|
Name |
Accession |
Description |
Interval |
E-value |
| NanM |
COG3055 |
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis]; |
77-391 |
9.95e-25 |
|
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442289 [Multi-domain] Cd Length: 277 Bit Score: 104.85 E-value: 9.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 77 KLKNSPFPRyRHSSSFIVtnDNRIFVTGGLHDQSVYGDVWqiaanadgtsftskRIDIDQNT-------PPPRVGHAST- 148
Cdd:COG3055 5 SLPDLPTPR-SEAAAALL--DGKVYVAGGLSGGSASNSFE--------------VYDPATNTwselaplPGPPRHHAAAv 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 149 -ICGNAYvVFGGDTHKLNKNGLLdDDLYLFNINSYKWTipqPIGRRPLGRYGHkisiiASNPMQTKLYLFGGQVDETYFN 227
Cdd:COG3055 68 aQDGKLY-VFGGFTGANPSSTPL-NDVYVYDPATNTWT---KLAPMPTPRGGA-----TALLLDGKIYVVGGWDDGGNVA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 228 DLVVFDLSSfrrpNShWeflEPVGDLPPPLTNHT-MVAYDNKLWVFGGetpktisndtYRYDPAQSEWSkvkTTGEKPPP 306
Cdd:COG3055 138 WVEVYDPAT----GT-W---TQLAPLPTPRDHLAaAVLPDGKILVIGG----------RNGSGFSNTWT---TLAPLPTA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 307 IQEHASVVYKHLMCVLGGKdthNAYSNDVYFLNLLSLKWYKLPRMkegiPQERSGHSLTLMKNEKLLIMGGDKTDYASPN 386
Cdd:COG3055 197 RAGHAAAVLGGKILVFGGE---SGFSDEVEAYDPATNTWTALGEL----PTPRHGHAAVLTDGKVYVIGGETKPGVRTPL 269
|
....*
gi 398366259 387 IHDLQ 391
Cdd:COG3055 270 VTSAE 274
|
|
| PLN02153 |
PLN02153 |
epithiospecifier protein |
139-379 |
1.67e-20 |
|
epithiospecifier protein
Pssm-ID: 177814 [Multi-domain] Cd Length: 341 Bit Score: 93.90 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 139 PPPRVGHASTICGNAYVVFGGDthkLNKNGLLDDDLYLFNINSYKWTIPQPIGRRP-LGRYGHKISIIAsnpmqTKLYLF 217
Cdd:PLN02153 20 PGPRCSHGIAVVGDKLYSFGGE---LKPNEHIDKDLYVFDFNTHTWSIAPANGDVPrISCLGVRMVAVG-----TKLYIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 218 GGQVDETYFNDLVVFDLSSfrrpnSHWEFLEPVGDL--PPPLTNHTMVAYDNKLWVFGG-------ETPK---TI----- 280
Cdd:PLN02153 92 GGRDEKREFSDFYSYDTVK-----NEWTFLTKLDEEggPEARTFHSMASDENHVYVFGGvskgglmKTPErfrTIeayni 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 281 -------------------------------------------------SNDTYRYDPAQSEWSKVKTTGEKPPPIQEHA 311
Cdd:PLN02153 167 adgkwvqlpdpgenfekrggagfavvqgkiwvvygfatsilpggksdyeSNAVQFFDPASGKWTEVETTGAKPSARSVFA 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366259 312 SVVYKHLMCVLGGK---DTHNAY-----SNDVYFLNLLSLKWYKLPRMKE-GIPQERSGHSLTLMKNEKLLIMGGDK 379
Cdd:PLN02153 247 HAVVGKYIIIFGGEvwpDLKGHLgpgtlSNEGYALDTETLVWEKLGECGEpAMPRGWTAYTTATVYGKNGLLMHGGK 323
|
|
| PLN02193 |
PLN02193 |
nitrile-specifier protein |
130-379 |
4.26e-19 |
|
nitrile-specifier protein
Pssm-ID: 177844 [Multi-domain] Cd Length: 470 Bit Score: 91.17 E-value: 4.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 130 KRIDIDQNT--PPPRVGHASTICGNAYVVFGGDthkLNKNGLLDDDLYLFNINSYKWTIPQPIGRRP-LGRYGHKISIIA 206
Cdd:PLN02193 152 KWIKVEQKGegPGLRCSHGIAQVGNKIYSFGGE---FTPNQPIDKHLYVFDLETRTWSISPATGDVPhLSCLGVRMVSIG 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 207 SNpmqtkLYLFGGQVDETYFNDLVVFDLSSfrrpnSHWEFLEPVGDLPPPLTNHTMVAYDNKLWVFGG----ETPKTIS- 281
Cdd:PLN02193 229 ST-----LYVFGGRDASRQYNGFYSFDTTT-----NEWKLLTPVEEGPTPRSFHSMAADEENVYVFGGvsatARLKTLDs 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 282 --------------------------------------------NDTYRYDPAQSEWSKVKTTGEKPPPIQEHAS-VVYK 316
Cdd:PLN02193 299 ynivdkkwfhcstpgdsfsirggaglevvqgkvwvvygfngcevDDVHYYDPVQDKWTQVETFGVRPSERSVFASaAVGK 378
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366259 317 HLMcVLGGKDTHN--------AYSNDVYFLNLLSLKWYKLPRM--KEGIPQER--SGHSLTLMKNEKLLIMGGDK 379
Cdd:PLN02193 379 HIV-IFGGEIAMDplahvgpgQLTDGTFALDTETLQWERLDKFgeEEETPSSRgwTASTTGTIDGKKGLVMHGGK 452
|
|
| NanM |
COG3055 |
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis]; |
248-378 |
3.02e-16 |
|
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442289 [Multi-domain] Cd Length: 277 Bit Score: 79.81 E-value: 3.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 248 EPVGDLPPPLTNHTMVAYDNKLWVFGGETPKTISNDTYRYDPAQSEWSKvktTGEKP-PPIQEHASVVYKHLMCVLGGKD 326
Cdd:COG3055 4 SSLPDLPTPRSEAAAALLDGKVYVAGGLSGGSASNSFEVYDPATNTWSE---LAPLPgPPRHHAAAVAQDGKLYVFGGFT 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 398366259 327 THNA---YSNDVYFLNLLSLKWYKLPRMkegiPQERSGHSLTLMKNEKLLIMGGD 378
Cdd:COG3055 81 GANPsstPLNDVYVYDPATNTWTKLAPM----PTPRGGATALLLDGKIYVVGGWD 131
|
|
| PLN02153 |
PLN02153 |
epithiospecifier protein |
186-384 |
4.92e-12 |
|
epithiospecifier protein
Pssm-ID: 177814 [Multi-domain] Cd Length: 341 Bit Score: 68.09 E-value: 4.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 186 IPQPIGRRPLGRYGHKISIIASnpmqtKLYLFGGQV--DETYFNDLVVFDLssfrrpNSH-WEFLEPVGDLPPPLT-NHT 261
