRILAAGGKSNHLHLWCLEARQLFRIIQMPTkvRAIRHLEFLPDSfdagsnQVLG 280
Cdd:COG2319 238 LLRTLTGHSGSvRSV-----AFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHS--GGVNSVAFSPDG------KLLA 304
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 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 |
1.81e-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: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 39 HPKVLRFlnVAFDGTGDCLIAGDHQGNIYVFDLHGNRFNLVQR----TAQACTALAFNLRrkseFLVALADYSIKCFDTV 114
Cdd:cd00200 8 HTGGVTC--VAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKghtgPVRDVAASADGTY----LASGSSDKTIRLWDLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 115 TKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 193
Cdd:cd00200 82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDkTIKVWDVETGKCLTTLRGHTD-WVNSVAFSPDGTFVASSSQDGTIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 194 AWECDTLFCKYQLPAPPESssilykVFAVT--RDGRILAAGGKSNHLHLWCLEARQLFRiiQMPTKVRAIRHLEFLPDsf 271
Cdd:cd00200 161 LWDLRTGKCVATLTGHTGE------VNSVAfsPDGEKLLSSSSDGTIKLWDLSTGKCLG--TLRGHENGVNSVAFSPD-- 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387845350 272 dagsNQVLGVLSQDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYIASIMENGSLNIYS 334
Cdd:cd00200 231 ----GYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
684-1026 |
4.06e-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: 67.07 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 684 IVDYQTQERERIRNDELDYL---RERQTVEDMQAKVDQQRVEDEAwyqkqELLRKAEETRREMLLQEEEKMIQQRQR-LA 759
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMeqeRLRQEKEEKAREVERRRKLEEA-----EKARQAEMDRQAAIYAEQERMAMEREReLE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 760 AVKRELKVKEMHlqdaaRRRFLKLQQDQQEM-ELRRLDDEIGRKNLTENQE-ALAKEMRADADAYRRKVDLEEHMFHKLI 837
Cdd:pfam17380 352 RIRQEERKRELE-----RIRQEEIAMEISRMrELERLQMERQQKNERVRQElEAARKVKILEEERQRKIQQQKVEMEQIR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 838 EAGETQSQKTQKVIKE----NLAKAEQACLNTDWQIQSLHKQKcDDLQRNKCYQEvakllRENRRKeieiinAMVEEEAK 913
Cdd:pfam17380 427 AEQEEARQREVRRLEEerarEMERVRLEEQERQQQVERLRQQE-EERKRKKLELE-----KEKRDR------KRAEEQRR 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 914 KWKEAEGKEfrlrsaKKASALSDASRKWFLKQEInaavEHAENPCHKEEPRFQNEQDSsclpRTSQlndssEMDPSTQIs 993
Cdd:pfam17380 495 KILEKELEE------RKQAMIEEERKRKLLEKEM----EERQKAIYEEERRREAEEER----RKQQ-----EMEERRRI- 554
|
330 340 350
....*....|....*....|....*....|...
gi 1387845350 994 lnrravewdttgQNLIKKVRNLRQRLTARARHR 1026
Cdd:pfam17380 555 ------------QEQMRKATEERSRLEAMERER 575
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
690-955 |
5.49e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 5.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 690 QERERIRNDELDYLRE-RQTVEDMQAKVDQQ--------RVEDEAWYQKQELLRKAEETRR---EMLLQEEEKMIQQRQR 757
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEeKKKVEQLKKKEAEEkkkaeelkKAEEENKIKAAEEAKKAEEDKKkaeEAKKAEEDEKKAAEAL 1694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 758 LAAVKRELKVKEMHLQDAARRRflKLQQDQQEMELRRLDDEIGRKNLTENQEAlAKEMRADaDAYRRKVdleEHMFHKLI 837
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKK--KAEELKKAEEENKIKAEEAKKEAEEDKKK-AEEAKKD-EEEKKKI---AHLKKEEE 1767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 838 EAGETQSQKTQKVIKENLAKA-EQACLNTDWQIQSLhKQKCDDLQ----RNKCYQEVAKLLRENRRKEIEIINAMVEEEA 912
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEdEKRRMEVDKKIKDI-FDNFANIIeggkEGNLVINDSKEMEDSAIKEVADSKNMQLEEA 1846
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1387845350 913 KKWKEAEGKEFRLrSAKKASALSDASRKWFLKQEINAAVEHAE 955
Cdd:PTZ00121 1847 DAFEKHKFNKNNE-NGEDGNKEADFNKEKDLKEDDEEEIEEAD 1888
|
|
| RabGAP-TBC |
pfam00566 |
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ... |
462-605 |
1.19e-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: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 462 LQKKYPIKSRKLLRVLQRTLSALAHWsviFSDTPY---LPLLAFPFVkLFQNNQLICFEVIATLIINwcQHWFEYFPN-- 536
Cdd:pfam00566 20 FPHSFFFDNGPGQNSLRRILKAYSIY---NPDVGYcqgMNFIAAPLL-LVYLDEEDAFWCFVSLLEN--YLLRDFYTPdf 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 537 PPINILSMI-ENVLAFHDKELLQHFIDHDITSQLYAWPLLETVFSEVLTREEWLKLFDNIFSNHPSFLLM 605
Cdd:pfam00566 94 PGLKRDLYVfEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVLF 163
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
688-941 |
7.65e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 7.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 688 QTQERERIRNDELDYLRERQTVEdMQAKVDQQRVEDEAwyQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKV 767
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLE-QDIARLEERRRELE--ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 768 KEMHLQDAARRRfLKLQQDQQEMELRRLDDEIGRKNLTENQEALAKEMRADADAYRRKVDLEEHMFHKLIEAGETQSQKT 847
Cdd:COG1196 356 AEAELAEAEEAL-LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 848 QKVIKENLAKAEQAclNTDWQIQSLHKQKCDDLQRNkcyQEVAKLLRENRRKEIEIINAMVEEEAKKWKEAEGKEFRLRS 927
Cdd:COG1196 435 EEEEEEEEALEEAA--EEEAELEEEEEALLELLAEL---LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
|
250
....*....|....
gi 1387845350 928 AKKASALSDASRKW 941
Cdd:COG1196 510 VKAALLLAGLRGLA 523
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
690-1000 |
1.32e-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: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 690 QERERIRNdELDYLRerqtvedmqakvdqQRVEDEAwyQKQELLRKaeetRREMLLQEEEKmiqQRQRLAAVKRELKVKE 769
Cdd:TIGR02169 695 SELRRIEN-RLDELS--------------QELSDAS--RKIGEIEK----EIEQLEQEEEK---LKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 770 MHLQDAarrrflklqqdqqEMELRRLDDEIGrknltenqealakEMRADADAYRRKV-DLEEHMFHKLIEAGETQSQKTQ 848
Cdd:TIGR02169 751 QEIENV-------------KSELKELEARIE-------------ELEEDLHKLEEALnDLEARLSHSRIPEIQAELSKLE 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 849 KVIKEN---LAKAEQAcLNTDWQIQSLHKQKCDDLQRnkcYQEVAKLLRENRRKEIEIINAMVEEEAKKWKEAEGKEFRL 925
Cdd:TIGR02169 805 EEVSRIearLREIEQK-LNRLTLEKEYLEKEIQELQE---QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 926 RSAKKA---------SALSDASRKwflKQEINAAVEHAENPCH--KEEPRFQNEQDSSCLPRTSQLNDSSEMDPST-QIS 993
Cdd:TIGR02169 881 ESRLGDlkkerdeleAQLRELERK---IEELEAQIEKKRKRLSelKAKLEALEEELSEIEDPKGEDEEIPEEELSLeDVQ 957
|
....*..
gi 1387845350 994 LNRRAVE 1000
Cdd:TIGR02169 958 AELQRVE 964
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
115-153 |
8.19e-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: 8.19e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1387845350 115 TKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWD 153
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDgTIKLWD 40
|
|
| TBC |
smart00164 |
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ... |
501-609 |
8.25e-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: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 501 AFP-FVKLFQNNQLIcFEVIATLIINWCQHWFEYFpnppinilsmienvLAFHDKELLQHFIDHDITSQLYAWPLLETVF 579
Cdd:smart00164 112 AFWcLVKLMERYGPN-FYLPDMSGLQLDLLQLDRL--------------VKEYDPDLYKHLKDLGITPSLYALRWFLTLF 176
|
90 100 110
....*....|....*....|....*....|
gi 1387845350 580 SEVLTREEWLKLFDNIFSNHPSFLLMTVVA 609
Cdd:smart00164 177 ARELPLEIVLRIWDVLFAEGSDFLFRVALA 206
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
690-1029 |
9.07e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 43.28 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 690 QERERIRNDELDYLRE-RQTVEDMQAkvDQQRVEDEAWYQKQELLRKAEETRREML-----LQEeekmiQQRQRLAAvkr 763
Cdd:NF041483 728 QERERAREQSEELLASaRKRVEEAQA--EAQRLVEEADRRATELVSAAEQTAQQVRdsvagLQE-----QAEEEIAG--- 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 764 eLKVKEMHLQDAARRrflklqQDQQEMELRRLDDEIGRKNLTENQEALAKEMRADADAYRRkvdLEEHMFHKLIEAGE-- 841
Cdd:NF041483 798 -LRSAAEHAAERTRT------EAQEEADRVRSDAYAERERASEDANRLRREAQEETEAAKA---LAERTVSEAIAEAErl 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 842 --TQSQKTQKVIKE---NLAKAEQACLNTDWQIQslhkqkcDDLQRNKC-YQEVAKLLRENRRKEIEIINAMVEEEAKKW 915
Cdd:NF041483 868 rsDASEYAQRVRTEasdTLASAEQDAARTRADAR-------EDANRIRSdAAAQADRLIGEATSEAERLTAEARAEAERL 940
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 916 KE---AEGKEFRLRSAKKASAL-----SDASRkwfLKQE----INAAVEHAENpCHKEEPRFQNEQDSSCLPRTSQLNDS 983
Cdd:NF041483 941 RDearAEAERVRADAAAQAEQLiaeatGEAER---LRAEaaetVGSAQQHAER-IRTEAERVKAEAAAEAERLRTEAREE 1016
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387845350 984 SE--MDPSTQISLNRRA----------VEWDTTGQNLIKKVRNLRQRLTARARHRCQT 1029
Cdd:NF041483 1017 ADrtLDEARKDANKRRSeaaeqadtliTEAAAEADQLTAKAQEEALRTTTEAEAQADT 1074
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
116-153 |
1.45e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 37.32 E-value: 1.45e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1387845350 116 KELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWD 153
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDgTVKVWD 39
|
|
| COG5210 |
COG5210 |
GTPase-activating protein [General function prediction only]; |
542-658 |
3.43e-03 |
|
GTPase-activating protein [General function prediction only];
Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 41.33 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 542 LSMIENVLAFHDKELLQHFIDHDITSQLYAWPLLETVFSEVLTREEWLKLFDNIFSNHPSFLLMTVVAYNICSRTPLLSC 621
Cdd:COG5210 350 LKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKL 429
|
90 100 110
....*....|....*....|....*....|....*..
