|
Name |
Accession |
Description |
Interval |
E-value |
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
100-292 |
3.69e-67 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 219.00 E-value: 3.69e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 100 VTKRILSARLLKINELQNEVSELQVKLAELLKENKSLKRLQYRQEKALNKFEDAENEISQLIFRHNNEITALKERLRKSQ 179
Cdd:pfam15619 1 VTQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 180 EKERATEKRVKDTESELFRTKFSLQKLKEISEARHLPERDDLAKKLVSAELKLDDTERRIKELSKNLELSTNSFQRQLLA 259
Cdd:pfam15619 81 EKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAA 160
|
170 180 190
....*....|....*....|....*....|...
gi 1622929213 260 ERKRAYEAYDENKVLQKEIQRLYHKLKEKEREL 292
Cdd:pfam15619 161 EKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
105-328 |
5.84e-10 |
|
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: 61.70 E-value: 5.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 105 LSARLLKINELQNEVSELQVKLAELLKENKSLKRLQYRQEKALNKFEDAENEISQLIFRHNNEITALKERLRKSQEKERA 184
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 185 TEKRVKDTESELFRTKFSLQKLKEISEARHLPERDDLAKKLVSAEL-------------KLDDTERRIKELSKNLELSTN 251
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYlkylaparreqaeELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622929213 252 SfQRQLLAERKRAYEAYDENKVLQKE-IQRLYHKLKEKERELDIKNIYSNRLPKSSPNKEKELALRKNAACQSDFADL 328
Cdd:COG4942 175 E-LEALLAELEEERAALEALKAERQKlLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
105-331 |
3.22e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 105 LSARLLKINELQNEVSELQVKLAELLKENKSLKRLQYRQEKALNKFEDAENEISQL---IFRHNNEITALKERLRKSQEK 181
Cdd:COG4913 656 YSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELkgeIGRLEKELEQAEEELDELQDR 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 182 ERATEKRVKDTESELFRTKFSLQKLKEIsearhlpeRDDLAKKLVSaelKLDDTERRIKELSKNLELSTNSFQRQ---LL 258
Cdd:COG4913 736 LEAAEDLARLELRALLEERFAAALGDAV--------ERELRENLEE---RIDALRARLNRAEEELERAMRAFNREwpaET 804
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622929213 259 AERKRAYEAYDenkvlqkEIQRLYHKLKEkereldikniysNRLPKsspnKEKELALRKNAACQSDFADLCTK 331
Cdd:COG4913 805 ADLDADLESLP-------EYLALLDRLEE------------DGLPE----YEERFKELLNENSIEFVADLLSK 854
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
111-292 |
1.41e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 111 KINELQNEVSELQVKLAELLKEnksLKRLQYRQEKALNKFEDAENEISQLifrhNNEITALKERLRKSQEKeraTEKRVK 190
Cdd:COG3883 24 ELSELQAELEAAQAELDALQAE---LEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEERREE---LGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 191 DteseLFRTKFSLQKLKEISEARHLPE---RDDLAKKLVSAELKLDDTERRIKELSKNLELSTNSFQRQLLAERKRAYEA 267
Cdd:COG3883 94 A----LYRSGGSVSYLDVLLGSESFSDfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180
....*....|....*....|....*
gi 1622929213 268 YDENKVLQKEIQRLYHKLKEKEREL 292
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAA 194
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
111-292 |
1.51e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 111 KINELQNEVSELQVKL----AELLKENKSLKRLQYRQEKALNKFEDAENEISQLIfrhnNEITALKERLRKSQEKERATE 186
Cdd:COG1196 247 ELEELEAELEELEAELaeleAELEELRLELEELELELEEAQAEEYELLAELARLE----QDIARLEERRRELEERLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 187 KRVKDTESELFRTKFSLQKLKEiSEARHLPERDDLAKKLVSAELKLDDTERRIKELSKNLElstnSFQRQLLAERKRAYE 266
Cdd:COG1196 323 EELAELEEELEELEEELEELEE-ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE----ELAEELLEALRAAAE 397
|
170 180
....*....|....*....|....*.