Cdd:PLN02153 12 VEQKGGKGPGPRCSHGIAVVGD-----KLYSFGGELkpNEHIDKDLYVFDF------NTHtWSIAPANGDVPRISClGVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 262 MVAYDNKLWVFGGETPKTISNDTYRYDPAQSEWSKVKTTGEKPPPIQE--HASVVYKHLMCVLGGKDTHNAYSNDVYF-- 337
Cdd:PLN02153 81 MVAVGTKLYIFGGRDEKREFSDFYSYDTVKNEWTFLTKLDEEGGPEARtfHSMASDENHVYVFGGVSKGGLMKTPERFrt 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 398366259 338 ---LNLLSLKWYKLPRMKEGIpQERSGHSLTLMKNEKLLIMG-------GDKTDYAS 384
Cdd:PLN02153 161 ieaYNIADGKWVQLPDPGENF-EKRGGAGFAVVQGKIWVVYGfatsilpGGKSDYES 216
|
|
| PLN02193 |
PLN02193 |
nitrile-specifier protein |
167-377 |
2.66e-09 |
|
nitrile-specifier protein
Pssm-ID: 177844 [Multi-domain] Cd Length: 470 Bit Score: 60.35 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 167 NGLLDDDLYLFNINSYKWTIPQPIGRRPlgryghkisiiasnpmQTKLYLFGGQVDETYFNDLVVFD-----LSSFRRPN 241
Cdd:PLN02193 85 NDMTSEMITFLSFKTYKGKTSHPIEKRP----------------GVKFVLQGGKIVGFHGRSTDVLHslgayISLPSTPK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 242 SH--WEFLEPVGDLPPPLTNHTMVAYDNKLWVFGGE-TP-KTISNDTYRYDPAQSEWSKVKTTGEKPppiqehasvvykH 317
Cdd:PLN02193 149 LLgkWIKVEQKGEGPGLRCSHGIAQVGNKIYSFGGEfTPnQPIDKHLYVFDLETRTWSISPATGDVP------------H 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366259 318 LMC-------------VLGGKDTHNAYsNDVYFLNLLSLKWYKLPRMKEGiPQERSGHSLTlMKNEKLLIMGG 377
Cdd:PLN02193 217 LSClgvrmvsigstlyVFGGRDASRQY-NGFYSFDTTTNEWKLLTPVEEG-PTPRSFHSMA-ADEENVYVFGG 286
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
603-872 |
1.93e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.54 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 603 ARLKNLEIQKTFLESRINDLKNLLMVKLSQASKLCDQI-TIQNNGLKTCSEHVTIKRDIIDLENKCDVLKRQNEILVNNM 681
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIgEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 682 QKITPELHTYLNESSCYLGKLLKSYPTSARPPSSEKDNQIYE-KDSLNKIEKVINEMHetvRAKEKLHLETQKLNDERDS 760
Cdd:TIGR02169 761 KELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKlEEEVSRIEARLREIE---QKLNRLTLEKEYLEKEIQE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 761 LRANLLDNNNKLDALRKLSDGSSKSMDLTKKAIHLSQSELEKYRKNNDDLQKEIDRIKTEQAEQDDKQEQrgaITHGNFD 840
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE---LEAQIEK 914
|
250 260 270
....*....|....*....|....*....|..
gi 398366259 841 AFHRMKinNLKAELYMSKENRDSLKDELLALK 872
Cdd:TIGR02169 915 KRKRLS--ELKAKLEALEEELSEIEDPKGEDE 944
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
561-827 |
4.93e-08 |
|
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: 55.93 E-value: 4.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 561 QTLRLEAQQKELEtarhisQLEKEvqrlmvIKEASKDSNFQTARLKNLEIQKTFLESRINDLKNLLmvklsqaSKLCDQI 640
Cdd:COG4942 18 QADAAAEAEAELE------QLQQE------IAELEKELAALKKEEKALLKQLAALERRIAALARRI-------RALEQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 641 TIQNNGLKTcsehvtIKRDIIDLENKcdvLKRQNEILVNNMQKItpelhtYLNESSCYLGKLLksyptSARPPSSEKDNQ 720
Cdd:COG4942 79 AALEAELAE------LEKEIAELRAE---LEAQKEELAELLRAL------YRLGRQPPLALLL-----SPEDFLDAVRRL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 721 IYEKDSLNKIEKVINEMHETvraKEKLHLETQKLNDERDSLRANLLDNNNKLDALRKLSDGSSKSMDLTKKAIHLSQSEL 800
Cdd:COG4942 139 QYLKYLAPARREQAEELRAD---LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
250 260
....*....|....*....|....*..
gi 398366259 801 EKYRKNNDDLQKEIDRIKTEQAEQDDK 827
Cdd:COG4942 216 AELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
557-824 |
9.64e-08 |
|
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: 56.22 E-value: 9.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 557 NLNLQTLRLEAQQKELETARH-ISQLEKEV-QRLMVIKEASKDSNFQTARLKNLEIQKTFLESRINDLKNLLMVKLSQAS 634
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKeLEELEEELeQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 635 KLCDQITIQNNGLKTCSEH-VTIKRDIIDLENKCDVLKRQNEILvnNMQkitpelHTYLNESSCYLGKLLKSYPTSARPP 713
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEiEELEAQIEQLKEELKALREALDEL--RAE------LTLLNEEAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 714 SSEKDNQIYEKDSLNK-IEKVINEMHETVRAKEKLHLETQKLNDERDSLRANLLDNNNKLDALR-KLSDGSSKSMDLTKK 791
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEdIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSeELRELESKRSELRRE 916
|
250 260 270
....*....|....*....|....*....|...
gi 398366259 792 AIHLsQSELEKYRKNNDDLQKEIDRIKTEQAEQ 824
Cdd:TIGR02168 917 LEEL-REKLAQLELRLEGLEVRIDNLQERLSEE 948
|
|
| Kelch_1 |
pfam01344 |
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ... |
256-299 |
1.21e-07 |
|
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.
