|
Name |
Accession |
Description |
Interval |
E-value |
| CC1_SLMAP |
cd21911 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal ... |
35-97 |
1.16e-24 |
|
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal membrane-associated protein (SLMAP), also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. SLMAP contains an N-terminal FHA domain followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409287 [Multi-domain] Cd Length: 63 Bit Score: 97.37 E-value: 1.16e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952581430 35 QELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQ 97
Cdd:cd21911 1 QELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQLS 63
|
|
| CC1_SLMAP-like |
cd21868 |
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ... |
39-76 |
1.59e-12 |
|
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar proteins; The family includes Sarcolemmal membrane-associated protein (SLMAP), its paralog TRAF3-interacting JNK-activating modulator (T3JAM), and similar proteins. SLMAP, also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. T3JAM, also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. SLMAP contains an N-terminal FHA domain, followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409286 [Multi-domain] Cd Length: 38 Bit Score: 62.12 E-value: 1.59e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1952581430 39 QLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSW 76
Cdd:cd21868 1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
54-743 |
1.81e-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: 68.17 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 54 LEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAysknqTEDGIRKELVTLQEDKHSYETTAKESLrrv 133
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA-----EIEELEREIEEERKRRDKLTEEYAELK--- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 134 lQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKAL---SE 210
Cdd:TIGR02169 364 -EELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINeleEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 211 KKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNIKdhnsIGIQVDDLLPKINGSTDKEHFLLK 290
Cdd:TIGR02169 443 KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE----AEAQARASEERVRGGRAVEEVLKA 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 291 SGGDCSELFQQFIECKNKLKAPVEPTQNNRISN--VED--------------------------MFESHLENNQTTEE-- 340
Cdd:TIGR02169 519 SIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNvvVEDdavakeaiellkrrkagratflplnkMRDERRDLSILSEDgv 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 341 -----DLKNDSERFKA--------TLIAEDdhtkvTEETKLLKEN----QLEAKESDMSDTLSPSKDRSSEDTTDYQMDE 403
Cdd:TIGR02169 599 igfavDLVEFDPKYEPafkyvfgdTLVVED-----IEAARRLMGKyrmvTLEGELFEKSGAMTGGSRAPRGGILFSRSEP 673
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 404 QELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKcfemQALL 483
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED----LSSL 749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 484 EEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLASTHKEIVA---LRQTAVEAATGRES-DIA 559
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSrieARLREIEQKLNRLTlEKE 829
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 560 ILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQqqkdkqkgEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLL 639
Cdd:TIGR02169 830 YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE--------ELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 640 TEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETN--GLRVKLAHAENETQKFQ-------KQY 710
Cdd:TIGR02169 902 ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSleDVQAELQRVEEEIRALEpvnmlaiQEY 981
|
730 740 750
....*....|....*....|....*....|...
gi 1952581430 711 EADQTMYLELKEKLDKTQKENESITDELENCKE 743
Cdd:TIGR02169 982 EEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
75-738 |
3.39e-11 |
|
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: 67.00 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 75 SWQALIDE-DRLLSRLEVMGNQLQAYSKNQTE-----DGIRKELVTLQEDKHSYETT---AKESLRRVLQEKIEVVRKLS 145
Cdd:TIGR02168 233 RLEELREElEELQEELKEAEEELEELTAELQEleeklEELRLEVSELEEEIEELQKElyaLANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 146 EVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQH---RIDEME 222
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETlrsKVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 223 EKEQLLQARIEALQAdndftneRLTALQVRLEQLQEKNIKDHNSIGIQVDDLLPKINGSTDKEHFLLKSGGD-----CSE 297
Cdd:TIGR02168 393 LQIASLNNEIERLEA-------RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELErleeaLEE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 298 LFQQFIECKNKLKAPVEPTQ--NNRISNVEDMFEsHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTEE---------- 365
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAqlQARLDSLERLQE-NLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyeaaieaalg 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 366 ---TKLLKENQLEAKE------------------SDMSDTLSPSKDR----SSEDTTDYQMDEQELNESLNKV--SLLKD 418
Cdd:TIGR02168 545 grlQAVVVENLNAAKKaiaflkqnelgrvtflplDSIKGTEIQGNDReilkNIEGFLGVAKDLVKFDPKLRKAlsYLLGG 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 419 LL-------AEARASSRKHESELDHLKYELQCAH-VQTGDSE----------REKQELQQELKEAQELAISSKQKCFEM- 479
Cdd:TIGR02168 625 VLvvddldnALELAKKLRPGYRIVTLDGDLVRPGgVITGGSAktnssilerrREIEELEEKIEELEEKIAELEKALAELr 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 480 --QALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILRE---DKEIEIIETRDQLASTHKEIVALRQTAVEAATGR 554
Cdd:TIGR02168 705 keLEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEEriaQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 555 ESdiaiLQGELHKVQTELEQWRQTASEYESEIFNlqtklqlqtqqqkdkQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQ 634
Cdd:TIGR02168 785 EE----LEAQIEQLKEELKALREALDELRAELTL---------------LNEEAANLRERLESLERRIAATERRLEDLEE 845
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 635 EKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVklahAENETQKFQKQYEADQ 714
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE----LESKRSELRRELEELR 921
|
730 740
....*....|....*....|....
gi 1952581430 715 TMYLELKEKLDKTQKENESITDEL 738
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRIDNLQERL 945
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
428-716 |
3.61e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 428 RKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQkcfemqALLEEERKTAKKQVEESTRQIQALQAH 507
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAEL------AELEAELEELRLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 508 LHKLQKDIEILREDKE------IEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASE 581
Cdd:COG1196 290 EYELLAELARLEQDIArleerrRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 582 YESEIfNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLT 661
Cdd:COG1196 370 AEAEL-AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1952581430 662 KDASGLEVSRKALEVEVgtlkEQRLQETNGLRVKLAHAENETQKFQKQYEADQTM 716
Cdd:COG1196 449 EEEAELEEEEEALLELL----AELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
44-751 |
1.52e-10 |
|
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: 65.08 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 44 LQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIDEDRllsrlevmgnqlqaySKNQTEDGIRKELVTLQEDKHsye 123
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS---------------ELEEEIEELQKELYALANEIS--- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 124 ttAKESLRRVLQEKIE-VVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEE 202
Cdd:TIGR02168 299 --RLEQQKQILRERLAnLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 203 IQQKALSEKKElqhrIDEMEEKEQLLQARIEALQAdndftneRLTALQVRLEQLQEKNIKDHNSIGIQVDDLLPKINGST 282
Cdd:TIGR02168 377 LEEQLETLRSK----VAQLELQIASLNNEIERLEA-------RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 283 DKEHFLLKSGGD-----CSELFQQFIECKNKLKAPVEPTQ--NNRISNVEDMFEsHLENNQTTEEDLKNDSERFKATLIA 355
Cdd:TIGR02168 446 EEELEELQEELErleeaLEELREELEEAEQALDAAERELAqlQARLDSLERLQE-NLEGFSEGVKALLKNQSGLSGILGV 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 356 EDDHTKVTEETKLLKENQLEA---------KESDMSDTLSPSKDRSS------EDTTDYQMDEQELNESLNKVSLLKDLL 420
Cdd:TIGR02168 525 LSELISVDEGYEAAIEAALGGrlqavvvenLNAAKKAIAFLKQNELGrvtflpLDSIKGTEIQGNDREILKNIEGFLGVA 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 421 AEARASSRKHESELDHLkyelqCAHVQTGDSEREKQELQQELKEAQEL------------AISSKQKCFEMQAL-LEEER 487
Cdd:TIGR02168 605 KDLVKFDPKLRKALSYL-----LGGVLVVDDLDNALELAKKLRPGYRIvtldgdlvrpggVITGGSAKTNSSILeRRREI 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 488 KTAKKQVEESTRQIQALQAHLHKLQK---DIEILREDKEIEIIETRDQLASTHKEIVALRQTaVEAATGRESDIAILQGE 564
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKeleELEEELEQLRKELEELSRQISALRKDLARLEAE-VEQLEERIAQLSKELTE 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 565 LHKVQTELEQWRQTASEYESEIfnlqTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQ 644
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEA----EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 645 WFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQR---LQETNGLRVKLAHAENETQKFQKQYEADQTMYLELK 721
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELealLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
730 740 750
....*....|....*....|....*....|
gi 1952581430 722 EKLDKTQKENESITDELENCKENLKLLQQK 751
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
28-675 |
1.89e-10 |
|
