|
Name |
Accession |
Description |
Interval |
E-value |
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
84-478 |
2.40e-13 |
|
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: 73.99 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 84 SRIYQvtekQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQ-----------ETKKQNLILSDEAIKYKDKIK---- 148
Cdd:pfam05483 77 SRLYS----KLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEaqrkaiqelqfENEKVSLKLEEEIQENKDLIKenna 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 149 ------VLEETNVSLGDKAKslrlQLESEREQNvknQDLILENKKSIEKLKdvismnaselsevqVALNEAKLSEENVKS 222
Cdd:pfam05483 153 trhlcnLLKETCARSAEKTK----KYEYEREET---RQVYMDLNNNIEKMI--------------LAFEELRVQAENARL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 223 ECH-RVQEENARLKKKKEQLQQQIEEWSRSHAELTEQIRSFETSQKDLEVALTHKDDNISALTNcitqlnrlECELESED 301
Cdd:pfam05483 212 EMHfKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEE--------KTKLQDEN 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 302 ADKGGNESDELangemggdrSKKIKDrIKqmMDVSRTQTAVSIVEEDLKLlqlklraSMSTKCNL----EDQIKKLEDDR 377
Cdd:pfam05483 284 LKELIEKKDHL---------TKELED-IK--MSLQRSMSTQKALEEDLQI-------ATKTICQLteekEAQMEELNKAK 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 378 SS-------LQTAKAGLEDECKTLRQKVEILNELYQQKEMALQKKLSQ-EEYERQDREQKLTAADEKVVLAAEEVKTY-K 448
Cdd:pfam05483 345 AAhsfvvteFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSElEEMTKFKNNKEVELEELKKILAEDEKLLDeK 424
|
410 420 430
....*....|....*....|....*....|
gi 2168985272 449 RRIEEMEEELQKTERSFKNQIAAHEKKAHD 478
Cdd:pfam05483 425 KQFEKIAEELKGKEQELIFLLQAREKEIHD 454
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
79-457 |
3.82e-13 |
|
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: 73.55 E-value: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 79 ILVVKSRIYQVTEK--QISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNLILSDEAIKYKDKIKVLEETNVS 156
Cdd:TIGR02168 672 ILERRREIEELEEKieELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 157 LGDKAKSLRLQLESEREQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLKK 236
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 237 KKEQLQQQIEEWSRSHAELTEQIRSFETSQKDLEvalthkddnisaltnciTQLNRLECELESEDADKGGnesdelange 316
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELE-----------------ELIEELESELEALLNERAS---------- 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 317 mggdrskkikdrikqmmdvsrtqtavsiVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQ 396
Cdd:TIGR02168 885 ----------------------------LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV 936
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2168985272 397 KV----EILNELYQQKEMALQKKLSQEEYERQDREQKLTAADEK------VVLAA-EEVKTYKRRIEEMEEE 457
Cdd:TIGR02168 937 RIdnlqERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKikelgpVNLAAiEEYEELKERYDFLTAQ 1008
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
90-475 |
1.35e-12 |
|
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: 71.20 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 90 TEKQISEKLENIKKENAELMQK------LSSYEQKIKESKKYVQETKKQNLILSDEAIK--------------------- 142
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKLelllsnLKKKIQKNKSLESQISELKKQNNQLKDNIEKkqqeinektteisntqtqlnq 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 143 -----------YKDKIKVLEETNVSLGDKAKSLRlQLESERE--QNVKNQDLILENKKSIEKLKDVISMNASELSEVQVA 209
Cdd:TIGR04523 258 lkdeqnkikkqLSEKQKELEQNNKKIKELEKQLN-QLKSEISdlNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKI 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 210 LNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQIEEWSRSHAELTEQIRSFETSQKDLEVALTH-------KDDNISA 282
Cdd:TIGR04523 337 ISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNqeklnqqKDEQIKK 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 283 LTnciTQLNRLECELE--SEDADKGGNESDELANgemgGDRSKKIKdrikqmmdVSRTQTAVSIVEEDLKLLQLKLRasm 360
Cdd:TIGR04523 417 LQ---QEKELLEKEIErlKETIIKNNSEIKDLTN----QDSVKELI--------IKNLDNTRESLETQLKVLSRSIN--- 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 361 STKCNLEDQIKKLEDDRS---SLQTAKAGLEDECKTLRQKVEILNElyqqKEMALQKKLSQEEYERQDREQKLTAADE-- 435
Cdd:TIGR04523 479 KIKQNLEQKQKELKSKEKelkKLNEEKKELEEKVKDLTKKISSLKE----KIEKLESEKKEKESKISDLEDELNKDDFel 554
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2168985272 436 KVVLAAEEVKTYKRRIEEMEEE---LQKTERSFKNQIAAHEKK 475
Cdd:TIGR04523 555 KKENLEKEIDEKNKEIEELKQTqksLKKKQEEKQELIDQKEKE 597
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
93-459 |
5.35e-12 |
|
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: 69.71 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 93 QISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNlilsDEAIKYKDKIKVLEETNVSLgdkaksLRLQLESER 172
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRER----EKAERYQALLKEKREYEGYE------LLKEKEALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 173 EQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEA-----KLSEEN---VKSECHRVQEENARLKKKKEQLQQQ 244
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkikDLGEEEqlrVKEKIGELEAEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 245 IEEWSRSHAELTEQIRSFETSQKDLEVALTHKDDNISALTNCI----TQLNRLECELESEDAdKGGNESDELAngemggD 320
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYaelkEELEDLRAELEEVDK-EFAETRDELK------D 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 321 RSKKIKDRIKQMMDVSRTQTavsiveedlKLLQLKLRASMSTKcNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEI 400
Cdd:TIGR02169 390 YREKLEKLKREINELKRELD---------RLQEELQRLSEELA-DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2168985272 401 LNEL---YQQKEMALQKKLSQEEYERQDREQKLTAADEKVVLAAEEVKTYKRRIEEMEEELQ 459
Cdd:TIGR02169 460 LAADlskYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
159-471 |
8.09e-12 |
|
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: 69.32 E-value: 8.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 159 DKAKSLRLQLESEREQNVKNQDLILEnkkSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKK 238
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEE---KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 239 EQLQQQIEEWSRSHAELTEQIRSFETSQKDLEVALTHKDDNISALTNCITQLNRlECELESEDADKGGNE----SDELAN 314
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE-ELKALREALDELRAEltllNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 315 GEMGGDRSKKIKDRIKQMMDVSRTQTAVsiVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTL 394
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEE--LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 395 RQKVEILN----ELYQQKEmALQKKLSQEEYE----RQDREQKLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTERSFK 466
Cdd:TIGR02168 900 SEELRELEskrsELRRELE-ELREKLAQLELRleglEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
....*
gi 2168985272 467 NQIAA 471
Cdd:TIGR02168 979 NKIKE 983
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
93-475 |
4.30e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.09 E-value: 4.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 93 QISEKLENIKKEnAELMQKLSSYEQKIKESKKYVQETKKqnlilSDEAIKYKDKIKVLEETNVSLGDKAKSLRLQLESER 172
Cdd:PTZ00121 1395 EAKKKAEEDKKK-ADELKKAAAAKKKADEAKKKAEEKKK-----ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 173 EQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQIEEWSRSH 252
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA 1548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 253 AEL--TEQIRSFETSQKdLEVALTHKDDNISALTNCiTQLNRLEcELESEDADKGGNESDELANGEMGGDRSKKIK-DRI 329
Cdd:PTZ00121 1549 DELkkAEELKKAEEKKK-AEEAKKAEEDKNMALRKA-EEAKKAE-EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaEEL 1625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 330 KQMMDVSRT--QTAVSIVEEDLKLLQLKlRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDEcktlRQKVEILNELYQQ 407
Cdd:PTZ00121 1626 KKAEEEKKKveQLKKKEAEEKKKAEELK-KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE----KKAAEALKKEAEE 1700
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2168985272 408 KEMALQKKLSQEEYERqdREQKLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTERSfKNQIAAHEKK 475
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKK--KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKIAHLKKE 1765
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
95-404 |
7.40e-11 |
|
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: 65.86 E-value: 7.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 95 SEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNLILSDEAIKYKDKIKVLEETNVSLGDKAKSLRLQLESEREQ 174
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIP 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 175 NVKNQdlilenkksIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQIEEWSRSHAE 254
Cdd:TIGR02169 795 EIQAE---------LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 255 LTEQIRSFETSQKDLEVALTHKDDNISALTNCITQLNRLECELESEDADKGGNESDELANGEMGGDRSKKIKDRIKQMMD 334
Cdd:TIGR02169 866 LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 335 VSRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNEL 404
Cdd:TIGR02169 946 IPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
92-469 |
1.53e-09 |
|
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: 61.57 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 92 KQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQ----NLILSDeAIKYKDKIKVLEETNVSLGDKAKSLRLQ 167
Cdd:TIGR04523 155 EKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKllklELLLSN-LKKKIQKNKSLESQISELKKQNNQLKDN 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 168 LESEREQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEA--KLSE-----ENVKSECHRVQEENArlkkkkeq 240
Cdd:TIGR04523 234 IEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNnkKIKElekqlNQLKSEISDLNNQKE-------- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 241 lqqqiEEWSRshaELTEQIRSFETSQKDLEVALTHKDDNISALTNCITQLNRLECELESEDAD---------------KG 305
Cdd:TIGR04523 306 -----QDWNK---ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEkqreleekqneieklKK 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 306 GNES--DELANGEmggDRSKKIKDRIKQMMDVSRT-QTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQT 382
Cdd:TIGR04523 378 ENQSykQEIKNLE---SQINDLESKIQNQEKLNQQkDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 383 AKAGLEDECKTLRQKVEILNELYQQkemaLQKKLSQEEYERQDREQKLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTE 462
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINK----IKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
|
....*..
gi 2168985272 463 rSFKNQI 469
Cdd:TIGR04523 531 -SEKKEK 536
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
86-530 |
1.78e-09 |
|
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: 61.28 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 86 IYQVTEKQISEKLENIKKENA------ELMQKLSSYEQKIKESKKYVQETKKQNLILS----------DEAIKYKDKIKV 149
Cdd:pfam05483 326 ICQLTEEKEAQMEELNKAKAAhsfvvtEFEATTCSLEELLRTEQQRLEKNEDQLKIITmelqkksselEEMTKFKNNKEV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 150 -LEETNVSLGDKAKSLrlqleserEQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQ 228
Cdd:pfam05483 406 eLEELKKILAEDEKLL--------DEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLK 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 229 EENARLKKKKEQLQQQIEEWSRSHAELTEqirsfETSQKDLEVAlTHKDDnisaLTNCITQLNRLECELESEDaDKGGNE 308
Cdd:pfam05483 478 TELEKEKLKNIELTAHCDKLLLENKELTQ-----EASDMTLELK-KHQED----IINCKKQEERMLKQIENLE-EKEMNL 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 309 SDELangEMGGDRSKKIKDRIKQMMDVSRtQTAVSIVEEDLKllQLKLRASMSTKC-NLEDQ-------IKKLEDDRSSL 380
Cdd:pfam05483 547 RDEL---ESVREEFIQKGDEVKCKLDKSE-ENARSIEYEVLK--KEKQMKILENKCnNLKKQienknknIEELHQENKAL 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 381 QTAKAG--------------LEDECKTLRQKVEILNELYqQKEMALqKKLSQEEYERQDREQKLTaADEKVVLAAEEVKT 446
Cdd:pfam05483 621 KKKGSAenkqlnayeikvnkLELELASAKQKFEEIIDNY-QKEIED-KKISEEKLLEEVEKAKAI-ADEAVKLQKEIDKR 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 447 YKRRIEEMEEELQKTERSFKNQIAAHEKKAHDNWLKARAAERAMAEEKREAANLRHKLLEMTQKMAMRQDEPVIVKpMPG 526
Cdd:pfam05483 698 CQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLK-MEA 776
|
....