gi 1622929213 267 AYDENKVLQKEIQRLYHKLKEKEREL 292
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEEL 423
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
108-298 |
1.86e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 51.08 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 108 RLLKINELQNEVSELQVKLAELLKENKSLKRLQYRQ-----EKALNKFEDAENEISQLIFRHNNEITALKERLRK-SQEK 181
Cdd:PRK05771 44 RLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVsvkslEELIKDVEEELEKIEKEIKELEEEISELENEIKElEQEI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 182 ERAteKRVKDTESE---LFRTKFSLQKLKEISEArHLPERDDLAKKLVSAELKLDDTERRI-----KELSKNL--ELSTN 251
Cdd:PRK05771 124 ERL--EPWGNFDLDlslLLGFKYVSVFVGTVPED-KLEELKLESDVENVEYISTDKGYVYVvvvvlKELSDEVeeELKKL 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622929213 252 SFQRQLLAERKRAYEAY----DENKVLQKEIQRLYHKLKE--KERELDIKNIY 298
Cdd:PRK05771 201 GFERLELEEEGTPSELIreikEELEEIEKERESLLEELKElaKKYLEELLALY 253
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
93-292 |
3.38e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 93 LRKDTDLVTKRILSARLlKINELQNEVSELQVKLAELLKE----NKSLKRLQYRQEKALNKFEDAENEISQLIFRHNN-- 166
Cdd:COG1196 258 LEAELAELEAELEELRL-ELEELELELEEAQAEEYELLAElarlEQDIARLEERRRELEERLEELEEELAELEEELEEle 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 167 --------EITALKERLRKSQEKERATEKRVKDTESELfRTKFSLQKLKEISEARHLPERDDLAKKLVSAELKLDDTERR 238
Cdd:COG1196 337 eeleeleeELEEAEEELEEAEAELAEAEEALLEAEAEL-AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622929213 239 IKELSKN---LELSTNSFQRQLLAERKRAYEAYDENKVLQKEIQRLYHKLKEKEREL 292
Cdd:COG1196 416 LERLEEEleeLEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
84-319 |
3.48e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 84 RSQSLNREPLRKDTDLVTKRIlsarllkiNELQNEVSELQVKLAellkenkslkrlQYRQEKALNKFEDAENEISQLIFR 163
Cdd:COG3206 164 QNLELRREEARKALEFLEEQL--------PELRKELEEAEAALE------------EFRQKNGLVDLSEEAKLLLQQLSE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 164 HNNEITALKERLRKSQEKERATEKRVKDTESELFRTKFS--LQKLK-EISEARHlpERDDLAKKL-------VSAELKLD 233
Cdd:COG3206 224 LESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRaQLAELEA--ELAELSARYtpnhpdvIALRAQIA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 234 DTERRIKELSKNLELSTNSfQRQLLAERKRAYEA-YDENKVLQKEIQRLYHKLKEKERELDI-KNIYSNRLpksspNKEK 311
Cdd:COG3206 302 ALRAQLQQEAQRILASLEA-ELEALQAREASLQAqLAQLEARLAELPELEAELRRLEREVEVaRELYESLL-----QRLE 375
|
....*...
gi 1622929213 312 ELALRKNA 319
Cdd:COG3206 376 EARLAEAL 383
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
107-288 |
4.38e-05 |
|
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: 45.30 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 107 ARLLKINELQNEVSELQVKLAELLKEnksLKRLQYRQEKALNKFEDAENEISQL---IFRHNNEITALKERLRKSQEK-- 181
Cdd:COG1579 7 RALLDLQELDSELDRLEHRLKELPAE---LAELEDELAALEARLEAAKTELEDLekeIKRLELEIEEVEARIKKYEEQlg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 182 ERATEKRVKDTESELFRTKfSLQKLKEISEARHLPERDDLAKKLVSAELKLDDTERRIKELSKNLELSTNSFQRQLLAER 261
Cdd:COG1579 84 NVRNNKEYEALQKEIESLK-RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170 180
....*....|....*....|....*..