Pssm-ID: 396078 [Multi-domain] Cd Length: 46 Bit Score: 48.76 E-value: 1.21e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 398366259 256 PLTNHTMVAYDNKLWVFGGETPKTISNDTYRYDPAQSEWSKVKT 299
Cdd:pfam01344 1 RRSGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSKLPS 44
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
564-882 |
2.14e-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: 55.07 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 564 RLEAQQKELETARHISQLEKEVQ------RLMVIKEASKDSNFQTARLKNLEIQKTFLESRINDLKNllmvKLSQASKLC 637
Cdd:TIGR02169 199 QLERLRREREKAERYQALLKEKReyegyeLLKEKEALERQKEAIERQLASLEEELEKLTEEISELEK----RLEEIEQLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 638 DQITIQNNGLkTCSEHVTIKRDIIDLENKCDVLKRQNEILVNNMQKITPELHTYlnesscylgkllksyptsarppSSEK 717
Cdd:TIGR02169 275 EELNKKIKDL-GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKL----------------------EAEI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 718 DNQIYEKDSLNKiekvinEMHETVRAKEKLHLETQKLNDERDSLRANLLDNNNKLDALRKlsdgssKSMDLtkkaihlsQ 797
Cdd:TIGR02169 332 DKLLAEIEELER------EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD------ELKDY--------R 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 798 SELEKYRKNNDDLQKEIDRIkteqaeQDDKQEQRGAIthgnfdAFHRMKINNLKAELYMSKENRDSLKDELLALKKKLYT 877
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRL------QEELQRLSEEL------ADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
|
....*
gi 398366259 878 LEQKK 882
Cdd:TIGR02169 460 LAADL 464
|
|
| PRK14131 |
PRK14131 |
N-acetylneuraminate epimerase; |
240-300 |
2.38e-07 |
|
N-acetylneuraminate epimerase;
Pssm-ID: 237617 [Multi-domain] Cd Length: 376 Bit Score: 53.87 E-value: 2.38e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366259 240 PNSHWEflePVGDLPPPLTNH-TMVAYDNKLWVFGG------ETPKTISNDTYRYDPAQSEWSKVKTT 300
Cdd:PRK14131 60 PSKGWT---KIAAFPGGPREQaVAAFIDGKLYVFGGigktnsEGSPQVFDDVYKYDPKTNSWQKLDTR 124
|
|
| Kelch_4 |
pfam13418 |
Galactose oxidase, central domain; |
259-299 |
3.08e-07 |
|
Galactose oxidase, central domain;
Pssm-ID: 433191 [Multi-domain] Cd Length: 49 Bit Score: 47.61 E-value: 3.08e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 398366259 259 NHTMVA-YDNKLWVFGGETPK-TISNDTYRYDPAQSEWSKVKT 299
Cdd:pfam13418 4 YHTSTSiPDDTIYLFGGEGEDgTLLSDLWVFDLSTNEWTRLGS 46
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
553-882 |
4.30e-07 |
|
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: 53.96 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 553 FDDLNLNLQTLRLEAQQKELETARHISQLEKEVQrlmvikeasKDSNFQTARLKNLEIQKTFLESRINDLKNLLMVKLSQ 632
Cdd:pfam05483 199 FEELRVQAENARLEMHFKLKEDHEKIQHLEEEYK---------KEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDK 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 633 ASKLCDQITIQNNGLKTCSE---HVTIKRDIIDLEnkcdvLKRQneilvNNMQKITPELHTYLNESSCYLgkllksypts 709
Cdd:pfam05483 270 ANQLEEKTKLQDENLKELIEkkdHLTKELEDIKMS-----LQRS-----MSTQKALEEDLQIATKTICQL---------- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 710 arppSSEKDNQIYEkdsLNKIEK----VINEMHETV-RAKEKLHLETQKLNDERDSLR---ANLLDNNNKLDALRKLSDG 781
Cdd:pfam05483 330 ----TEEKEAQMEE---LNKAKAahsfVVTEFEATTcSLEELLRTEQQRLEKNEDQLKiitMELQKKSSELEEMTKFKNN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 782 SSKSMDLTKKAIHLSQS---ELEKYRKNNDDL----QKEIDRIKTEQAEQDDKQEQRGAITHGnfDAFHRMKINNLKAEL 854
Cdd:pfam05483 403 KEVELEELKKILAEDEKlldEKKQFEKIAEELkgkeQELIFLLQAREKEIHDLEIQLTAIKTS--EEHYLKEVEDLKTEL 480
|
330 340
....*....|....*....|....*...
gi 398366259 855 ymskeNRDSLKDELLALKKKLYTLEQKK 882
Cdd:pfam05483 481 -----EKEKLKNIELTAHCDKLLLENKE 503
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
721-882 |
7.62e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.21 E-value: 7.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 721 IYEKDSLNKIEKVINEMHETVRAKEKLHLETQKLNDERDSLRANLLDNNNKLDALRKLSDGSSKSMDLTKKAIHLSQSEL 800
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 801 EKYRKNNDDLQKEIDRIkteQAEQDDKQEQRGAITHgnfdafhrmKINNLKAELYMSKENRDSLKDELLALKKKLYTLEQ 880
Cdd:COG4372 104 ESLQEEAEELQEELEEL---QKERQDLEQQRKQLEA---------QIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
..
gi 398366259 881 KK 882
Cdd:COG4372 172 EL 173
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
555-882 |
1.90e-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: 51.65 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 555 DLNLNLQTLRLEAQQKELETARHISQLEKEVQRLMVIKEASKDSnfQTARLKNLEIQKTFLESRinDLKNLlmvklsQAS 634
Cdd:pfam05483 422 DEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTS--EEHYLKEVEDLKTELEKE--KLKNI------ELT 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 635 KLCDQITIQNNGLKTCSEHVTI-----KRDIIDLENKCDVLKRQNEILV-------NNMQKITPELHTYLNESSCYLGKL 702
Cdd:pfam05483 492 AHCDKLLLENKELTQEASDMTLelkkhQEDIINCKKQEERMLKQIENLEekemnlrDELESVREEFIQKGDEVKCKLDKS 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 703 LKSYPT-SARPPSSEKDNQIYEKDSLN---KIE---KVINEMHETVRA-KEKLHLETQKLNDERDSLRANLLDNNNKLDA 774
Cdd:pfam05483 572 EENARSiEYEVLKKEKQMKILENKCNNlkkQIEnknKNIEELHQENKAlKKKGSAENKQLNAYEIKVNKLELELASAKQK 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 775 LRKLSDGSSKSMDLTKKAIHLSQSELEKYRKNNDD---LQKEID-RIKTEQAEQDDKQEQrgaithgnfdafHRMKINNL 850
Cdd:pfam05483 652 FEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEavkLQKEIDkRCQHKIAEMVALMEK------------HKHQYDKI 719
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 398366259 851 KAE------LYMSKENRDS------------LKDELLALKKKLYTLEQKK 882
Cdd:pfam05483 720 IEErdselgLYKNKEQEQSsakaaleielsnIKAELLSLKKQLEIEKEEK 769
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
560-825 |
1.90e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 51.75 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 560 LQTLRLEAQQKELETARHISQLEKEVQrlMVIKEASKDSNFQTARLKNLEIQKT---FLESRINDLKNLLMVKLSQASKL 636
Cdd:pfam10174 231 LQTVIEMKDTKISSLERNIRDLEDEVQ--MLKTNGLLHTEDREEEIKQMEVYKShskFMKNKIDQLKQELSKKESELLAL 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 637 CDQITIQNNGLKTCSEHVTI-KRDIIDLENKCDVLKRQNEILVNNMQkitpELHTYLNESSCYLGKLLKSYPTSARPPSS 715
Cdd:pfam10174 309 QTKLETLTNQNSDCKQHIEVlKESLTAKEQRAAILQTEVDALRLRLE----EKESFLNKKTKQLQDLTEEKSTLAGEIRD 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 716 EKDNQIYEKDSLNKIEKVINEMHETVRAKEKlhletqKLNDERDSLRANLLDNNNKLDALRKLSDGSS---KSMDLTKKA 792
Cdd:pfam10174 385 LKDMLDVKERKINVLQKKIENLQEQLRDKDK------QLAGLKERVKSLQTDSSNTDTALTTLEEALSekeRIIERLKEQ 458
|
250 260 270
....*....|....*....|....*....|....*..