gi 2168985272 527 RPNT 530
Cdd:pfam05483 777 KENT 780
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
91-475 |
1.82e-09 |
|
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: 61.19 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 91 EKQISEKLENIKKE--NAELMQK-----LSSYEQKIKESKKYVQETKKQNLILSDEAIKYKDKIKVLEETNVSLGDKAKS 163
Cdd:TIGR04523 35 EKQLEKKLKTIKNElkNKEKELKnldknLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 164 LRLQ----------LESEREQNVKNQDLILENKKSIEKLKDVISMNASElsevqvaLNEAKLSEENVK----SECHRVQE 229
Cdd:TIGR04523 115 DKEQknklevelnkLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND-------LKKQKEELENELnlleKEKLNIQK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 230 ENARLKKKKEQLQ---QQIEEWSRSHAELTEQIRSFETSQKDLEVALTHKDDNISALTNCI----TQLNRL--------- 293
Cdd:TIGR04523 188 NIDKIKNKLLKLElllSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIsntqTQLNQLkdeqnkikk 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 294 ---ECELESEDADKGGNE-SDELA---------NGEMGGDRSKKIKDRIKQmmdvsrtqtavsiVEEDLKLLQLKLRASM 360
Cdd:TIGR04523 268 qlsEKQKELEQNNKKIKElEKQLNqlkseisdlNNQKEQDWNKELKSELKN-------------QEKKLEEIQNQISQNN 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 361 STKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNELYQQKEMALQKKLSQeeyeRQDREQKLTAADEKVVLA 440
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ----INDLESKIQNQEKLNQQK 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2168985272 441 AEEVKTYKRRIEEMEEELQ----------KTERSFKNQIAAHEKK 475
Cdd:TIGR04523 411 DEQIKKLQQEKELLEKEIErlketiiknnSEIKDLTNQDSVKELI 455
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
79-479 |
4.55e-09 |
|
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: 60.03 E-value: 4.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 79 ILVVKSRIYQVTEKQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQ-------NLILSDEAIKYKDKIKVLE 151
Cdd:TIGR04523 297 ISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKEltnseseNSEKQRELEEKQNEIEKLK 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 152 ETNVSLGDKAKSLRLQLeSEREQNVKNQDLILENK---------------KSIEKLKDVISMNASELSEV---------- 206
Cdd:TIGR04523 377 KENQSYKQEIKNLESQI-NDLESKIQNQEKLNQQKdeqikklqqekelleKEIERLKETIIKNNSEIKDLtnqdsvkeli 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 207 -----------QVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQIEEWSRSHAELTEQIRSFETSQKDLEVALTH 275
Cdd:TIGR04523 456 iknldntreslETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 276 KDDNISALTNCITQLN------RLECELESEDAD----KGGNESDELANGEMG---GDRSKKIKDRIKQ----MMDVSRT 338
Cdd:TIGR04523 536 KESKISDLEDELNKDDfelkkeNLEKEIDEKNKEieelKQTQKSLKKKQEEKQeliDQKEKEKKDLIKEieekEKKISSL 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 339 QTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNELYQQ--KEMALQKKl 416
Cdd:TIGR04523 616 EKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDwlKELSLHYK- 694
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2168985272 417 sqEEYERQDREQKLTAADEKvvlaaeevktYKrRIEEMEEELQKTERSFKNQIAAHEKKAHDN 479
Cdd:TIGR04523 695 --KYITRMIRIKDLPKLEEK----------YK-EIEKELKKLDEFSKELENIIKNFNKKFDDA 744
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
82-463 |
6.95e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.28 E-value: 6.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 82 VKSRIYQVTEKQISEKLENIKKENAELMQKLSSYEqkikESKKYVQETKKQ-NLILS------------DEAI-KYKDKI 147
Cdd:PRK02224 192 LKAQIEEKEEKDLHERLNGLESELAELDEEIERYE----EQREQARETRDEaDEVLEeheerreeletlEAEIeDLRETI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 148 KVLEETNVSLGDKAKSLR---LQLESEREQNVKNQDLILENKKSIEKLKDVISMNASELSE--------VQVALNEAKLS 216
Cdd:PRK02224 268 AETEREREELAEEVRDLRerlEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDrleecrvaAQAHNEEAESL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 217 EENVK---SECHRVQEENARLKKKKEQLQQQIEEWSRSHAELTEQIRS----FETSQKDLEVALTHKDDNISALTNCITQ 289
Cdd:PRK02224 348 REDADdleERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEElrerFGDAPVDLGNAEDFLEELREERDELRER 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 290 LNRLECELESEDADKGGNEsDELANG---EMGGDrskkIKDrikqmmdvsrtQTAVSIVEEDLKLLQlKLRASMSTkcnL 366
Cdd:PRK02224 428 EAELEATLRTARERVEEAE-ALLEAGkcpECGQP----VEG-----------SPHVETIEEDRERVE-ELEAELED---L 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 367 EDQIKKLEDDRSSLQTAKAgLEDECKTLRQKVEILNELYQQKEM----------ALQKKLSQEEYERQDREQKLTAADEK 436
Cdd:PRK02224 488 EEEVEEVEERLERAEDLVE-AEDRIERLEERREDLEELIAERREtieekreraeELRERAAELEAEAEEKREAAAEAEEE 566
|
410 420
....*....|....*....|....*..
gi 2168985272 437 VVLAAEEVKTYKRRIEEMEEELQKTER 463
Cdd:PRK02224 567 AEEAREEVAELNSKLAELKERIESLER 593
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
96-501 |
1.22e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 96 EKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNLILSDEAIKYKDKIKVLEET-NVSLGDKAKSLRLQLESEREQ 174
Cdd:PTZ00121 1070 EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDArKAEEARKAEDARKAEEARKAE 1149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 175 NVKNQDLileNKKSIEKLKDVISMNASELSEVQVALN--EAKLSEENVKSECHRVQEENARLKKKKEqlqqqIEEWSRSH 252
Cdd:PTZ00121 1150 DAKRVEI---ARKAEDARKAEEARKAEDAKKAEAARKaeEVRKAEELRKAEDARKAEAARKAEEERK-----AEEARKAE 1221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 253 -AELTEQIRSFETSQKDLEVA-----LTHKDDNISALTNCITQLNRLECELESEDADKggneSDELANGEmggdrSKKIK 326
Cdd:PTZ00121 1222 dAKKAEAVKKAEEAKKDAEEAkkaeeERNNEEIRKFEEARMAHFARRQAAIKAEEARK----ADELKKAE-----EKKKA 1292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 327 DRIKQMMDVSRTQTAVSIVEEDLKLLQLKLRASMSTKcNLEDQIKKLEDDRSSLQTAKAGLEDECKTL------------ 394
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK-KADAAKKKAEEAKKAAEAAKAEAEAAADEAeaaeekaeaaek 1371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 395 -----RQKVEILNELYQQKEMALQKKLSQEEYERQDREQKLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTERSFKNQI 469
Cdd:PTZ00121 1372 kkeeaKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK 1451
|
410 420 430
....*....|....*....|....*....|..
gi 2168985272 470 AAHEKKAHDNWLKARAAERAMAEEKREAANLR 501
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
139-481 |
1.33e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 139 EAIKYKDKIKVLEetNVSLGDKAKSLRLQLESEREQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEE 218
Cdd:COG1196 214 RYRELKEELKELE--AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 219 NVKSECHRVQEENARLKKKKEQLQQQIEEWSRSHAELTEQIRSFETSQKDLEVALTHKDDNISALTNCITQLNRLECELE 298
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 299 SEDADKGGNESDELAngemggdrskkikdrikqmmDVSRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRS 378
Cdd:COG1196 372 AELAEAEEELEELAE--------------------ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 379 SLQTAKAGLEDEcktLRQKVEILNELyQQKEMALQKKLSQEEYERQDREQKLTAADEKVVLAAEEVKTYKRRIEEMEEEL 458
Cdd:COG1196 432 ELEEEEEEEEEA---LEEAAEEEAEL-EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
|
330 340
....*....|....*....|...
gi 2168985272 459 QKTERSFKNQIAAHEKKAHDNWL 481
Cdd:COG1196 508 EGVKAALLLAGLRGLAGAVAVLI 530
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
253-516 |
3.30e-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: 57.37 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 253 AELTEQIRSFETSQKDLEVALTHKDDNISALTNCITQLNRLECELESEDADkggnesdelangemggdrskkikdrikQM 332
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA---------------------------LR 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 333 MDVSRTQTAVSIVEEDLKLLQLKLRasmstkcNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVE-ILNELYQQKEM- 410
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELT-------ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEqLKEELKALREAl 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 411 -ALQKKLSQEEYERQDREQKLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTERSFKNQIAAHEK--KAHDNWLKARAAE 487
Cdd:TIGR02168 806 dELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEleSELEALLNERASL 885
|
250 260 270
....*....|....*....|....*....|.