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: 64.69 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 28 NSPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALID-EDRLLSRLEVMGNQLQAY-SKNQTE 105
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEElESRLEELEEQLETLRSKVaQLELQI 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 106 DGIRKELVTLQEDKHSyettAKESLRRVLQEKIEVVRKLSEVERSLsnTEDECTHLKEMNDRTQEELRELANKYNGAVNE 185
Cdd:TIGR02168 396 ASLNNEIERLEARLER----LEDRRERLQQEIEELLKKLEEAELKE--LQAELEELEEELEELQEELERLEEALEELREE 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 186 LKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQAR----------IEALQADNDFTNERLTALQVRLEQ 255
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQsglsgilgvlSELISVDEGYEAAIEAALGGRLQA 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 256 LQEKNIKDH---------NSIGIQVDDLLPKINGSTDK--EHFLLKSGGDCSELFQQFIECKNKLKAPVEP--------- 315
Cdd:TIGR02168 550 VVVENLNAAkkaiaflkqNELGRVTFLPLDSIKGTEIQgnDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvvd 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 316 --TQNNRISNVEDmfesHLENNQTTEEDLKNdsERFKATLIAEDDHTKVTEETKLLKEN-----QLEAKESDMSDTLSPS 388
Cdd:TIGR02168 630 dlDNALELAKKLR----PGYRIVTLDGDLVR--PGGVITGGSAKTNSSILERRREIEELeekieELEEKIAELEKALAEL 703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 389 KDRSSEDTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQcahvqtgDSEREKQELQQELKEAQEL 468
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT-------ELEAEIEELEERLEEAEEE 776
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 469 AISSKQKcfemQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDK---EIEIIETRDQLASTHKEIVALRQ 545
Cdd:TIGR02168 777 LAEAEAE----IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLeslERRIAATERRLEDLEEQIEELSE 852
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 546 TaVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIfnlqTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGL 625
Cdd:TIGR02168 853 D-IESLAAEIEELEELIEELESELEALLNERASLEEALALL----RSELEELSEELRELESKRSELRRELEELREKLAQL 927
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1952581430 626 KNDCDSLRQEKVLLTEKL-QWFEEELRCAQQQSVKLTKDASGLEVSRKALE 675
Cdd:TIGR02168 928 ELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
29-259 |
3.11e-09 |
|
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: 60.85 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 29 SPSMYSQELFQLSQY--LQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEd 106
Cdd:TIGR02169 659 SRAPRGGILFSRSEPaeLQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE- 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 107 girkelvtLQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQ-EELRELANKYNGAVNE 185
Cdd:TIGR02169 738 --------RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSR 809
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952581430 186 LKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEK 259
Cdd:TIGR02169 810 IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
|
|
| CC1_T3JAM |
cd21912 |
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ... |
36-76 |
9.12e-09 |
|
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; TRAF3-interacting JNK-activating modulator (T3JAM), also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. The model corresponds to a conserved region that shows high sequence similarity with the first CC (CC1) domain of Sarcolemmal membrane-associated protein (SLMAP), which is responsible for the binding of suppressor of IKBKE 1 (SIKE1).
Pssm-ID: 409288 [Multi-domain] Cd Length: 45 Bit Score: 51.58 E-value: 9.12e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1952581430 36 ELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSW 76
Cdd:cd21912 5 EILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
483-750 |
2.31e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 483 LEEERKTAKK----QVEESTRQIQALQAHLHKLQKDIEILRED---KEIEIIETRDQLASTHKEIVALRQTAVEAatgrE 555
Cdd:COG1196 205 LERQAEKAERyrelKEELKELEAELLLLKLRELEAELEELEAEleeLEAELEELEAELAELEAELEELRLELEEL----E 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 556 SDIAILQGELHKVQTELEQWRQTASEYESEIfnlqtklqlqtqqqkDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQE 635
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERR---------------RELEERLEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 636 KVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYEADQT 715
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270
....*....|....*....|....*....|....*
gi 1952581430 716 MYLELKEKLDKTQKENESITDELENCKENLKLLQQ 750
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
201-753 |
5.18e-08 |
|
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: 56.65 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 201 EEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQaDNDFTNERLTALQVRLEQLQEKNIKDHNSIGIQVDDLLPKING 280
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQ-ELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCAR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 281 STDKEHfllKSGGDCSELFQQFIECKNKLKAPVEPTQNNRISNVEDMFESHLENNQTTEEdLKNDSERFKATLIAEDDHT 360
Cdd:pfam05483 167 SAEKTK---KYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEK-IQHLEEEYKKEINDKEKQV 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 361 KVTeetkLLKENQLEAKESDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYE 440
Cdd:pfam05483 243 SLL----LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEED 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 441 LQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIE---I 517
Cdd:pfam05483 319 LQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEemtK 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 518 LREDKEIEIIETRDQLASTHKEIVALRQTA--VEAATGRESDIAIL----QGELHKVQTELEQWRQTASEYESEIfnlqt 591
Cdd:pfam05483 399 FKNNKEVELEELKKILAEDEKLLDEKKQFEkiAEELKGKEQELIFLlqarEKEIHDLEIQLTAIKTSEEHYLKEV----- 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 592 klqlqtqqqkDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSR 671
Cdd:pfam05483 474 ----------EDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKE 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 672 KALEVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQK 751
Cdd:pfam05483 544 MNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK 623
|
..
gi 1952581430 752 GN 753
Cdd:pfam05483 624 GS 625
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
33-574 |
6.75e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 6.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 33 YSQELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGIRKEL 112
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 113 VTLQEDKHSyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEK 192
Cdd:COG1196 298 ARLEQDIAR----LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 193 LKQAEGKQEEIQQK---ALSEKKELQHRIDEMEEKEQLLQARIEALQA------------------------DNDFTNER 245
Cdd:COG1196 374 LAEAEEELEELAEElleALRAAAELAAQLEELEEAEEALLERLERLEEeleeleealaeleeeeeeeeealeEAAEEEAE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 246 LTALQVRLEQLQEKNIKDHNSIGIQVDDLLPKINGSTDKEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQNNRISNVE 325
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 326 DMFESHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTEETKLLKENQLEAKESDMSDTLSPSKDRSSEDTTDYQMDEQE 405
Cdd:COG1196 534 AAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 406 LNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEE 485
Cdd:COG1196 614 RYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 486 ERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLAsthkEIVALRQTAVEAATGRESDIAILQGEL 565
Cdd:COG1196 694 ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL----EEEELLEEEALEELPEPPDLEELEREL 769
|
....*....
gi 1952581430 566 HKVQTELEQ 574
Cdd:COG1196 770 ERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
166-740 |
8.95e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 8.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 166 DRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALsekkELQHRIDEMEEKEQLLQARIEALQADNDFTNER 245
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE----ELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 246 LTALQVRLEQLQEKNIKDHNSIGIQVDDLLpkingstdkehfllksggdcsELFQQFIECKNKLKApveptQNNRISNVE 325
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELE---------------------ELEEELEEAEEELEE-----AEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 326 DMFESHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTEETKLLKENQLEAKESdmsdtlspskdrssedttdYQMDEQE 405
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER-------------------LEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 406 LNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEE 485
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 486 ERKTAKKQVEES----------------TRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLASTHKEIVALRQTAVE 549
Cdd:COG1196 506 FLEGVKAALLLAglrglagavavligveAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRAR 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 550 AATGRESDIAILQGELHKVQTELEqWRQTASEYESEIFNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDC 629
Cdd:COG1196 586 AALAAALARGAIGAAVDLVASDLR-EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTG 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 630 DSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQ 709
Cdd:COG1196 665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744
|
570 580 590
....*....|....*....|....*....|....
