|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
122-433 |
8.28e-135 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 392.36 E-value: 8.28e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 122 EEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKW-QFYQNQRCCESNLEPLFSGYIETLRREAECVEADSGRLASELNHV 200
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKIsELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 201 QEVLEGYKKKYEEEVALRATAENEFVVLKKDVDCAYLRKSDLEANVEALVEESSFLRRLYEEEIRVLQAHISDTSVIVKM 280
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 281 DNSRDLNMDCIVAEIKAQYDDVASRSRAEAESWYRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEIENAKCQR 360
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622845037 361 AKLEAAVAEAEQQGEAALSDARCKLAELEGALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEHR 433
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
17-119 |
1.19e-22 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 94.34 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 17 NFSSCSAVAP-----KTGNRCCISAAPYRGVSCYRGLTGFGSRSLCNLG---SCGPRIAVGGFRAGS---------CGRS 79
Cdd:pfam16208 1 GFSSCSAVVPsrsrrSYSSVSSSRRGGGGGGGGGGGGGGFGSRSLYNLGgskSISISVAGGGSRPGSgfgfgggggGGFG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622845037 80 FGYRSGGVCGP--------------------------------SPPC----ITTVSVNESLLTPLNLEIDPNAQCV 119
Cdd:pfam16208 81 GGFGGGGGGGFgggggfgggfggggyggggfggggfggrggfgGPPCppggIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
176-406 |
8.54e-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: 67.79 E-value: 8.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 176 IETLRREAECVEADSGRLASELNHVQEVLEGYKKKYEEEVALRATA--------ENEFVVLKKDVDCAYLRKSDLEANVE 247
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkikdlgEEEQLRVKEKIGELEAEIASLERSIA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 248 AL---VEESSFLRRLYEEEIRVLQAHISDTSVIVKMDNSRDLNMDCIVAEIKAQYDDVASRSRAEAESWYRSKCEEMKAT 324
Cdd:TIGR02169 312 EKereLEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 325 virhgETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQ---QGEAALSDARCKLAELEGALQKAKQDMAC 401
Cdd:TIGR02169 392 -----EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAkinELEEEKEDKALEIKKQEWKLEQLAADLSK 466
|
....*
gi 1622845037 402 LLKEY 406
Cdd:TIGR02169 467 YEQEL 471
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
140-434 |
9.44e-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: 55.06 E-value: 9.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 140 KVRFLEQQNKLLEtKWQFYQNQrccESNLEPLFSGY-IETLRREAECVEADSGRLASELNHVQEVLEGYKKKYEEEVALR 218
Cdd:TIGR02168 201 QLKSLERQAEKAE-RYKELKAE---LRELELALLVLrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 219 ATAENEFVVLKKDVDCAYLRKSDLEANVEALVEESSFLRRLYEEEIRVLQAHISdtsvivKMDNSRDlnmdcIVAEIKAQ 298
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES------KLDELAE-----ELAELEEK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 299 YDDVASR--SRAEAESWYRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGEA 376
Cdd:TIGR02168 346 LEELKEEleSLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE 425
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622845037 377 ALSDA-RCKLAELEGALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLL---EGEEHRL 434
Cdd:TIGR02168 426 LLKKLeEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALdaaERELAQL 487
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
121-425 |
2.84e-07 |
|