gi 2168985272 488 RAMAEEKREA-ANLRHKLLEM-TQKMAMRQD 516
Cdd:TIGR02168 886 EEALALLRSElEELSEELRELeSKRSELRRE 916
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
88-476 |
6.10e-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: 56.60 E-value: 6.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 88 QVTEKQISEKLENikkenaelMQKLssyEQKIKESKKYVQETKKQnlilSDEAIKYKDKIKVLEETNVSLgdkaksLRLQ 167
Cdd:TIGR02168 175 KETERKLERTREN--------LDRL---EDILNELERQLKSLERQ----AEKAERYKELKAELRELELAL------LVLR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 168 LESEREQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQIEE 247
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 248 WSRSHAELTEQIRSFETSQKDLEVALTHKDDNISALTNcitqlnrlECELESEDADKGGNESDELANgemggdrskKIKD 327
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKE--------ELESLEAELEELEAELEELES---------RLEE 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 328 RIKQMMDVSRtqtavsiveeDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDEcKTLRQKVEILNELYQQ 407
Cdd:TIGR02168 377 LEEQLETLRS----------KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK-LEEAELKELQAELEEL 445
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2168985272 408 KEMALQKKLSQEEYERQDREQK--LTAADEKVVLAAEEVKTYKRRI---EEMEEELQKTERSFKNQIAAHEKKA 476
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELReeLEEAEQALDAAERELAQLQARLdslERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
95-510 |
8.79e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 8.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 95 SEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNLILSDEAIKYKDKIKVLEETNVSLGDKAKSLRLQLESEREQ 174
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA 1393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 175 NVKNQDLILENKKSIE-KLKDVISMNASEL----SEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQqqieEWS 249
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADElKKAAAAKKKADEAkkkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKA----EEA 1469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 250 RSHAEL---TEQIRSFETSQKDLEVALTHKDdnisaltncitqlnrlecelESEDADKGGNESDELANGEMGGDRSKKIK 326
Cdd:PTZ00121 1470 KKADEAkkkAEEAKKADEAKKKAEEAKKKAD--------------------EAKKAAEAKKKADEAKKAEEAKKADEAKK 1529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 327 DRIKQMMDVSRTQTAVSIVEEDLKLLQLKlRASMSTKCnleDQIKKLEDDRSSL--------QTAKAGLEDECKTLRQKV 398
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKKAEELK-KAEEKKKA---EEAKKAEEDKNMAlrkaeeakKAEEARIEEVMKLYEEEK 1605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 399 EILNELYQQKEMALQK--KLSQEEYERQDREQkLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTERSFKNQiAAHEKKA 476
Cdd:PTZ00121 1606 KMKAEEAKKAEEAKIKaeELKKAEEEKKKVEQ-LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK-AEEAKKA 1683
|
410 420 430
....*....|....*....|....*....|....
gi 2168985272 477 HDNWLKARAAERAMAEEKREAANLRHKLLEMTQK 510
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK 1717
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
92-482 |
1.01e-07 |
|
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: 55.89 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 92 KQISEKLENIKKENAELMQKLSSYEQKIKESKKYV-------QETKKQNLILSDEAIKYKDKIKVLeetnvsLGDKAKSL 164
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLvlanselTEARTERDQFSQESGNLDDQLQKL------LADLHKRE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 165 RlQLESEREQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALneaklseENVKSEChrvQEENARLKKKKEQLQQQ 244
Cdd:pfam15921 391 K-ELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALL-------KAMKSEC---QGQMERQMAAIQGKNES 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 245 IEEWSRSHA--------------ELTEQIRSFETSQK---DLEVALTHKDDNISALTNCITQLnRLECELESEDADKGGN 307
Cdd:pfam15921 460 LEKVSSLTAqlestkemlrkvveELTAKKMTLESSERtvsDLTASLQEKERAIEATNAEITKL-RSRVDLKLQELQHLKN 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 308 ESDELANGEMGGDRSKKIKDRIKQMMDVSRTQtavsiVEEDLKLLQLKLR---ASMSTKCNLEDQIKKLEDDRSSLQTAK 384
Cdd:pfam15921 539 EGDHLRNVQTECEALKLQMAEKDKVIEILRQQ-----IENMTQLVGQHGRtagAMQVEKAQLEKEINDRRLELQEFKILK 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 385 AGLEDECKTLRQKVEILnELYQQKEM-ALQKKLSQEEYERQDREQKLTaadekvvlaaeEVKTYKRRIEEMEEELQKTER 463
Cdd:pfam15921 614 DKKDAKIRELEARVSDL-ELEKVKLVnAGSERLRAVKDIKQERDQLLN-----------EVKTSRNELNSLSEDYEVLKR 681
|
410
....*....|....*....
gi 2168985272 464 SFKNQiaAHEKKAHDNWLK 482
Cdd:pfam15921 682 NFRNK--SEEMETTTNKLK 698
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
80-461 |
1.23e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 55.36 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 80 LVVKSRIYQVTEKQISEKLENIKKENAELMQKLSSYEQKIKES--KKYVQETKKQNLILSDEAIKYKDKIKVLEETNVSL 157
Cdd:pfam02463 669 SELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEElkKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEE 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 158 gdKAKSLRLQLESEREQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKlsEENVKSECHRVQEENARLKKK 237
Cdd:pfam02463 749 --EEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL--RALEEELKEEAELLEEEQLLI 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 238 KEQLQQQIEEWSRSHAELTEQIRSFETSQKDLEvalthkddNISALTNCITQLNRLECELESEDADKggnESDELANGEM 317
Cdd:pfam02463 825 EQEEKIKEEELEELALELKEEQKLEKLAEEELE--------RLEEEITKEELLQELLLKEEELEEQK---LKDELESKEE 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 318 GGDRSKKIKDRIKQ--MMDVSRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRsslqtakagLEDECKTLR 395
Cdd:pfam02463 894 KEKEEKKELEEESQklNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK---------EEEEERNKR 964
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2168985272 396 QKVEILNELYQQKEMALQKKLSQEEYERQDREQKLTAADEKVVLAAEEVKTYKRRIEEMEEELQKT 461
Cdd:pfam02463 965 LLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSIN 1030
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
92-506 |
2.71e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 92 KQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKqnlilsdeaikykdKIKVLEEtnvslgdKAKSLRlQLESE 171
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKK--------------EIEELEE-------KVKELK-ELKEK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 172 REQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAklseENVKSECHRVQEEnarlkkkkeqlqqqIEEWSRS 251
Cdd:PRK03918 292 AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL----EEKEERLEELKKK--------------LKELEKR 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 252 HAELTEQIRSFETSQkdlevALTHKDDNISALTNCITqLNRLECELESEDADKGGNESDELANGEMGGDRSKKIKDRIKQ 331
Cdd:PRK03918 354 LEELEERHELYEEAK-----AKKEELERLKKRLTGLT-PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKA 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 332 MMDVSRTQTAV-----SIVEEDLKLLQLKLRASMStkcNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRqkveilnELYQ 406
Cdd:PRK03918 428 IEELKKAKGKCpvcgrELTEEHRKELLEEYTAELK---RIEKELKEIEEKERKLRKELRELEKVLKKES-------ELIK 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 407 QKEMALQKKLSQEEYERQDREqKLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTErSFKNQIAAHEKKAHDnwlkaraa 486
Cdd:PRK03918 498 LKELAEQLKELEEKLKKYNLE-ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE-ELKKKLAELEKKLDE-------- 567
|
410 420
....*....|....*....|
gi 2168985272 487 eramaeEKREAANLRHKLLE 506
Cdd:PRK03918 568 ------LEEELAELLKELEE 581
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
261-508 |
6.37e-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: 53.15 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 261 SFETSQKDLEVALTHKDDNISALTN-CITQLNRLEC---ELESEDADKGGNESDELANGEMGGDRSKKIKDRIKQMM-DV 335
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRELSsLQSELRRIENrldELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEeDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 336 SRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDD--RSSLQTAKAGLEDECKTLRQKVEILNELyQQKEMALQ 413
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlsHSRIPEIQAELSKLEEEVSRIEARLREI-EQKLNRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 414 KKLSQEEYERQDREQKLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTERSFKNQIAAH-----EKKAHDNWLKARAAER 488
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLgdlkkERDELEAQLRELERKI 905
|
250 260
....*....|....*....|
gi 2168985272 489 AMAEEKREAANLRHKLLEMT 508
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAK 925
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
329-475 |
7.71e-07 |
|
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: 51.08 E-value: 7.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 329 IKQMMDVSRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNELYQQ- 407
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNv 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2168985272 408 ---KEM-ALQKKLSQEEYERQDREQKLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTERSFKNQIAAHEKK 475
Cdd:COG1579 86 rnnKEYeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
92-474 |
1.07e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 92 KQISEKLENIKKENAELMQKLSSYEQKIKESKKY--VQETKKQNLILSDEAIKYKDKIKVLEEtnvsLGDKAKSLRLQLE 169
Cdd:COG4717 98 EELEEELEELEAELEELREELEKLEKLLQLLPLYqeLEALEAELAELPERLEELEERLEELRE----LEEELEELEAELA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 170 SEREQ-NVKNQDLILENKKSIEKLKDvismnasELSEVQVALNEAKLSEENVKSECHRVQEE--NARLKKKKEQLQQQIE 246
Cdd:COG4717 174 ELQEElEELLEQLSLATEEELQDLAE-------ELEELQQRLAELEEELEEAQEELEELEEEleQLENELEAAALEERLK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 247 EWSRShAELTEQIRSFETSQKDLEVALThkddNISALTNCITQLNRLECELESEDADKGGNESDELANGEMGGDRSKKIK 326
Cdd:COG4717 247 EARLL-LLIAAALLALLGLGGSLLSLIL----TIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEEL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 327 DRIKQMMDVSRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQtAKAGLEDEcKTLRQKVEILNElYQ 406
Cdd:COG4717 322 EELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALL-AEAGVEDE-EELRAALEQAEE-YQ 398
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2168985272 407 QKEMALQKKLSQEEYERQDREQKLTAADEKVVlaAEEVKTYKRRIEEMEEE---LQKTERSFKNQIAAHEK 474
Cdd:COG4717 399 ELKEELEELEEQLEELLGELEELLEALDEEEL--EEELEELEEELEELEEEleeLREELAELEAELEQLEE 467
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
92-512 |
1.36e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 92 KQISEKLENIKKENAELMQKLSSYEQKIKESKKyVQETKKQNLILSDEAIKYKDKIKVLEETNVSLGDKAKSLRLQLEsE 171
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-E 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 172 REQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEA-KLSEENVKSECHRVQEEnarlkkkkeqlqqqIEEWSR 250
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELeRLKKRLTGLTPEKLEKE--------------LEELEK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 251 SHAELTEQIRSFETSQKDLEVALTHKDDNISALTNCitqlnRLEC-----ELESEDADKGGNE-SDELANGEmggDRSKK 324
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELKKAIEELKKA-----KGKCpvcgrELTEEHRKELLEEyTAELKRIE---KELKE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 325 IKDRIKQMMDVSR-TQTAVSIVEEDLKLL----QLKLRASMSTKCNLEDQIKKLEDDRSsLQTAKAGLEDECKTLRQKVE 399
Cdd:PRK03918 471 IEEKERKLRKELReLEKVLKKESELIKLKelaeQLKELEEKLKKYNLEELEKKAEEYEK-LKEKLIKLKGEIKSLKKELE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 400 ILNELYQQKEmALQKKLSQEEYERQDREQKLTAadekvvLAAEEVKTYKRRIEEMEeelqktersfknqiaahekKAHDN 479
Cdd:PRK03918 550 KLEELKKKLA-ELEKKLDELEEELAELLKELEE------LGFESVEELEERLKELE-------------------PFYNE 603
|
410 420 430
....*....|....*....|....*....|...