gi 1952581430 710 YEADQTM---YLELKEKLDKTQKENESITDELEN 740
Cdd:COG1196 745 EELLEEEaleELPEPPDLEELERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
368-703 |
2.51e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 368 LLKENQLEAKESDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQ 447
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 448 TGDSEREKQELQQELKEAQelaisskqkcfEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREdKEIEII 527
Cdd:COG1196 311 RRELEERLEELEEELAELE-----------EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA-ELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 528 ETRDQLASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIfNLQTKLQLQTQQQKDKQKGE 607
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE-EEEEEALEEAAEEEAELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 608 AVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQ--QSVKLTKDASGLEVSRKALEVEVGTLKEQR 685
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGflEGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
330
....*....|....*...
gi 1952581430 686 LQETNGLRVKLAHAENET 703
Cdd:COG1196 538 AALEAALAAALQNIVVED 555
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
452-739 |
6.10e-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: 6.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 452 EREK----QELQQELKEAQELAISSKQKCFEMQ-ALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEIL----REDK 522
Cdd:TIGR02169 206 EREKaeryQALLKEKREYEGYELLKEKEALERQkEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkiKDLG 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 523 EIEIIETRDQLASTHKEIVALRQTAVEAatgrESDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKD 602
Cdd:TIGR02169 286 EEEQLRVKEKIGELEAEIASLERSIAEK----ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 603 KQKGEAVqLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLK 682
Cdd:TIGR02169 362 LKEELED-LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE 440
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1952581430 683 EqrlqETNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELE 739
Cdd:TIGR02169 441 E----EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
456-751 |
6.71e-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: 53.14 E-value: 6.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 456 QELQQELKEAQeLAISSKQKCFemqalLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEilredkeieiiETRDQLAS 535
Cdd:TIGR02168 216 KELKAELRELE-LALLVLRLEE-----LREELEELQEELKEAEEELEELTAELQELEEKLE-----------ELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 536 THKEIVALrQTAVEAATgreSDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQqqkdkqkgEAVQLQGKL 615
Cdd:TIGR02168 279 LEEEIEEL-QKELYALA---NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE--------ELAELEEKL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 616 DELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLK---EQRLQETNGL 692
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEdrrERLQQEIEEL 426
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1952581430 693 RVKLahAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQK 751
Cdd:TIGR02168 427 LKKL--EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
405-730 |
7.35e-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: 7.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 405 ELNESLNKVSLLKDLLAEARA-SSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALL 483
Cdd:TIGR02169 195 EKRQQLERLRREREKAERYQAlLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 484 EEERKTAKKQVEESTRQIqalQAHLHKLQKDIEILrEDKEIEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQG 563
Cdd:TIGR02169 275 EELNKKIKDLGEEEQLRV---KEKIGELEAEIASL-ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 564 ELHKVQTELEQWRQTASEYESEIfnlqtklqLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKL 643
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEDLRAEL--------EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 644 QWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRlqetnglrvklahaenetQKFQKQYEADQTMYLELKEK 723
Cdd:TIGR02169 423 ADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL------------------SKYEQELYDLKEEYDRVEKE 484
|
....*..
gi 1952581430 724 LDKTQKE 730
Cdd:TIGR02169 485 LSKLQRE 491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
400-675 |
7.14e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 7.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 400 QMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQE--LAISSKQKCF 477
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKelYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 478 EMQ-ALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKE---IEIIETRDQLASTHKEIVALRQTAVEAATG 553
Cdd:TIGR02168 301 EQQkQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEelkEELESLEAELEELEAELEELESRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 554 RE---SDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKGEavqLQGKLDELQKQSNGLKNDCD 630
Cdd:TIGR02168 381 LEtlrSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE---LQAELEELEEELEELQEELE 457
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1952581430 631 SLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALE 675
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
126-685 |
1.50e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 126 AKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQ 205
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 206 kalsEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNIKDHNSIGIQVDDLlpkingstdke 285
Cdd:COG1196 317 ----RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL----------- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 286 hfllksggdcSELFQQFIECKNKLKApveptQNNRISNVEDMFESHLENNQTTEEDLKNDSERFKATLIAEDDHTKvTEE 365
Cdd:COG1196 382 ----------EELAEELLEALRAAAE-----LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE-ALE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 366 TKLLKENQLEAKESDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLA--EARASSRKHESELDHLKYELQC 443
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAdyEGFLEGVKAALLLAGLRGLAGA 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 444 AHVQTGDSEREKQELQ---------------QELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHL 508
Cdd:COG1196 526 VAVLIGVEAAYEAALEaalaaalqnivveddEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVA 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 509 HKLQKDIEILREDKEIEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIFN 588
Cdd:COG1196 606 SDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 589 LQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNglkndcDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLE 668
Cdd:COG1196 686 ERLAEEELELEEALLAEEEEERELAEAEEERLEEE------LEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP 759
|
570
....*....|....*..
gi 1952581430 669 VSRKALEVEVGTLKEQR 685
Cdd:COG1196 760 PDLEELERELERLEREI 776
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
450-673 |
2.31e-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: 47.45 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 450 DSEREKQELQQELKEAQELAISSKQKcfemQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREdkeiEIIET 529
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK----EIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 530 RDQLASTHKEIValRQTAVEAATGRESDIAIL--QGELHKVQTELeQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKGE 607
Cdd:COG4942 96 RAELEAQKEELA--ELLRALYRLGRQPPLALLlsPEDFLDAVRRL-QYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952581430 608 AVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKA 673
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
169-748 |
3.01e-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: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 169 QEELRELanKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQH---RIDEMEEKEQLLQARIEALQADNDFTNER 245
Cdd:COG1196 219 KEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAELAEleaELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 246 LTALQVRLEQLQEKNIkdhnsigiqvddllpkingstDKEHFLLKSGGDCSELFQQFIECKNKLKapveptqnnRISNVE 325
Cdd:COG1196 297 LARLEQDIARLEERRR---------------------ELEERLEELEEELAELEEELEELEEELE---------ELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 326 DMFESHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTEETKLLKENQLEAKESDMSDTLSpSKDRSSEDTTDYQMDEQE 405
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE-AEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 406 LNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEE 485
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 486 ERKTAKKQVEES-----TRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLASthKEIVALRQTAVEAAT-------- 552
Cdd:COG1196 506 FLEGVKAALLLAglrglAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA--AAIEYLKAAKAGRATflpldkir 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 553 -GRESDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDS 631
Cdd:COG1196 584 aRAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 632 LRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYE 711
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
570 580 590
....*....|....*....|....*....|....*..