gi 398366259 793 IHLS----QSELEKYRKNNDDLQKEIDRIKTEQAEQD 825
Cdd:pfam10174 459 REREdrerLEELESLKKENKDLKEKVSALQPELTEKE 495
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
555-880 |
2.88e-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: 51.21 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 555 DLNLNLQTLRLEAQQKELETARhiSQLEKEVQRLmviKEASKDSNFQTARLKNLEIQKTFLESRINDLKNLLMVKLSQAS 634
Cdd:TIGR02168 224 ELELALLVLRLEELREELEELQ--EELKEAEEEL---EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 635 KLCDQITIQNNGLKtcsehvtikrdiiDLENKcdvLKRQNEILVNNMQKITpELHTYLNESSCYLGKLLKsyptsarpps 714
Cdd:TIGR02168 299 RLEQQKQILRERLA-------------NLERQ---LEELEAQLEELESKLD-ELAEELAELEEKLEELKE---------- 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 715 sEKDNQiyeKDSLNKIEKVINEMHETVRAKEKLHletQKLNDERDSLRANLLDNNNKLDALRKLSDGSSKSMDLTKKAIH 794
Cdd:TIGR02168 352 -ELESL---EAELEELEAELEELESRLEELEEQL---ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 795 LSQSELEKYRKnnDDLQKEIDRIKTEQAEQDDKQEqrgaithgnfdaFHRMKINNLKAELYMSKENRDSLKDELLALKKK 874
Cdd:TIGR02168 425 ELLKKLEEAEL--KELQAELEELEEELEELQEELE------------RLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
....*.
gi 398366259 875 LYTLEQ 880
Cdd:TIGR02168 491 LDSLER 496
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
605-880 |
5.59e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.50 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 605 LKNLEIQKTFLESRINDLKNLLMVKLSQASKLCDQITIQNNGL--KTCSEHvtiKRDIIDLENKCDVLKRQNEILVNNMQ 682
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRieQLISEH---EVEITGLTEKASSARSQANSIQSQLE 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 683 KITPELHtylNESSCYLGKL--LKSYPTSARPPSSEKdNQIYEkDSLNKIEKVI----NEMHETVRAKEKLHLETQKLND 756
Cdd:pfam15921 303 IIQEQAR---NQNSMYMRQLsdLESTVSQLRSELREA-KRMYE-DKIEELEKQLvlanSELTEARTERDQFSQESGNLDD 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 757 ERDSLRANLLDNNNKL----DALRKLSD---GSSKSMDltkkaiHLsqselekyRKNNDDLQKEIDRI----KTEQAEQD 825
Cdd:pfam15921 378 QLQKLLADLHKREKELslekEQNKRLWDrdtGNSITID------HL--------RRELDDRNMEVQRLeallKAMKSECQ 443
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 398366259 826 DKQEQRGAITHGNFDAFHrmKINNLKAELYMSKENRDSLKDELLALKKKLYTLEQ 880
Cdd:pfam15921 444 GQMERQMAAIQGKNESLE--KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSER 496
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
485-874 |
7.61e-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: 49.72 E-value: 7.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 485 FERKSDREEKKPQSSKVDSSINKESpgtgikVSKKNFpvlrgLTVDSEEYGSSSYKDTSCQKGipknLFDDLNLNLQTL- 563
Cdd:pfam05483 263 LEESRDKANQLEEKTKLQDENLKEL------IEKKDH-----LTKELEDIKMSLQRSMSTQKA----LEEDLQIATKTIc 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 564 ----RLEAQQKELETARH-----ISQLEKEV---QRLMVIKEASKDSNFQTARLKNLEIQKTFLEsrindlknllmvkLS 631
Cdd:pfam05483 328 qlteEKEAQMEELNKAKAahsfvVTEFEATTcslEELLRTEQQRLEKNEDQLKIITMELQKKSSE-------------LE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 632 QASKLCDQITIQNNGLKTC-SEHVTIKRDIIDLENKCDVLKRQNEILVNNMQKITPELH------TYLNESSCYLGKLLK 704
Cdd:pfam05483 395 EMTKFKNNKEVELEELKKIlAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHdleiqlTAIKTSEEHYLKEVE 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 705 SYPTSarppssekdnqiYEKDSLNKIEKVINemhetvraKEKLHLETQKLNDERDSLRANLLDNNNKLDALRKLSDGSSK 784
Cdd:pfam05483 475 DLKTE------------LEKEKLKNIELTAH--------CDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLK 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 785 SMD-LTKKAIHLsQSELEKYRKNNDDLQKEIdRIKTEQAEQDDKQEQRGAITHGNFDAFHRMKINNLKAELYMSKENRDS 863
Cdd:pfam05483 535 QIEnLEEKEMNL-RDELESVREEFIQKGDEV-KCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE 612
|
410
....*....|.