gi 1387845350 622 NLKDDFEFFFHHRNNLDINVVIRQVYHLMETTPTDIH 658
Cdd:COG5210 430 DSDELLDLLLKQLFLHSGKEAWSSILKFRHGTDRDIL 466
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
713-795 |
5.72e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 39.87 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 713 QAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKEMHLQDAARRRFLKLQQDQQEMEL 792
Cdd:cd16269 208 EAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEI 287
|
...
gi 1387845350 793 RRL 795
Cdd:cd16269 288 RSL 290
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
44-340 |
2.08e-28 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 118.86 E-value: 2.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 44 RFLNVAFDGTGDCLIAGDHQGNIYVFDL-HGNRFNLVQRTAQACTALAFNLRRKSeFLVALADYSIKCFDTVTKELVSWM 122
Cdd:COG2319 80 AVLSVAFSPDGRLLASASADGTVRLWDLaTGLLLRTLTGHTGAVRSVAFSPDGKT-LASGSADGTVRLWDLATGKLLRTL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 123 RGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLF 201
Cdd:COG2319 159 TGHSGAVTSVAFSPDGKLLASGSDDgTVRLWDLATGKLLRTLTGHTG-AVRSVAFSPDGKLLASGSADGTVRLWDLATGK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 202 CKYQLPAPPES-SSIlykvfAVTRDGRILAAGGKSNHLHLWCLEARQLFRIIQMPTkvRAIRHLEFLPDSfdagsnQVLG 280
Cdd:COG2319 238 LLRTLTGHSGSvRSV-----AFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHS--GGVNSVAFSPDG------KLLA 304
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 281 VLSQDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYIASIMENGSLNIYSVQALTQ 340
Cdd:COG2319 305 SGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL 364
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
48-336 |
3.91e-28 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 118.09 E-value: 3.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 48 VAFDGTGDCLIAGDHQGNIYVFDLH-GNRFNLVQRTAQACTALAFNlrRKSEFLV-ALADYSIKCFDTVTKELVSWMRGH 125
Cdd:COG2319 126 VAFSPDGKTLASGSADGTVRLWDLAtGKLLRTLTGHSGAVTSVAFS--PDGKLLAsGSDDGTVRLWDLATGKLLRTLTGH 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 126 ESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLFCKY 204
Cdd:COG2319 204 TGAVRSVAFSPDGKLLASGSADgTVRLWDLATGKLLRTLTGHSG-SVRSVAFSPDGRLLASGSADGTVRLWDLATGELLR 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 205 QLPAPPES-SSIlykvfAVTRDGRILAAGGKSNHLHLWCLEARQLFRIIQMPTkvRAIRHLEFLPDsfdagsNQVLGVLS 283
Cdd:COG2319 283 TLTGHSGGvNSV-----AFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHT--GAVRSVAFSPD------GKTLASGS 349
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1387845350 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 |
1.81e-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: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 39 HPKVLRFlnVAFDGTGDCLIAGDHQGNIYVFDLHGNRFNLVQR----TAQACTALAFNLRrkseFLVALADYSIKCFDTV 114
Cdd:cd00200 8 HTGGVTC--VAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKghtgPVRDVAASADGTY----LASGSSDKTIRLWDLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 115 TKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIF 193
Cdd:cd00200 82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDkTIKVWDVETGKCLTTLRGHTD-WVNSVAFSPDGTFVASSSQDGTIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 194 AWECDTLFCKYQLPAPPESssilykVFAVT--RDGRILAAGGKSNHLHLWCLEARQLFRiiQMPTKVRAIRHLEFLPDsf 271
Cdd:cd00200 161 LWDLRTGKCVATLTGHTGE------VNSVAfsPDGEKLLSSSSDGTIKLWDLSTGKCLG--TLRGHENGVNSVAFSPD-- 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387845350 272 dagsNQVLGVLSQDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYIASIMENGSLNIYS 334
Cdd:cd00200 231 ----GYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
49-336 |
1.22e-21 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 98.83 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 49 AFDGTGDCLIAGDHQGNIYVFDLHGNRFNLVQRTAQACTALAFNLRRKSEFLVALADYSIKCFDTVTKELVSWMRGHESS 128
Cdd:COG2319 1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 129 VFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLFCKYQLP 207
Cdd:COG2319 81 VLSVAFSPDGRLLASASADgTVRLWDLATGLLLRTLTGHTG-AVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 208 APPES-SSIlykvfAVTRDGRILAAGGKSNHLHLWCLEARQLFRIIQMPTkvRAIRHLEFLPDSfdagsnQVLGVLSQDG 286
Cdd:COG2319 160 GHSGAvTSV-----AFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHT--GAVRSVAFSPDG------KLLASGSADG 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1387845350 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 |
5.03e-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: 5.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 86 CTALAFNlrRKSEFLV-ALADYSIKCFDTVTKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKL 163
Cdd:cd00200 12 VTCVAFS--PDGKLLAtGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDkTIRLWDLETGECVRTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 164 NIRQSvGIQKVFFLPLSNTILSCFKDNSIFAWECDTLFCKYQLPAPPESssilYKVFAVTRDGRILAAGGKSNHLHLWCL 243
Cdd:cd00200 90 TGHTS-YVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDW----VNSVAFSPDGTFVASSSQDGTIKLWDL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 244 EARQLFRIIQMPTKvrAIRHLEFLPD--SFDAGSNqvlgvlsqDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYI 321
Cdd:cd00200 165 RTGKCVATLTGHTG--EVNSVAFSPDgeKLLSSSS--------DGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLL 234
|
250
....*....|....*
gi 1387845350 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 |
6.07e-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: 6.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 123 RGHESSVFSISVHASGKYAITTSSD-TAQLWDLDTFQRKRKLNIrQSVGIQKVFFLPLSNTILSCFKDNSIFAWECDTLF 201
Cdd:cd00200 6 KGHTGGVTCVAFSPDGKLLATGSGDgTIKVWDLETGELLRTLKG-HTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 202 CKYQLPAppESSSILYkvFAVTRDGRILAAGGKSNHLHLWCLEARQLfrIIQMPTKVRAIRHLEFLPDsfdagsNQVLGV 281
Cdd:cd00200 85 CVRTLTG--HTSYVSS--VAFSPDGRILSSSSRDKTIKVWDVETGKC--LTTLRGHTDWVNSVAFSPD------GTFVAS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387845350 282 LSQDGIMRFINMQTCKLLFEIGSLDEGISSSAISPHGRYIASIMENGSLNIYSVQA 337
Cdd:cd00200 153 SSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLST 208
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
684-1026 |
4.06e-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: 67.07 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 684 IVDYQTQERERIRNDELDYL---RERQTVEDMQAKVDQQRVEDEAwyqkqELLRKAEETRREMLLQEEEKMIQQRQR-LA 759
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMeqeRLRQEKEEKAREVERRRKLEEA-----EKARQAEMDRQAAIYAEQERMAMEREReLE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 760 AVKRELKVKEMHlqdaaRRRFLKLQQDQQEM-ELRRLDDEIGRKNLTENQE-ALAKEMRADADAYRRKVDLEEHMFHKLI 837
Cdd:pfam17380 352 RIRQEERKRELE-----RIRQEEIAMEISRMrELERLQMERQQKNERVRQElEAARKVKILEEERQRKIQQQKVEMEQIR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 838 EAGETQSQKTQKVIKE----NLAKAEQACLNTDWQIQSLHKQKcDDLQRNKCYQEvakllRENRRKeieiinAMVEEEAK 913
Cdd:pfam17380 427 AEQEEARQREVRRLEEerarEMERVRLEEQERQQQVERLRQQE-EERKRKKLELE-----KEKRDR------KRAEEQRR 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 914 KWKEAEGKEfrlrsaKKASALSDASRKWFLKQEInaavEHAENPCHKEEPRFQNEQDSsclpRTSQlndssEMDPSTQIs 993
Cdd:pfam17380 495 KILEKELEE------RKQAMIEEERKRKLLEKEM----EERQKAIYEEERRREAEEER----RKQQ-----EMEERRRI- 554
|
330 340 350
....*....|....*....|....*....|...
gi 1387845350 994 lnrravewdttgQNLIKKVRNLRQRLTARARHR 1026
Cdd:pfam17380 555 ------------QEQMRKATEERSRLEAMERER 575
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
48-156 |
1.81e-09 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 61.08 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 48 VAFDGTGDCLIAGDHQGNIYVFDLH-GNRFNLVQRTAQACTALAFNlrRKSEFLV-ALADYSIKCFDTVTKELVSWMRGH 125
Cdd:COG2319 294 VAFSPDGKLLASGSDDGTVRLWDLAtGKLLRTLTGHTGAVRSVAFS--PDGKTLAsGSDDGTVRLWDLATGELLRTLTGH 371
|
90 100 110
....*....|....*....|....*....|..