gi 1952581430 712 ADQTMYLELKEKLDKTQKENEsITDELENCKENLKLL 748
Cdd:COG1196 744 EEELLEEEALEELPEPPDLEE-LERELERLEREIEAL 779
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
119-758 |
5.28e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 119 KHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTE--DECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQA 196
Cdd:PTZ00121 1207 KAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKkaEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 197 EGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALQAdndftNERLTALQVRLEQLQEKnikdhnsigiqvDDLLP 276
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA-----KKKADAAKKKAEEAKKA------------AEAAK 1349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 277 KINGSTDKEHFLLKSGGDCSELFQQfiecKNKLKAPVEPTQNNRISNVEDMFESHLENNQTTEEDLKNDSERFKAtliae 356
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKE----EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKA----- 1420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 357 DDHTKVTEETKLLKENQLEAKESDMSDTLSP-SKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELD 435
Cdd:PTZ00121 1421 DEAKKKAEEKKKADEAKKKAEEAKKADEAKKkAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAD 1500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 436 HLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAK-KQVEESTRQIQALQAHLHKLQ-- 512
Cdd:PTZ00121 1501 EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElKKAEEKKKAEEAKKAEEDKNMal 1580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 513 KDIEILREDKEIEIIETRDQLASTHKEIVALRQTAVEAATGREsdiailqgELHKVQTELEQWRQTASEYESEIFNLQTK 592
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE--------ELKKAEEEKKKVEQLKKKEAEEKKKAEEL 1652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 593 LQLQTQQQ--KDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLR---QEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGL 667
Cdd:PTZ00121 1653 KKAEEENKikAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKkeaEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA 1732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 668 EVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELencKENLKL 747
Cdd:PTZ00121 1733 EEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDI---FDNFAN 1809
|
650
....*....|.
gi 1952581430 748 LQQKGNNGGLF 758
Cdd:PTZ00121 1810 IIEGGKEGNLV 1820
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
139-271 |
8.16e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.00 E-value: 8.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 139 EVVRKLSEveRSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLK-QAEGKQEEIQ--QKALSEKKELQ 215
Cdd:COG2433 380 EALEELIE--KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEaELEEKDERIErlERELSEARSEE 457
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1952581430 216 HRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNIKDHNSIGIQV 271
Cdd:COG2433 458 RREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGELVPV 513
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
118-753 |
1.07e-04 |
|
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: 45.88 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 118 DKHSYETTAKESLRRVLQEKIEvvrklsEVERSLSNTEDecthLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAE 197
Cdd:pfam15921 131 DIRRRESQSQEDLRNQLQNTVH------ELEAAKCLKED----MLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEAS 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 198 GKQ-------------------EEIQQKALSEKKELQHRI----DEMEEKEQLLQARIE-ALQADNDFTNERLTALQVRL 253
Cdd:pfam15921 201 GKKiyehdsmstmhfrslgsaiSKILRELDTEISYLKGRIfpveDQLEALKSESQNKIElLLQQHQDRIEQLISEHEVEI 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 254 EQLQEKNI---KDHNSIGIQVDDLLPKI-NGSTDKEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQNNRISNVEDMFE 329
Cdd:pfam15921 281 TGLTEKASsarSQANSIQSQLEIIQEQArNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 330 SHLENNQTTEEDLKNDSERFKatLIAedDHTKVTEETKLLKENQLEAKESDMSDTLSPSKDRSSEDttDYQMDEQEL--- 406
Cdd:pfam15921 361 ARTERDQFSQESGNLDDQLQK--LLA--DLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELD--DRNMEVQRLeal 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 407 ----------------------NESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELkE 464
Cdd:pfam15921 435 lkamksecqgqmerqmaaiqgkNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAI-E 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 465 AQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDkeieiIETRDQLASTHKEIVALR 544
Cdd:pfam15921 514 ATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQ-----IENMTQLVGQHGRTAGAM 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 545 QtaVEAATgresdiaiLQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKGEAVQLQGKLDeLQKQSNG 624
Cdd:pfam15921 589 Q--VEKAQ--------LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKD-IKQERDQ 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 625 LKNDCDSLRQEKVLLTEKLQWFEEELRC-AQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENET 703
Cdd:pfam15921 658 LLNEVKTSRNELNSLSEDYEVLKRNFRNkSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQIT 737
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1952581430 704 QKfQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQKGN 753
Cdd:pfam15921 738 AK-RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKN 786
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
170-724 |
1.69e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 170 EELRELANKYNGAVNELKEftEKLKQAEGKQEEIQQKalsEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTAL 249
Cdd:PRK02224 165 EEYRERASDARLGVERVLS--DQRGSLDQLKAQIEEK---EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 250 QVRLEQLQEKNiKDHNSIGIQVDDLLPKINGSTDKEHFLLKSGGDCSELFQQFIECKNKL--KAPVEPTQNNRISNVEDM 327
Cdd:PRK02224 240 DEVLEEHEERR-EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaEAGLDDADAEAVEARREE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 328 FESHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTEETKLLKENQLEAKESDMSDTLSPSKDRSSE-DTTDYQMDEQE- 405
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEiEELEEEIEELRe 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 406 ----LNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQcahvqtgDSEREKQELQ---------QELKEAQElaISS 472
Cdd:PRK02224 399 rfgdAPVDLGNAEDFLEELREERDELREREAELEATLRTAR-------ERVEEAEALLeagkcpecgQPVEGSPH--VET 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 473 KQKCFEMQALLEEERKTAKKQVE------ESTRQIQALQAHLHKLQ---KDIEILREDKEIEIIETRDQLASTHKEIVAL 543
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEeveerlERAEDLVEAEDRIERLEerrEDLEELIAERRETIEEKRERAEELRERAAEL 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 544 RQTAVEAatgrESDIAILQGELHKVQTELEQWRQTASEYESEIfnLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSN 623
Cdd:PRK02224 550 EAEAEEK----REAAAEAEEEAEEAREEVAELNSKLAELKERI--ESLERIRTLLAAIADAEDEIERLREKREALAELND 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 624 GLKNDCDSLRQEKVLLTEKLQWFE-EELRCAQQQSVKLTKDASG----LEVSRKALEVEVGTLkEQRLQETNGLRVKLAH 698
Cdd:PRK02224 624 ERRERLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEkldeLREERDDLQAEIGAV-ENELEELEELRERREA 702
|
570 580
....*....|....*....|....*....