gi 2168985272 480 WLKARAAERAMAEEKREAANLRHKLLEMTQKMA 512
Cdd:PRK03918 604 YLELKDAEKELEREEKELKKLEEELDKAFEELA 636
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
96-501 |
2.04e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 96 EKLENIKKenAELMQKLSSYEQKIKESKKYVQETKKQnlilSDEAIKYKDKIKVLEETNVSLGDKAKSlrlQLESEREQN 175
Cdd:PTZ00121 1296 KKAEEKKK--ADEAKKKAEEAKKADEAKKKAEEAKKK----ADAAKKKAEEAKKAAEAAKAEAEAAAD---EAEAAEEKA 1366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 176 VKNQDLILENKKSIEKLKdvismnaSELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQIEEWSRSHAEL 255
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAK-------KKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKK 1439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 256 TEQIRSFETSQKDLEVAltHKDDNISaltncitqlNRLECELESEDADKGGNESDELANGEMGGDRSKKIKDRIKQMMDV 335
Cdd:PTZ00121 1440 AEEAKKADEAKKKAEEA--KKAEEAK---------KKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 336 SRTQTAVSIVEEDLKLLQLKlRASMSTKCnleDQIKKLEDDRSSLQTAKAGLEDECKTLRqKVEILNELYQQKEMALQKK 415
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAK-KAEEAKKA---DEAKKAEEKKKADELKKAEELKKAEEKK-KAEEAKKAEEDKNMALRKA 1583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 416 LSQEEYERQDREQKLTAADEKVVLAAEEVKT---YKRRIEEM--EEELQKTERSFKNQIAAHEKKA-------HDNWLKA 483
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKaeeAKIKAEELkkAEEEKKKVEQLKKKEAEEKKKAeelkkaeEENKIKA 1663
|
410
....*....|....*...
gi 2168985272 484 RAAERAMAEEKREAANLR 501
Cdd:PTZ00121 1664 AEEAKKAEEDKKKAEEAK 1681
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
115-429 |
5.41e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 50.36 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 115 YEQKIKESKKYVQET--------------------------------KKQNLILSDEAIKYKDKIKVLEETNVSLGDKAK 162
Cdd:pfam02463 168 KRKKKEALKKLIEETenlaeliidleelklqelklkeqakkaleyyqLKEKLELEEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 163 SLRLQLES-------EREQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLK 235
Cdd:pfam02463 248 DEQEEIESskqeiekEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 236 KKKEQLQQQIEEWSRSHAELTEQIRSFETSQKDLEVALTHkddNISALTNCITQLNRLECELESEDADKggNESDELANG 315
Cdd:pfam02463 328 KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK---LEQLEEELLAKKKLESERLSSAAKLK--EEELELKSE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 316 EMGGDRSKKIKDRIKQMMDVSRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSL-QTAKAGLEDECKTL 394
Cdd:pfam02463 403 EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELkKSEDLLKETQLVKL 482
|
330 340 350
....*....|....*....|....*....|....*
gi 2168985272 395 RQKVEILNELYQQKEMALQKKLSQEEYERQDREQK 429
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQKESKARSGLKVLLALIK 517
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
90-356 |
1.11e-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: 49.30 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 90 TEKQISEK---LENIKKENAELMQKLSSYEQKIKEskkyvqETKKQNLILSDEAIKYKDKIKVLEETNVSLGDKAKSLRL 166
Cdd:TIGR02169 242 IERQLASLeeeLEKLTEEISELEKRLEEIEQLLEE------LNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKER 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 167 QLESEREQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQIE 246
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 247 EWSRSHAEL-TEQIRSFETSQKDLEVALTHKDDnisaLTNCITQLNRLECELESEDAdkggnesdELANGEmgGDRSKKI 325
Cdd:TIGR02169 396 KLKREINELkRELDRLQEELQRLSEELADLNAA----IAGIEAKINELEEEKEDKAL--------EIKKQE--WKLEQLA 461
|
250 260 270
....*....|....*....|....*....|.
gi 2168985272 326 KDRIKQMMDVSRTQTAVSIVEEDLKLLQLKL 356
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
366-478 |
2.55e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 366 LEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNELYQQ----KEMALQKKLSQEEYERQDREQK-------LTAAD 434
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRrarlealLAALG 372
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2168985272 435 EKVVLAAEEVKTYKRRIEEMEEELQKTERSFKNQIAAHEKKAHD 478
Cdd:COG4913 373 LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD 416
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
91-440 |
2.89e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 91 EKQIsEKLEnIKKENAELMQKLSSyEQKIKESKKYV---QETKKQNLILSDEAIKYKDKIKVLEETNVSLGDKAKSLRLQ 167
Cdd:COG1196 199 ERQL-EPLE-RQAEKAERYRELKE-ELKELEAELLLlklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 168 LESEREQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEenarlkkkkeqlqqQIEE 247
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE--------------ELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 248 WSRSHAELTEQIRSFETSQKDLEVALTHKDDNISALtncITQLNRLECELESEDADKGGNESDELANGEMGGDRSKKIKD 327
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA---EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 328 RIKQMMDVSRTQTAVSIVEEDLKLLQLKLRASMStkcNLEDQIKKLEDDRSSLQTAKAGLEDEcktLRQKVEILNELYQQ 407
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEA---ELEEEEEALLELLAELLEEAALLEAA---LAELLEELAEAAAR 492
|
330 340 350
....*....|....*....|....*....|...
gi 2168985272 408 KEMALQKKLSQEEYERQDREQKLTAADEKVVLA 440
Cdd:COG1196 493 LLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
83-463 |
3.47e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 83 KSRIYQVTEKQISEKLENIKKENAELMQKLS-------SYEQKIKESKKYVQETKKQNLI-------LSDE-----AIKY 143
Cdd:PRK03918 378 KKRLTGLTPEKLEKELEELEKAKEEIEEEISkitarigELKKEIKELKKAIEELKKAKGKcpvcgreLTEEhrkelLEEY 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 144 KDKIKVLEETNVSLGDKAKSLRLQLEsEREQNVKNQDLILENKKSIEKLKDVismnaselsevqvalnEAKLSEENVKse 223
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELR-ELEKVLKKESELIKLKELAEQLKEL----------------EEKLKKYNLE-- 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 224 chrvqeenarlkkkkeqlqqQIEEWSRSHAELTEQIRSFETSQKDLEVALTHKDDNISALTNCITQLNRLECELesedad 303
Cdd:PRK03918 519 --------------------ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEEL------ 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 304 kgGNESDELanGEMGGDRSKKIKDRIKQMMDVSRtqtavsiveedlKLLQLKlrasmSTKCNLEDQIKKLEDDRSSLQTA 383
Cdd:PRK03918 573 --AELLKEL--EELGFESVEELEERLKELEPFYN------------EYLELK-----DAEKELEREEKELKKLEEELDKA 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 384 KAGLEDECKTLRQKVEILNElyqqkemaLQKKLSQEEYERQDRE-----QKLTAADEKVVLAAEEVKTYKRRIEEMEEEL 458
Cdd:PRK03918 632 FEELAETEKRLEELRKELEE--------LEKKYSEEEYEELREEylelsRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
....*
gi 2168985272 459 QKTER 463
Cdd:PRK03918 704 EEREK 708
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
323-518 |
3.61e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 323 KKIKDRIKQMMD-VSRTQTAVSIVEEDLKLLQLKLRAsmstkcnLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEIL 401
Cdd:COG4942 30 EQLQQEIAELEKeLAALKKEEKALLKQLAALERRIAA-------LARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 402 NELYQQKEMALQKK---------LSQEEY---------------ERQDREQKLTAADEKVVLAAEEVKTYKRRIEEMEEE 457
Cdd:COG4942 103 KEELAELLRALYRLgrqpplallLSPEDFldavrrlqylkylapARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2168985272 458 LQKTERSFKNQIAAHEKKAHDNWLKARAAERAMAEEKREAANLRHKLLEMTQKMAMRQDEP 518
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
525-780 |
5.90e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 46.70 E-value: 5.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 525 PGRPNTQNPPRRGLLSQNGSFGPSPVSG----GECSPPLPVESPGRPLSATLSRRDTPRsefgsldrHLPRPRWPSEASG 600
Cdd:PHA03307 106 PTPPGPSSPDPPPPTPPPASPPPSPAPDlsemLRPVGSPGPPPAASPPAAGASPAAVAS--------DAASSRQAALPLS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 601 KHSASDPGPPPVVNSSSRSSSPAkamdegkvnmAPKGPPPFPGVPLMGGPVPPPIRYGPPPQLcgPFGPRPLPPPFVPGM 680
Cdd:PHA03307 178 SPEETARAPSSPPAEPPPSTPPA----------AASPRPPRRSSPISASASSPAPAPGRSAAD--DAGASSSDSSSSESS 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 681 RPPLGVREYAPGVLPGKRDLPVDPREFVPGHTPFRPPGSLGPREFFIPGTRLPPPSHGPQDYPPPPPALRDSLPSGPREE 760
Cdd:PHA03307 246 GCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESS 325
|
250 260
....*....|....*....|
gi 2168985272 761 AQPASPSSVQDRSQASKPTP 780
Cdd:PHA03307 326 SSSTSSSSESSRGAAVSPGP 345
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
99-462 |
6.30e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 99 ENIKKENAELMQKLSSYEQKIKESKKYVQETKKQnlilsdeAIKYKDKIKVLEETNVSLGDKAKSLRLQLESEREQnvkn 178
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEECRVAAQAHNEE-------AESLREDADDLEERAEELREEAAELESELEEAREA---- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 179 qdlILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQIEEwsrsHAELTEQ 258
Cdd:PRK02224 379 ---VEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEE----AEALLEA 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 259 IRSFETSQkDLEVAlthkdDNISALTNCITQLNRLECELES-----EDADKGGNESDELANGEMGGDRSKKIKDRIKQMM 333
Cdd:PRK02224 452 GKCPECGQ-PVEGS-----PHVETIEEDRERVEELEAELEDleeevEEVEERLERAEDLVEAEDRIERLEERREDLEELI 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 334 DVSRTqtavSIVEEDLKLLQL-----KLRASMSTK--------------------CN-----LEDQIKKLEDDRSSLQTA 383
Cdd:PRK02224 526 AERRE----TIEEKRERAEELreraaELEAEAEEKreaaaeaeeeaeeareevaeLNsklaeLKERIESLERIRTLLAAI 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 384 kAGLEDECKTLRQKVEILNELYQQKEMALQkklsqeeyERQDREQKLTAA--DEKVVLAAEEVKTYKRRIEEMEEELQKT 461
Cdd:PRK02224 602 -ADAEDEIERLREKREALAELNDERRERLA--------EKRERKRELEAEfdEARIEEAREDKERAEEYLEQVEEKLDEL 672
|
.