gi 1387845350 126 ESSVFSISVHASGKYAITTSSD-TAQLWDLDT 156
Cdd:COG2319 372 TGAVTSVAFSPDGRTLASGSADgTVRLWDLAT 403
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
688-929 |
2.28e-09 |
|
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: 60.32 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 688 QTQERERIRndELDYLRERQTVEDMQAKVDQQRVEDEAwyQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRE-LK 766
Cdd:pfam13868 81 QIEEREQKR--QEEYEEKLQEREQMDEIVERIQEEDQA--EAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEdER 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 767 VKEMHLQDAARRRFLKLQQDQQEMELRRLDDEIgRKNLTENQEALAK--EMRAD--ADAYRRKVDLEEH--MFHKLIEAG 840
Cdd:pfam13868 157 ILEYLKEKAEREEEREAEREEIEEEKEREIARL-RAQQEKAQDEKAErdELRAKlyQEEQERKERQKEReeAEKKARQRQ 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 841 ETQSQKTQKVIKENLAKAEQACLNTDWQIQSLHKQKCDD-----------LQRNKCYQEVAKLLRENRRKEIEIINAMVE 909
Cdd:pfam13868 236 ELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEeieqeeaekrrMKRLEHRRELEKQIEEREEQRAAEREEELE 315
|
250 260
....*....|....*....|
gi 1387845350 910 EEAKKWKEAEGKEFRLRSAK 929
Cdd:pfam13868 316 EGERLREEEAERRERIEEER 335
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
690-955 |
5.49e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 5.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 690 QERERIRNDELDYLRE-RQTVEDMQAKVDQQ--------RVEDEAWYQKQELLRKAEETRR---EMLLQEEEKMIQQRQR 757
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEeKKKVEQLKKKEAEEkkkaeelkKAEEENKIKAAEEAKKAEEDKKkaeEAKKAEEDEKKAAEAL 1694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 758 LAAVKRELKVKEMHLQDAARRRflKLQQDQQEMELRRLDDEIGRKNLTENQEAlAKEMRADaDAYRRKVdleEHMFHKLI 837
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKK--KAEELKKAEEENKIKAEEAKKEAEEDKKK-AEEAKKD-EEEKKKI---AHLKKEEE 1767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 838 EAGETQSQKTQKVIKENLAKA-EQACLNTDWQIQSLhKQKCDDLQ----RNKCYQEVAKLLRENRRKEIEIINAMVEEEA 912
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEdEKRRMEVDKKIKDI-FDNFANIIeggkEGNLVINDSKEMEDSAIKEVADSKNMQLEEA 1846
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1387845350 913 KKWKEAEGKEFRLrSAKKASALSDASRKWFLKQEINAAVEHAE 955
Cdd:PTZ00121 1847 DAFEKHKFNKNNE-NGEDGNKEADFNKEKDLKEDDEEEIEEAD 1888
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
693-922 |
6.18e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 6.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 693 ERIRNDELDYLRERQTVEDMQaKVDQQRVEDE---AWYQKQELLRKAEETRRE--MLLQEEEKMIQQRQRLAAVKRELKV 767
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAEEKK-KAEEAKKAEEdknMALRKAEEAKKAEEARIEevMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 768 KEMHLQDAARRRFLKLQQDQQE-----MELRRLDD-------EIGRKNLTENQEA-----LAKEMRADADAYRRKVDlEE 830
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEekkkaEELKKAEEenkikaaEEAKKAEEDKKKAeeakkAEEDEKKAAEALKKEAE-EA 1701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 831 HMFHKLIEAGETQSQKTQKVIKE---NLAKAEQACLNTDWQIQSLHKQKCDDLQRNKcyqeVAKLLRENRRKEIEI---I 904
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAEELKKAeeeNKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK----IAHLKKEEEKKAEEIrkeK 1777
|
250
....*....|....*...
gi 1387845350 905 NAMVEEEAKKWKEAEGKE 922
Cdd:PTZ00121 1778 EAVIEEELDEEDEKRRME 1795
|
|
| RabGAP-TBC |
pfam00566 |
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ... |
462-605 |
1.19e-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: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 462 LQKKYPIKSRKLLRVLQRTLSALAHWsviFSDTPY---LPLLAFPFVkLFQNNQLICFEVIATLIINwcQHWFEYFPN-- 536
Cdd:pfam00566 20 FPHSFFFDNGPGQNSLRRILKAYSIY---NPDVGYcqgMNFIAAPLL-LVYLDEEDAFWCFVSLLEN--YLLRDFYTPdf 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 537 PPINILSMI-ENVLAFHDKELLQHFIDHDITSQLYAWPLLETVFSEVLTREEWLKLFDNIFSNHPSFLLM 605
Cdd:pfam00566 94 PGLKRDLYVfEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVLF 163
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
692-969 |
3.35e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 692 RERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREmllQEEEKMIQQRQRLAAVKRelKVKEMH 771
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKA---AAAKKKADEAKKKAEEKK--KADEAK 1437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 772 LQDAARRrflKLQQDQQEMELRRLDDEIGRKnltENQEALAKEMRADADAYRRKVDLEEHMFHKLIEAGETQSQKTQKVI 851
Cdd:PTZ00121 1438 KKAEEAK---KADEAKKKAEEAKKAEEAKKK---AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK 1511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 852 KENLAKAEQAcLNTDWQIQSLHKQKCDDLQRNkcyQEVAKllRENRRKEIEIINAmveEEAKKWKEA----EGKEFRLRS 927
Cdd:PTZ00121 1512 ADEAKKAEEA-KKADEAKKAEEAKKADEAKKA---EEKKK--ADELKKAEELKKA---EEKKKAEEAkkaeEDKNMALRK 1582
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1387845350 928 AKKASALSDASRKWFLKQEINAAVEHAENPCHKEEPRFQNEQ 969
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
690-919 |
4.17e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 57.44 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 690 QERERIRNdELDYLRERQTVE-DMQAKVDQQRVEDEAWYQKQE------LLRKAEETRREMllqeeekmiqQRQRLAAVK 762
Cdd:pfam17380 389 QKNERVRQ-ELEAARKVKILEeERQRKIQQQKVEMEQIRAEQEearqreVRRLEEERAREM----------ERVRLEEQE 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 763 RELKVKEMHLQDAARRRfLKLQQDQQEMELRRLDDeigrknltENQEALAKEMRAdadayRRKVDLEEHMFHKLIEAgET 842
Cdd:pfam17380 458 RQQQVERLRQQEEERKR-KKLELEKEKRDRKRAEE--------QRRKILEKELEE-----RKQAMIEEERKRKLLEK-EM 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 843 QSQKTQKVIKENLAKAEQaclntdwqiqslHKQKCDDLQRNKCYQEVAKLLRENR------RKEIEIINAMVEEEaKKWK 916
Cdd:pfam17380 523 EERQKAIYEEERRREAEE------------ERRKQQEMEERRRIQEQMRKATEERsrleamEREREMMRQIVESE-KARA 589
|
...
gi 1387845350 917 EAE 919
Cdd:pfam17380 590 EYE 592
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
696-969 |
5.20e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 5.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 696 RNDELDYLRERQTVEDMQAKVDQQRVEDEawyQKQELLRKAEETRR---------------------------EMLLQEE 748
Cdd:PTZ00121 1183 KAEEVRKAEELRKAEDARKAEAARKAEEE---RKAEEARKAEDAKKaeavkkaeeakkdaeeakkaeeernneEIRKFEE 1259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 749 EKMIQQRQRLAAVKRELKVKEMHLQDAARRRflKLQQDQQEMELRRLDDeiGRKNLTENQEA-----LAKEMRADADAYR 823
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKADELKKAEEKK--KADEAKKAEEKKKADE--AKKKAEEAKKAdeakkKAEEAKKKADAAK 1335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 824 RKVDLEEhmfhKLIEAGETQSQKTQKVIKENLAKAEQACLNTdwqiqSLHKQKCDDLQRN----KCYQEVAKLLRENRRK 899
Cdd:PTZ00121 1336 KKAEEAK----KAAEAAKAEAEAAADEAEAAEEKAEAAEKKK-----EEAKKKADAAKKKaeekKKADEAKKKAEEDKKK 1406
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387845350 900 EIEIINAmvEEEAKKWKEAEGKEFRLRSAKKASALSDASRKwflKQEINAAVEH---AENPCHKEEPRFQNEQ 969
Cdd:PTZ00121 1407 ADELKKA--AAAKKKADEAKKKAEEKKKADEAKKKAEEAKK---ADEAKKKAEEakkAEEAKKKAEEAKKADE 1474
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
693-985 |
7.16e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 7.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 693 ERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKEMHL 772
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 773 QDAARRRFLKLQQD--QQEMELRRLDDEIGRKnlTENQEALAKEMRADADAYR------------RKVDLEEHMFHKLIE 838
Cdd:PTZ00121 1368 AAEKKKEEAKKKADaaKKKAEEKKKADEAKKK--AEEDKKKADELKKAAAAKKkadeakkkaeekKKADEAKKKAEEAKK 1445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 839 AGETQSQKTQKVIKENLA-KAEQACLNTDWQIQSLHKQKCDDLQRNKcyQEVAKLLRENRRKEIEIINAmveEEAKKWKE 917
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAEEAKkKAEEAKKADEAKKKAEEAKKADEAKKKA--EEAKKKADEAKKAAEAKKKA---DEAKKAEE 1520
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387845350 918 AEGKE--FRLRSAKKASALSDASRKWfLKQEINAA--VEHAENPCHKEEPRFQNEQDSSCLPRTSQLNDSSE 985
Cdd:PTZ00121 1521 AKKADeaKKAEEAKKADEAKKAEEKK-KADELKKAeeLKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE 1591
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
688-941 |
7.65e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 7.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 688 QTQERERIRNDELDYLRERQTVEdMQAKVDQQRVEDEAwyQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKV 767
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLE-QDIARLEERRRELE--ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 768 KEMHLQDAARRRfLKLQQDQQEMELRRLDDEIGRKNLTENQEALAKEMRADADAYRRKVDLEEHMFHKLIEAGETQSQKT 847
Cdd:COG1196 356 AEAELAEAEEAL-LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 848 QKVIKENLAKAEQAclNTDWQIQSLHKQKCDDLQRNkcyQEVAKLLRENRRKEIEIINAMVEEEAKKWKEAEGKEFRLRS 927
Cdd:COG1196 435 EEEEEEEEALEEAA--EEEAELEEEEEALLELLAEL---LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
|
250
....*....|....
gi 1387845350 928 AKKASALSDASRKW 941
Cdd:COG1196 510 VKAALLLAGLRGLA 523
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
690-1000 |
1.32e-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: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 690 QERERIRNdELDYLRerqtvedmqakvdqQRVEDEAwyQKQELLRKaeetRREMLLQEEEKmiqQRQRLAAVKRELKVKE 769
Cdd:TIGR02169 695 SELRRIEN-RLDELS--------------QELSDAS--RKIGEIEK----EIEQLEQEEEK---LKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 770 MHLQDAarrrflklqqdqqEMELRRLDDEIGrknltenqealakEMRADADAYRRKV-DLEEHMFHKLIEAGETQSQKTQ 848
Cdd:TIGR02169 751 QEIENV-------------KSELKELEARIE-------------ELEEDLHKLEEALnDLEARLSHSRIPEIQAELSKLE 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 849 KVIKEN---LAKAEQAcLNTDWQIQSLHKQKCDDLQRnkcYQEVAKLLRENRRKEIEIINAMVEEEAKKWKEAEGKEFRL 925
Cdd:TIGR02169 805 EEVSRIearLREIEQK-LNRLTLEKEYLEKEIQELQE---QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 926 RSAKKA---------SALSDASRKwflKQEINAAVEHAENPCH--KEEPRFQNEQDSSCLPRTSQLNDSSEMDPST-QIS 993
Cdd:TIGR02169 881 ESRLGDlkkerdeleAQLRELERK---IEELEAQIEKKRKRLSelKAKLEALEEELSEIEDPKGEDEEIPEEELSLeDVQ 957
|
....*..