gi 1622929213 262 KRAYEAYdenKVLQKEIQRLYHKLKEK 288
Cdd:COG1579 163 AEREELA---AKIPPELLALYERIRKR 186
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
111-316 |
8.02e-05 |
|
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: 46.21 E-value: 8.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 111 KINELQNEVSELQVKLAELLKENKSLKRLQYRQEKalnKFEDAENEISQLifrhNNEITALKERLRKSQEKERATEKRVK 190
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASR---KIGEIEKEIEQL----EQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 191 DTESELFRTKFSLQKLKEISEARHLPERDDLAKKLVSAELKLDDTERRIKELSKNLELSTNSFQRQLlaERKRAYEAYDE 270
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL--NRLTLEKEYLE 832
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622929213 271 NKVLQKEIQRLYHKLKEKERELDIKNIYSNRLPKSSPNKEKELALR 316
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
102-196 |
8.37e-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: 45.53 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 102 KRILSARLLKINELQNEVSELQVKLAELLKENKSLKRLQYRQEKALNKFEDAENEISQLIFRHNNEITALKERLRKSQEK 181
Cdd:COG4942 142 KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
90
....*....|....*
gi 1622929213 182 ERATEKRVKDTESEL 196
Cdd:COG4942 222 AEELEALIARLEAEA 236
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
112-314 |
1.58e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 112 INELQNEVSELQVKLAELLKEnksLKRLQYRQEKALNKFEDAENEISQLIFRHNNEITALKERLRKSQEKERATEKRVKD 191
Cdd:COG1196 325 LAELEEELEELEEELEELEEE---LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 192 TESELfrtkfSLQKLKEISEARHLPERDDLAKKLVSAELKLDDTERRIKELSKNLElstNSFQRQLLAERKRAYEAYDEN 271
Cdd:COG1196 402 LEELE-----EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA---ELEEEEEALLELLAELLEEAA 473
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622929213 272 KVLQKEIQRLYHKLKEKERELDIKNIYSNRLPKSSPNKEKELA 314
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
105-392 |
1.88e-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: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 105 LSARLLKINELQNEVSELQVKLAELLKENKSLKrlqyrqekalnkfedaeNEISQLifrhNNEITALKERLRKSQEKERA 184
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALA-----------------NEISRL----EQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 185 TEKRVKDTESELFRTKFSLQKLKEISEaRHLPERDDLAKKLVSAELKLDDTERRIKELsknlelstnsfQRQLLAERKRA 264
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLE-ELKEELESLEAELEELEAELEELESRLEEL-----------EEQLETLRSKV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 265 YEAYDENKVLQKEIQRLYHKLKEKERELDikniysnRLPKSSPNKEKELALRKNAACQSDFADLCTKGVQTTEDFkpeey 344
Cdd:TIGR02168 389 AQLELQIASLNNEIERLEARLERLEDRRE-------RLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL----- 456
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1622929213 345 pltPETIMCYENKWEEPEHLTLDLQSQKQDGHGEAGILNPIVEREENF 392
Cdd:TIGR02168 457 ---ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
46-449 |
1.99e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 46 VKRKNPKRQTSDGQVHHQAPRKPSPKGLPNRKGVRVGFRSQSLNREPLRK-----DTDLVTKRILSARllKINELQNEVS 120
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKaeekkKADEAKKKAEEAK--KADEAKKKAE 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 121 ELQVKLAELLKENKSLKRL----QYRQEKALNKFEDAENEISQLIFRHNNEITALKERLRKSQEKERATEKRVKDTES-- 194
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAaeaaKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDkk 1405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 195 ---ELFRTKFSLQKLKEISEARHLPERDDLAKKLVSAELKLDDTERRIKELSKNLELSTNSFQRQLLAERKRAYEAYDEN 271
Cdd:PTZ00121 1406 kadELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA 1485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 272 KVLQKEIQRLYHKLKEKERELDIKNiYSNRLPKSSPNKEKELALRKNAACQSDFADLCTKGVQTTEDFKPEEYPLTPETI 351
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKK-KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKK 1564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 352 MCYENKWEEPEHLTLDLQSQKQDGHGEAGILNPI-VEREENFVKGEELHVVKQEVEKLEdEWEREELDKKQKEKTYLLER 430
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMkLYEEEKKMKAEEAKKAEEAKIKAE-ELKKAEEEKKKVEQLKKKEA 1643
|
410
....*....|....*....