gi 1952581430 699 AENETQKFQKQY---EADQTMYLELKEKL 724
Cdd:PRK02224 703 LENRVEALEALYdeaEELESMYGDLRAEL 731
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
209-574 |
1.73e-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: 45.43 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 209 SEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQekniKDHNSIGIQVDDLLPKINGSTDKehfl 288
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS----RQISALRKDLARLEAEVEQLEER---- 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 289 lksggdcselfQQFIECKNKLKAPVEPTQNNRISNVEDMFESHLENNQTTEEDLKNDSERFKATliaEDDHTKVTEETKL 368
Cdd:TIGR02168 749 -----------IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL---REALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 369 LKENQLEAKEsdmsdTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLkyelqcahvqt 448
Cdd:TIGR02168 815 LNEEAANLRE-----RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL----------- 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 449 gdsEREKQELQQELKEAQELAISskqkcfemqalLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILredkEIEIIE 528
Cdd:TIGR02168 879 ---LNERASLEEALALLRSELEE-----------LSEELRELESKRSELRRELEELREKLAQLELRLEGL----EVRIDN 940
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1952581430 529 TRDQLASTHKeivALRQTAVEAATGRESDIAILQGELHKVQTELEQ 574
Cdd:TIGR02168 941 LQERLSEEYS---LTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
403-582 |
2.91e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 403 EQELNESLNKVSLLKDLLAEARASSRKHESELDHLK--YELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQ 480
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRqkNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 481 ALLEEERKTAKKQVEEStrQIQALQAHLHKLQKDIEILRE---DKEIEIIETRDQLASTHKEIVALRQTAVEAAtgrESD 557
Cdd:COG3206 247 AQLGSGPDALPELLQSP--VIQQLRAQLAELEAELAELSArytPNHPDVIALRAQIAALRAQLQQEAQRILASL---EAE 321
|
170 180
....*....|....*....|....*
gi 1952581430 558 IAILQGELHKVQTELEQWRQTASEY 582
Cdd:COG3206 322 LEALQAREASLQAQLAQLEARLAEL 346
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
50-231 |
3.71e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 50 REQML--EQKLATLQRLLANTQEAsDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGIRKELVTLQEDKHSYE---T 124
Cdd:COG4913 241 HEALEdaREQIELLEPIRELAERY-AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEarlD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 125 TAKESLRRV--------------LQEKIE-VVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEF 189
Cdd:COG4913 320 ALREELDELeaqirgnggdrleqLEREIErLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEE 399
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1952581430 190 TEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEK-----EQLLQAR 231
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERRksnipARLLALR 446
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
128-750 |
5.32e-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: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 128 ESLRRVLQEKIEVVRK--LSEVERSLSNTEDECTHLKEMN--DRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEI 203
Cdd:TIGR01612 1058 DEIEKEIGKNIELLNKeiLEEAEINITNFNEIKEKLKHYNfdDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEI 1137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 204 QQKALSEKKELQHRIDEMEEkeqllqariealQADNDFTNERLTALQVRLEQLQEKnIKDHNSIGIQVDDLLPKINGSTD 283
Cdd:TIGR01612 1138 KKKSENYIDEIKAQINDLED------------VADKAISNDDPEEIEKKIENIVTK-IDKKKNIYDEIKKLLNEIAEIEK 1204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 284 KEHFL-------LKSGGDCSELFQQFIECKNKLKAPVEPTQNNRISNVEDMFES--HLENNQTTEEDLKNDSERFKATLI 354
Cdd:TIGR01612 1205 DKTSLeevkginLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKspEIENEMGIEMDIKAEMETFNISHD 1284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 355 AEDDHTKVTEE---------TKLLKENQLEAKESDMSDTlspsKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLaeara 425
Cdd:TIGR01612 1285 DDKDHHIISKKhdenisdirEKSLKIIEDFSEESDINDI----KKELQKNLLDAQKHNSDINLYLNEIANIYNIL----- 1355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 426 ssrkhesELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQ 505
Cdd:TIGR01612 1356 -------KLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKIESTLDDKDIDECIKKIKELK 1428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 506 AHlhklqkdieILREDKEieiIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQ-----GELHKVQTELEQWRQTAS 580
Cdd:TIGR01612 1429 NH---------ILSEESN---IDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKkdnatNDHDFNINELKEHIDKSK 1496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 581 EYESEI--------FNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKlqwFEEELRC 652
Cdd:TIGR01612 1497 GCKDEAdknakaieKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEK---SEQKIKE 1573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 653 AQQQSVKLTKDASGLEVSRKA---LEVEVGTLKEQRLQETNgLRVKLAHAENETQKFQKQ-----YEADQTMYLELKEKL 724
Cdd:TIGR01612 1574 IKKEKFRIEDDAAKNDKSNKAaidIQLSLENFENKFLKISD-IKKKINDCLKETESIEKKissfsIDSQDTELKENGDNL 1652
|
650 660
....*....|....*....|....*.
gi 1952581430 725 DKTQKENESITDELENCKENLKLLQQ 750
Cdd:TIGR01612 1653 NSLQEFLESLKDQKKNIEDKKKELDE 1678
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
54-725 |
5.80e-04 |
|
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: 43.57 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 54 LEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQTEDGIRKELVTLQEDKHSYETTakeslrrv 133
Cdd:pfam15921 243 VEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSM-------- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 134 lqekieVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKE 213
Cdd:pfam15921 315 ------YMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 214 LQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNIKDHNSIGIQVDDLLPKINGSTDkehfllkSGG 293
Cdd:pfam15921 389 REKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNE-------SLE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 294 DCSELFQQFIECKNKLKAPVEPTQNNRISnvedmfeshLENNQTTEEDLKNDSERFKATLIAEDdhtkvTEETKLLKENQ 373
Cdd:pfam15921 462 KVSSLTAQLESTKEMLRKVVEELTAKKMT---------LESSERTVSDLTASLQEKERAIEATN-----AEITKLRSRVD 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 374 LEAKESDMsdtLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKyelqcahVQTGDSER 453
Cdd:pfam15921 528 LKLQELQH---LKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQ-------VEKAQLEK 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 454 EKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALqahlhklqKDIEILREDKEIEIIETRDQL 533
Cdd:pfam15921 598 EINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAV--------KDIKQERDQLLNEVKTSRNEL 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 534 ASTHKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESeifnlqtklqlqtqqqkdkQKGEAVQLQG 613
Cdd:pfam15921 670 NSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEG-------------------SDGHAMKVAM 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 614 KldeLQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGL--EVSRKALEVEVGTLKEQRLQE-TN 690
Cdd:pfam15921 731 G---MQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVatEKNKMAGELEVLRSQERRLKEkVA 807
|
650 660 670
....*....|....*....|....*....|....*..
gi 1952581430 691 GLRVKLAHAENETQKFQK--QYEADQTMYLELKEKLD 725
Cdd:pfam15921 808 NMEVALDKASLQFAECQDiiQRQEQESVRLKLQHTLD 844
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
342-627 |
6.96e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 342 LKNDSERFKATLIAEDDHTKVTEETKLLKENQLEAKESDMSDTlspsKDRSSEDTTDYQMDEQELNESLNKVS------- 414
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL----RLEVSELEEEIEELQKELYALANEISrleqqkq 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 415 LLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEM---QALLEEERKTAK 491
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELesrLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 492 KQVEESTRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLASTHKEIVALRQTAVEAatgresdiaiLQGELHKVQTE 571
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE----------LEEELEELQEE 455
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1952581430 572 LEQWRQTASEYESEIfNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKN 627
Cdd:TIGR02168 456 LERLEEALEELREEL-EEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
452-635 |
7.78e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 452 EREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAkkQVEESTRQIQALQAHLHKLQKDIEILREDKeIEIIETRD 531
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLA--EYSWDEIDVASAEREIAELEAELERLDASS-DDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 532 QLASTHKEIVALRQ---TAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEIFNLQTKLQLQTQQQKDKQKgea 608
Cdd:COG4913 693 QLEELEAELEELEEeldELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE--- 769
|
170 180
....*....|....*....|....*..
gi 1952581430 609 vQLQGKLDELQKQSNGLKNDCDSLRQE 635
Cdd:COG4913 770 -NLEERIDALRARLNRAEEELERAMRA 795
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
485-685 |
1.06e-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: 42.06 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 485 EERKTAKKQVEESTRQIQALQAHLHKLQKDI-EILREDKEIE--IIETRDQLASTHKEIVALRQTAVEAatgrESDIAIL 561
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEkALLKQLAALErrIAALARRIRALEQELAALEAELAEL----EKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 562 QGELHKVQTELEQ-----WRQTASEYESEIFNLQTKLQLQTQQQKDKQKGEAvqLQGKLDELQKQSNGLKNDCDSLRQEK 636
Cdd:COG4942 96 RAELEAQKEELAEllralYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA--RREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1952581430 637 VLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQR 685
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
111-754 |
1.07e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 111 ELVTLQEDKHSYETTAKESLRRV--LQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKE 188
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 189 FTEKLKQAEGKQEEIQQKA--LSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKNIKDHNS 266
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKAdaAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 267 IGIQVDDLLPKINGSTDKEHFLLKSggdcsELFQQFIECKNKLKapvEPTQNNRISNVEDMFESHLENNQTTEEDLKNDS 346
Cdd:PTZ00121 1442 EAKKADEAKKKAEEAKKAEEAKKKA-----EEAKKADEAKKKAE---EAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD 1513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 347 ERFKATLIAEDDHTKVTEETKLLKENQlEAKESDMSDTLSPSKD-RSSEDTtdyQMDEQELNESLNKVSLLKDLlAEARA 425
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAK-KAEEKKKADELKKAEElKKAEEK---KKAEEAKKAEEDKNMALRKA-EEAKK 1588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 426 SSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELaissKQKCFEMQALLEEERKTA---KKQVEESTRQIQ 502
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE----KKKVEQLKKKEAEEKKKAeelKKAEEENKIKAA 1664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 503 ALQAHLHKLQKDIEILREDKEIEiietrdqlasthkeivalrqTAVEAATGRESDIAILQGELHKVQTElEQWRQTASEY 582
Cdd:PTZ00121 1665 EEAKKAEEDKKKAEEAKKAEEDE--------------------KKAAEALKKEAEEAKKAEELKKKEAE-EKKKAEELKK 1723
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 583 ESEIFNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEK-VLLTEKLQWFEEELRCAQQQSVKLT 661
Cdd:PTZ00121 1724 AEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKeAVIEEELDEEDEKRRMEVDKKIKDI 1803
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 662 KDASG-LEVSRKALEVEVGTLKEQRLQETNGLRVKLAHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELEN 740
Cdd:PTZ00121 1804 FDNFAnIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEE 1883
|
650
....*....|....
