|
Name |
Accession |
Description |
Interval |
E-value |
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1-561 |
0e+00 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 728.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 1 MLQEISIKDFAIIDQLEVNFYSGMTVLSGETGAGKSIIIDAVGLLAGGRGSSHFIRKGANKSILQGMFAIPTDGLTARVL 80
Cdd:COG0497 1 MLTELSIRNFALIDELELEFGPGLTVLTGETGAGKSILLDALGLLLGGRADASLVRHGADKAEVEAVFDLSDDPPLAAWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 81 DKFGIDHDDDTVILQRELYRNGRNVCRINGMLVNTNTLKQVGETLVDIYGQNEYQALMQPDKHIGLLDEFAGsnLKPTLK 160
Cdd:COG0497 81 EENGLDLDDGELILRREISADGRSRAFINGRPVTLSQLRELGELLVDIHGQHEHQSLLDPDAQRELLDAFAG--LEELLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 161 KYRNKYEKYLKLKKELNSKNKNEKEWAQRIDMLKYQVNEIEAADLTDGEEEDLIAERDRLNNFQAISDSLGRSFNDINGD 240
Cdd:COG0497 159 EYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAALQPGEEEELEEERRRLSNAEKLREALQEALEALSGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 241 ESiSPIDMIGDAMSALEDVERLDDEFKSISENVKNAYYTLQDASGEISNQIDTLEFDPDRLNEVEQRLNTIFELKRKYGD 320
Cdd:COG0497 239 EG-GALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEERLALLRRLARKYGV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 321 SIAQILKYYDKISGELAEMESDEKSGNNLEERYNAAVDELNHLGKELSKIRHQQAEKLTTEIHQQLADLYMDKTQFEVRF 400
Cdd:COG0497 318 TVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAAKKLEKAVTAELADLGMPNARFEVEV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 401 SnlPKDTFNRNGIEDVEFYIRTNPGEDMAPLAKIASGGELSRIMLALKTIFSRVQGVTSIVFDEVDTGVSGRVAQAIADK 480
Cdd:COG0497 398 T--PLEEPGPNGADQVEFLFSANPGEPPKPLAKVASGGELSRIMLALKVVLADKDAVPTLIFDEVDTGVGGRVAEAVGEK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 481 ISAIGQKSQVLCITHLPQVAAMADNHDFISKHVDaNNRTETSVQPLSGSERVKELARMLAGTTVTKLTMEHASELLNLAN 560
Cdd:COG0497 476 LARLARNHQVLCVTHLPQVAAMADHHFRVSKEVD-GGRTVTRVRPLDEEERVEEIARMLGGAEITEAALAHARELLALAA 554
|
.
gi 948929654 561 K 561
Cdd:COG0497 555 S 555
|
|
| recN |
TIGR00634 |
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ... |
1-556 |
0e+00 |
|
DNA repair protein RecN; All proteins in this family for which functions are known are ATP binding proteins involved in the initiation of recombination and recombinational repair. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273187 [Multi-domain] Cd Length: 563 Bit Score: 521.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 1 MLQEISIKDFAIIDQLEVNFYSGMTVLSGETGAGKSIIIDAVGLLAGGRGSSHFIRKGANKSILQGMFAIpTDGLTARVL 80
Cdd:TIGR00634 1 MLTELRINNFALIRVLTVEFERGLTVLTGETGAGKSMIIDALSLLGGQRAGASRVRSGENRAVVEGRFTT-ESLDDADYP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 81 DKFGID----HDDDTVILQRELYRNGRNVCRINGMLVNTNTLKQVGETLVDIYGQNEYQALMQPDKHIGLLDEFAGSNlk 156