gi 1387845350 994 LNRRAVE 1000
Cdd:TIGR02169 958 AELQRVE 964
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
686-853 |
1.35e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 686 DYQTQERERIRNDELDYLRERQTVEDMQAKVD--QQRVED-EAWYQKQELLRKAEETRREMLLQEEEKMIQQR-----QR 757
Cdd:COG4913 260 LAERYAAARERLAELEYLRAALRLWFAQRRLEllEAELEElRAELARLEAELERLEARLDALREELDELEAQIrgnggDR 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 758 LAAVKRELKVKEMHLQDAARRRfLKLQQDQQEMELRRLDDEigrKNLTENQEAlAKEMRADADAYRRKVDLEEHMFHKLI 837
Cdd:COG4913 340 LEQLEREIERLERELEERERRR-ARLEALLAALGLPLPASA---EEFAALRAE-AAALLEALEEELEALEEALAEAEAAL 414
|
170
....*....|....*.
gi 1387845350 838 EAGETQSQKTQKVIKE 853
Cdd:COG4913 415 RDLRRELRELEAEIAS 430
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
704-986 |
1.01e-06 |
|
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: 52.87 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 704 RERQTVEDMQAKVDQQRVEDEawyQKQELLRKAEETRREMLLQEEEKMI---QQRQRLAAVKRELKVKEMHLQD-----A 775
Cdd:pfam01576 152 KERKLLEERISEFTSNLAEEE---EKAKSLSKLKNKHEAMISDLEERLKkeeKGRQELEKAKRKLEGESTDLQEqiaelQ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 776 ARRRFLKLQQDQQEMELR----RLDDEIGRKN------------LTENQEALAKEMRADADAYRRKVDLEEHMfhkliEA 839
Cdd:pfam01576 229 AQIAELRAQLAKKEEELQaalaRLEEETAQKNnalkkireleaqISELQEDLESERAARNKAEKQRRDLGEEL-----EA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 840 GETQ---------------SQKTQKVikENLAKA-EQACLNTDWQIQSL---HKQKCDDLQ-------RNKCYQEVAKLL 893
Cdd:pfam01576 304 LKTEledtldttaaqqelrSKREQEV--TELKKAlEEETRSHEAQLQEMrqkHTQALEELTeqleqakRNKANLEKAKQA 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 894 RENRRKEIEI-----INAMVEEEAKKWK-EAEGKEFRLR---SAKKASALSDASRKWFLKQE-INAAVEHAENPCHKeep 963
Cdd:pfam01576 382 LESENAELQAelrtlQQAKQDSEHKRKKlEGQLQELQARlseSERQRAELAEKLSKLQSELEsVSSLLNEAEGKNIK--- 458
|
330 340
....*....|....*....|...
gi 1387845350 964 rfqNEQDSSCLprTSQLNDSSEM 986
Cdd:pfam01576 459 ---LSKDVSSL--ESQLQDTQEL 476
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
688-969 |
1.33e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 688 QTQERERIRNDELDY-LRERQTVEDMQAKVDQQRVEDEAwYQKQELLRKAEETRREmllQEEEKMIQQRQRLAAVKR--- 763
Cdd:PTZ00121 1411 KKAAAAKKKADEAKKkAEEKKKADEAKKKAEEAKKADEA-KKKAEEAKKAEEAKKK---AEEAKKADEAKKKAEEAKkad 1486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 764 ELKVKEMHLQDAARRRFLKLQQDQQEMELRRLDDEIGRKNLTENQEAL-AKEMRA-----DADAYRRKVDLEEHMFHKLI 837
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKkADEAKKaeekkKADELKKAEELKKAEEKKKA 1566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 838 EAGETQSQKTQKVIK--ENLAKAEQACLNTDWQI-QSLHKQKCDDLQRNKCYQEVAKLLR--ENRRKEIEIINAMVEEEA 912
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRkaEEAKKAEEARIEEVMKLyEEEKKMKAEEAKKAEEAKIKAEELKkaEEEKKKVEQLKKKEAEEK 1646
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 913 KKWKE--AEGKEFRLRSAKKASALSDASRKW-FLKQEINAAVEHAENPCHKEEPRFQNEQ 969
Cdd:PTZ00121 1647 KKAEElkKAEEENKIKAAEEAKKAEEDKKKAeEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
690-794 |
3.10e-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: 48.11 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 690 QERERIRNDEldylRERQTVEDMQAKVDQQRVEDEAWYQKQE---------LLRKAEETRREMLLQE-EEKMIQQRQRLA 759
Cdd:pfam05672 30 EEQERLEKEE----EERLRKEELRRRAEEERARREEEARRLEeerrreeeeRQRKAEEEAEEREQREqEEQERLQKQKEE 105
|
90 100 110
....*....|....*....|....*....|....*...
gi 1387845350 760 AvkrELKVKEmhlqDAARRRF---LKLQQDQQEMELRR 794
Cdd:pfam05672 106 A---EAKARE----EAERQRQereKIMQQEEQERLERK 136
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
713-922 |
3.16e-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: 51.11 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 713 QAKVDQQRVEDEawyQKQELLRKAEETRREmllQEEEKMIQQRQrlaaVKRELKVKEmHLQDAARRRF--LKLQQDQQEM 790
Cdd:pfam15709 330 QEKASRDRLRAE---RAEMRRLEVERKRRE---QEEQRRLQQEQ----LERAEKMRE-ELELEQQRRFeeIRLRKQRLEE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 791 ELRRLDDEIGRKNLtenQEALAKE-MRADADAYRRKV-DLEEHMFHKLIEAGETQSQKtQKVIKENLAkAEQACLntdwq 868
Cdd:pfam15709 399 ERQRQEEEERKQRL---QLQAAQErARQQQEEFRRKLqELQRKKQQEEAERAEAEKQR-QKELEMQLA-EEQKRL----- 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1387845350 869 IQSLHKQKCDDLQRNKCYQEVAKLLRENRRKEIEIINAMVEEEAKKWKEAEGKE 922
Cdd:pfam15709 469 MEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
649-917 |
3.32e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.26 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 649 LMETTPTDIHpDSMLNVFVALTKGQYpvfnqYPKFIVDYQTQ-ERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWY 727
Cdd:pfam05483 444 LLQAREKEIH-DLEIQLTAIKTSEEH-----YLKEVEDLKTElEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKK 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 728 QKQELL--RKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKemhlQDAARRRFLKLQQDQQEMELRRLDDEIGRKNLT 805
Cdd:pfam05483 518 HQEDIIncKKQEERMLKQIENLEEKEMNLRDELESVREEFIQK----GDEVKCKLDKSEENARSIEYEVLKKEKQMKILE 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 806 ENQEALAKEMRadadayRRKVDLEE-HMFHKLIEAGETQSQKTQKVIKENLAKAEQACLNTdwqiqslhKQKCDDLQRNk 884
Cdd:pfam05483 594 NKCNNLKKQIE------NKNKNIEElHQENKALKKKGSAENKQLNAYEIKVNKLELELASA--------KQKFEEIIDN- 658
|
250 260 270
....*....|....*....|....*....|....*.
gi 1387845350 885 cYQ---EVAKLLRENRRKEIEIINAMVEEEAKKWKE 917
Cdd:pfam05483 659 -YQkeiEDKKISEEKLLEEVEKAKAIADEAVKLQKE 693
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
713-955 |
3.57e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.58 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 713 QAKVDQQRvedeawyqKQELLRKAEETRREMLLQEEEKmiqQRQRLAAVKRE-LKVKEMHLQDAARRRFLKLQQDQQEME 791
Cdd:PRK09510 69 QQQKSAKR--------AEEQRKKKEQQQAEELQQKQAA---EQERLKQLEKErLAAQEQKKQAEEAAKQAALKQKQAEEA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 792 LRRLDDEIGRKnltenqeALAKEMRADADAYRRKVDleehmfHKLIEAGETQSQKTQKVIKENLAKAeqaclntdwqiqs 871
Cdd:PRK09510 138 AAKAAAAAKAK-------AEAEAKRAAAAAKKAAAE------AKKKAEAEAAKKAAAEAKKKAEAEA------------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 872 lhKQKCDDLQRNKCYQEVAKllrenrrkeieiinaMVEEEAKKWKEAEGKEFRLRSAKKASALSDASRKWFLKQEINAAV 951
Cdd:PRK09510 192 --AAKAAAEAKKKAEAEAKK---------------KAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAK 254
|
....
gi 1387845350 952 EHAE 955
Cdd:PRK09510 255 AAAE 258
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
735-941 |
4.35e-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: 50.72 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 735 KAEETRREMLLQEEEKMIQQRQRL---AAVKRELKVKEMHLQDAARRRflkLQQDQQEMElrrlddEIGRKNLTENQEAL 811
Cdd:pfam15709 315 RSEEDPSKALLEKREQEKASRDRLraeRAEMRRLEVERKRREQEEQRR---LQQEQLERA------EKMREELELEQQRR 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 812 AKEMRAdadayrRKVDLEEhmfhklieagETQSQKTQKVIKENLAKAEQAclNTDWQIQSLHKqKCDDLQRNKcYQEVAK 891
Cdd:pfam15709 386 FEEIRL------RKQRLEE----------ERQRQEEEERKQRLQLQAAQE--RARQQQEEFRR-KLQELQRKK-QQEEAE 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387845350 892 LLREN--RRKEIEIINA--------MVEEE----AKKWKEAEGK-----EFRLRSAKKASALSDASRKW 941
Cdd:pfam15709 446 RAEAEkqRQKELEMQLAeeqkrlmeMAEEErleyQRQKQEAEEKarleaEERRQKEEEAARLALEEAMK 514
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
685-860 |
5.12e-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: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 685 VDYQTQERE---RIRNDELDylRERQTVEDMQakVDQQRVEDEAWYQKQellRKAEETRRemllQEEEKMIQQRQRLAAV 761
Cdd:pfam15709 350 VERKRREQEeqrRLQQEQLE--RAEKMREELE--LEQQRRFEEIRLRKQ---RLEEERQR----QEEEERKQRLQLQAAQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 762 KRELKvkemhLQDAARRRFLKLQQDQQEMELRRLDDEIGRK-----NLTENQEALAKEMRADADAYRRKVDLEEHMFHKL 836
Cdd:pfam15709 419 ERARQ-----QQEEFRRKLQELQRKKQQEEAERAEAEKQRQkelemQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLE 493
|
170 180
....*....|....*....|....