gi 1952581430 741 CKENlKLLQQKGNN 754
Cdd:PTZ00121 1884 IEEA-DEIEKIDKD 1896
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
54-258 |
1.52e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 54 LEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEvmgNQLQAYSKNQTEdgIRKELVTLQEDKHSYETtAKESLRRV 133
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALA---RRIRALEQELAA--LEAELAELEKEIAELRA-ELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 134 LQEKIEVVRKLSEVER--SLSNTED--ECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALS 209
Cdd:COG4942 106 LAELLRALYRLGRQPPlaLLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1952581430 210 EKKELQHRIDEMEEKEQLLQARIEALQAdndftneRLTALQVRLEQLQE 258
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAA-------ELAELQQEAEELEA 227
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
403-576 |
1.90e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 403 EQELNESLNKVSLLKDLLAEARASSRKHE--------SELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQ 474
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEaqirgnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 475 KCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREdkEIEIIETRDqlASTHKEIVALRQTAVEAATGR 554
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA--EIASLERRK--SNIPARLLALRDALAEALGLD 456
|
170 180
....*....|....*....|..
gi 1952581430 555 ESDIAILqGELHKVQTELEQWR 576
Cdd:COG4913 457 EAELPFV-GELIEVRPEEERWR 477
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
161-418 |
2.26e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 161 LKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEALqadnd 240
Cdd:PHA02562 165 LSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEEL----- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 241 ftNERLTALQVRLEQlQEKNIKDHNSIGIQVDDLLPKINgstdKEHFLLKSGGDCSELFQQFIECKNKLKA----PVEPT 316
Cdd:PHA02562 240 --TDELLNLVMDIED-PSAALNKLNTAAAKIKSKIEQFQ----KVIKMYEKGGVCPTCTQQISEGPDRITKikdkLKELQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 317 Q-----NNRISNVEDMFESHLEnNQTTEEDLKNDSERFKATLIAEDDHTKVTEetKLLKenQLEAKESDMSDTLSPSKDR 391
Cdd:PHA02562 313 HsleklDTAIDELEEIMDEFNE-QSKKLLELKNKISTNKQSLITLVDKAKKVK--AAIE--ELQAEFVDNAEELAKLQDE 387
|
250 260
....*....|....*....|....*..
gi 1952581430 392 SSEDTTDYQMDEQELNESLNKVSLLKD 418
Cdd:PHA02562 388 LDKIVKTKSELVKEKYHRGIVTDLLKD 414
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
143-750 |
2.43e-03 |
|
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: 41.54 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 143 KLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKAlsekKELQHRIDEME 222
Cdd:TIGR04523 97 KINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKY----NDLKKQKEELE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 223 EKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEKnIKDHNSIGIQVDDLLPKINGSTDKehfLLKSGGDCSELFQQF 302
Cdd:TIGR04523 173 NELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKK-IQKNKSLESQISELKKQNNQLKDN---IEKKQQEINEKTTEI 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 303 IECKNKLKAPVEptQNNRISNVEDMFESHLENNQTTEEDLKNDSERFKATlIAEDDHTKVTEETKLLKEnQLEAKESDMS 382
Cdd:TIGR04523 249 SNTQTQLNQLKD--EQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSE-ISDLNNQKEQDWNKELKS-ELKNQEKKLE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 383 DTlspskdrssedttdyqmdEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQEL 462
Cdd:TIGR04523 325 EI------------------QNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 463 KEAqelaISSKQKcfemqalLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREdkeiEIIETRDQLASTHKEIVA 542
Cdd:TIGR04523 387 KNL----ESQIND-------LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKE----TIIKNNSEIKDLTNQDSV 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 543 LRQTAVEAATGRES---DIAILQGELHKVQTELEQWRQTASEYESEIFNLQTklqlqtqqqkdkqkgEAVQLQGKLDELQ 619
Cdd:TIGR04523 452 KELIIKNLDNTRESletQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE---------------EKKELEEKVKDLT 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 620 KQSNGLKNDCDSLRQEKVLLTEKLQWFEEELrcaqqQSVKLTKDASGLEVSRKALEVEVGTLKEQR---LQETNGLRVKL 696
Cdd:TIGR04523 517 KKISSLKEKIEKLESEKKEKESKISDLEDEL-----NKDDFELKKENLEKEIDEKNKEIEELKQTQkslKKKQEEKQELI 591
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1952581430 697 AHAENETQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQ 750
Cdd:TIGR04523 592 DQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQ 645
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
105-554 |
2.57e-03 |
|
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: 41.58 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 105 EDGIRKELVTLQ----EDKHSYETTAK--ESLRRVLQEKIEVVRKLSE------VERSL-SNTEDECTHLKEMNdrtqEE 171
Cdd:TIGR01612 1269 EMDIKAEMETFNishdDDKDHHIISKKhdENISDIREKSLKIIEDFSEesdindIKKELqKNLLDAQKHNSDIN----LY 1344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 172 LRELANKYN-GAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQL--LQARIEALQADNDFTN--ERL 246
Cdd:TIGR01612 1345 LNEIANIYNiLKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLeeCKSKIESTLDDKDIDEciKKI 1424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 247 TALQVRLEQlQEKNIKDHNSigiqvddllpkiNGSTDKEHFLLksggdcseLFQQFIECKNKLKAPVEPTQNNRIS---- 322
Cdd:TIGR01612 1425 KELKNHILS-EESNIDTYFK------------NADENNENVLL--------LFKNIEMADNKSQHILKIKKDNATNdhdf 1483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 323 NVEDMFESHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTE----ETKLLKENQLEAKESDMSDTLSPSKDRSSEDTTD 398
Cdd:TIGR01612 1484 NINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTEllnkYSALAIKNKFAKTKKDSEIIIKEIKDAHKKFILE 1563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 399 YQMDEQELNESLNKVSLLKDLLAEARASSRKH---ESELDHLKYE-LQCAHVQT--GDSEREKQELQQELK----EAQEL 468
Cdd:TIGR01612 1564 AEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAidiQLSLENFENKfLKISDIKKkiNDCLKETESIEKKISsfsiDSQDT 1643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 469 AISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEIEIIETRDQLASTHKEIVALRQTAV 548
Cdd:TIGR01612 1644 ELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKEEIESIKELI 1723
|
....*.