Cdd:TIGR00634 80 ALQAIEleeeDEDGEVILRRSISRDGRSRAYLNGKPVSASSLLEFTSELLDLHGQHDQQLLFRPDEQRQLLDTFAGAN-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 157 PTLKKYRNKYEKYLKLKKELNSKNKNEKEWAQRIDMLKYQVNEIEAADLTDGEEEDLIAERDRLNNFQAISDSLGRSFND 236
Cdd:TIGR00634 158 EKVKAYRELYQAWLKARQQLKDRQQKEQELAQRLDFLQFQLEELEEADLQPGEDEALEAEQQRLSNLEKLRELSQNALAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 237 INGDESISPI-DMIGDAMSALEDVERLDDEFKSISENVKNAYYTLQDASGEISNQIDTLEFDPDRLNEVEQRLNTIFELK 315
Cdd:TIGR00634 238 LRGDVDVQEGsLLEGLGEAQLALASVIDGSLRELAEQVGNALTEVEEATRELQNYLDELEFDPERLNEIEERLAQIKRLK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 316 RKYGDSIAQILKYYDKISGELAEMESDEKSGNNLEERYNAAVDELNHLGKELSKIRHQQAEKLTTEIHQQLADLYMDKTQ 395
Cdd:TIGR00634 318 RKYGASVEEVLEYAEKIKEELDQLDDSDESLEALEEEVDKLEEELDKAAVALSLIRRKAAERLAKRVEQELKALAMEKAE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 396 FEVRF-SNLPKDTFNR---NGIEDVEFYIRTNPGEDMAPLAKIASGGELSRIMLALKTIFSRVQGVTSIVFDEVDTGVSG 471
Cdd:TIGR00634 398 FTVEIkTSLPSGAKARagaYGADQVEFLFSANTGEPVKPLAKVASGGELSRVMLALKVVLSSSAAVTTLIFDEVDVGVSG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 472 RVAQAIADKISAIGQKSQVLCITHLPQVAAMADNHDFISKHVdANNRTETSVQPLSGSERVKELARMLAGTTVTKLTMEH 551
Cdd:TIGR00634 478 ETAQAIAKKLAQLSERHQVLCVTHLPQVAAHADAHFKVEKEG-LDGRTATRVRPLSGEERVAELARMLAGLEKSDLTLAH 556
|
....*
gi 948929654 552 ASELL 556
Cdd:TIGR00634 557 AQELL 561
|
|
| PRK10869 |
PRK10869 |
recombination and repair protein; Provisional |
1-557 |
7.82e-117 |
|
recombination and repair protein; Provisional
Pssm-ID: 236781 [Multi-domain] Cd Length: 553 Bit Score: 357.32 E-value: 7.82e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 1 MLQEISIKDFAIIDQLEVNFYSGMTVLSGETGAGKSIIIDAVGLLAGGRGSSHFIRKGANKSILQGMFAIPTDGLTARVL 80
Cdd:PRK10869 1 MLAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEASMVRPGATRADLCARFSLKDTPAALRWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 81 DKFGIDhDDDTVILQRELYRNGRNVCRINGMLVNTNTLKQVGETLVDIYGQNEYQALMQPDKHIGLLDEFAGSNLkpTLK 160
Cdd:PRK10869 81 EDNQLE-DGNECLLRRVISSDGRSRGFINGTPVPLSQLRELGQLLIQIHGQHAHQLLLKPEHQKTLLDAYANETS--LLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 161 KYRNKYEKYLKLKKELNSKNKNEKEWAQRIDMLKYQVNEIEAADLTDGEEEDLIAERDRLNNFQAISDSLGRSFNDINGD 240
Cdd:PRK10869 158 EMRAAYQLWHQSCRDLAQHQQQSQERAARKQLLQYQLKELNEFAPQPGEFEQIDEEYKRLANSGQLLTTSQNALQLLADG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 241 ESISPIDMIGDAMSALEDVERLDDEFKSISENVKNAYYTLQDASGEISNQIDTLEFDPDRLNEVEQRLNTIFELKRKYGD 320
Cdd:PRK10869 238 EEVNILSQLYSAKQLLSELIGMDSKLSGVLDMLEEALIQIQEASDELRHYLDRLDLDPNRLAELEQRLSKQISLARKHHV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 321 SIAQILKYYDKISGELAEMESDEKSGNNLEERYNAAVDELNHLGKELSKIRHQQAEKLTTEIHQQLADLYMDKTQF--EV 398