gi 398366259 864 LKDELLALKKK 874
Cdd:pfam05483 613 LHQENKALKKK 623
|
|
| Kelch_3 |
pfam13415 |
Galactose oxidase, central domain; |
266-315 |
8.80e-06 |
|
Galactose oxidase, central domain;
Pssm-ID: 433188 [Multi-domain] Cd Length: 49 Bit Score: 43.43 E-value: 8.80e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 398366259 266 DNKLWVFGGETPK--TISNDTYRYDPAQSEWskvKTTGEKPPPIQEHASVVY 315
Cdd:pfam13415 1 GDKLYIFGGLGFDgqTRLNDLYVYDLDTNTW---TQIGDLPPPRSGHSATYI 49
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
560-882 |
3.86e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.32 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 560 LQTLRLEAQQKELEtarhISQLEKEVQRL-MVIKEASKDSNFQTARLKNLEIQKTFLESRINDLKNLLMVKLSQASKLCD 638
Cdd:TIGR04523 372 IEKLKKENQSYKQE----IKNLESQINDLeSKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 639 QITIQNNGLKtcsehvTIKRDIIDLENKCDVLKRQNEILVNNMQKITPELHTYLNEsscyLGKLlksyptsarppSSEKd 718
Cdd:TIGR04523 448 QDSVKELIIK------NLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE----LKKL-----------NEEK- 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 719 nqiyeKDSLNKIEKVINEMHETVRAKEKLHLETQKLNDERDSLRANL--LDNNNKLDALRKLSDGSSKSMD---LTKKAI 793
Cdd:TIGR04523 506 -----KELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkDDFELKKENLEKEIDEKNKEIEelkQTQKSL 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 794 HLSQSELE----KYRKNNDDLQKEIDrIKTEQAEQDDKQeqrgaITHGNfdAFHRmKINNLKAELYMSKEnrdSLKDELL 869
Cdd:TIGR04523 581 KKKQEEKQelidQKEKEKKDLIKEIE-EKEKKISSLEKE-----LEKAK--KENE-KLSSIIKNIKSKKN---KLKQEVK 648
|
330
....*....|...
gi 398366259 870 ALKKKLYTLEQKK 882
Cdd:TIGR04523 649 QIKETIKEIRNKW 661
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
566-879 |
3.92e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.32 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 566 EAQQKELEtaRHISQLEKEV-QRLMVIKEASKDSNFQTARLKNLEIQKTFLESRINDLKNLLMVKLSQASKLCDQITIQN 644
Cdd:TIGR04523 32 DTEEKQLE--KKLKTIKNELkNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 645 NGLKtcsehvTIKRDIIDLENKCDVLKRQ------NEILVNNMQKITPELHTYLNESSCYLGKLLKSYptsarppssEKD 718
Cdd:TIGR04523 110 SEIK------NDKEQKNKLEVELNKLEKQkkenkkNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEEL---------ENE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 719 NQIYEKDsLNKIEKVINEMHETVRAKEKLHLETQKLNDERDSLRANLLDNNNKLDALRKlsDGSSKSMDLTKKAIHLS-- 796
Cdd:TIGR04523 175 LNLLEKE-KLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKD--NIEKKQQEINEKTTEISnt 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 797 ---------------------QSELEKYRKNNDDLQKEIDRIKTE------QAEQDDKQEQRGAITHgnfdafHRMKINN 849
Cdd:TIGR04523 252 qtqlnqlkdeqnkikkqlsekQKELEQNNKKIKELEKQLNQLKSEisdlnnQKEQDWNKELKSELKN------QEKKLEE 325
|
330 340 350
....*....|....*....|....*....|
gi 398366259 850 LKAELYMSKENRDSLKDELLALKKKLYTLE 879
Cdd:TIGR04523 326 IQNQISQNNKIISQLNEQISQLKKELTNSE 355
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
559-882 |
5.32e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 47.35 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 559 NLQTLRLEAQQKELETARH-ISQLEKEVQRLMVIKEASKDSNFQTARLKNLEIQKTFLESRINDLKNLLMVKLSQASKLC 637
Cdd:TIGR01612 1222 NLGKLFLEKIDEEKKKSEHmIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENIS 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 638 DqitIQNNGLKTcSEHVTIKRDIIDLenkcdvlKRQNEILVNNMQKITPELHTYLNESScylgkllksyptsarppssek 717
Cdd:TIGR01612 1302 D---IREKSLKI-IEDFSEESDINDI-------KKELQKNLLDAQKHNSDINLYLNEIA--------------------- 1349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 718 dnQIYEKDSLNKIEKVINEMHETVRAKEKLHLETQKLNDERDSLRANLLDNNNKLDALRKLS--------DGSSKSMDLT 789
Cdd:TIGR01612 1350 --NIYNILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKIEstlddkdiDECIKKIKEL 1427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 790 KKAIHLSQSELEKYRKNNDDLQKEIDRIKTEQAEQDDKQEQRGAITHGNFDAFHRMKINNLKAELYMSKENRDSLKDELL 869
Cdd:TIGR01612 1428 KNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAK 1507
|
330
....*....|...
gi 398366259 870 ALKKKLYTLEQKK 882
Cdd:TIGR01612 1508 AIEKNKELFEQYK 1520
|
|
| Kelch_3 |
pfam13415 |
Galactose oxidase, central domain; |
151-205 |
6.15e-05 |
|
Galactose oxidase, central domain;
Pssm-ID: 433188 [Multi-domain] Cd Length: 49 Bit Score: 41.12 E-value: 6.15e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 398366259 151 GNAYVVFGGDTHKlnkNGLLDDDLYLFNINSYKWTipqPIGRRPLGRYGHKISII 205
Cdd:pfam13415 1 GDKLYIFGGLGFD---GQTRLNDLYVYDLDTNTWT---QIGDLPPPRSGHSATYI 49
|
|
| Kelch_6 |
pfam13964 |
Kelch motif; |
258-297 |
8.71e-05 |
|
Kelch motif;
Pssm-ID: 404790 [Multi-domain] Cd Length: 50 Bit Score: 40.78 E-value: 8.71e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 398366259 258 TNHTMVAYDNKLWVFGGET-PKTISNDTYRYDPAQSEWSKV 297
Cdd:pfam13964 3 TFHSVVSVGGYIYVFGGYTnASPALNKLEVYNPLTKSWEEL 43
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
571-831 |
1.07e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.32 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 571 ELETARHISQLEKEVQRLMVIKEASKDSNFQTARLK-NLEIQKTFLESRINDLKNLLMVkLSQAsklcdqitiqnnglKT 649
Cdd:pfam01576 337 EEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKaNLEKAKQALESENAELQAELRT-LQQA--------------KQ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 650 CSEHVTIKRD--IIDLENKCDVLKRQNEILVNNMQKITPELH---TYLNESScylGKLLKSYPTSARPPSSEKDNQiyek 724
Cdd:pfam01576 402 DSEHKRKKLEgqLQELQARLSESERQRAELAEKLSKLQSELEsvsSLLNEAE---GKNIKLSKDVSSLESQLQDTQ---- 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 725 dslnkiekviNEMHETVRAKEKLHLETQKLNDERDSLRANLLDNNNKLDAL-RKLSDGSSKSMDLTKKAIHLSQS--ELE 801
Cdd:pfam01576 475 ----------ELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVeRQLSTLQAQLSDMKKKLEEDAGTleALE 544
|
250 260 270
....*....|....*....|....*....|....*.