gi 1952581430 549 EAATGR 554
Cdd:TIGR01612 1724 EPTIEN 1729
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
398-751 |
2.62e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 398 DYQMDEQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELQCAHVQTGDS---------------EREKQELQQEL 462
Cdd:COG4913 282 RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqlereierlERELEERERRR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 463 KEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREDKEiEIIETRDQLASTHK---- 538
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR-ELEAEIASLERRKSnipa 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 539 EIVALRQTAVEAATGRESDIAILqGELHKVQTELEQWRQTA--------------SEYE---SEIFNLQTKLQ------- 594
Cdd:COG4913 441 RLLALRDALAEALGLDEAELPFV-GELIEVRPEEERWRGAIervlggfaltllvpPEHYaaaLRWVNRLHLRGrlvyerv 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 595 LQTQQQKDKQKGEAVQLQGKL---------------------------DELQ------------KQSNGL--KNDCDSLR 633
Cdd:COG4913 520 RTGLPDPERPRLDPDSLAGKLdfkphpfrawleaelgrrfdyvcvdspEELRrhpraitragqvKGNGTRheKDDRRRIR 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 634 QEKVL---LTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLkeQRLQETNGLRVKLAHAENETQKFQKQY 710
Cdd:COG4913 600 SRYVLgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL--QRLAEYSWDEIDVASAEREIAELEAEL 677
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1952581430 711 ---EADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQK 751
Cdd:COG4913 678 erlDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE 721
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
130-259 |
2.76e-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: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 130 LRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQ----- 204
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkey 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1952581430 205 QKALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEK 259
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE 146
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
106-544 |
2.79e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 106 DGIRKELVTLQEDKHSYETTAKEsLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEmNDRTQEELRELANKYNgavnE 185
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKE-LESLEGSKRKLEEKIRELEERIEELKKEIEELEE-KVKELKELKEKAEEYI----K 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 186 LKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQL----------LQARIEALQADNDfTNERLTALQVRLEQ 255
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERleelkkklkeLEKRLEELEERHE-LYEEAKAKKEELER 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 256 LQEKniKDHNSIGIQVDDLLPKINGSTDKEHFLLKSGGDCSELFQQFIECKN--------KLKAPVEPTQNNRISNVEDM 327
Cdd:PRK03918 377 LKKR--LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKaieelkkaKGKCPVCGRELTEEHRKELL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 328 FESHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTEETKLLKENQL-EAKESDMSDTLSPSKDRSSEDTTDYQMDEQEL 406
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaEQLKELEEKLKKYNLEELEKKAEEYEKLKEKL 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 407 NESLNKVSLLKDLLAEARA---SSRKHESELDHLKYELQCAHVQTGD----SEREKQELQQELKEAQELAISSKQKCFEM 479
Cdd:PRK03918 535 IKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEElgfeSVEELEERLKELEPFYNEYLELKDAEKEL 614
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1952581430 480 QAlLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILR--------EDKEIEIIETRDQLASTHKEIVALR 544
Cdd:PRK03918 615 ER-EEKELKKLEEELDKAFEELAETEKRLEELRKELEELEkkyseeeyEELREEYLELSRELAGLRAELEELE 686
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
35-234 |
3.57e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.83 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 35 QELFQLSQYLQEALHREQML----------------EQKLATLQRLLANTQ---EASDSSWQALIDEDR-LLSRLEVMGN 94
Cdd:COG0497 172 KELEELRADEAERARELDLLrfqleeleaaalqpgeEEELEEERRRLSNAEklrEALQEALEALSGGEGgALDLLGQALR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 95 QLQAYSknqtedgirkelvtlqedkhSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRtQEELRE 174
Cdd:COG0497 252 ALERLA--------------------EYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEER-LALLRR 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952581430 175 LANKYNGAVNELKEFTEKLKQaegKQEEIQQKAlSEKKELQHRIDEMEEK-----EQLLQARIEA 234
Cdd:COG0497 311 LARKYGVTVEELLAYAEELRA---ELAELENSD-ERLEELEAELAEAEAElleaaEKLSAARKKA 371
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
458-656 |
3.61e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 458 LQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILREdkeiEIIETRDQLASTH 537
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA----ELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 538 KEIVALRQTAVEAATGREsdIAILQGELHKVQTELEQWRQTASEYES---EIFNLQTKLQLQTQQQKDKQKGEAVQLQGK 614
Cdd:COG4717 123 KLLQLLPLYQELEALEAE--LAELPERLEELEERLEELRELEEELEEleaELAELQEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1952581430 615 LDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQ 656
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
169-751 |
3.65e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 169 QEELRELANKYngAVNELKEFTEKLKQAEGKQEEIQQK---ALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNER 245
Cdd:TIGR02168 219 KAELRELELAL--LVLRLEELREELEELQEELKEAEEEleeLTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 246 LTALQVRLEQLQEKNIKDHNSIGIQVDDLLPKINGSTDKEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQN--NRISN 323
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEleSRLEE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 324 VEDMFE-----------------SHLENNQTTEEDLKNDSERFKATLIAEDDHTKVTE--------ETKLLKENQLEAKE 378
Cdd:TIGR02168 377 LEEQLEtlrskvaqlelqiaslnNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElkelqaelEELEEELEELQEEL 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 379 SDMSDTLSPSKDRSSEDTTDYQMDEQELNESLNKVSLLKDLLaearassRKHESELDHLKYELQCAHVQTGDSER--EKQ 456
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ-------ENLEGFSEGVKALLKNQSGLSGILGVlsELI 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 457 ELQQELKEAQELAISSKqkcfeMQALLEEERKTAKKQVE-----------------ESTRQIQALQAHLHKLQKDIEILR 519
Cdd:TIGR02168 530 SVDEGYEAAIEAALGGR-----LQAVVVENLNAAKKAIAflkqnelgrvtflpldsIKGTEIQGNDREILKNIEGFLGVA 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 520 EDKEIEIIETRDQLAS--THKEIVALRQTAVEAA--TGRESDIAILQGEL------------------HKVQTELEQWRQ 577
Cdd:TIGR02168 605 KDLVKFDPKLRKALSYllGGVLVVDDLDNALELAkkLRPGYRIVTLDGDLvrpggvitggsaktnssiLERRREIEELEE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 578 TASEYESEIfNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELRCAQQQS 657
Cdd:TIGR02168 685 KIEELEEKI-AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 658 VKLTKDASGLEVSRKALEVEVGTLKEQRLQ-----------------ETNGLRVKLAHAENETQKFQKQYEADQTMYLEL 720
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQlkeelkalrealdelraELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
650 660 670
....*....|....*....|....*....|.