Cdd:PRK10869 318 SPEELPQHHQQLLEEQQQLDDQEDDLETLALAVEKHHQQALETAQKLHQSRQRYAKELAQLITESMHELSMPHGKFtiDV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 399 RFSNlpkDTFNRNGIEDVEFYIRTNPGEDMAPLAKIASGGELSRIMLALKTIFSRVQGVTSIVFDEVDTGVSGRVAQAIA 478
Cdd:PRK10869 398 KFDP---EHLSADGADRIEFRVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVG 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 948929654 479 DKISAIGQKSQVLCITHLPQVAAMADNHDFISKHVDANNrTETSVQPLSGSERVKELARMLAGTTVTKLTMEHASELLN 557
Cdd:PRK10869 475 KLLRQLGESTQVMCVTHLPQVAGCGHQHFFVSKETDGGM-TETHMQPLDKKARLQELARLLGGSEVTRNTLANAKELLA 552
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
411-541 |
2.77e-66 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 216.68 E-value: 2.77e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 411 NGIEDVEFYIRTNPGEDMAPLAKIASGGELSRIMLALKTIFSRVQGVTSIVFDEVDTGVSGRVAQAIADKISAIGQKSQV 490
Cdd:cd03241 147 GGLDDVEFLFSTNPGEPLKPLAKIASGGELSRLMLALKAILARKDAVPTLIFDEIDTGISGEVAQAVGKKLKELSRSHQV 226
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 948929654 491 LCITHLPQVAAMADNHDFISKHVDaNNRTETSVQPLSGSERVKELARMLAG 541
Cdd:cd03241 227 LCITHLPQVAAMADNHFLVEKEVE-GGRTVTKVRELDKEERVEEIARMLSG 276
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
2-148 |
3.15e-54 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 185.10 E-value: 3.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 2 LQEISIKDFAIIDQLEVNFYSGMTVLSGETGAGKSIIIDAVGLLAGGRGSSHFIRKGANKSILQGMFAIPTDGLTARVLD 81
Cdd:cd03241 1 LLELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSLLLGGRASADLIRSGAEKAVVEGVFDISDEEEAKALLL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 948929654 82 KFGIDhDDDTVILQRELYRNGRNVCRINGMLVNTNTLKQVGETLVDIYGQNEYQALMQPDKHIGLLD 148
Cdd:cd03241 81 ELGIE-DDDDLIIRREISRKGRSRYFINGQSVTLKLLRELGSLLVDIHGQHDHQNLLNPERQLDLLD 146
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
435-504 |
2.44e-14 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 70.85 E-value: 2.44e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 948929654 435 ASGGELSRIMLALKTIFSRVQGVTSIVFDEVDTGVSGRVAQAIADKISAI-GQKSQVLCITHLPQVAAMAD 504
Cdd:cd03227 78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHlVKGAQVIVITHLPELAELAD 148
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
5-194 |
5.83e-08 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 52.88 E-value: 5.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 5 ISIKDFAIIDQLEVNFYSGMTVLSGETGAGKSIIIDAVGLLAGGRGSShfIRKGANKSILQGMFAIPTDGLTARVLD-KF 83
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSR--LKRKSGGGFVKGDIRIGLEGKGKAYVEiTF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 84 GIDHDDDTVILQRELYRNGRNVCRINGMLVNTNTLKQVGETLVDIYGQNEYQALMQPDKHIGLLDEFAGSNLKPTLKKYR 163
Cdd:pfam13476 79 ENNDGRYTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVFLGQEREEEFERKEKKERLEELE 158
|
170 180 190
....*....|....*....|....*....|.