gi 1622929213 431 EEKPEWEAGKYQLEIYQIQ 449
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIK 1662
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
111-292 |
2.41e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 111 KINELQNEVSELQVKLAELLKENKSLKrlqyRQEKALNKFEDAENEISQLIFRHNNEITALKERLRKSQEKERATEkrvk 190
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALE----AELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDA---- 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 191 dTESELFRTKFSLQKLK-EISEARHlpERDDLAKKLVSAELKLDDTERRIKELSKNLE---LSTNSFQRQLLAERKRAYE 266
Cdd:COG4913 683 -SSDDLAALEEQLEELEaELEELEE--ELDELKGEIGRLEKELEQAEEELDELQDRLEaaeDLARLELRALLEERFAAAL 759
|
170 180
....*....|....*....|....*.
gi 1622929213 267 AYDENKVLQKEIQRLYHKLKEKEREL 292
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNRA 785
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
114-293 |
4.14e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 114 ELQNEVSELQVKLAELLKENKSLKRLQYRQEKALNKFEDAENEISQlifrHNNEITALKERLRKSQEKERATEKRVKDTE 193
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 194 SELFRTKFSLQKLKE-ISEARHLPERDDLAKKLVSAELKLDDTERRIKELSKNLELSTNSFQRQlLAERKRAYEAYDENK 272
Cdd:PRK03918 266 ERIEELKKEIEELEEkVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER-IKELEEKEERLEELK 344
|
170 180
....*....|....*....|.
gi 1622929213 273 VLQKEIQRLYHKLKEKERELD 293
Cdd:PRK03918 345 KKLKELEKRLEELEERHELYE 365
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
108-293 |
4.84e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 108 RLLKINELQNEVSELQVKLAELlkeNKSLKRLQ-YRQEKALNKFEDAENEISQLIFRHNNEITALKERLRKSQEKERATE 186
Cdd:COG4913 253 LLEPIRELAERYAAARERLAEL---EYLRAALRlWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 187 --------KRVKDTESELfrtkfslqKLKEISEARHLPERDDLAKKLVSAELKLDDTERRIKELSKNLElstnSFQRQLL 258
Cdd:COG4913 330 aqirgnggDRLEQLEREI--------ERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA----ALLEALE 397
|
170 180 190
....*....|....*....|....*....|....*
gi 1622929213 259 AERKRAYEAYDENKVlqkEIQRLYHKLKEKERELD 293
Cdd:COG4913 398 EELEALEEALAEAEA---ALRDLRRELRELEAEIA 429
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
102-313 |
9.57e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 102 KRILSARLLKINELQNEVSELQVKLAELLKENKSLKRLQYRQEKALNKFEDAEneisQLIFRHNNEITALKERLRKSQEK 181
Cdd:PRK03918 451 KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE----QLKELEEKLKKYNLEELEKKAEE 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 182 ERATEKRVKDTESELFRTKFSLQKLKEisearhlperddLAKKLVSAELKLDDTERRIKELSKNLELSTNSFQRQL---L 258
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKLEE------------LKKKLAELEKKLDELEEELAELLKELEELGFESVEELeerL 594
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622929213 259 AERKRAYEAYDENKVLQKEIQRLYHKLKEKERELDIKNIYSNRLPKSSPNKEKEL 313
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL 649
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
103-267 |