gi 1387845350 837 IEAGETQSQKTQKVIKENLAKAEQ 860
Cdd:pfam15709 494 AEERRQKEEEAARLALEEAMKQAQ 517
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
686-970 |
5.46e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 686 DYQTQERERIRNDELdYLRERQTVEDMQaKVDQQRVEDEAwyQKQELLRKAEETRR--EMLLQEEEKMIQQRQRLAAVKR 763
Cdd:PTZ00121 1078 DFDFDAKEDNRADEA-TEEAFGKAEEAK-KTETGKAEEAR--KAEEAKKKAEDARKaeEARKAEDARKAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 764 EL---KVKEMHLQDAARR--RFLKLQQDQQEMELRRLDD----------EIGRK--NLTENQEALAKEMRADADAYRR-- 824
Cdd:PTZ00121 1154 VEiarKAEDARKAEEARKaeDAKKAEAARKAEEVRKAEElrkaedarkaEAARKaeEERKAEEARKAEDAKKAEAVKKae 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 825 --KVDLEE----------HMFHKLIEAGETQSQKTQKVIK-------ENLAKAEQAcLNTDWQIQSLHKQKCDDLQRN-- 883
Cdd:PTZ00121 1234 eaKKDAEEakkaeeernnEEIRKFEEARMAHFARRQAAIKaeearkaDELKKAEEK-KKADEAKKAEEKKKADEAKKKae 1312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 884 -KCYQEVAKLLRENRRKEIEIINAMVEE-----EAKKwKEAEGKEFRLRSAKKaSALSDASRKWFLKQEINAAVEHAENP 957
Cdd:PTZ00121 1313 eAKKADEAKKKAEEAKKKADAAKKKAEEakkaaEAAK-AEAEAAADEAEAAEE-KAEAAEKKKEEAKKKADAAKKKAEEK 1390
|
330
....*....|...
gi 1387845350 958 CHKEEPRFQNEQD 970
Cdd:PTZ00121 1391 KKADEAKKKAEED 1403
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
690-917 |
7.19e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 7.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 690 QERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELK-VK 768
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKaLR 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 769 EMH--LQDAA---RRRFLKLQQDQQEME---------LRRLDDEIgrKNLTENQEALAKEM---RADADAYRRKVD---- 827
Cdd:TIGR02168 803 EALdeLRAELtllNEEAANLRERLESLErriaaterrLEDLEEQI--EELSEDIESLAAEIeelEELIEELESELEalln 880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 828 ----LEEHMfhKLIEAGETQSQKTQKVIKENLAKAEQAC---------LNTDWQ-----IQSLHKQ-------------- 875
Cdd:TIGR02168 881 erasLEEAL--ALLRSELEELSEELRELESKRSELRRELeelreklaqLELRLEglevrIDNLQERlseeysltleeaea 958
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1387845350 876 --KCDDLQRNKCYQEVAKLlrENRRKEIEIINAMVEEEAKKWKE 917
Cdd:TIGR02168 959 leNKIEDDEEEARRRLKRL--ENKIKELGPVNLAAIEEYEELKE 1000
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
691-934 |
7.63e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 7.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 691 ERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKEM 770
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 771 HLQDAARRRFLKLQQDQQEMELRRLDdeigRKNLTENQEALAKEMRADADAYRRKVDLEEHMFHKLIEAGETQSQKTQKv 850
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEE----LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE- 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 851 ikenLAKAEQACLNTDWQIQSLHKQkcddLQRNKcyQEVAKLLRENRRKEIEIINAMVEEEAKKWKEAEGKEFRLRSAKK 930
Cdd:COG1196 388 ----LLEALRAAAELAAQLEELEEA----EEALL--ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
....
gi 1387845350 931 ASAL 934
Cdd:COG1196 458 EEAL 461
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
691-962 |
1.24e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.58 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 691 ERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAwYQKQELLRKAEETRREM------LLQEEEKMIQQRQRLAAVKRE 764
Cdd:pfam02463 690 AKEEILRRQLEIKKKEQREKEELKKLKLEAEELLA-DRVQEAQDKINEELKLLkqkideEEEEEEKSRLKKEEKEEEKSE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 765 LKVKEMHLQDAARRRFLKLQQDQQEMELRRLDDEIGRKNLTENQEALAKEmradadayrrkvdleehmfhKLIEAGETQS 844
Cdd:pfam02463 769 LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLE--------------------EEQLLIEQEE 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 845 QKTQKVIKENLAKAEQAclntdwQIQSLHKQKCDDLQRNKCYQEVAKLLRENRRKEIEIINAMVEEEAKKWKEAEGKEFR 924
Cdd:pfam02463 829 KIKEEELEELALELKEE------QKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKEL 902
|
250 260 270
....*....|....*....|....*....|....*...
gi 1387845350 925 LRSAKKASALSDASRKWFLKQEINAAVEHAENPCHKEE 962
Cdd:pfam02463 903 EEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEEL 940
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
692-970 |
1.32e-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: 49.28 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 692 RERIRNDELDYL--------RERQTVEDMQAKVDQQRVEDEAwyQKQELLRKAEETRREMLLQEEEKMIQQrQRLAAVKR 763
Cdd:TIGR02168 219 KAELRELELALLvlrleelrEELEELQEELKEAEEELEELTA--ELQELEEKLEELRLEVSELEEEIEELQ-KELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 764 ELKVKEMHLQDA-ARRRFLKLQQDQQEMEL----RRLDDEIGRKNLTENQEALAKEMRADADAyrrkvDLEEhmFHKLIE 838
Cdd:TIGR02168 296 EISRLEQQKQILrERLANLERQLEELEAQLeeleSKLDELAEELAELEEKLEELKEELESLEA-----ELEE--LEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 839 AGETQSQKTQKVI-----KENLAKAEQACLNTdwQIQSLHKQKCD-DLQRNKCYQEVAKLLRENRRKEIEIINAMVEEEA 912
Cdd:TIGR02168 369 ELESRLEELEEQLetlrsKVAQLELQIASLNN--EIERLEARLERlEDRRERLQQEIEELLKKLEEAELKELQAELEELE 446
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387845350 913 KKWKEAEGKEFRLRSAKKasALSDASRKwfLKQEINAA---VEHAENPCHKEEPRFQNEQD 970
Cdd:TIGR02168 447 EELEELQEELERLEEALE--ELREELEE--AEQALDAAereLAQLQARLDSLERLQENLEG 503
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
688-914 |
1.53e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 48.38 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 688 QTQERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKV 767
Cdd:pfam13868 133 DEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQ 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 768 KEmhLQDAARRRFLKLQQDQQEMELrrlddeigrknltENQEALAKEMRADADAYRRKVDLEEHMFHKLIEAGETQSQKT 847
Cdd:pfam13868 213 EE--QERKERQKEREEAEKKARQRQ-------------ELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIE 277
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387845350 848 QKVIKENLAKAEQACLNTDWQIQSLHKQKCDDLQRNkcYQEVAKLlrenrRKEIEIINAMVEEEAKK 914
Cdd:pfam13868 278 QEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEE--LEEGERL-----REEEAERRERIEEERQK 337
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
691-1024 |
1.95e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 691 ERERIRNDELDYLRE-RQTVEDMQAKVDQQRVEDEAwYQKQELLRKAEETRREmllQEEEKMIQQRQRLAAVKRelkvke 769
Cdd:PTZ00121 1401 EEDKKKADELKKAAAaKKKADEAKKKAEEKKKADEA-KKKAEEAKKADEAKKK---AEEAKKAEEAKKKAEEAK------ 1470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 770 mhlqdaarrrflKLQQDQQEMELRRLDDEIGRKnlTENQEALAKEMRADADAYRRKVDL----EEHMFHKLIEAGET--- 842
Cdd:PTZ00121 1471 ------------KADEAKKKAEEAKKADEAKKK--AEEAKKKADEAKKAAEAKKKADEAkkaeEAKKADEAKKAEEAkka 1536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 843 -QSQKTQKVIK-ENLAKAEQacLNTDWQIQSLHKQKCDDLQRNKCYQ--EVAKLLRENRRKEI----EIINAMVEEEAKK 914
Cdd:PTZ00121 1537 dEAKKAEEKKKaDELKKAEE--LKKAEEKKKAEEAKKAEEDKNMALRkaEEAKKAEEARIEEVmklyEEEKKMKAEEAKK 1614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 915 WKEAEGKEFRLRSAKKASALSDASRKWfLKQEINAAVE----HAENPCHKEEPRFQNEQDSSclpRTSQLNDSSEMDPST 990
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKK-EAEEKKKAEElkkaEEENKIKAAEEAKKAEEDKK---KAEEAKKAEEDEKKA 1690
|
330 340 350
....*....|....*....|....*....|....
gi 1387845350 991 QISLNRRAVEwdttgqnlIKKVRNLRQRLTARAR 1024
Cdd:PTZ00121 1691 AEALKKEAEE--------AKKAEELKKKEAEEKK 1716
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
704-952 |
2.61e-05 |
|
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: 47.72 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 704 RERQTVEDMQAKV-------DQQRVEDEAWyqkqELLRKAEETRREMLLQEEEKMIQQ--RQRLAAV------------- 761
Cdd:pfam15558 5 RDRKIAALMLARHkeeqrmrELQQQAALAW----EELRRRDQKRQETLERERRLLLQQsqEQWQAEKeqrkarlgreerr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 762 KRELKVKEMHLQDAARRRFLKLQ--QDQQEMELRRLDDEIgRKnltENQEALAKEMRADADAYRRKVDLEEHmfHKLIEA 839
Cdd:pfam15558 81 RADRREKQVIEKESRWREQAEDQenQRQEKLERARQEAEQ-RK---QCQEQRLKEKEEELQALREQNSLQLQ--ERLEEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 840 G------ETQSQK--------------TQKVIKENLAKAEQACLNTDWQIQSLHKQKCDDLQRNKCYQEvaklLRENRRK 899
Cdd:pfam15558 155 ChkrqlkEREEQKkvqennlsellnhqARKVLVDCQAKAEELLRRLSLEQSLQRSQENYEQLVEERHRE----LREKAQK 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387845350 900 EIEIIN------AMVEEEAKKWKEA--EGKEFRLRSAKKASALSdASRKWFLKQEINAAVE 952
Cdd:pfam15558 231 EEEQFQrakwraEEKEEERQEHKEAlaELADRKIQQARQVAHKT-VQDKAQRARELNLERE 290
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
684-902 |
3.78e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 47.22 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 684 IVDYQTQERERIRNDELDYLRErqtvEDMQAKVDQQRVEDEawYQKQELLRKAE------------ETRREMLLQEEEKM 751
Cdd:pfam13868 23 ERDAQIAEKKRIKAEEKEEERR----LDEMMEEERERALEE--EEEKEEERKEErkryrqeleeqiEEREQKRQEEYEEK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 752 IQQRQRLAAVKRELKVKEMHLQDAARRRFLKLQQDQQEM-ELRRLDDEIgrknltENQEALAKEMRadADAYRRKVDLEE 830
Cdd:pfam13868 97 LQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFnEEQAEWKEL------EKEEEREEDER--ILEYLKEKAERE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387845350 831 HMFHKLIEAGETQSQKTQKVIKENLAKAEQaclntdwqiqslhKQKCDDLQRNKCYQEVAKllRENRRKEIE 902
Cdd:pfam13868 169 EEREAEREEIEEEKEREIARLRAQQEKAQD-------------EKAERDELRAKLYQEEQE--RKERQKERE 225
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
649-1034 |
3.94e-05 |
|
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: 47.66 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 649 LMETTPTDIHPDSMLNVF----------VALTKgQYPVFNQYPKFIVDYQTqERERIRNDELDYLRE-RQTVEDMQAKVD 717
Cdd:TIGR00618 169 LMNLFPLDQYTQLALMEFakkkslhgkaELLTL-RSQLLTLCTPCMPDTYH-ERKQVLEKELKHLREaLQQTQQSHAYLT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 718 QQRVEDEAWYQKQELLRKA--------------EETRREM--------LLQEEEKMIQQRQRLAAVKRELKVKE------ 769
Cdd:TIGR00618 247 QKREAQEEQLKKQQLLKQLrarieelraqeavlEETQERInrarkaapLAAHIKAVTQIEQQAQRIHTELQSKMrsrakl 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 770 -MHLQDAARRRFLKLQQDQQEMELRRLDDEIGRKNlteNQEALAKEMRADADAyrrkvdlEEHMFHKLieagetQSQKTQ 848
Cdd:TIGR00618 327 lMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAH---EVATSIREISCQQHT-------LTQHIHTL------QQQKTT 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 849 KVIKENLAKAEQACLNTDWQIQSLHKQKCDDLQRNKCyqeVAKLLRENRRKEIEIINAMVEEEAKKWKEAEGKEFRLRSA 928
Cdd:TIGR00618 391 LTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLA---HAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQS 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 929 KKASALSDASRKWFLKQ--EINAAVEHAENPcHKEEPRFQNEQDSSCLPRTSQLNDSSEMDPSTQISLNRRA----VEWD 1002
Cdd:TIGR00618 468 LKEREQQLQTKEQIHLQetRKKAVVLARLLE-LQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAqletSEED 546
|
410 420 430
....*....|....*....|....*....|..