gi 2168985272 462 E 462
Cdd:PRK02224 673 R 673
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
89-507 |
8.21e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 89 VTEKQISEKLENIKKENAELMQKLSSYEqkIKESKKYVQETKKQNLILSDEA----IKYKDKIKVLEETNVSLGDKAKSL 164
Cdd:PRK03918 97 LKYLDGSEVLEEGDSSVREWVERLIPYH--VFLNAIYIRQGEIDAILESDESrekvVRQILGLDDYENAYKNLGEVIKEI 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 165 RLQLES-----EREQNVKNqdLILENKKSIEKLKDVISMNASELSEVQVALNEA---KLSEENVKSECHRVQEENARLKK 236
Cdd:PRK03918 175 KRRIERlekfiKRTENIEE--LIKEKEKELEEVLREINEISSELPELREELEKLekeVKELEELKEEIEELEKELESLEG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 237 KKEQLQQQIEEWSRSHAELTEQIRSFETSQKDLEvALTHKDDNISAL----TNCITQLNRLECELESEDADKGGNEsDEL 312
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLsefyEEYLDELREIEKRLSRLEEEINGIE-ERI 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 313 ANGEMGGDRSKKIKDRIKQmmdvsrTQTAVSIVEEDLKLLQlKLRASMSTKCNLEDQIK-----KLEDDRSSLQTAKAGL 387
Cdd:PRK03918 331 KELEEKEERLEELKKKLKE------LEKRLEELEERHELYE-EAKAKKEELERLKKRLTgltpeKLEKELEELEKAKEEI 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 388 EDECKTLRQKVEILNELYQQKEMALQK-------------KLSQEEYERQDREQKLTAAD--EKVVLAAEEVKTYKRRIE 452
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrELTEEHRKELLEEYTAELKRieKELKEIEEKERKLRKELR 483
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2168985272 453 EMEEELQKTERSFKNQIAAHEKKAHDNWLKaRAAERAMAEEKREAANLRHKLLEM 507
Cdd:PRK03918 484 ELEKVLKKESELIKLKELAEQLKELEEKLK-KYNLEELEKKAEEYEKLKEKLIKL 537
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
85-519 |
9.57e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 9.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 85 RIYQVTEKQISEKLENIKKENAElmqKLSSYEQKIKESKKyVQETKKqnlilSDEAIKYKDKIKVLEETNVSLGDKAKSL 164
Cdd:PTZ00121 1129 KAEEARKAEDARKAEEARKAEDA---KRVEIARKAEDARK-AEEARK-----AEDAKKAEAARKAEEVRKAEELRKAEDA 1199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 165 RLQLESEREQNVKNQDLI--LENKKSIEKLKDVismnaselSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQ 242
Cdd:PTZ00121 1200 RKAEAARKAEEERKAEEArkAEDAKKAEAVKKA--------EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAA 1271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 243 QQIEEwSRSHAEL--TEQIRSFETSQKDLEVALTHKDDNISALTNCITQLNRLECEL------------ESEDADKGGNE 308
Cdd:PTZ00121 1272 IKAEE-ARKADELkkAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkkadaakkkaeEAKKAAEAAKA 1350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 309 SDELANGEMGGDRSKKIKDRIKQMMDVSRTQTAVSIVEEDLKLLQLKLRASMSTKcnLEDQIKKLEDDRSSLQTAKAGLE 388
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKK--KADELKKAAAAKKKADEAKKKAE 1428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 389 DECKT--LRQKVEILNELYQQKEMALQKKLSQEEYERQDREQKLTAADEKVVLA--AEEVKTYKRRIEEMEEELQKTERS 464
Cdd:PTZ00121 1429 EKKKAdeAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAkkADEAKKKAEEAKKKADEAKKAAEA 1508
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2168985272 465 FKNqiAAHEKKAHDnwlKARAAERAMAEEKREAANLRhKLLEMTQKMAMRQDEPV 519
Cdd:PTZ00121 1509 KKK--ADEAKKAEE---AKKADEAKKAEEAKKADEAK-KAEEKKKADELKKAEEL 1557
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
83-474 |
1.01e-04 |
|
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: 46.20 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 83 KSRIYQVtEKQISEKLENIKKENAELMQ------------KLSSYEQKIKESKKYVQETKKQNLILSDEAIKYKDKIKVL 150
Cdd:TIGR01612 1317 ESDINDI-KKELQKNLLDAQKHNSDINLylneianiynilKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKI 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 151 EEtNVSLgdkaKSLRLQLESERE--------QNVK-NQDLILENKKSIeklkDVISMNASELSEvQVALNEAKLSEENVK 221
Cdd:TIGR01612 1396 KD-DINL----EECKSKIESTLDdkdideciKKIKeLKNHILSEESNI----DTYFKNADENNE-NVLLLFKNIEMADNK 1465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 222 SE-CHRVQEENARLKKKKEQLQQQiEEWSRSHAELTEQIRSFETSQKDLEVALTHKDDnisaltncITQLNRLECELESE 300
Cdd:TIGR01612 1466 SQhILKIKKDNATNDHDFNINELK-EHIDKSKGCKDEADKNAKAIEKNKELFEQYKKD--------VTELLNKYSALAIK 1536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 301 DA-DKGGNESDELANgemggdrskKIKDRIKQMMDVSRTQtavsiveedlkllQLKLRASMSTKCNLEDQIKKleDDRSS 379
Cdd:TIGR01612 1537 NKfAKTKKDSEIIIK---------EIKDAHKKFILEAEKS-------------EQKIKEIKKEKFRIEDDAAK--NDKSN 1592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 380 -----LQTAKAGLEDECKTLRQKVEILNELYQQKEmALQKKLSQEEYERQDREQKLTAADEKVVLA-AEEVKTYKRRIEE 453
Cdd:TIGR01612 1593 kaaidIQLSLENFENKFLKISDIKKKINDCLKETE-SIEKKISSFSIDSQDTELKENGDNLNSLQEfLESLKDQKKNIED 1671
|
410 420
....*....|....*....|....
gi 2168985272 454 MEEELQKTE---RSFKNQIAAHEK 474
Cdd:TIGR01612 1672 KKKELDELDseiEKIEIDVDQHKK 1695
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
91-460 |
1.07e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 91 EKQISEKLENIKKENAELMQKlssyEQKIKESKKYVQETKKQNLILSDEAIKYKDKIKVLEETNVSLGDKAKSLRLQLES 170
Cdd:COG1196 371 EAELAEAEEELEELAEELLEA----LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 171 EREQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSechrvQEENARLKKKKEQLQQQIEEWSR 250
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE-----AEADYEGFLEGVKAALLLAGLRG 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 251 SHAELTE--------------------QIRSFETSQKDLEVALTHKDDNISALT-------------------------- 284
Cdd:COG1196 522 LAGAVAVligveaayeaaleaalaaalQNIVVEDDEVAAAAIEYLKAAKAGRATflpldkiraraalaaalargaigaav 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 285 NCITQLNRLECELESEDADKGGNESDELANGEMGGDRSKKIKDRIKQM---MDVSRTQTAVSIVEEDLKLLQLKLRASMS 361
Cdd:COG1196 602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVtleGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 362 TKcnLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQDREQKLTAADEKVVLAA 441
Cdd:COG1196 682 EE--LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP 759
|
410
....*....|....*....
gi 2168985272 442 EEVKTYKRRIEEMEEELQK 460
Cdd:COG1196 760 PDLEELERELERLEREIEA 778
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
90-509 |
1.29e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 90 TEKQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNlilsdeaiKYKDKIKVLEETNVSLGDKAKSLRLQLE 169
Cdd:TIGR00618 227 ELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIE--------ELRAQEAVLEETQERINRARKAAPLAAH 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 170 SER-EQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQIEEW 248
Cdd:TIGR00618 299 IKAvTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLT 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 249 SR--------SHAELTEQIRSFETSQKDLEVALTH---------KDDNISALTNCITQLNRLE-CELESEdadkggNESD 310
Cdd:TIGR00618 379 QHihtlqqqkTTLTQKLQSLCKELDILQREQATIDtrtsafrdlQGQLAHAKKQQELQQRYAElCAAAIT------CTAQ 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 311 ELANGEMGGDRS-KKIKDRIKQMMDV-------SRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQt 382
Cdd:TIGR00618 453 CEKLEKIHLQESaQSLKEREQQLQTKeqihlqeTRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQ- 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 383 akaGLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQDrEQKLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTE 462
Cdd:TIGR00618 532 ---RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS-FSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE 607
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2168985272 463 RSFKNQIAAHEKKAHDNWLKARAAERAMAEEKREAANLRHK---LLEMTQ 509
Cdd:TIGR00618 608 DMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALhalQLTLTQ 657
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
85-470 |
1.98e-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: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 85 RIYQVTEKQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNLILSDEAIKYKDKIKVLEETNV-------SL 157
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEeleeqleTL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 158 GDKAKSLRLQLESEREQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSE-----ENVKSECHRVQEENA 232
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEleeelEELQEELERLEEALE 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 233 RLKKKKEQLQQQIEEWSRSHAELTEQIRSFETSQKDLE------VALTHKDDNISALTNCITQLNRLECELESE-DADKG 305
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEgfsegvKALLKNQSGLSGILGVLSELISVDEGYEAAiEAALG 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 306 GN------ESDELANGEMGGDRSKK-----------IKDRIKQ--MMDVSRTQTAVSIVEEDLKLLQLKLRASMStkcNL 366
Cdd:TIGR02168 545 GRlqavvvENLNAAKKAIAFLKQNElgrvtflpldsIKGTEIQgnDREILKNIEGFLGVAKDLVKFDPKLRKALS---YL 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 367 EDQIKKLEDDRSSLQTAKA---------------------------------GLEDECKTLRQKVEILNELYQQKEMALQ 413
Cdd:TIGR02168 622 LGGVLVVDDLDNALELAKKlrpgyrivtldgdlvrpggvitggsaktnssilERRREIEELEEKIEELEEKIAELEKALA 701
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 414 ---KKLSQEEYERQDREQKLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTERSFKNQIA 470
Cdd:TIGR02168 702 elrKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
90-463 |
2.05e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.73 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 90 TEKQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNLILSDEAIKYKDKIKVLEETNVSLgdKAKSLRLQlE 169
Cdd:pfam05557 98 QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSL--AEAEQRIK-E 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 170 SEREQNVKNQD-LILENKKS-------IEKLKDVI-SMNA--------SELSEVQVALNEAKLS-EENVKSECHRVQEEN 231
Cdd:pfam05557 175 LEFEIQSQEQDsEIVKNSKSelaripeLEKELERLrEHNKhlnenienKLLLKEEVEDLKRKLErEEKYREEAATLELEK 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 232 ARLKKkkeqlqqQIEEWSRSHAELTEQIRSFETSQKDLEV----ALTHKDDNiSALTNCITQLNRLECELESEDADKGGN 307
Cdd:pfam05557 255 EKLEQ-------ELQSWVKLAQDTGLNLRSPEDLSRRIEQlqqrEIVLKEEN-SSLTSSARQLEKARRELEQELAQYLKK 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 308 ESDElangEMGGDRSKKIKDRIkqmmdvsrtQTAVSIVEEDLKLLqlklrasmstKCNLEDQIKKLEDDRSSLQTAK--- 384
Cdd:pfam05557 327 IEDL----NKKLKRHKALVRRL---------QRRVLLLTKERDGY----------RAILESYDKELTMSNYSPQLLErie 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 385 --AGLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQDREQKLTAADekVVLAAEEVKTYKRRIEEMEEELQKTE 462
Cdd:pfam05557 384 eaEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLAD--PSYSKEEVDSLRRKLETLELERQRLR 461
|
.