gi 1952581430 721 KEKLDKTQKENESITDELENCKENLKLLQQK 751
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESE 874
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
111-523 |
4.18e-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: 40.26 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 111 ELVTLQEDKHSYE------------TTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRElanK 178
Cdd:pfam07888 5 ELVTLEEESHGEEggtdmllvvpraELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELES---R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 179 YNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQllqaRIEALQADNDFTNERLTALQVRLEQLQE 258
Cdd:pfam07888 82 VAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEA----RIRELEEDIKTLTQRVLERETELERMKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 259 KNIKDHNSIGIQVDDllpkingSTDKEHFLLKSGGDCSELFQQFIECKNKLKAPVEPTQnnrisnvedmfesHLENNQTT 338
Cdd:pfam07888 158 RAKKAGAQRKEEEAE-------RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVL-------------QLQDTITT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 339 EEDLKNDSERFKATLIAEDDHTKVTEETKLLKENQLEAKESDMSDTLSpSKDRSSEDTTDYQMDEQELNESLNKVSLlkd 418
Cdd:pfam07888 218 LTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAA-QRDRTQAELHQARLQAAQLTLQLADASL--- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 419 LLAEARASSRKHESELdhlkyeLQCAHVQTGDSEREKQELQQELKEAQElAISSKQKcfeMQALLEEERKTAKKQVEEST 498
Cdd:pfam07888 294 ALREGRARWAQERETL------QQSAEADKDRIEKLSAELQRLEERLQE-ERMEREK---LEVELGREKDCNRVQLSESR 363
|
410 420
....*....|....*....|....*
gi 1952581430 499 RQIQALQAHLHKLQKDIEILREDKE 523
Cdd:pfam07888 364 RELQELKASLRVAQKEKEQLQAEKQ 388
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
53-562 |
4.28e-03 |
|
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: 40.48 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 53 MLEQKLATLQRLLANTQEASDSSWQALIDEDRLLSRLEVMGNQLQAYSKNQT--EDGIRKELVTLQEDKHSYETTAKESL 130
Cdd:pfam05483 262 LLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKalEEDLQIATKTICQLTEEKEAQMEELN 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 131 RRVLQEKIEVvrklSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQ------ 204
Cdd:pfam05483 342 KAKAAHSFVV----TEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKkilaed 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 205 QKALSEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRlEQLQEKNIKDHNSIgiQVDDLLPKINGSTDK 284
Cdd:pfam05483 418 EKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTS-EEHYLKEVEDLKTE--LEKEKLKNIELTAHC 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 285 EHFLLKSggdcSELFQQFIECKNKLKAPVEPTQNNRisNVEDMFESHLENNQTTEEDLKNDSERFKATLIAEDDHTKV-- 362
Cdd:pfam05483 495 DKLLLEN----KELTQEASDMTLELKKHQEDIINCK--KQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCkl 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 363 --TEETKLLKENQLEAKESDMSDTLSPSKD--RSSEDTTDYQMDEQELNESLNKVSLLKD------------LLAEARAS 426
Cdd:pfam05483 569 dkSEENARSIEYEVLKKEKQMKILENKCNNlkKQIENKNKNIEELHQENKALKKKGSAENkqlnayeikvnkLELELASA 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 427 SRKHESELDHLKYELQCAHVQT----GDSEREKQELQQELKEAQELAISSKQKCFEMQALLEEERKTAKKQVEESTRQIQ 502
Cdd:pfam05483 649 KQKFEEIIDNYQKEIEDKKISEekllEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELG 728
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 503 ALQAHlhklQKDIEILREDKEIEIIETRDQLASTHKEIVALRQTAVEAATGRESDIAILQ 562
Cdd:pfam05483 729 LYKNK----EQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILK 784
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
24-235 |
4.92e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 24 KVAANSPSMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDsswqaliDEDRLLSRLEVMGNQLQAYSKNQ 103
Cdd:COG4717 60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA-------ELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 104 TEDGIRKELVTLQEdkhsyettAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMND-RTQEELRELANKYNGA 182
Cdd:COG4717 133 ELEALEAELAELPE--------RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEEL 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1952581430 183 VNELKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDEMEEKEQLLQARIEAL 235
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAA 257
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
403-586 |
5.23e-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: 39.75 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 403 EQELNESLNKVSLLKDLLAEARASSRKHESELDHLKYELqcahvqtGDSEREKQELQQELKEAQELAISSKQKCFEMQAL 482
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-------AALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 483 LEEERKTAKKQV---------------------EESTRQIQALQAHLHKLQKDIEILREDKEI------EIIETRDQLAS 535
Cdd:COG4942 99 LEAQKEELAELLralyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAElaalraELEAERAELEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1952581430 536 THKEIVALRQTAVEAATGRESDIAILQGELHKVQTELEQWRQTASEYESEI 586
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
418-651 |
5.35e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 418 DLLAEARASSRKHES---ELDHLKYELQCAHVQTGdsEREKQELQQELKEAQELAISSKQKcfemQALLEEERKTAKKQV 494
Cdd:COG4913 252 ELLEPIRELAERYAAareRLAELEYLRAALRLWFA--QRRLELLEAELEELRAELARLEAE----LERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 495 EESTRQIQALQ-AHLHKLQKDIEILREDKEiEIIETRDQLASthkeivALRQTAVEAATGREsdiailqgELHKVQTELE 573
Cdd:COG4913 326 DELEAQIRGNGgDRLEQLEREIERLERELE-ERERRRARLEA------LLAALGLPLPASAE--------EFAALRAEAA 390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581430 574 QWRQTASEYESEIFNlqtklqlqtqqqkdkqkgEAVQLQGKLDELQKQSNGLKNDCDSLRQEKVLLTEKLQWFEEELR 651
Cdd:COG4913 391 ALLEALEEELEALEE------------------ALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
|
| prfA |
PRK00591 |
peptide chain release factor 1; Validated |
453-504 |
5.59e-03 |
|
peptide chain release factor 1; Validated
Pssm-ID: 234801 [Multi-domain] Cd Length: 359 Bit Score: 39.68 E-value: 5.59e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1952581430 453 REKQELQQELKEAQELAISSKQKcfEMQALLEEERKTAKKQVEESTRQIQAL 504
Cdd:PRK00591 52 REYKQAQEDLEEAKEMLEEESDP--EMREMAKEELKELEERLEELEEELKIL 101
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
406-751 |
6.17e-03 |
|
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: 40.00 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 406 LNESLNKVSLLKDLLAEAR-ASSRKHESELDHLKYELQCAHVQTGDSEREKQELQQELKEAQELAISSKQKCFEMQAL-L 483
Cdd:TIGR04523 144 LTEIKKKEKELEKLNNKYNdLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISeL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 484 EEERKTAKKQVEESTRQIQALQAHLHKLQKDIEILR----------EDKEIEIIETRDQLASTHKEIVALRQTAVEAATG 553
Cdd:TIGR04523 224 KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKdeqnkikkqlSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 554 RESDI-AILQGELHKVQTELEQWRQTASEYESEIfNLQTKLQLQTQQQKDKQKGEAVQLQGKLDELQKQSNGLKNDCDSL 632
Cdd:TIGR04523 304 KEQDWnKELKSELKNQEKKLEEIQNQISQNNKII-SQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 633 RQEKVLLTEKLQWFEEELRCAQQQSVKLTKDASGLEVSRKALEVEVGTLKEQRLQ----------ETNGLRVKLAHAENE 702
Cdd:TIGR04523 383 KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKnnseikdltnQDSVKELIIKNLDNT 462
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1952581430 703 TQKFQKQYEADQTMYLELKEKLDKTQKENESITDELENCKENLKLLQQK 751
Cdd:TIGR04523 463 RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK 511
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
70-259 |
6.19e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 70 EASDSSWQALIdEDRLLSRLEVMGNQLQAYSKNQTEDGIrKELVTLQEDKHSYETTAKEsLRRVLQEKIEVVRKLSEVER 149
Cdd:COG4717 33 EAGKSTLLAFI-RAMLLERLEKEADELFKPQGRKPELNL-KELKELEEELKEAEEKEEE-YAELQEELEELEEELEELEA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 150 SLSNTEDECTHLKEMND---------RTQEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQKALSEKKELQHRIDE 220
Cdd:COG4717 110 ELEELREELEKLEKLLQllplyqeleALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA 189
|
170 180 190
....*....|....*....|....*....|....*....
gi 1952581430 221 MEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEK 259
Cdd:COG4717 190 TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
182-259 |
7.29e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 7.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952581430 182 AVNELKEFTEKLKQAEGKQEEIQQkalsEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTALQVRLEQLQEK 259
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQA----ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
169-259 |
7.47e-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: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 169 QEELRELANKYNGAVNELKEFTEKLKQAEGKQEEIQQkalsEKKELQHRIDEMEEKEQLLQARIEALQADNDFTNERLTA 248
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK----QLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90
....*....|.
gi 1952581430 249 LQVRLEQLQEK 259
Cdd:COG4942 95 LRAELEAQKEE 105
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
31-197 |
8.50e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.61 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 31 SMYSQELFQLSQYLQEALHREQMLEQKLATLQRLLANTQEASDSSWQALIdEDRLLSRLEVMGNQLQAYSKNQTEDGIRk 110
Cdd:COG3206 215 KLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPV-IQQLRAQLAELEAELAELSARYTPNHPD- 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952581430 111 eLVTLQEDKHSYETTAKESLRRVLQEKIEVVRKLSEVERSLSNTEDECTHLKEMNDRTQEELRELANKYNGAVNELKEFT 190
Cdd:COG3206 293 -VIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLL 371
|
....*..
gi 1952581430 191 EKLKQAE 197
Cdd:COG3206 372 QRLEEAR 378
|
|
| |