1.02e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 103 RILSARLLKINELQNEVSELQVKLAELLKENKSLKRLQYRQEKALNKFEDAEnEISQLifrhNNEITALKERLRKSQEKE 182
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ-ELEAL----EAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 183 RA---TEKRVKDTESELFRTKFSLQKLKEISEA-------RHLPERDDLAKKLVSAELKLDDTERRIKELSKNLELSTNS 252
Cdd:COG4717 156 EElreLEEELEELEAELAELQEELEELLEQLSLateeelqDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
170
....*....|....*
gi 1622929213 253 FQRQLLAERKRAYEA 267
Cdd:COG4717 236 LEAAALEERLKEARL 250
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
99-346 |
1.74e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 41.96 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 99 LVTKRILSARLLKINELQNEVSELQVKLAELLKE------NKSLKRLqyrqEKALNKFEDAENEISQLIFRHNNEITALK 172
Cdd:PTZ00108 1091 LLSMPIWSLTKEKVEKLNAELEKKEKELEKLKNTtpkdmwLEDLDKF----EEALEEQEEVEEKEIAKEQRLKSKTKGKA 1166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 173 ERLRKSQEKERATEKRVKDTESELFRTKFSLQKLKEISEARHLPERDDLAKKLVSAELKLDDTERRIKELSKNLELSTNS 252
Cdd:PTZ00108 1167 SKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSK 1246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 253 fqrqllaerkrayEAYDENKVLQKEIQRLYHKLKEKERELDIKNI----YSNRLPKSSPNKEKELALRKNAA-CQSDFAD 327
Cdd:PTZ00108 1247 -------------KNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVsavqYSPPPPSKRPDGESNGGSKPSSPtKKKVKKR 1313
|
250
....*....|....*....
gi 1622929213 328 LCTKGVQTTEDFKPEEYPL 346
Cdd:PTZ00108 1314 LEGSLAALKKKKKSEKKTA 1332
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
144-292 |
2.19e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.89 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 144 EKALNKFEDAENEIsqlifRHNN--EITALKERLRKSQEKERATEKRVKDTESELFRTKFSLQKLKEISEA--RHLPERD 219
Cdd:pfam13851 7 EKAFNEIKNYYNDI-----TRNNleLIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEElrKQLENYE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 220 DLAKKLVSAELKLDDTERRIKELSKNLELSTNSFQrQLLAERKRAYEAYDE------------NKVLQKEIQRLYHKLKE 287
Cdd:pfam13851 82 KDKQSLKNLKARLKVLEKELKDLKWEHEVLEQRFE-KVERERDELYDKFEAaiqdvqqktglkNLLLEKKLQALGETLEK 160
|
....*
gi 1622929213 288 KEREL 292
Cdd:pfam13851 161 KEAQL 165
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
112-302 |
2.39e-03 |
|
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: 41.26 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 112 INELQNEVSELQVKLAELLKENKSLK-RLQYRQEKALNKFEDaenEISQLIFRHNNEITALKERLRKSQEKERATEKRVK 190
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALKsESQNKIELLLQQHQD---RIEQLISEHEVEITGLTEKASSARSQANSIQSQLE 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 191 DTEsELFRTKFSLQklkeiseARHLPERDDLAKKLVSAELKLDDT-ERRIKELSKNLELSTNsfqrQLLAERKRAYEAYD 269
Cdd:pfam15921 303 IIQ-EQARNQNSMY-------MRQLSDLESTVSQLRSELREAKRMyEDKIEELEKQLVLANS----ELTEARTERDQFSQ 370
|
170 180 190
....*....|....*....|....*....|...