gi 398366259 802 KYRKNnddLQKEIDRI------KTEQAEQDDKQEQR 831
Cdd:pfam01576 545 EGKKR---LQRELEALtqqleeKAAAYDKLEKTKNR 577
|
|
| Kelch_4 |
pfam13418 |
Galactose oxidase, central domain; |
141-185 |
1.64e-04 |
|
Galactose oxidase, central domain;
Pssm-ID: 433191 [Multi-domain] Cd Length: 49 Bit Score: 39.90 E-value: 1.64e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 398366259 141 PRVGHASTICGNAYV-VFGGdthkLNKNGLLDDDLYLFNINSYKWT 185
Cdd:pfam13418 1 PRAYHTSTSIPDDTIyLFGG----EGEDGTLLSDLWVFDLSTNEWT 42
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
554-866 |
2.25e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 554 DDLNLNLQTLR---------LEAQQKELETARH-ISQLEKEVQRLM-VIKEASKDSNFQTARLKNLEIQKTFLESRINDL 622
Cdd:COG4372 41 DKLQEELEQLReeleqareeLEQLEEELEQARSeLEQLEEELEELNeQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 623 KNllmvKLSQASKLCDQITIQNNGLKtcSEHVTIKRDIIDLENKCDVLKRQNEILVNNMQKITPElhtylnESSCYLGKL 702
Cdd:COG4372 121 QK----ERQDLEQQRKQLEAQIAELQ--SEIAEREEELKELEEQLESLQEELAALEQELQALSEA------EAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 703 LKSYPTSArPPSSEKDNQIYEKDSLNKIEKVINEMHETVRAKEKLHLETQKLNDERDSLRANLLDNNNKLDALRKLSDGS 782
Cdd:COG4372 189 LKEANRNA-EKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 783 SKSMDLTKKAIHLSQSELEKYRKNNDDLQKEIDRIKTEQAEQDDKQEQRGAITHGNFDAFHRMKINNLKAELYMSKENRD 862
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLL 347
|
....
gi 398366259 863 SLKD 866
Cdd:COG4372 348 VGLL 351
|
|
| Kelch_3 |
pfam13415 |
Galactose oxidase, central domain; |
213-265 |
2.44e-04 |
|
Galactose oxidase, central domain;
Pssm-ID: 433188 [Multi-domain] Cd Length: 49 Bit Score: 39.58 E-value: 2.44e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 398366259 213 KLYLFGGQVDE--TYFNDLVVFDLSSfrrpnshWEFlEPVGDLPPPLTNHTMVAY 265
Cdd:pfam13415 3 KLYIFGGLGFDgqTRLNDLYVYDLDT-------NTW-TQIGDLPPPRSGHSATYI 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
724-882 |
2.54e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 724 KDSLNKIEKVINEMHetvRAKEKLHLETQK------LNDERDSLRANLLdnNNKLDALRKlsdgsskSMDLTKKAIHLSQ 797
Cdd:TIGR02168 185 RENLDRLEDILNELE---RQLKSLERQAEKaerykeLKAELRELELALL--VLRLEELRE-------ELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 798 SELEKYRKNNDDLQKEIDRIKTEQAEQDDKQEQrgaITHGNFDafHRMKINNLKAELYMSKENRDSLKDELLALKKKLYT 877
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEE---LQKELYA--LANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
....*
gi 398366259 878 LEQKK 882
Cdd:TIGR02168 328 LESKL 332
|
|
| PHA03098 |
PHA03098 |
kelch-like protein; Provisional |
165-387 |
3.06e-04 |
|
kelch-like protein; Provisional
Pssm-ID: 222983 [Multi-domain] Cd Length: 534 Bit Score: 44.37 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 165 NKNGLLDDDLYLFNINSYKW-TIPQPIGRRPLgryghkISIIASNpmqTKLYLFGGQVDETYFNDLvvfdlssfrrpnSH 243
Cdd:PHA03098 304 NKNNLSVNSVVSYDTKTKSWnKVPELIYPRKN------PGVTVFN---NRIYVIGGIYNSISLNTV------------ES 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 244 WEFLEPVGDLPPPL----TNHTMVAYDNKLWVFGG-ETPKTISNDTYRYDPAQSEWSKVKTTgekPPPIQEHASVVYKHL 318
Cdd:PHA03098 363 WKPGESKWREEPPLifprYNPCVVNVNNLIYVIGGiSKNDELLKTVECFSLNTNKWSKGSPL---PISHYGGCAIYHDGK 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366259 319 MCVLGGKDTHNAYS--NDVYFLNLLSLKWYKLPRMKegipQERSGHSLTLMkNEKLLIMGGDKTDYASPNI 387
Cdd:PHA03098 440 IYVIGGISYIDNIKvyNIVESYNPVTNKWTELSSLN----FPRINASLCIF-NNKIYVVGGDKYEYYINEI 505
|
|
| PHA03098 |
PHA03098 |
kelch-like protein; Provisional |
93-298 |
3.22e-04 |
|
kelch-like protein; Provisional
Pssm-ID: 222983 [Multi-domain] Cd Length: 534 Bit Score: 44.37 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 93 IVTNDNRIFVTGGLHDQSVYGDV--WQIAANAdgtsftskridiDQNTPP---PRVGHASTICGNAYVVFGGdthkLNKN 167
Cdd:PHA03098 338 VTVFNNRIYVIGGIYNSISLNTVesWKPGESK------------WREEPPlifPRYNPCVVNVNNLIYVIGG----ISKN 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 168 GLLDDDLYLFNINSYKWTIPQPIgrrplgRYGHKISIIASNpmQTKLYLFGGQvdeTYFNDLVVFD-LSSFRRPNSHWEF 246
Cdd:PHA03098 402 DELLKTVECFSLNTNKWSKGSPL------PISHYGGCAIYH--DGKIYVIGGI---SYIDNIKVYNiVESYNPVTNKWTE 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 398366259 247 LEPvgdLPPPLTNHTMVAYDNKLWVFGGETPKTISNDTYRYDPAQSEWSKVK 298
Cdd:PHA03098 471 LSS---LNFPRINASLCIFNNKIYVVGGDKYEYYINEIEVYDDKTNTWTLFC 519
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
716-881 |
3.89e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 716 EKDNQIYE-KDSLNKIEKVINEMHETVRAKEKlhlETQKLNDERDSLRANLLDNNNKLDALRKLSDGSSKSMDLTKKAIH 794
Cdd:COG1579 14 ELDSELDRlEHRLKELPAELAELEDELAALEA---RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 795 LS--QSELEKYRKNNDDLQKEI----DRIKTEQAEQDDKQEQRGAITHgnfdafhrmKINNLKAELymsKENRDSLKDEL 868
Cdd:COG1579 91 YEalQKEIESLKRRISDLEDEIlelmERIEELEEELAELEAELAELEA---------ELEEKKAEL---DEELAELEAEL 158
|
170
....*....|...
gi 398366259 869 LALKKKLYTLEQK 881
Cdd:COG1579 159 EELEAEREELAAK 171
|
|
| Kelch_6 |
pfam13964 |
Kelch motif; |
310-354 |
4.87e-04 |
|
Kelch motif;
Pssm-ID: 404790 [Multi-domain] Cd Length: 50 Bit Score: 38.86 E-value: 4.87e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 398366259 310 HASVVYKHLMCVLGGKDTHNAYSNDVYFLNLLSLKWYKLPRMKEG 354
Cdd:pfam13964 5 HSVVSVGGYIYVFGGYTNASPALNKLEVYNPLTKSWEELPPLPTP 49
|
|
| Kelch_5 |
pfam13854 |
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ... |
254-290 |
6.88e-04 |
|
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.