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: 53.52 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 121 QEEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKWQFYQNQ----RCCESNLEPLFSGY---IETLRREAECVEADSGRL 193
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEEleqlRKELEELSRQISALrkdLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 194 ASELNHVQEVLEGYKKKYEEEVALRATAENEFVVLKKDVDCAylrKSDLEANVEALVEESSFLRRLyeeEIRVLQAhisd 273
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL---KEELKALREALDELRAELTLL---NEEAANL---- 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 274 tsvivkmdnsrdlnmdcivaeikaqyddvasrsraeaeswyRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEI 353
Cdd:TIGR02168 823 -----------------------------------------RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622845037 354 ENAKCQRAKLEAAVAEAEQ---QGEAALSDARCKLAELEGALQKAKQDMACLLKEYQEVMN--SKLGLDIEIATYRR 425
Cdd:TIGR02168 862 EELEELIEELESELEALLNeraSLEEALALLRSELEELSEELRELESKRSELRRELEELREklAQLELRLEGLEVRI 938
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
121-445 |
3.09e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.12 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 121 QEEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKWQFYQN-QRCCESnLEPLFSG---YIETLRREAEcveaDSGRLASE 196
Cdd:pfam15921 506 QEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNvQTECEA-LKLQMAEkdkVIEILRQQIE----NMTQLVGQ 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 197 LNHVQEVLEGYKKKYEEEVALRATAENEFVVLKKDVDcAYLRksDLEANVEALVEESSFLRRLYEEEIRVLQAhisdtsv 276
Cdd:pfam15921 581 HGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKD-AKIR--ELEARVSDLELEKVKLVNAGSERLRAVKD------- 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 277 iVKMDNSRDLNmdcivaEIKAQYDDVASRSRaEAESW---YRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLtaei 353
Cdd:pfam15921 651 -IKQERDQLLN------EVKTSRNELNSLSE-DYEVLkrnFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSM---- 718
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 354 ENAKCQRAKLEAAVAEAEQQGEAALSDARCKLAELEGALQKAKQDMAcLLKEYQEVMNSKLGldiEIATYRRLLEGE--- 430
Cdd:pfam15921 719 EGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKH-FLKEEKNKLSQELS---TVATEKNKMAGElev 794
|
330
....*....|....*....
gi 1622845037 431 ----EHRLCEGVGSVNVCV 445
Cdd:pfam15921 795 lrsqERRLKEKVANMEVAL 813
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
186-409 |
1.15e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 186 VEADSGRLASELNHVQEVLEGYKKKYEE-EVALRA-TAENEFVVLKKDVDCAYLRKSDLEANVEALVEESSFLRRLYEEe 263
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEaEAALEEfRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 264 irvLQAHISDTSvivkmDNSRDLNMDCIVAEIKAQYDDVASRsRAEAESWYRSKCEEMKATVirhgETLRRTKEEIN-EL 342
Cdd:COG3206 245 ---LRAQLGSGP-----DALPELLQSPVIQQLRAQLAELEAE-LAELSARYTPNHPDVIALR----AQIAALRAQLQqEA 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622845037 343 NRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGeAALSDARCKLAELEGALQKAKQDMACLLKEYQEV 409
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQLAQLEARL-AELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
178-395 |
3.27e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.71 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 178 TLRREAECVEADSGRLASELNHVQEVLEGYKKKYEEEVALRATAENEFVVLKKDVDCAYLRKSDLEANVEALveessflr 257
Cdd:pfam01576 500 SLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL-------- 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 258 rlyEEEIRVLQAHISDtsVIVKMDNSRDL---------NMDCIVAE---IKAQYDDvaSRSRAEAESwyRSKceEMKA-T 324