gi 1622929213 270 ENKVLQKEIQRLYHKLKEKERELDIKNIYSNRL 302
Cdd:pfam15921 371 ESGNLDDQLQKLLADLHKREKELSLEKEQNKRL 403
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
119-320 |
2.58e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 119 VSELQVKLAELLKENKSLKRLQyrqekaLNKFEDAENEISQLiFRHNNEITALKERLRKSQEKERATEKRVKDTESELFR 198
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELN------LKELKELEEELKEA-EEKEEEYAELQEELEELEEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 199 TKFSLQKLKEISEARHLPER----DDLAKKLVSAELKLDDTERRIKELSKNLELSTNSFQRQL----LAERKRAYEAYDE 270
Cdd:COG4717 121 LEKLLQLLPLYQELEALEAElaelPERLEELEERLEELRELEEELEELEAELAELQEELEELLeqlsLATEEELQDLAEE 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622929213 271 NKVLQKEIQRLYHKLKEKERELDIKNIYSNRLPKSSPNKEKELALRKNAA 320
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
91-282 |
2.72e-03 |
|
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: 41.21 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 91 EPLRKDTDLVTKRILSARLlKINELQNEVSELQVKLAELLKENKSLKRlqyRQEKALNKFEDAENEISQLIFR------- 163
Cdd:TIGR02169 346 EEERKRRDKLTEEYAELKE-ELEDLRAELEEVDKEFAETRDELKDYRE---KLEKLKREINELKRELDRLQEElqrlsee 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 164 ---HNNEITALKERLRKSQekERATEKRVKDTESElfrtkfslQKLKEISEarhlpERDDLAKKLVSAELKLDDTERRIK 240
Cdd:TIGR02169 422 ladLNAAIAGIEAKINELE--EEKEDKALEIKKQE--------WKLEQLAA-----DLSKYEQELYDLKEEYDRVEKELS 486
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622929213 241 ELSKnlELSTNSFQRQLLAERKRAYEAYDEnkVLQKEIQRLY 282
Cdd:TIGR02169 487 KLQR--ELAEAEAQARASEERVRGGRAVEE--VLKASIQGVH 524
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
111-293 |
4.73e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.43 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 111 KINELQNEVSELQVKLAELlkenkslkrlqyrqEKALN----KFEDAENEISQL---IFRHNNEITALKERLRKSQEKER 183
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAEL--------------EKALAelrkELEELEEELEQLrkeLEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 184 ATEKRVKDTESELFRTKFSLQKLKEISE------ARHLPERDDLAKKLVSAELKLDDTERRIKELSK----------NLE 247
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEeaeeelAEAEAEIEELEAQIEQLKEELKALREALDELRAeltllneeaaNLR 823
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622929213 248 LSTNSFQRQLLAERKRAYEAYDENKVLQKEIQRLYHKLKEKERELD 293
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
112-244 |
5.94e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 112 INELQNEVSELQVKLAELlKENKSLKRLQYRQEKALNKFEDAENEISQLIFRHNNEITALKERLRKSQEKER---ATEKR 188
Cdd:PRK03918 268 IEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEErleELKKK 346
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622929213 189 VKDTESELFRTKFSLQKLKEISEArhLPERDDLAKKLvsAELKLDDTERRIKELSK 244
Cdd:PRK03918 347 LKELEKRLEELEERHELYEEAKAK--KEELERLKKRL--TGLTPEKLEKELEELEK 398
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
96-223 |
8.56e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 38.94 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622929213 96 DTDLVTKRILSA----------RLLKINELQNEVSELQVKLAELLKENKSLKRlqyRQEKALNKFEDAENEISQLifrhN 165
Cdd:COG4026 104 DVELVRKEIKNAiiraglkslqNIPEYNELREELLELKEKIDEIAKEKEKLTK---ENEELESELEELREEYKKL----R 176
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622929213 166 NEITALKERLRKSQEKERATEKRVKDTESELFRTKFSLQKLKEISEARHLPERDDLAK 223
Cdd:COG4026 177 EENSILEEEFDNIKSEYSDLKSRFEELLKKRLLEVFSLEELWKELFPEELPEEDFIYF 234
|
|
| |