Pssm-ID: 433528 [Multi-domain] Cd Length: 41 Bit Score: 37.93 E-value: 6.88e-04
10 20 30
....*....|....*....|....*....|....*....
gi 398366259 254 PPPLTNHTMVAYDNKLWVFGGETP--KTISNDTYRYDPA 290
Cdd:pfam13854 1 PVPRYGHCAVTVGDYIYLYGGYTGgeGQPSDDVYVLSLP 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
729-871 |
7.54e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 7.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 729 KIEKVINEMHETVRAKEKLHLETQKLNDERDSLRAnlldnnnKLDALRKLSDGSSKSMDL--TKKAIHLSQSELEKYRKN 806
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQE-------RREALQRLAEYSWDEIDVasAEREIAELEAELERLDAS 683
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366259 807 NDDLQKEIDRIKTEQAEQDDKQEQRGAITHgnfdafhrmKINNLKAELYMSKENRDSLKDELLAL 871
Cdd:COG4913 684 SDDLAALEEQLEELEAELEELEEELDELKG---------EIGRLEKELEQAEEELDELQDRLEAA 739
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
714-882 |
1.25e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 714 SSEKDNQIYEKdslnkiekvINEMHETVRAKEKLHLETQKLNDER---DSLRANLLDNNNKLDALRKLSDGSSKSMDLTK 790
Cdd:COG1340 131 SPEEEKELVEK---------IKELEKELEKAKKALEKNEKLKELRaelKELRKEAEEIHKKIKELAEEAQELHEEMIELY 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 791 KaihlsqsELEKYRKNNDDLQKEIDRIKtEQAEQddkqeqrgaithgnfdafHRMKINNLKAELymsKENRDSLKdellA 870
Cdd:COG1340 202 K-------EADELRKEADELHKEIVEAQ-EKADE------------------LHEEIIELQKEL---RELRKELK----K 248
|
170
....*....|..
gi 398366259 871 LKKKLYTLEQKK 882
Cdd:COG1340 249 LRKKQRALKREK 260
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
727-882 |
1.37e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.93 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 727 LNKIEKVINEMHET-VRAKEKLHLETQKLNDERDSLRANLLDNNNKLDALRKLSDGSSKsmdltkkaihLSQSELEKYRK 805
Cdd:smart00787 142 LEGLKEGLDENLEGlKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELED----------CDPTELDRAKE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 806 NNDDLQKEIDRIKTEQAE-QDDKQEQRGAITHGNfdafhrMKINNLKAELYMS----KENRDSLKDELLALKKKLYTLEQ 880
Cdd:smart00787 212 KLKKLLQEIMIKVKKLEElEEELQELESKIEDLT------NKKSELNTEIAEAekklEQCRGFTFKEIEKLKEQLKLLQS 285
|
..
gi 398366259 881 KK 882
Cdd:smart00787 286 LT 287
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
557-880 |
1.44e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 557 NLNLQTLRLEAQQKELETarHISQLEKEVQRLmviKEASKDSNFQTARLKNLEiQKTFLESRINDLKNLLMVKLSQASKL 636
Cdd:PRK03918 242 ELEKELESLEGSKRKLEE--KIRELEERIEEL---KKEIEELEEKVKELKELK-EKAEEYIKLSEFYEEYLDELREIEKR 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 637 CDQITIQNNGlktcsehvtIKRDIIDLENKcdvLKRQNEIlvnnmQKITPELHTYLNEsscyLGKLLKSYPTsARPPSSE 716
Cdd:PRK03918 316 LSRLEEEING---------IEERIKELEEK---EERLEEL-----KKKLKELEKRLEE----LEERHELYEE-AKAKKEE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 717 KdNQIYEKDSLNKIEKVINEMHETVRAKEKLHLETQKLNDERDSLRANLLDNNNKLDALRKlsdgssksmdlTKKAIHLS 796
Cdd:PRK03918 374 L-ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK-----------AKGKCPVC 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 797 QSEL-EKYRKN-NDDLQKEIDRIKTEQAEQDDKQEQrgaithgnfdafhrMKINNLKAELYMSKENR----DSLKDELLA 870
Cdd:PRK03918 442 GRELtEEHRKElLEEYTAELKRIEKELKEIEEKERK--------------LRKELRELEKVLKKESEliklKELAEQLKE 507
|
330
....*....|..
gi 398366259 871 LKKKL--YTLEQ 880
Cdd:PRK03918 508 LEEKLkkYNLEE 519
|
|
| PHA03098 |
PHA03098 |
kelch-like protein; Provisional |
206-377 |
1.67e-03 |
|
kelch-like protein; Provisional
Pssm-ID: 222983 [Multi-domain] Cd Length: 534 Bit Score: 42.06 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 206 ASNPMQTKLYLFGGQVDETYFNDLVV-FDLSSFRrpnshwefLEPVGDLPPPLTNHTMVAYDNKLWVFGGETPKTISNDT 284
Cdd:PHA03098 289 GSVVLNNVIYFIGGMNKNNLSVNSVVsYDTKTKS--------WNKVPELIYPRKNPGVTVFNNRIYVIGGIYNSISLNTV 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 285 YRYDPAQSEWSkvkttgEKPPPIQ---EHASVVYKHLMCVLGGKDTHNAYSNDVYFLNLLSLKWYKLPRMkegiPQERSG 361
Cdd:PHA03098 361 ESWKPGESKWR------EEPPLIFpryNPCVVNVNNLIYVIGGISKNDELLKTVECFSLNTNKWSKGSPL----PISHYG 430
|
170
....*....|....*.