Cdd:pfam01576 572 ---EKTKNRLQQELDD--LLVDLDHQRQLvsnlekkqkKFDQMLAEekaISARYAE--ERDRAEAEA--REK--ETRAlS 640
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622845037 325 VIRHGETLRRTKEEINELNRMiqrLTAEIE---NAKCQRAK----LEAAVAEAEQQgeaaLSDARCKLAELEGALQKA 395
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQ---LRAEMEdlvSSKDDVGKnvheLERSKRALEQQ----VEEMKTQLEELEDELQAT 711
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
178-429 |
4.70e-05 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 46.47 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 178 TLRREAeCVEADSGRLASELNHVQEVLEGYKKKYEEEVALRATAENEFVVLKKDVDCAYLRKSDLEANVEALVEESSFLR 257
Cdd:PLN03188 875 AIRREM-ALEEFCTKQASEITQLNRLVQQYKHERECNAIIGQTREDKIIRLESLMDGVLSKEDFLEEELASLMHEHKLLK 953
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 258 RLYEEEIRVLQAHISDTSVIVKMDNSRDL----NMDCIVAEI---KAQ---YDDVASRSRAEAESWYR--SKCEEMKATV 325
Cdd:PLN03188 954 EKYENHPEVLRTKIELKRVQDELEHYRNFydmgEREVLLEEIqdlRSQlqyYIDSSLPSARKRNSLLKltYSCEPSQAPP 1033
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 326 IrhgETLRRTKEEINELNRMIQRL---TAE---IENAKCQRAKLEAAVAEAEQQGEAALSDARCKlAELEGALQKAKQDM 399
Cdd:PLN03188 1034 L---NTIPESTDESPEKKLEQERLrwtEAEskwISLAEELRTELDASRALAEKQKHELDTEKRCA-EELKEAMQMAMEGH 1109
|
250 260 270
....*....|....*....|....*....|
gi 1622845037 400 ACLLKEYQEVMNSKLGLdieIATYRRLLEG 429
Cdd:PLN03188 1110 ARMLEQYADLEEKHIQL---LARHRRIQEG 1136
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
320-410 |
6.53e-05 |
|
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: 45.27 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 320 EMKATVIRHGETLRRT----KEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGEAALSDARCKLAELEGALQKA 395
Cdd:pfam07888 297 EGRARWAQERETLQQSaeadKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVA 376
|
90
....*....|....*
gi 1622845037 396 KQDMACLLKEYQEVM 410
Cdd:pfam07888 377 QKEKEQLQAEKQELL 391
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
176-398 |
1.05e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 176 IETLRREAECVEADSGRLASELNHVQEVlegykKKYEEEVALRATAENEFVVLKKDVdcaylRKSDLEANVEAL--VEES 253
Cdd:PTZ00121 1166 AEEARKAEDAKKAEAARKAEEVRKAEEL-----RKAEDARKAEAARKAEEERKAEEA-----RKAEDAKKAEAVkkAEEA 1235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 254 sflrRLYEEEIRVLQaHISDTSVIVKMDNSRDLNMDCIVAEIKAQYDDVASRSRAEAEswyRSKCEEM-KATVIRHGETL 332
Cdd:PTZ00121 1236 ----KKDAEEAKKAE-EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE---KKKADEAkKAEEKKKADEA 1307
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622845037 333 RRTKEEinelNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGEAALSDARCKLAELEGALQKAKQD 398
Cdd:PTZ00121 1308 KKKAEE----AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
176-425 |
1.15e-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: 44.37 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 176 IETLRREAECVEADSGRLASELNHVQEVLEGYKKKYEEEVALRATAENEFVVLKKDVdcaylrkSDLEANVEALVEESSF 255
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-------AELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 256 LRRLYEEEIRVLQAH--ISDTSVIVKMDNSRDlnmdcivAEIKAQYDDVASRSRAEaeswyrskceemkatvirHGETLR 333
Cdd:COG4942 102 QKEELAELLRALYRLgrQPPLALLLSPEDFLD-------AVRRLQYLKYLAPARRE------------------QAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 334 RTKEEINELNrmiqrltAEIENAKCQRAKLEAAVAEAEQQGEAALSDARCKLAELEGALQKAKQDMACLLKEYQEVMNSK 413
Cdd:COG4942 157 ADLAELAALR-------AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
250
....*....|..