gi 2168985272 463 R 463
Cdd:pfam05557 462 E 462
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
514-780 |
2.52e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.93 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 514 RQDEPVIVKPMPGRPNTQNPPRRGLLSQNGSFGPSPV----------SGGECSPPLPVESPGRPLSATLS-RRDTPRS-- 580
Cdd:PHA03247 2610 GPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVppperprddpAPGRVSRPRRARRLGRAAQASSPpQRPRRRAar 2689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 581 ----EFGSLDRHLPRPRWPseasgkhsasDPGPPPVVNSSSRSSSPAKAMDEGKVNMAPKGPPPFPGVPLM-GGPVPPPI 655
Cdd:PHA03247 2690 ptvgSLTSLADPPPPPPTP----------EPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATpGGPARPAR 2759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 656 RYGPPPQLCGPFGPRPLPPPFVPGMRPPLGVREYAPGVLPGKRDlPVDPREFVPGHTPFRPPGSLgpreffiPGTRLPPP 735
Cdd:PHA03247 2760 PPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWD-PADPPAAVLAPAAALPPAAS-------PAGPLPPP 2831
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2168985272 736 -SHGPQDYPPPPPALRDSLPSGprEEAQPASPSSVQDRSQASKPTP 780
Cdd:PHA03247 2832 tSAQPTAPPPPPGPPPPSLPLG--GSVAPGGDVRRRPPSRSPAAKP 2875
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
194-434 |
3.60e-04 |
|
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: 43.60 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 194 DVISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQIEEWSRSHAELTEQIRSFETSQKDLEVAL 273
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 274 THKDDNISALTNCITQLNR---LECELESEDAdkggneSDELANGEMGGDRSKKIKDRIKQMMdvsRTQTAVSIVEEDLK 350
Cdd:COG4942 100 EAQKEELAELLRALYRLGRqppLALLLSPEDF------LDAVRRLQYLKYLAPARREQAEELR---ADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 351 LLQLKLRASMStkcNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILnelyQQKEMALQKKLSQEEYERQDREQKL 430
Cdd:COG4942 171 AERAELEALLA---ELEEERAALEALKAERQKLLARLEKELAELAAELAEL----QQEAEELEALIARLEAEAAAAAERT 243
|
....
gi 2168985272 431 TAAD 434
Cdd:COG4942 244 PAAG 247
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
289-467 |
3.71e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 289 QLNRLECELESEDadkggnesDELANGEMGGDRSKKIKDRIKQMMDVSR-TQTAVSIVEEDLKLLQLKLRASMSTKCNLE 367
Cdd:PRK02224 207 RLNGLESELAELD--------EEIERYEEQREQARETRDEADEVLEEHEeRREELETLEAEIEDLRETIAETEREREELA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 368 DQIKKLEDDRSSLQTAKAGLEDEC--------------KTLRQKVEILNELYQQKEMALQKKLSQEEYERQDREQKLTAA 433
Cdd:PRK02224 279 EEVRDLRERLEELEEERDDLLAEAglddadaeavearrEELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA 358
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2168985272 434 DEK----------VVLAAEEVKTYKRRIEEMEEELQKTERSFKN 467
Cdd:PRK02224 359 EELreeaaeleseLEEAREAVEDRREEIEELEEEIEELRERFGD 402
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
365-473 |
4.21e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 365 NLEDQIKKLEDDRSSLQTAKAgledECKTLRQKVEILNELYQQKEMALQKKLsQEEYERQDREqkltaadekvvlAAEEV 444
Cdd:PRK00409 517 KLNELIASLEELERELEQKAE----EAEALLKEAEKLKEELEEKKEKLQEEE-DKLLEEAEKE------------AQQAI 579
|
90 100
....*....|....*....|....*....
gi 2168985272 445 KTYKRRIEEMEEELQKTERSFKNQIAAHE 473
Cdd:PRK00409 580 KEAKKEADEIIKELRQLQKGGYASVKAHE 608
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
78-476 |
4.62e-04 |
|
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: 43.89 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 78 TILVVKSRIYQVTEKQISEKLENIKKENAELMQK----------LSSYEQKIKESKKYV----------QETKKQNLILS 137
Cdd:TIGR01612 737 IIVEIKKHIHGEINKDLNKILEDFKNKEKELSNKindyakekdeLNKYKSKISEIKNHYndqinidnikDEDAKQNYDKS 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 138 DEAIKykdKIKVLEETNVSLGDKAKSLRLQLESEREQNVKNQDLILENKKS--------IEKLKDVISmnASELSEVQVA 209
Cdd:TIGR01612 817 KEYIK---TISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEKIDSeheqfaelTNKIKAEIS--DDKLNDYEKK 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 210 LNEAK-LSEENVKSECHRVQEENArlkkkkeqlQQQIEEWSRSHAELTEQIRSFETSQKDLEVALTHKDDNI-------- 280
Cdd:TIGR01612 892 FNDSKsLINEINKSIEEEYQNINT---------LKKVDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIkesnliek 962
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 281 -------SALTNCITQLNRLECELESEDADKGGNESDELANgEMGGDRSKKIKDRIKQMMDvsRTQTAVSIVEEdlkllq 353
Cdd:TIGR01612 963 sykdkfdNTLIDKINELDKAFKDASLNDYEAKNNELIKYFN-DLKANLGKNKENMLYHQFD--EKEKATNDIEQ------ 1033
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 354 lklrasmstkcNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQK-VEILN-ELYQQKEMA------LQKKLSQEEYERQD 425
Cdd:TIGR01612 1034 -----------KIEDANKNIPNIEIAIHTSIYNIIDEIEKEIGKnIELLNkEILEEAEINitnfneIKEKLKHYNFDDFG 1102
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2168985272 426 REQKLTAADEkVVLAAEEVKTYKRRIE----EMEEELQKTER---SFKNQIAAHEKKA 476
Cdd:TIGR01612 1103 KEENIKYADE-INKIKDDIKNLDQKIDhhikALEEIKKKSENyidEIKAQINDLEDVA 1159
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
93-214 |
4.62e-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: 42.60 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 93 QISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNLILSDEAIKYKDKIKVLEE--TNVSLGDKAKSLRLQLES 170
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlGNVRNNKEYEALQKEIES 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2168985272 171 EREQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAK 214
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK 144
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
522-767 |
4.74e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.16 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 522 KPMPGRPNTQNPPrrGLLSQNGSF-------GPSPVSGGECSPPLPVESPGRPLSATLSRRDTPRSEFGSLDRHLPRPRW 594
Cdd:PHA03247 2711 APHALVSATPLPP--GPAAARQASpalpaapAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAV 2788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 595 PSEASGKHSA---SDPGPPPVVNSSSRSSSPAKAMDEG-------KVNMAPKGPPPFPGVPL-MGGPVPPPIRygpppqL 663
Cdd:PHA03247 2789 ASLSESRESLpspWDPADPPAAVLAPAAALPPAASPAGplppptsAQPTAPPPPPGPPPPSLpLGGSVAPGGD------V 2862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 664 CGPFGPRPLPPPFVPGMRPPLGvREYAPGVLPGKRDLPVDPREFVPGHTPFRPPGSLGPREFFIPGTRLPPPSHGPQDYP 743
Cdd:PHA03247 2863 RRRPPSRSPAAKPAAPARPPVR-RLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQP 2941
|
250 260
....*....|....*....|....
gi 2168985272 744 PpppaLRDSLPSGPREEAQPASPS 767
Cdd:PHA03247 2942 P----LAPTTDPAGAGEPSGAVPQ 2961
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
283-510 |
5.17e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 283 LTNCITQLNRLECELESEDADKGGNESDELANGEMGGDRSKKIKDRIKQMMDVSRTQTAVSIVEEDLKLLQLKLRASMST 362
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 363 KCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNEL----------------YQQKEMALQKKLSQEEYERQDR 426
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELkekaeeyiklsefyeeYLDELREIEKRLSRLEEEINGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 427 EQKLTAADEKVvlaaEEVKTYKRRIEEMEEELQKTERSFKNQIAAHEKKAHDNWLKARAAERAMAEEKREAANLRHKLLE 506
Cdd:PRK03918 327 EERIKELEEKE----ERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE 402
|
....
gi 2168985272 507 MTQK 510
Cdd:PRK03918 403 IEEE 406
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
93-403 |
5.75e-04 |
|
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: 43.50 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 93 QISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNLILSDEAIK--YKDKIKVLE---ETNVSLGDKAKSLRLQ 167
Cdd:TIGR01612 1112 EINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKaiSNDDPEEIEkkiENIVTKIDKKKNIYDE 1191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 168 LESEREQNVKnqdlILENKKSIEKLKDVismNASELSEVQVALNEaKLSEENVKSEcHRVQ--EENARLKKKKEQLQQQI 245
Cdd:TIGR01612 1192 IKKLLNEIAE----IEKDKTSLEEVKGI---NLSYGKNLGKLFLE-KIDEEKKKSE-HMIKamEAYIEDLDEIKEKSPEI 1262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 246 EEWSRSHAELTEQIRSFETSQ---KDLEVALTHKDDNISALTN---CITQ-------LNRLECELESEDADKGGNESD-- 310
Cdd:TIGR01612 1263 ENEMGIEMDIKAEMETFNISHdddKDHHIISKKHDENISDIREkslKIIEdfseesdINDIKKELQKNLLDAQKHNSDin 1342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 311 ----ELAN--GEMGGDRSKKIKDRIKQMMDVsrtqtavsiVEEDLKLLQLKLRASmstkcnlEDQIKKLEDDrSSLQTAK 384
Cdd:TIGR01612 1343 lylnEIANiyNILKLNKIKKIIDEVKEYTKE---------IEENNKNIKDELDKS-------EKLIKKIKDD-INLEECK 1405
|
330 340
....*....|....*....|....*....
gi 2168985272 385 AGLE--------DEC--KTLRQKVEILNE 403
Cdd:TIGR01612 1406 SKIEstlddkdiDECikKIKELKNHILSE 1434
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
334-522 |
1.01e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 334 DVSRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNELYQQkemaLQ 413
Cdd:COG4372 46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE----LQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 414 KKLSQEEYERQDREQKLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTERSFKNQIAAHEKKAHDNWLKARAAERAMAEE 493
Cdd:COG4372 122 KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEE 201
|
170 180
....*....|....*....|....*....