gi 398366259 362 HSlTLMKNEKLLIMGG 377
Cdd:PHA03098 431 GC-AIYHDGKIYVIGG 445
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
743-882 |
2.02e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 743 AKEKLHLETQKLNDERDSLRANLLDNNNKLDALRKLSDGSSKSMDLTKKAIHLSQSELEKYRKNNDDLQKEIDRIKTEQA 822
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366259 823 EQDDKQEQ--RGAITHGNFDA----FHRMKINNLKAELYMSKENRDSLKDELLALKKKLYTLEQKK 882
Cdd:COG4942 101 AQKEELAEllRALYRLGRQPPlallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
588-881 |
2.27e-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: 41.48 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 588 LMVIKEASKDSNFQTARLKNLEIQKTFLESRINDLKNLLMVKLSQASKLCDQITIQNNglktcsehvTIKRDIIDLEnkc 667
Cdd:COG5185 228 IINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENAN---------NLIKQFENTK--- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 668 dvlkrqnEILVNNMQKITPELHTylNESSCYLGK--LLKSYPTSARPPSSEKDNQIYE----KDSLNKIEKVINEMHETV 741
Cdd:COG5185 296 -------EKIAEYTKSIDIKKAT--ESLEEQLAAaeAEQELEESKRETETGIQNLTAEieqgQESLTENLEAIKEEIENI 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 742 RAKEKLHLETQKLNDERDSLRANLLDNNNKLDALRKLSDGSSKSMDLTKKAiHLSQSE-----LEKYRKNNDDLQKEIDR 816
Cdd:COG5185 367 VGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKA-ADRQIEelqrqIEQATSSNEEVSKLLNE 445
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366259 817 IKTEQAEQDDKQEqrgAITHGNFDAFHRMKINNLKAELYMSKENRDSLKDELLALKKKLYTLEQK 881
Cdd:COG5185 446 LISELNKVMREAD---EESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAK 507
|
|
| PHA03098 |
PHA03098 |
kelch-like protein; Provisional |
56-233 |
2.53e-03 |
|
kelch-like protein; Provisional
Pssm-ID: 222983 [Multi-domain] Cd Length: 534 Bit Score: 41.29 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 56 STALPWSPeskntGKYIWNRvkLKNSPFPRYrhsSSFIVTNDNRIFVTGGLHDQSVYGDVWQIaanadgTSFTSKRIDID 135
Cdd:PHA03098 358 NTVESWKP-----GESKWRE--EPPLIFPRY---NPCVVNVNNLIYVIGGISKNDELLKTVEC------FSLNTNKWSKG 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 136 QNTPPPRVGHASTICGNAYVVFGGDTHKLNKNGLldDDLYLFNINSYKWTIPQPIgRRPlgRYGHKISIIasnpmQTKLY 215
Cdd:PHA03098 422 SPLPISHYGGCAIYHDGKIYVIGGISYIDNIKVY--NIVESYNPVTNKWTELSSL-NFP--RINASLCIF-----NNKIY 491
|
170
....*....|....*...
gi 398366259 216 LFGGQVDETYFNDLVVFD 233
Cdd:PHA03098 492 VVGGDKYEYYINEIEVYD 509
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
564-882 |
4.57e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 564 RLEAQQKELETARhisQLEKEVQRLMV-------------IKEASKDSNFQTARLKNLEIQKTFLESRINDLKNLLMvKL 630
Cdd:PRK03918 356 ELEERHELYEEAK---AKKEELERLKKrltgltpeklekeLEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE-EL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 631 SQASKLCD----QITIQNNGLKTCSEHVTIKR------DIIDLENKCDVLKRQNEILVNNMQKITPELHTY--LNEsscy 698
Cdd:PRK03918 432 KKAKGKCPvcgrELTEEHRKELLEEYTAELKRiekelkEIEEKERKLRKELRELEKVLKKESELIKLKELAeqLKE---- 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 699 LGKLLKSYPTSarppSSEKDNQIYEK----------------DSLNKIEKVINEMHETVRAKEKLHLETQKLNDERDSLR 762
Cdd:PRK03918 508 LEEKLKKYNLE----ELEKKAEEYEKlkekliklkgeikslkKELEKLEELKKKLAELEKKLDELEEELAELLKELEELG 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 763 ANLLDN-NNKLDALRKLSD------GSSKSMDLTKKAIHLSQSELEKYRKNNDDLQKEIDRIKT--EQAEQDDKQEqrga 833
Cdd:PRK03918 584 FESVEElEERLKELEPFYNeylelkDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKelEELEKKYSEE---- 659
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 398366259 834 iTHGNFDAFH---RMKINNLKAELYMSKENRDSLKDELLALKKKLYTLEQKK 882
Cdd:PRK03918 660 -EYEELREEYlelSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAK 710
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
565-824 |
4.77e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 565 LEAQQKELETAR--HISQLEKEVQRLMVIKEASKDSNFQTARLKNlEIQKTFleSRINDLKNllmvKLSQASKLCDQITI 642
Cdd:COG1340 34 LNEELKELAEKRdeLNAQVKELREEAQELREKRDELNEKVKELKE-ERDELN--EKLNELRE----ELDELRKELAELNK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 643 QNNGLKTcsehvtIKRDIIDLENKCD--VLKRQNEI-LVNNMQKITPELHtylnesscylgkllksyptsARPPSSEKDN 719
Cdd:COG1340 107 AGGSIDK------LRKEIERLEWRQQteVLSPEEEKeLVEKIKELEKELE--------------------KAKKALEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366259 720 QIYE-KDSLNKIEKVINEMHETVRAK----EKLHLETQKLNDERDSLRANLLDNNNKLDALRKLSDGSSKSMDLTKKAIH 794
Cdd:COG1340 161 KLKElRAELKELRKEAEEIHKKIKELaeeaQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
|
250 260 270
....*....|....*....|....*....|.
gi 398366259 795 LSQSELEKYRKNNDDLQKEIDR-IKTEQAEQ 824
Cdd:COG1340 241 ELRKELKKLRKKQRALKREKEKeELEEKAEE 271
|
|
| Kelch_4 |
pfam13418 |
Galactose oxidase, central domain; |
196-255 |
6.32e-03 |
|
Galactose oxidase, central domain;
Pssm-ID: 433191 [Multi-domain] Cd Length: 49 Bit Score: 35.67 E-value: 6.32e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366259 196 GRYGHKISIIASNpmqtKLYLFGGQ-VDETYFNDLVVFDLSSfrrpNsHWeflEPVGDLPP 255
Cdd:pfam13418 1 PRAYHTSTSIPDD----TIYLFGGEgEDGTLLSDLWVFDLST----N-EW---TRLGSLPS 49
|
|
| Kelch_3 |
pfam13415 |
Galactose oxidase, central domain; |
316-366 |
6.74e-03 |
|
Galactose oxidase, central domain;
Pssm-ID: 433188 [Multi-domain] Cd Length: 49 Bit Score: 35.34 E-value: 6.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 398366259 316 KHLMCVLGGKDT-HNAYSNDVYFLNLLSLKWYKLPRMkegiPQERSGHSLTL 366
Cdd:pfam13415 1 GDKLYIFGGLGFdGQTRLNDLYVYDLDTNTWTQIGDL----PPPRSGHSATY 48
|
|
|