gi 1622845037 414 LGLDIEIATYRR 425
Cdd:COG4942 230 ARLEAEAAAAAE 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
207-434 |
2.10e-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: 44.28 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 207 YKKKYEE-EVALRATAENefvvLKKDVDCAylrkSDLEANVEALVEESSFLRRL--YEEEIRVLQAHISDTSVIVKMDNS 283
Cdd:TIGR02168 170 YKERRKEtERKLERTREN----LDRLEDIL----NELERQLKSLERQAEKAERYkeLKAELRELELALLVLRLEELREEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 284 RDLNMdcIVAEIKAQYDDVASRSRAEAESW--YRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEIENAKCQRA 361
Cdd:TIGR02168 242 EELQE--ELKEAEEELEELTAELQELEEKLeeLRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622845037 362 KLEAAVAEAEQQGE---AALSDARCKLAELEGALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEHRL 434
Cdd:TIGR02168 320 ELEAQLEELESKLDelaEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
292-396 |
2.17e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.71 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 292 VAEIKAQYDDVASRSRAEAESWYRSKCEEMKATVIRHGETLRRTKE-EINELNRM--IQRLTAEIEnakcQRAKLEAAVA 368
Cdd:COG2268 246 LAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREiELQEKEAEreEAELEADVR----KPAEAEKQAA 321
|
90 100
....*....|....*....|....*...
gi 1622845037 369 EAEQQGEAALSDARCKlAELEGALQKAK 396
Cdd:COG2268 322 EAEAEAEAEAIRAKGL-AEAEGKRALAE 348
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
293-400 |
2.65e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 293 AEIKAQYDDVASRSRAEAESwyrskceemKATVIRHGETLR------RTKEEINELNRMIQRLTAEIENAKCQRAKLEAA 366
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAED---------KLVQQDLEQTLAlldkidRQKEETEQLKQQLAQAPAKLRQAQAELEALKDD 109
|
90 100 110
....*....|....*....|....*....|....*.
gi 1622845037 367 VAEAEQQGEAALSDARC--KLAELEGALQKAKQDMA 400
Cdd:PRK11281 110 NDEETRETLSTLSLRQLesRLAQTLDQLQNAQNDLA 145
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
294-408 |
3.13e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 294 EIKAQYDDVASRSRAEAESWYRSKCEEMKAT---VIRHGETLRRTKEEI----NELNRMIQRLTAEIENAKCQRAKLEAA 366
Cdd:PRK12704 57 EALLEAKEEIHKLRNEFEKELRERRNELQKLekrLLQKEENLDRKLELLekreEELEKKEKELEQKQQELEKKEEELEEL 136
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622845037 367 VAEAEQQGE--AALS--DARCKLaeLEGALQKAKQDMACLLKEYQE 408
Cdd:PRK12704 137 IEEQLQELEriSGLTaeEAKEIL--LEKVEEEARHEAAVLIKEIEE 180
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
320-434 |
4.13e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 320 EMKATVIRHGETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQG----------EAALSDARCKLAELE 389
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELeeaeeeleeaEAELAEAEEALLEAE 371
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1622845037 390 GALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEHRL 434
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
332-434 |
8.06e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 8.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 332 LRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQ---GEAALSDARCKLAELEGALQKAKQDMACLLKEYQE 408
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQlqaAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126
|
90 100
....*....|....*....|....*.
gi 1622845037 409 VMNSKLGLDIEIATYRRLLEGEEHRL 434
Cdd:COG4372 127 LEQQRKQLEAQIAELQSEIAEREEEL 152
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
215-425 |
8.24e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 215 VALRATAENEFVVLKKDVDCAYLRKSDLEANVEALVEESSFLRRLY---EEEIRVLQAHISDTSvivkmDNSRDLNmdci 291
Cdd:COG3883 8 APTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYnelQAELEALQAEIDKLQ-----AEIAEAE---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 292 vAEIKAQYDDVASRSRAEAESWYRSKCEEM------KATVIRHGETLRRTKEEINELNRMIQRLTAEIENAKcqrAKLEA 365
Cdd:COG3883 79 -AEIEERREELGERARALYRSGGSVSYLDVllgsesFSDFLDRLSALSKIADADADLLEELKADKAELEAKK---AELEA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 366 AVAEAEQQGEAALSdarcKLAELEGALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRR 425
Cdd:COG3883 155 KLAELEALKAELEA----AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
330-427 |
8.71e-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: 41.67 E-value: 8.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 330 ETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQgeaaLSDARCKLAELEGALQKAKQDMACLLKEYQEV 409
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90
....*....|....*...