gi 2168985272 494 KREAANLRHKLLEMTQKMAMRQDEPVIVK 522
Cdd:COG4372 202 LAEAEKLIESLPRELAEELLEAKDSLEAK 230
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
98-464 |
1.17e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.51 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 98 LENIKKENAELmqKLSSYEQKIKESKKYVQETKKQ--NLILSDEAIKYKDKIKVLEETNVSLGDKAKSLRLQLESEREQN 175
Cdd:PTZ00440 839 LQKFPTEDENL--NLKELEKEFNENNQIVDNIIKDieNMNKNINIIKTLNIAINRSNSNKQLVEHLLNNKIDLKNKLEQH 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 176 VK----------NQDLILEN-----KKSIEKLKDVISMNASELsEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQ 240
Cdd:PTZ00440 917 MKiintdniiqkNEKLNLLNnlnkeKEKIEKQLSDTKINNLKM-QIEKTLEYYDKSKENINGNDGTHLEKLDKEKDEWEH 995
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 241 LQQQIEEWSRSHAELTEQIRSFETSQKDLEVAL-----THKDDNISALT-NCITQLNRLECELESEDAdkggnesdelaN 314
Cdd:PTZ00440 996 FKSEIDKLNVNYNILNKKIDDLIKKQHDDIIELidkliKEKGKEIEEKVdQYISLLEKMKTKLSSFHF-----------N 1064
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 315 GEMGGDRSKKIKDRIK----QMMDVSRtqtavSIVEEDLKLLQLKLRAS---MSTKCNLEDQIKKLEDDRSSLQTAKAGL 387
Cdd:PTZ00440 1065 IDIKKYKNPKIKEEIKlleeKVEALLK-----KIDENKNKLIEIKNKSHehvVNADKEKNKQTEHYNKKKKSLEKIYKQM 1139
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 388 EDECKTLRQKVEILNELYQQKEMALQkklsqeeYER---QDREQKLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTERS 464
Cdd:PTZ00440 1140 EKTLKELENMNLEDITLNEVNEIEIE-------YERiliDHIVEQINNEAKKSKTIMEEIESYKKDIDQVKKNMSKERND 1212
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
98-474 |
1.60e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 98 LENIKKENAELMQKLSSYEQKIKESKKYVQeTKKQNLILSDEAIKykdKIKVLEETNVSLGDKAKSLRLQLESEREQNVK 177
Cdd:PRK01156 199 LENIKKQIADDEKSHSITLKEIERLSIEYN-NAMDDYNNLKSALN---ELSSLEDMKNRYESEIKTAESDLSMELEKNNY 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 178 NQDlILENKKSIEKLKDVISMN-ASELSEVQVALNEAKLSEENVKSECHRVqEENARLKKKKEQLQQQIEEWSRSHAELT 256
Cdd:PRK01156 275 YKE-LEERHMKIINDPVYKNRNyINDYFKYKNDIENKKQILSNIDAEINKY-HAIIKKLSVLQKDYNDYIKKKSRYDDLN 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 257 EQIRSFETSQkdlevalthkdDNISALTNCITQLNRLECELESEDADKGGNESDELANGEMGGDRSKKIKDRIKQMMDVs 336
Cdd:PRK01156 353 NQILELEGYE-----------MDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQD- 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 337 rtqtavsiVEEDLKLLQLKLRASMSTKCNLEDQIKKLEdDRSSLQTAKAGLEDEcktlrqKVEILNELYQQKEMALQKKL 416
Cdd:PRK01156 421 --------ISSKVSSLNQRIRALRENLDELSRNMEMLN-GQSVCPVCGTTLGEE------KSNHIINHYNEKKSRLEEKI 485
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2168985272 417 SQEEYERQD-REQKLTAADEKVVLAAEEVK---TYKRRIEEMEEELQKTERSFKNQIAAHEK 474
Cdd:PRK01156 486 REIEIEVKDiDEKIVDLKKRKEYLESEEINksiNEYNKIESARADLEDIKIKINELKDKHDK 547
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
92-441 |
1.80e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.42 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 92 KQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNLILSDEAIKYKDKIKVLEETNVSLGDKAKSLRLQLESE 171
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 172 REQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSEENVKSECHRVQEENARLKKKKEQLQQQIEEWSRS 251
Cdd:pfam07888 156 KERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 252 HAELTEQIRSFETSQK-------DLEVALTHKDDNISAL-------TNCITQLNRLECELESEDADKGGNESDELANGEM 317
Cdd:pfam07888 236 LEELRSLQERLNASERkveglgeELSSMAAQRDRTQAELhqarlqaAQLTLQLADASLALREGRARWAQERETLQQSAEA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 318 GGDRSKKIKDRIKQMMDvsrtqtavSIVEEDLKLLQLKLRASMSTKCNLedqiKKLEDDRSSLQTAKAGLEdecktLRQK 397
Cdd:pfam07888 316 DKDRIEKLSAELQRLEE--------RLQEERMEREKLEVELGREKDCNR----VQLSESRRELQELKASLR-----VAQK 378
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2168985272 398 veilnelyqQKEMALQKKLSQEEYERQdREQKL-TAADEKVVLAA 441
Cdd:pfam07888 379 ---------EKEQLQAEKQELLEYIRQ-LEQRLeTVADAKWSEAA 413
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
98-478 |
1.96e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.60 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 98 LENIKKENAELMQKLSSYEQKIKESKKYVQETKKQN---LILSDEAIKYKDKIKVLEETNvslgDKAKSLRLQLESEREQ 174
Cdd:pfam05622 68 LEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNeelTSLAEEAQALKDEMDILRESS----DKVKKLEATVETYKKK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 175 -----NVKNQDLILENKKSI---------EKLKDVISMNAS-ELSEVQVALNEAKLSEENVKS-----ECHRVQEENArl 234
Cdd:pfam05622 144 ledlgDLRRQVKLLEERNAEymqrtlqleEELKKANALRGQlETYKRQVQELHGKLSEESKKAdklefEYKKLEEKLE-- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 235 kKKKEQLQQQIEEwSRSHAELTEQIRSFETSQKDLEVALTHKDDNISALTNCITQ---------LNRLECELESEDADKG 305
Cdd:pfam05622 222 -ALQKEKERLIIE-RDTLRETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEimpaeirekLIRLQHENKMLRLGQE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 306 GNESDELANGEMGGDRSKKIKDRIKQMMDVSRTQTAV--SIVEEDLKLLQL---KLRASMSTKCNLEDQIKKLEDDRSSL 380
Cdd:pfam05622 300 GSYRERLTELQQLLEDANRRKNELETQNRLANQRILElqQQVEELQKALQEqgsKAEDSSLLKQKLEEHLEKLHEAQSEL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 381 QTAKAGLEDECKTLRQKVeilnelyQQKEMALQKKLSQEEYERQDREQKLTAADEKvvlAAEEVKTYKRRIEEMEE-ELQ 459
Cdd:pfam05622 380 QKKKEQIEELEPKQDSNL-------AQKIDELQEALRKKDEDMKAMEERYKKYVEK---AKSVIKTLDPKQNPASPpEIQ 449
|
410
....*....|....*....
gi 2168985272 460 kterSFKNQIAAHEKKAHD 478
Cdd:pfam05622 450 ----ALKNQLLEKDKKIEH 464
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
85-367 |
2.22e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 85 RIYQVTEKQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNlilSDEAIKYKDKIkvleetnVSLGDKAKSL 164
Cdd:PHA02562 163 SVLSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKN---GENIARKQNKY-------DELVEEAKTI 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 165 RLQLESEREQnVKNQDLILEN-KKSIEKLKDVISMNASELSEVQvalNEAKLSEENvkSEC----HRVQEENARlkkkke 239
Cdd:PHA02562 233 KAEIEELTDE-LLNLVMDIEDpSAALNKLNTAAAKIKSKIEQFQ---KVIKMYEKG--GVCptctQQISEGPDR------ 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 240 qlqqqIEEWSRSHAELTEQIRSFETSQKDLEValthKDDNISALTNCITQLNRlecELESEDADkggnesdeLANGEmgg 319
Cdd:PHA02562 301 -----ITKIKDKLKELQHSLEKLDTAIDELEE----IMDEFNEQSKKLLELKN---KISTNKQS--------LITLV--- 357
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2168985272 320 DRSKKIKDRIKQMmdvsrtQTAVSIVEEDLKLLQLKLRASMSTKCNLE 367
Cdd:PHA02562 358 DKAKKVKAAIEEL------QAEFVDNAEELAKLQDELDKIVKTKSELV 399
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
173-424 |
3.47e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 173 EQNVKNQDLILENKKSIeklkDVISMNASELSEvQVALNEAKLSEENVKSEchrvqEENARLKKKKEQLQQQIEEWSRSH 252
Cdd:PHA02562 167 EMDKLNKDKIRELNQQI----QTLDMKIDHIQQ-QIKTYNKNIEEQRKKNG-----ENIARKQNKYDELVEEAKTIKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 253 AELTEQIRSFETSQKDLEVALTHKDDNISALTNCITQLNRL--------EC-----ELESEDaDKGGNESDELANGEMGG 319
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVikmyekggVCptctqQISEGP-DRITKIKDKLKELQHSL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 320 DRSKKIKDRIKQMMDVSRTQTAVsiveedLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQ-KV 398
Cdd:PHA02562 316 EKLDTAIDELEEIMDEFNEQSKK------LLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDeLD 389
|
250 260
....*....|....*....|....*.
gi 2168985272 399 EILNELyqqkemalqKKLSQEEYERQ 424
Cdd:PHA02562 390 KIVKTK---------SELVKEKYHRG 406
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
269-441 |
3.48e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 40.81 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 269 LEVALTHKDDNISALTNCITQLNRLECELESEDADKGGNESDELANGEMGGDRSKKIKDRIKQMMDVSRTQTAVSIVEED 348
Cdd:pfam05911 642 SENKVAQVDNGCSEIDNLSSDPEIPSDGPLVSGSNDLKTEENKRLKEEFEQLKSEKENLEVELASCTENLESTKSQLQES 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 349 LKL---LQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILN------------------ELYQQ 407
Cdd:pfam05911 722 EQLiaeLRSELASLKESNSLAETQLKCMAESYEDLETRLTELEAELNELRQKFEALEveleeekncheeleakclELQEQ 801
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2168985272 408 KEMALQKKLS-----QEEYE-RQDREqkLTAADEKvvLAA 441
Cdd:pfam05911 802 LERNEKKESSncdadQEDKKlQQEKE--ITAASEK--LAE 837
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
367-468 |
3.56e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 367 EDQIKKLEDDRSSLQTAKAGLEDECKTLRQKVEILNELYQQKEmalqkklsqeeyerqdreQKLTAADEKVVLAAEEVKT 446
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQ------------------AELEALQAEIDKLQAEIAE 76
|
90 100
....*....|....*....|..
gi 2168985272 447 YKRRIEEMEEELQKTERSFKNQ 468
Cdd:COG3883 77 AEAEIEERREELGERARALYRS 98
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
381-469 |
4.18e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 38.33 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 381 QTAKAGLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQDREQKLtaadekvvlaAEEVKTYKRRIEEMEEELQK 460
Cdd:pfam03938 18 KAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQEL----------QKKEQELQQLQQKAQQELQK 87
|
....*....