gi 1387845350 1003 TTGQnlIKKVRNLRQRLTARARHRCQTPHLLA 1034
Cdd:TIGR00618 547 VYHQ--LTSERKQRASLKEQMQEIQQSFSILT 576
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
728-941 |
5.42e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 728 QKQELLRKAEETRREmLLQEEEKMIQQRQRLAAVKRELKVKEMHLQDAARR-RFLKLQQDQQEMELRRLDDEIG--RKNL 804
Cdd:COG4942 21 AAAEAEAELEQLQQE-IAELEKELAALKKEEKALLKQLAALERRIAALARRiRALEQELAALEAELAELEKEIAelRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 805 TENQEALAKEMRAD------------------ADAYRRKVDLEEHMFHKLIEAGETQSQKTQKVIKENLAKAEQACLNTD 866
Cdd:COG4942 100 EAQKEELAELLRALyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387845350 867 WQIQSLHKQKCDDLQRNKcyQEVAKLLRENRRKEIEIINAMVEEEA---KKWKEAEGKEFRLRSAKKASALSDASRKW 941
Cdd:COG4942 180 LAELEEERAALEALKAER--QKLLARLEKELAELAAELAELQQEAEeleALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
684-917 |
6.95e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 6.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 684 IVDYQTQERERIrnDELDYLRE--RQTVEDMQAKVDqqRVED--EAWYQKQELLRKAE------ETRREMLLQEEEKMIQ 753
Cdd:PRK02224 466 HVETIEEDRERV--EELEAELEdlEEEVEEVEERLE--RAEDlvEAEDRIERLEERREdleeliAERRETIEEKRERAEE 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 754 QRQRL------AAVKRELKVKEMHLQDAARRRFLKLQQDQQEmelrrLDDEIGRKNLTENQEALAKEMRADADAYRRK-- 825
Cdd:PRK02224 542 LRERAaeleaeAEEKREAAAEAEEEAEEAREEVAELNSKLAE-----LKERIESLERIRTLLAAIADAEDEIERLREKre 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 826 --VDLEEHMFHKLIEAGETQSQKTQKVIKENLAKAEQaclntdwqiqslhkqkcdDLQRNKCYQE-VAKLLRENRRKEIE 902
Cdd:PRK02224 617 alAELNDERRERLAEKRERKRELEAEFDEARIEEARE------------------DKERAEEYLEqVEEKLDELREERDD 678
|
250
....*....|....*..
gi 1387845350 903 IINA--MVEEEAKKWKE 917
Cdd:PRK02224 679 LQAEigAVENELEELEE 695
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
115-153 |
8.19e-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: 8.19e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1387845350 115 TKELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWD 153
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDgTIKLWD 40
|
|
| TBC |
smart00164 |
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ... |
501-609 |
8.25e-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: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 501 AFP-FVKLFQNNQLIcFEVIATLIINWCQHWFEYFpnppinilsmienvLAFHDKELLQHFIDHDITSQLYAWPLLETVF 579
Cdd:smart00164 112 AFWcLVKLMERYGPN-FYLPDMSGLQLDLLQLDRL--------------VKEYDPDLYKHLKDLGITPSLYALRWFLTLF 176
|
90 100 110
....*....|....*....|....*....|
gi 1387845350 580 SEVLTREEWLKLFDNIFSNHPSFLLMTVVA 609
Cdd:smart00164 177 ARELPLEIVLRIWDVLFAEGSDFLFRVALA 206
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
690-882 |
8.25e-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: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 690 QERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQR-----QRLAAVKRE 764
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKleelkEELESLEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 765 LKVKEMHLQDA-------------ARRRF--LKLQQDQQEMELRRLDDEI-----GRKNLTENQEALAKEM-RADADAYR 823
Cdd:TIGR02168 360 LEELEAELEELesrleeleeqletLRSKVaqLELQIASLNNEIERLEARLerledRRERLQQEIEELLKKLeEAELKELQ 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1387845350 824 RKVDLEEHMFHKLIEAGETQSQKTQKvIKENLAKAEQACLNTDWQIQSLhKQKCDDLQR 882
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEE-LREELEEAEQALDAAERELAQL-QARLDSLER 496
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
773-933 |
2.10e-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: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 773 QDAARR---RFLKLQQDQQEMELRRLDDEIGRKNLTENQEAlAKEMRADADAyrRKVDLEEHMfhkliEAGEtqsqKTQK 849
Cdd:TIGR02794 60 KPAAKKeqeRQKKLEQQAEEAEKQRAAEQARQKELEQRAAA-EKAAKQAEQA--AKQAEEKQK-----QAEE----AKAK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 850 VIKENLAKAEQAclntdwqiqsLHKQKCDDLQRnKCYQEVAKLLRENRRKEIEIINAMVEEEAKKWKEAEGKEFRLRSAK 929
Cdd:TIGR02794 128 QAAEAKAKAEAE----------AERKAKEEAAK-QAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKA 196
|
....
gi 1387845350 930 KASA 933
Cdd:TIGR02794 197 KAEA 200
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
688-861 |
2.60e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.65 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 688 QTQERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQE---LLRKAEETRREMLLQEEekmiQQRQRLAAVKRE 764
Cdd:COG3064 11 EAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEeeaREAKAEAEQRAAELAAE----AAKKLAEAEKAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 765 LKVKEMHLQDAARrrflKLQQDQQEMELRRLDDEIGRKNLTENQEALAKEMRADADAYRRKVDlEEHMFHKLIEAGETQS 844
Cdd:COG3064 87 AEAEKKAAAEKAK----AAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAE-AEAAAKAEAEAARAAA 161
|
170
....*....|....*..
gi 1387845350 845 QKTQKVIKENLAKAEQA 861
Cdd:COG3064 162 AAAAAAAAAAARAAAGA 178
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
690-853 |
2.77e-04 |
|
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: 45.10 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 690 QERERIRNDELDYLRE--RQTVEDMQAKVDQ-----QRVEDEAWYQKQEL---------LRKAEETRREML--LQEEEKM 751
Cdd:pfam05483 540 EEKEMNLRDELESVREefIQKGDEVKCKLDKseenaRSIEYEVLKKEKQMkilenkcnnLKKQIENKNKNIeeLHQENKA 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 752 IQQRQRlAAVKR----ELKVKEMHLQ-DAARRRFLKLQQD-QQEMELRRLDDEigrkNLTENQEAlAKEMRADADAYRRK 825
Cdd:pfam05483 620 LKKKGS-AENKQlnayEIKVNKLELElASAKQKFEEIIDNyQKEIEDKKISEE----KLLEEVEK-AKAIADEAVKLQKE 693
|
170 180
....*....|....*....|....*....
gi 1387845350 826 VDLE-EHMFHKLIEAGETQSQKTQKVIKE 853
Cdd:pfam05483 694 IDKRcQHKIAEMVALMEKHKHQYDKIIEE 722
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
707-950 |
4.45e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 43.68 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 707 QTVEDMQAK-VDQQRVEDEAWYQKQELL--RKAEETRREMLLQEEEKMIQQRQRLAAVKRELKvkemhlQDAARrrflkl 783
Cdd:TIGR02794 33 GGAEIIQAVlVDPGAVAQQANRIQQQKKpaAKKEQERQKKLEQQAEEAEKQRAAEQARQKELE------QRAAA------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 784 QQDQQEMELRRLDDEIGRKNLTENQEALAKEMRADADAYRRKvdleehmfhKLIEAGETQSQKTQKVIKENLAKAEQAcl 863
Cdd:TIGR02794 101 EKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAER---------KAKEEAAKQAEEEAKAKAAAEAKKKAE-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 864 NTDWQIQSLHKQKCDDLqrnkcyqevAKLLRENRRKEIEIINAMVEEEAKKWKEAEgKEFRLRSAKKASALSDASRKWF- 942
Cdd:TIGR02794 170 EAKKKAEAEAKAKAEAE---------AKAKAEEAKAKAEAAKAKAAAEAAAKAEAE-AAAAAAAEAERKADEAELGDIFg 239
|
....*...