gi 1622845037 410 MNSklgLDIEIATYRRLL 427
Cdd:COG4942 96 RAE---LEAQKEELAELL 110
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
177-428 |
8.76e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 177 ETLRREAECVEADSGRLASELNHVQEVLEGYKKKYEEEVALRATAENEFVVLKKDVDCAYLRKSDLEANVEALVEEssfl 256
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE---- 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 257 RRLYEEEIRVLQAHISDtsvivkmdnsrdlnMDCIVAEIKAQYDDVASRSRAEAESWYRSKCEEMKATVIRHGETLRRTK 336
Cdd:TIGR02169 753 IENVKSELKELEARIEE--------------LEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 337 EEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGE----------AALSDARCKLAELEGALQKAKQDMACLLKEY 406
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEnlngkkeeleEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
250 260
....*....|....*....|..
gi 1622845037 407 QEVMNSKLGLDIEIATYRRLLE 428
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRLS 920
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
336-416 |
1.26e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 336 KEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGEAALSDARCKLAELEGALQKAKQDMAC--------LLKEYQ 407
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREElaakippeLLALYE 181
|
....*....
gi 1622845037 408 EVMNSKLGL 416
Cdd:COG1579 182 RIRKRKNGL 190
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
330-414 |
1.85e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 330 ETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQgeaaLSDARCKLAELEGALQKAKQDMACLLKEYQEV 409
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSE----IAEREEELKELEEQLESLQEELAALEQELQAL 176
|
....*
gi 1622845037 410 MNSKL 414
Cdd:COG4372 177 SEAEA 181
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
330-434 |
2.00e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 330 ETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQgeaaLSDARCKLAELEGALQKAKQDMACLLKEYQEV 409
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSE----LEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100
....*....|....*....|....*
gi 1622845037 410 MNSKLGLDIEIATyrrlLEGEEHRL 434
Cdd:COG4372 107 QEEAEELQEELEE----LQKERQDL 127
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
176-397 |
5.16e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 176 IETLRREAECVEADSGRLASELNHVQEVLEGYKKKYEEEVALRATAENEFVVLKKDVDcaylrksDLEANVEALVEE-SS 254
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------EAEAEIEERREElGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 255 FLRRLYEEEIRVlqahiSDTSVIVkmdNSRDLnmdcivaeikaqyDDVASRSRA-----EAEswyRSKCEEMKATVIRHG 329
Cdd:COG3883 91 RARALYRSGGSV-----SYLDVLL---GSESF-------------SDFLDRLSAlskiaDAD---ADLLEELKADKAELE 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622845037 330 ETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGEAALSDARCKLAELEGALQKAKQ 397
Cdd:COG3883 147 AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
109-425 |
5.17e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.50 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 109 NLEIDPNAQCVKQEEK------EQIKSLNSRFAAFIDKVRFLEQQ----NKLLETKWQFYQNQRCCESNL--EPLFSGYI 176
Cdd:PRK01156 196 NLELENIKKQIADDEKshsitlKEIERLSIEYNNAMDDYNNLKSAlnelSSLEDMKNRYESEIKTAESDLsmELEKNNYY 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 177 ETLRREAECVEADSG-----------RLASELNHVQEVLEGYK---KKYEEevALRATAE-----NEFVVLKKDVDCAYL 237
Cdd:PRK01156 276 KELEERHMKIINDPVyknrnyindyfKYKNDIENKKQILSNIDaeiNKYHA--IIKKLSVlqkdyNDYIKKKSRYDDLNN 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 238 RKSDL---EANVEALV---EESSFLRRLYEEEIRVLQAHISDTSVIVKMDNSRdlnMDCIVAEIKAQYDDVASR------ 305