gi 2168985272 461 TERSFKNQI 469
Cdd:pfam03938 88 KQQELLQPI 96
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
92-230 |
4.67e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 92 KQISEKLENIKkenaELMQKLSS----YEQKIKESKKYVQETKKQNLILSDEAIKYKDKIkvleetnvslgdkaKSLRLQ 167
Cdd:PRK00409 509 KLIGEDKEKLN----ELIASLEElereLEQKAEEAEALLKEAEKLKEELEEKKEKLQEEE--------------DKLLEE 570
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2168985272 168 LESEREQNVKN----QDLILENKKSIEKLKDViSMNASELSEVQVALNEAKLSEENVKSECHRVQEE 230
Cdd:PRK00409 571 AEKEAQQAIKEakkeADEIIKELRQLQKGGYA-SVKAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
508-612 |
4.78e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 40.69 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 508 TQKMAMRQDEPVIVKPMPGRPNTQNPPRRGLLSQNGSFGPSPVSGGECSPPLPVESPGRPLSATLSRRDTPRSEFGSLdR 587
Cdd:PHA03247 2919 PQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPL-T 2997
|
90 100
....*....|....*....|....*
gi 2168985272 588 HLPRPRWPSEASGKHSASDPGPPPV 612
Cdd:PHA03247 2998 GHSLSRVSSWASSLALHEETDPPPV 3022
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
97-464 |
5.09e-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: 40.44 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 97 KLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNLILSDEAIKY-------KDKIKVLEETNVSLGDKAKSLRLQLE 169
Cdd:TIGR02169 372 ELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLseeladlNAAIAGIEAKINELEEEKEDKALEIK 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 170 sEREQNVKnqdlilENKKSIEKLKDVISMNASELSEVQvalneaklseenvkSECHRVQEENARLKKKKEQLQQQIEEWS 249
Cdd:TIGR02169 452 -KQEWKLE------QLAADLSKYEQELYDLKEEYDRVE--------------KELSKLQRELAEAEAQARASEERVRGGR 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 250 RS-----------HAELTEQIRSFETSQKDLEVAL----------------------------------------THKDD 278
Cdd:TIGR02169 511 AVeevlkasiqgvHGTVAQLGSVGERYATAIEVAAgnrlnnvvveddavakeaiellkrrkagratflplnkmrdERRDL 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 279 NISALTNCIT-QLNRLECELESEDA------DKGGNESDELANGEMGGDRSKKIKDRIkqmMDVSRTQTAVSIVEEDLKL 351
Cdd:TIGR02169 591 SILSEDGVIGfAVDLVEFDPKYEPAfkyvfgDTLVVEDIEAARRLMGKYRMVTLEGEL---FEKSGAMTGGSRAPRGGIL 667
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 352 LQLKLRASMStkcNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQKV--------EILNELYQ--QKEMALQKKLSQEEY 421
Cdd:TIGR02169 668 FSRSEPAELQ---RLRERLEGLKRELSSLQSELRRIENRLDELSQELsdasrkigEIEKEIEQleQEEEKLKERLEELEE 744
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2168985272 422 ERQDREQKLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTERS 464
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR 787
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
92-375 |
6.28e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 92 KQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNLILSDEAIKYKDKIKVLEETNVSLGDKAKSLRLQLESE 171
Cdd:COG4372 55 EQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 172 REQNVKNQDLILENKKSIEKLKDVISMNASELSEVQVALNEAKLSE-ENVKSECHRVQEENARLKKKKEQLQQQIEEWSR 250
Cdd:COG4372 135 EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 251 SHAELTEQIRSFETSQKDLEVALTHKDDNISALTNCITQLNRLECELESEDAD--KGGNESDELANGEMGGDRSKKIKDR 328
Cdd:COG4372 215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIlvEKDTEEEELEIAALELEALEEAALE 294
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2168985272 329 IKQMMDVSRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLED 375
Cdd:COG4372 295 LKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELAD 341
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
96-218 |
6.87e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 39.85 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 96 EKLENIKKENAELMQKLSSYEQKIKESKKYVQEtKKQNLILSDEAIKYKDKikVLEETNVSLGDKAKSLrlqleSEREQN 175
Cdd:PRK00106 76 EAKEEARKYREEIEQEFKSERQELKQIESRLTE-RATSLDRKDENLSSKEK--TLESKEQSLTDKSKHI-----DEREEQ 147
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2168985272 176 VKNqdliLENKKSIEkLKDVISMNASELSEVQVALNEAKLSEE 218
Cdd:PRK00106 148 VEK----LEEQKKAE-LERVAALSQAEAREIILAETENKLTHE 185
|
|
| cc_LAMB4_C |
cd22301 |
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called ... |
92-147 |
7.07e-03 |
|
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called laminin beta-1-related protein, is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Mutations or loss of LAMB4 may be features of gastric and colorectal cancers. Reduced LAMB4 levels may contribute to colonic dysmotility associated with diverticulitis. This model corresponds to the C-terminal coiled-coil domain of LAMB4, which may be involved in the integrin binding activity.
Pssm-ID: 411972 [Multi-domain] Cd Length: 70 Bit Score: 35.79 E-value: 7.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2168985272 92 KQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQNLILSDEAIKYKDKI 147
Cdd:cd22301 5 KNIKKEAENLAKEIEDKMKRIEDLEKRIQDLNKRKEDKANQLARLEKQVISLRKEI 60
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
401-475 |
7.10e-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: 39.36 E-value: 7.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2168985272 401 LNELyQQKEMALQKKLSQEEYERQDREQKLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTERsfknQIAAHEKK 475
Cdd:COG4942 29 LEQL-QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK----EIAELRAE 98
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
321-478 |
7.12e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 321 RSKKIKDRIKQMmdvsrTQTAVSIVEE---------DLKLLQLKlrasmstkcnleDQIKKLeddrsslqtaKAGLEDEC 391
Cdd:PRK12704 25 RKKIAEAKIKEA-----EEEAKRILEEakkeaeaikKEALLEAK------------EEIHKL----------RNEFEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 392 KTLRQKVEILNELYQQKEMALQKK---LSQEEYERQDREQKLTAADEKVVLAAEEVKT-YKRRIEEME-------EE--- 457
Cdd:PRK12704 78 RERRNELQKLEKRLLQKEENLDRKlelLEKREEELEKKEKELEQKQQELEKKEEELEElIEEQLQELErisgltaEEake 157
|
170 180
....*....|....*....|...
gi 2168985272 458 --LQKTERSFKNQIAAHEKKAHD 478
Cdd:PRK12704 158 ilLEKVEEEARHEAAVLIKEIEE 180
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
511-779 |
7.63e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 40.05 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 511 MAMRQDEPVIVKPMPGRPNTQNPP------RRGLLSQNGSFGPSPVSGGECSPPLPVESPGRPLSATLSRRDTPRSEFGs 584
Cdd:PHA03378 684 MLPIQWAPGTMQPPPRAPTPMRPPaappgrAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPG- 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 585 ldrhlpRPRWPSEASGkhsASDPGPPPVVnsssrsssPAKAMDEGKVNMAPKGPPPFPGVPLMGGPVPPPIRYGPPPQLC 664
Cdd:PHA03378 763 ------RARPPAAAPG---APTPQPPPQA--------PPAPQQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQIL 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 665 GPFGPRPLPPPFVPGMRPPLGVREYAPGVLP----GKRDLPVD-PREFVPGHTPFRPPGSLG-------------PREFf 726
Cdd:PHA03378 826 RQLLTGGVKRGRPSLKKPAALERQAAAGPTPspgsGTSDKIVQaPVFYPPVLQPIQVMRQLGsvraaaastvtqaPTEY- 904
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2168985272 727 iPGTRLPPPSHGPQDYPPPPPALRDSLPSG--PREEAQPASPSSVQDRSQASKPT 779
Cdd:PHA03378 905 -TGERRGVGPMHPTDIPPSKRAKTDAYVESqpPHGGQSHSFSVIWENVSQGQQQT 958
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
70-475 |
7.75e-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: 39.56 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 70 SFAIFSWRTILVVKSRIYQVTEKQISEKLENIKKENAELMQKLSSYEQKIKESKKYVQETKKQ--NLILSDEAIKYKDKI 147
Cdd:COG5185 149 IEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESEtgNLGSESTLLEKAKEI 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 148 KVLEETNVSLGDKAKSLRL--QLESEREQNV-KNQDLIL----ENKKSIEKLKDVISMNASELSEVQVALNEaklSEENV 220
Cdd:COG5185 229 INIEEALKGFQDPESELEDlaQTSDKLEKLVeQNTDLRLeklgENAESSKRLNENANNLIKQFENTKEKIAE---YTKSI 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 221 KSECHRVQEENarlKKKKEQLQQQIEEWSR-SHAELTEQIRSFETSQKDLEVALTHKDDNISALTNcITQLNRLECELES 299
Cdd:COG5185 306 DIKKATESLEE---QLAAAEAEQELEESKReTETGIQNLTAEIEQGQESLTENLEAIKEEIENIVG-EVELSKSSEELDS 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 300 EDADKggnESDELANGEMGGDRSKKIKDRIKQMMDvsrtqtAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLED---- 375
Cdd:COG5185 382 FKDTI---ESTKESLDEIPQNQRGYAQEILATLED------TLKAADRQIEELQRQIEQATSSNEEVSKLLNELISelnk 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 376 -DRSSLQTAKAGLEDECK----TLRQKVEILNELYQQKEMALQKKLSQEEYERQDREQKLTAADEKVVLAAEEVKTYKRR 450
Cdd:COG5185 453 vMREADEESQSRLEEAYDeinrSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRA 532
|
410 420
....*....|....*....|....*
gi 2168985272 451 IEEMEEELQKTERSFKNQIAAHEKK 475
Cdd:COG5185 533 RGYAHILALENLIPASELIQASNAK 557
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
241-463 |
8.31e-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: 39.36 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 241 LQQQIeewsrshAELTEQIRSFETSQKDLEVALTHKDDNISALTNcitQLNRLECELESEDADKGGNESDELANGEMGGD 320
Cdd:COG4942 32 LQQEI-------AELEKELAALKKEEKALLKQLAALERRIAALAR---RIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 321 RSKKIKDRIKQMMDVSRTQTAVSIVE-EDLKLLQLKLRASMSTKCNLEDQIKKLEDDRSSLQTAKAGLEDECKTLRQkve 399
Cdd:COG4942 102 QKEELAELLRALYRLGRQPPLALLLSpEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA--- 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2168985272 400 ILNELYQQKEmALQKKLSQEEYERQDREQKLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTER 463
Cdd:COG4942 179 LLAELEEERA-ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
322-463 |
8.96e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 8.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168985272 322 SKKIKDRIKQMMDVSRTQTAVSIVEEDLKLLQLKLRASMSTKCNLEDQIKKLED--DRSSLQTAKAGLEDECKTLRQKVE 399
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELEERLE 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2168985272 400 ILNELYQQKEMALQKKLSQEEYERQDREQKLTAADEKVVLAAEEVKTYKRRIEEMEEELQKTER 463
Cdd:COG4717 157 ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
|
| |