gi 1387845350 943 LKQEINAA 950
Cdd:TIGR02794 240 LASGSNAE 247
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
688-969 |
4.92e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 688 QTQERERIRNDE---------LDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRRemllQEEEKMIQQRQRL 758
Cdd:PTZ00121 1241 EAKKAEEERNNEeirkfeearMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK----ADEAKKKAEEAKK 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 759 AavkRELKVKEMHLQDAARRRFLKLQQDQQEMELRRLDDEIGRKNL---TENQEALAK---EMRADADAYRRKVDlEEHM 832
Cdd:PTZ00121 1317 A---DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAeaaEEKAEAAEKkkeEAKKKADAAKKKAE-EKKK 1392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 833 FHKLIEAGETQSQKTQKVIKENLA--KAEQAclntdwQIQSLHKQKCDDLQRNKcyqEVAKLLRENRRKeieiinamvEE 910
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADELKKAAAAkkKADEA------KKKAEEKKKADEAKKKA---EEAKKADEAKKK---------AE 1454
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 911 EAKKWKEAEGKEFRLRSAKKASALSDASRKW-FLKQEINAAVEHAENPCHKEEPRFQNEQ 969
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKAdEAKKKAEEAKKKADEAKKAAEAKKKADE 1514
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
689-845 |
5.39e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.71 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 689 TQERERIRNDeldylRERQTvEDMQAKVDQQRVEDEAwYQKQEL--LRKAEETRREMLLQEEEKMIQQRQR--------L 758
Cdd:COG2268 198 IRDARIAEAE-----AERET-EIAIAQANREAEEAEL-EQEREIetARIAEAEAELAKKKAEERREAETARaeaeaayeI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 759 AAVKRELKVkEMHLQDAARRRFLKLQQDQQEMELRRLDDEIGRKNLTENQEALAKEmRADADAYRRKVDLEEHMFHKLIE 838
Cdd:COG2268 271 AEANAEREV-QRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEA-EAEAEAIRAKGLAEAEGKRALAE 348
|
....*..
gi 1387845350 839 AGETQSQ 845
Cdd:COG2268 349 AWNKLGD 355
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
690-825 |
5.94e-04 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 43.05 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 690 QERERIR-NDELdyLRERqtvedMQAKVDQQRvedeawYQKQELLRKAEEtrremllqeeekmiqqrqrlaAVKRelkvk 768
Cdd:pfam12037 98 QKQQRAQyQDEL--ARKR-----YQDQLEAQR------RRNEELLRKQEE---------------------SVAK----- 138
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1387845350 769 emhlQDAARRRFLKLQQDQQEMELRRlddEIGRKNLTENQEALAKEMRADADAYRRK 825
Cdd:pfam12037 139 ----QEAMRIQAQRRQTEEHEAELRR---ETERAKAEAEAEARAKEERENEDLNLEQ 188
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
706-860 |
6.00e-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: 43.79 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 706 RQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQ----RLAavKRELKVKEMHLQDAARRRFL 781
Cdd:pfam15709 335 RDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRfeeiRLR--KQRLEEERQRQEEEERKQRL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 782 KLQQDQ-----QEMELRRLDDEIGRKNLTENQEalakemRADADAYRRKvDLEEHMF--HK-LIEAGETQSQKTQKVIKE 853
Cdd:pfam15709 413 QLQAAQerarqQQEEFRRKLQELQRKKQQEEAE------RAEAEKQRQK-ELEMQLAeeQKrLMEMAEEERLEYQRQKQE 485
|
....*..
gi 1387845350 854 NLAKAEQ 860
Cdd:pfam15709 486 AEEKARL 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
696-934 |
6.74e-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: 43.89 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 696 RNDELDYLRER-----QTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRR------EMLLQEEEKMIQQ---------- 754
Cdd:TIGR02168 675 RRREIEELEEKieeleEKIAELEKALAELRKELEELEEELEQLRKELEELSrqisalRKDLARLEAEVEQleeriaqlsk 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 755 -RQRLAAVKRELKVKEMHLQDAARRRFLKLQQDQQEMELRRLDDEIGRKNLTENQEALAKEMRADADAYRRKVDLEEHMF 833
Cdd:TIGR02168 755 eLTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 834 HKLIEAGETQSQKtqKVIKENLAKAEQACLNTDWQIQSLHKQkcddLQRNKCYQEVAKLLRENRRKEIEIINAMVEEEAK 913
Cdd:TIGR02168 835 ATERRLEDLEEQI--EELSEDIESLAAEIEELEELIEELESE----LEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260
....*....|....*....|.
gi 1387845350 914 KWKEAEGKEFRLRSAKKASAL 934
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLEL 929
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
690-838 |
8.15e-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: 8.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 690 QERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAwyQKQELLRKAEETRREMLLQEEEKMIQQRQRLAA----VKREL 765
Cdd:pfam13868 193 QEKAQDEKAERDELRAKLYQEEQERKERQKEREEAE--KKARQRQELQQAREEQIELKERRLAEEAEREEEeferMLRKQ 270
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387845350 766 KVKEMHLQDAARRRFLKLQQDQQEMElRRLDDEIGRKNLTENQEALAKEMRADADAYRRKVdLEEHMFHKLIE 838
Cdd:pfam13868 271 AEDEEIEQEEAEKRRMKRLEHRRELE-KQIEEREEQRAAEREEELEEGERLREEEAERRER-IEEERQKKLKE 341
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
690-1029 |
9.07e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 43.28 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 690 QERERIRNDELDYLRE-RQTVEDMQAkvDQQRVEDEAWYQKQELLRKAEETRREML-----LQEeekmiQQRQRLAAvkr 763
Cdd:NF041483 728 QERERAREQSEELLASaRKRVEEAQA--EAQRLVEEADRRATELVSAAEQTAQQVRdsvagLQE-----QAEEEIAG--- 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 764 eLKVKEMHLQDAARRrflklqQDQQEMELRRLDDEIGRKNLTENQEALAKEMRADADAYRRkvdLEEHMFHKLIEAGE-- 841
Cdd:NF041483 798 -LRSAAEHAAERTRT------EAQEEADRVRSDAYAERERASEDANRLRREAQEETEAAKA---LAERTVSEAIAEAErl 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 842 --TQSQKTQKVIKE---NLAKAEQACLNTDWQIQslhkqkcDDLQRNKC-YQEVAKLLRENRRKEIEIINAMVEEEAKKW 915
Cdd:NF041483 868 rsDASEYAQRVRTEasdTLASAEQDAARTRADAR-------EDANRIRSdAAAQADRLIGEATSEAERLTAEARAEAERL 940
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 916 KE---AEGKEFRLRSAKKASAL-----SDASRkwfLKQE----INAAVEHAENpCHKEEPRFQNEQDSSCLPRTSQLNDS 983
Cdd:NF041483 941 RDearAEAERVRADAAAQAEQLiaeatGEAER---LRAEaaetVGSAQQHAER-IRTEAERVKAEAAAEAERLRTEAREE 1016
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387845350 984 SE--MDPSTQISLNRRA----------VEWDTTGQNLIKKVRNLRQRLTARARHRCQT 1029
Cdd:NF041483 1017 ADrtLDEARKDANKRRSeaaeqadtliTEAAAEADQLTAKAQEEALRTTTEAEAQADT 1074
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
681-813 |
1.20e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 681 PKFIVDyqtQERERIRNDELDylrerqtVEDMQAKVDQQRVE-DEAWYQKQELLRKAEETRREMllqeEEKMIQQRQRLA 759
Cdd:PRK00409 500 PENIIE---EAKKLIGEDKEK-------LNELIASLEELERElEQKAEEAEALLKEAEKLKEEL----EEKKEKLQEEED 565
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1387845350 760 AVKRELKVKEMHLQDAARRRFLKLQQDQQEMElRRLDDEIGRKNLTENQEALAK 813
Cdd:PRK00409 566 KLLEEAEKEAQQAIKEAKKEADEIIKELRQLQ-KGGYASVKAHELIEARKRLNK 618
|
|
| PRK02292 |
PRK02292 |
V-type ATP synthase subunit E; Provisional |
709-838 |
1.34e-03 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 235026 [Multi-domain] Cd Length: 188 Bit Score: 41.14 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 709 VEDMQ--AKVDQQRVEDEAWYQKQELLRKAEETRREML---LQEEEKMIQQ--RQRLAAVKRELKVKEMhlqdAARRRFL 781
Cdd:PRK02292 7 VEDIRdeARARASEIRAEADEEAEEIIAEAEADAEEILedrEAEAEREIEQlrEQELSSAKLEAKRERL----NARKEVL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387845350 782 KLQQDQQEMELRRLDDeigrknltENQEALAKEMRADADA-----YRRKVDleEHMFHKLIE 838
Cdd:PRK02292 83 EDVRNQVEDEIASLDG--------DKREELTKSLLDAADAdgvrvYSRKDD--EDLVKSLLS 134
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
116-153 |
1.45e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 37.32 E-value: 1.45e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1387845350 116 KELVSWMRGHESSVFSISVHASGKYAITTSSD-TAQLWD 153
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDgTVKVWD 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
717-909 |
1.80e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 717 DQQRVEDEAWY-------QKQELLRKAEETRREMLLQEEekmiqQRQRLAAVKRELKVKEMHLQDAARRRFLKLQQDQQE 789
Cdd:COG4913 593 DDRRRIRSRYVlgfdnraKLAALEAELAELEEELAEAEE-----RLEALEAELDALQERREALQRLAEYSWDEIDVASAE 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 790 MELRRLDDEigRKNLTENQEALAK-EMRADAdAYRRKVDLEEHMFHKLIEAGETQSQKTQKV--IKENLAKAEQACLNTD 866
Cdd:COG4913 668 REIAELEAE--LERLDASSDDLAAlEEQLEE-LEAELEELEEELDELKGEIGRLEKELEQAEeeLDELQDRLEAAEDLAR 744
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1387845350 867 WQIQSLHKQKCDDLQRNKCYQEVAKLLRENR--------RKEIEIINAMVE 909
Cdd:COG4913 745 LELRALLEERFAAALGDAVERELRENLEERIdalrarlnRAEEELERAMRA 795
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
689-925 |
1.85e-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: 42.26 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 689 TQERER-----IRNDELDYLRERQTVED-MQAKVDQQRVEDEAWYQKQELLRKaeetrremLLQEEEKMIQQRQRLAAVK 762
Cdd:TIGR00618 656 TQERVRehalsIRVLPKELLASRQLALQkMQSEKEQLTYWKEMLAQCQTLLRE--------LETHIEEYDREFNEIENAS 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 763 RELKvKEMHLQDAARRRFLKLQQDQQEMELRRLDDEIGRKnlteNQEALAKEMRADADAyrrKVDLEEHMFHKLIEAGET 842
Cdd:TIGR00618 728 SSLG-SDLAAREDALNQSLKELMHQARTVLKARTEAHFNN----NEEVTAALQTGAELS---HLAAEIQFFNRLREEDTH 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 843 QSQKTQKVIKENLAKAEQACLNTDWQIQslhkqkcddlqrnKCYQEVAKLLRENRRKEIEIINAM--VEEEAKKWKEAEG 920
Cdd:TIGR00618 800 LLKTLEAEIGQEIPSDEDILNLQCETLV-------------QEEEQFLSRLEEKSATLGEITHQLlkYEECSKQLAQLTQ 866
|
....*
gi 1387845350 921 KEFRL 925
Cdd:TIGR00618 867 EQAKI 871
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
684-964 |
2.28e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.78 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 684 IVDYQTQERERIRNDELDYLRERQTvEDMQAKVDQQRVEDE--AWYQKQEL-----------------LRKAEETRREML 744
Cdd:pfam02029 1 IEDEEEAARERRRRAREERRRQKEE-EEPSGQVTESVEPNEhnSYEEDSELkpsgqggldeeeafldrTAKREERRQKRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 745 LQEEEKMIQQRQRLAAVKRELKVKEMHLQDAARRRFLklQQDQQEMELRRLDDEIGRKNLTENQEALAKEMRADADAYRR 824
Cdd:pfam02029 80 QEALERQKEFDPTIADEKESVAERKENNEEEENSSWE--KEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 825 KVDLEEhmfhKLIEAGETQSQKTQKVIKENlAKAEQACLNTD---WQIQSLH-KQKcddlQRNKCYQEVAKLLRENRRKE 900
Cdd:pfam02029 158 EEEDKS----EEAEEVPTENFAKEEVKDEK-IKKEKKVKYESkvfLDQKRGHpEVK----SQNGEEEVTKLKVTTKRRQG 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387845350 901 IEIINAMVEEEAKKWKEAEGK--EFRLRSAKKASAlsDASRKWFLKQEinAAVEHAENPCHKEEPR 964
Cdd:pfam02029 229 GLSQSQEREEEAEVFLEAEQKleELRRRRQEKESE--EFEKLRQKQQE--AELELEELKKKREERR 290
|
|
| PDCD7 |
pfam16021 |
Programmed cell death protein 7; |
718-825 |
2.49e-03 |
|
Programmed cell death protein 7;
Pssm-ID: 464979 [Multi-domain] Cd Length: 305 Bit Score: 41.25 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 718 QQRVEDEA-WyqkQELLRKAEETRREmlLQEEEKMIQQRQRLAAVKREL-KVKEMHLQDAARRRFLKLQQDQQEMELRRL 795
Cdd:pfam16021 28 RENVEDDSvW---SESYSRAAELKHE--LQEKLLLLEDPELLESLKRKLeRRQKKRLRRKRRKEERKEEKKEEQERRAER 102
|
90 100 110
....*....|....*....|....*....|....*...