Cdd:PRK01156 354 QILELegyEMDYNSYLksiESLKKKIEEYSKNIERMSAFISEILKIQEIDPDA---IKKELNEINVKLQDISSKvsslnq 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 306 ------------SRAEAESWYRSKC--------EEMKATVIRH-GETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLE 364
Cdd:PRK01156 431 riralrenldelSRNMEMLNGQSVCpvcgttlgEEKSNHIINHyNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLE 510
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622845037 365 AAVAEAEQQGEAALSDARCKLAELEGALQKAKQDMAcllkEYQEVMNSKLGLDIEIATYRR 425
Cdd:PRK01156 511 SEEINKSINEYNKIESARADLEDIKIKINELKDKHD----KYEEIKNRYKSLKLEDLDSKR 567
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
177-413 |
5.32e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 177 ETLRREAECVEADSGRLASELNHVQEVLEGYKKKYEEE---VALRATAENEFVVLKKDVDCAYLRKSDLEANVEALVEE- 252
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEdknMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAe 1616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 253 -----SSFLRRLYEEEIRVLQAHISDTSVIVKMDNSRDLNMDCIVAeiKAQYDDVASRSRAEAESWYRSKCEEMKATvir 327
Cdd:PTZ00121 1617 eakikAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK--AAEEAKKAEEDKKKAEEAKKAEEDEKKAA--- 1691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 328 hgETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGEAALSDARcKLAEL---EGALQKAKQDMACLLK 404
Cdd:PTZ00121 1692 --EALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK-KAEEAkkdEEEKKKIAHLKKEEEK 1768
|
....*....
gi 1622845037 405 EYQEVMNSK 413
Cdd:PTZ00121 1769 KAEEIRKEK 1777
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
293-407 |
5.44e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 293 AEIKAQYDDVASRsRAEAESWYRSKCEEMKAtvIRHGETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQ 372
Cdd:COG4717 391 LEQAEEYQELKEE-LEELEEQLEELLGELEE--LLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
90 100 110
....*....|....*....|....*....|....*
gi 1622845037 373 QGEaalsdarckLAELEGALQKAKQDMACLLKEYQ 407
Cdd:COG4717 468 DGE---------LAELLQELEELKAELRELAEEWA 493
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
332-400 |
7.55e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 37.30 E-value: 7.55e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622845037 332 LRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQ---GEAALSDARCKLAELEGALQKAKQDMA 400
Cdd:pfam11559 47 RDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERElalLQAKERQLEKKLKTLEQKLKNEKEELQ 118
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
327-400 |
8.83e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 38.52 E-value: 8.83e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622845037 327 RHGETLrrtkEEINEL-NRMIQRLtAEIENAKCQRAKLEAAVAEAEQQ-GEAA--LSDARCKLA-ELEGALQKAKQDMA 400
Cdd:COG0497 314 KYGVTV----EELLAYaEELRAEL-AELENSDERLEELEAELAEAEAElLEAAekLSAARKKAAkKLEKAVTAELADLG 387
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
261-434 |
9.16e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 38.88 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 261 EEEIRVLQAHISDTSVIVKMDNSRDLNMDCIVAEIKAQYDDVasrsraeaeswyRSKCEEMKATVIRHGETLRRTKEEIN 340
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL------------SRQISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622845037 341 ELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQqgeaalsdarcKLAELEGALQKAKQDMACLLKEYQEVMNSKLGLDIEI 420
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEA-----------EIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
170
....*....|....
gi 1622845037 421 ATYRRLLEGEEHRL 434
Cdd:TIGR02168 820 ANLRERLESLERRI 833
|
|
| |