gi 1387845350 796 DDEIG----RKNLTENQEALAKEMRADADAY----RRK 825
Cdd:pfam16021 103 EAKIDkwrrKQIQEVEEKKRERELKLAADAVlsevRKK 140
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
722-907 |
2.90e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 722 EDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLaavKRELKVKEMHLQDAARRrflkLQQ-----DQQEMELRRLD 796
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEF---EKELRERRNELQKLEKR----LLQkeenlDRKLELLEKRE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 797 DEI--GRKNLTENQEALaKEMRADADayrrkvDLEEHMFHKLIE-AGETQSQKTQKVIKENLAKAEQaclntdwQIQSLH 873
Cdd:PRK12704 110 EELekKEKELEQKQQEL-EKKEEELE------ELIEEQLQELERiSGLTAEEAKEILLEKVEEEARH-------EAAVLI 175
|
170 180 190
....*....|....*....|....*....|....
gi 1387845350 874 KQkcddlqrnkcYQEVAKLLRENRRKEIeIINAM 907
Cdd:PRK12704 176 KE----------IEEEAKEEADKKAKEI-LAQAI 198
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
728-955 |
3.02e-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: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 728 QKQELLRKAEETRREmLLQEEEKMIQQRQRLAAVKRELKVKEmhlqdaARRRFLklqqdqqEMELrrlddEIGRKNLTEN 807
Cdd:COG3096 279 ERRELSERALELRRE-LFGARRQLAEEQYRLVEMARELEELS------ARESDL-------EQDY-----QAASDHLNLV 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 808 QEALAKEMRADadayRRKVDLEEhmfhkLIEAGETQSQKTQKViKENLAKAEQACLNTDWQIQSLHKQKCD-----DLQ- 881
Cdd:COG3096 340 QTALRQQEKIE----RYQEDLEE-----LTERLEEQEEVVEEA-AEQLAEAEARLEAAEEEVDSLKSQLADyqqalDVQq 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 882 -RNKCYQEVAKLLRENRR----KEIEIINAMVEEEAKKWKEAEGKEfRLRSAKKASALSDASRKWF-----LKQEINAAV 951
Cdd:COG3096 410 tRAIQYQQAVQALEKARAlcglPDLTPENAEDYLAAFRAKEQQATE-EVLELEQKLSVADAARRQFekayeLVCKIAGEV 488
|
....
gi 1387845350 952 EHAE 955
Cdd:COG3096 489 ERSQ 492
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
690-861 |
3.11e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 41.18 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 690 QERERIRNDELDYLRERQTVEDmQAKVDQQRVEDEAwyQKQELLRKAEETRREM---LLQEEEKMIQQRQRLAAVKRELK 766
Cdd:COG3064 39 AEEERLAELEAKRQAEEEAREA-KAEAEQRAAELAA--EAAKKLAEAEKAAAEAekkAAAEKAKAAKEAEAAAAAEKAAA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 767 VKEMHLQDAARRRFLKLQQDQQEMELRRLDDEIGRKNLTENQEALAKEMRADADAYRRKVDLEEHMFHKLIEAGETQSQK 846
Cdd:COG3064 116 AAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADT 195
|
170
....*....|....*
gi 1387845350 847 TQKVIKENLAKAEQA 861
Cdd:COG3064 196 AAAAAAALAAAAAAA 210
|
|
| COG5210 |
COG5210 |
GTPase-activating protein [General function prediction only]; |
542-658 |
3.43e-03 |
|
GTPase-activating protein [General function prediction only];
Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 41.33 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 542 LSMIENVLAFHDKELLQHFIDHDITSQLYAWPLLETVFSEVLTREEWLKLFDNIFSNHPSFLLMTVVAYNICSRTPLLSC 621
Cdd:COG5210 350 LKVLDDLVEELDPELYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKL 429
|
90 100 110
....*....|....*....|....*....|....*..
gi 1387845350 622 NLKDDFEFFFHHRNNLDINVVIRQVYHLMETTPTDIH 658
Cdd:COG5210 430 DSDELLDLLLKQLFLHSGKEAWSSILKFRHGTDRDIL 466
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
693-861 |
4.03e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 693 ERIRN--DELDYLRE-RQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREM----LLQEEEKMIQQRQRLAAVKREL 765
Cdd:COG4913 225 EAADAlvEHFDDLERaHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRaalrLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 766 KVKEmhlqdaARRRFLKLQQDQQEMELRRLDDEIgRKNLTENQEALAKEMRaDADAYRRKVDLEEHMFHKLIEAGETQSQ 845
Cdd:COG4913 305 ARLE------AELERLEARLDALREELDELEAQI-RGNGGDRLEQLEREIE-RLERELEERERRRARLEALLAALGLPLP 376
|
170
....*....|....*.
gi 1387845350 846 KTQKVIKENLAKAEQA 861
Cdd:COG4913 377 ASAEEFAALRAEAAAL 392
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
673-907 |
4.29e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.22 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 673 QYPVFNQYPKFIVDYQTQERERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAwyQKQELLRKAE---------ETRREM 743
Cdd:COG5022 783 LRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRET--EEVEFSLKAEvliqkfgrsLKAKKR 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 744 --LLQEEEKMIQQRQRLAAVKRELKVKEmhlQDAARRRFLKLQQDQQEMELRRLDDEIgRKNLTENQEALAKEMRADADA 821
Cdd:COG5022 861 fsLLKKETIYLQSAQRVELAERQLQELK---IDVKSISSLKLVNLELESEIIELKKSL-SSDLIENLEFKTELIARLKKL 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 822 yRRKVDLEEH---MFHKLIEAGETQSQKTQK----VIKENLAKAEQ--------ACLNTDWQIQSLHKQKCDdlqrNKCY 886
Cdd:COG5022 937 -LNNIDLEEGpsiEYVKLPELNKLHEVESKLketsEEYEDLLKKSTilvregnkANSELKNFKKELAELSKQ----YGAL 1011
|
250 260
....*....|....*....|.
gi 1387845350 887 QEVAKLLRENRRKEIEIINAM 907
Cdd:COG5022 1012 QESTKQLKELPVEVAELQSAS 1032
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
692-853 |
4.58e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.85 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 692 RERIRNDELDYLRERQTVEDMQAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAvkRELKVKEMH 771
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDA--RAEKLDNLE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 772 LQDAARRRFLKLQQDQQEMELRRLDDEIGRK-NLTENQ--EALAKEMRADAdayrrkvDLEEHMFHKLI--EAGETQSQK 846
Cdd:PRK12705 105 NQLEEREKALSARELELEELEKQLDNELYRVaGLTPEQarKLLLKLLDAEL-------EEEKAQRVKKIeeEADLEAERK 177
|
....*..
gi 1387845350 847 TQKVIKE 853
Cdd:PRK12705 178 AQNILAQ 184
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
713-795 |
5.72e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 39.87 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 713 QAKVDQQRVEDEAWYQKQELLRKAEETRREMLLQEEEKMIQQRQRLAAVKRELKVKEMHLQDAARRRFLKLQQDQQEMEL 792
Cdd:cd16269 208 EAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEI 287
|
...
gi 1387845350 793 RRL 795
Cdd:cd16269 288 RSL 290
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
698-914 |
7.07e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 40.33 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 698 DELDYLRERQTVEDMQAKVDQQRVE--DEAWYQKQELLRKAEETRREMLLQEEE--KMIQQRQRLAAVKRELKVKEMHLQ 773
Cdd:COG5185 240 DPESELEDLAQTSDKLEKLVEQNTDlrLEKLGENAESSKRLNENANNLIKQFENtkEKIAEYTKSIDIKKATESLEEQLA 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845350 774 DAARRRFLKLQQDQQEMELRRLDDEI--GRKNLTENQEALaKEMRADADAYRRKVDLEEHMF------HKLIEAGETQSQ 845
Cdd:COG5185 320 AAEAEQELEESKRETETGIQNLTAEIeqGQESLTENLEAI-KEEIENIVGEVELSKSSEELDsfkdtiESTKESLDEIPQ 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387845350 846 KTQKVIKENLAKAEQACLNTDWQIQSLHKQkCDDLQRNkcYQEVAKLLRE-------NRRKEIEIINAMVEEEAKK 914
Cdd:COG5185 399 NQRGYAQEILATLEDTLKAADRQIEELQRQ-IEQATSS--NEEVSKLLNEliselnkVMREADEESQSRLEEAYDE 471
|
|
| |