gi 948929654 164 NKYEKYLKLKKELNsKNKNEKEWAQRIDMLK 194
Cdd:pfam13476 159 KALEEKEDEKKLLE-KLLQLKEKKKELEELK 188
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1-386 |
6.14e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 55.75 E-value: 6.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 1 MLQEISIKDF-AIIDQLEVNFYSGMTVLSGETGAGKSIIIDAVGLLAGGRGSSHF--------IRKGANKSILQGMFAIP 71
Cdd:pfam02463 1 YLKRIEIEGFkSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLrserlsdlIHSKSGAFVNSAEVEIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 72 TDGLTARVLDkfgidhDDDTVILQRELYRNGRNVCRINGMLVntnTLKQVGETLVD----------IYGQNEYQ--ALMQ 139
Cdd:pfam02463 81 FDNEDHELPI------DKEEVSIRRRVYRGGDSEYYINGKNV---TKKEVAELLESqgispeaynfLVQGGKIEiiAMMK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 140 PDKHIGLLDEFAGSNLKPTLKKYRNKYEKYLKLKKELNSKNKNEKEwaQRIDMLKYQVNEIEAADLTDGEEEDLIAER-- 217
Cdd:pfam02463 152 PERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKL--QELKLKEQAKKALEYYQLKEKLELEEEYLLyl 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 218 DRLNNFQAISDSLGRSFNDINGDESISPIDMIgDAMSALEDVERLDDEFKSISENVKNAYYTLQDASGEISNQIDTLEFD 297
Cdd:pfam02463 230 DYLKLNEERIDLLQELLRDEQEEIESSKQEIE-KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 298 PDRLNEVEQRLNTI-------FELKRKYGDSIAQILKYYDKISGELAEMESDEKSGNNLEERYNAAVDELNHLGKELSKI 370
Cdd:pfam02463 309 KVDDEEKLKESEKEkkkaekeLKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS 388
|
410
....*....|....*.
gi 948929654 371 RHQQAEKLTTEIHQQL 386
Cdd:pfam02463 389 AAKLKEEELELKSEEE 404
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
2-110 |
3.73e-07 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 52.47 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 2 LQEISIKDFAIIDQLEVNFYSGMTVLSGETGAGKSIIIDAVGLLAGGRG-----SSHFIRKGANKSILQGMfaiptdglt 76
Cdd:PRK00064 3 LTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYLLAPGRShrtarDKELIRFGAEAAVIHGR--------- 73
|
90 100 110
....*....|....*....|....*....|....
gi 948929654 77 arvldkfgIDHDDDTVILQRELYRNGRNVCRING 110
Cdd:PRK00064 74 --------VEKGGRELPLGLEIDKKGGRKVRING 99
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
2-115 |
2.06e-06 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 49.60 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 2 LQEISIKDFAIIDQLEVNFYSGMTVLSGETGAGKSIIIDAVGLLAGGRgsSH-------FIRKGAnksilqgmfaiPTDG 74
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGK--SHrtsrdkeLIRWGA-----------EEAK 67
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 948929654 75 LTARVldkfgiDHDDDTVILQRELYRNGRNVCRINGMLVNT 115
Cdd:cd03242 68 ISAVL------ERQGGELALELTIRSGGGRKARLNGIKVRR 102
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
1-70 |
1.43e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.16 E-value: 1.43e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 948929654 1 MLQEISIKDF-AIIDQLEVNFYSGMTVLSGETGAGKSIIIDAVGLLAGGRGS------SHFIRKGANKSILQGMFAI 70
Cdd:COG0419 1 KLLRLRLENFrSYRDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARsrsklrSDLINVGSEEASVELEFEH 77
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
4-62 |
4.98e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.89 E-value: 4.98e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 948929654 4 EISIKDFAII-DQLEVNFYSG-MTVLSGETGAGKSIIIDAVGLLAGGRgSSHFIRKGANKS 62
Cdd:cd03227 1 KIVLGRFPSYfVPNDVTFGEGsLTIITGPNGSGKSTILDAIGLALGGA-QSATRRRSGVKA 60
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
460-541 |
6.03e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 45.31 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 460 IVFDEVDTGVSGRVAQAIADKISAIGQKSQVLCITHLPQVAAMADNHDFIskHVDANNRTETSVQPLSGSERVKELARML 539
Cdd:COG4637 282 LCIEEPENGLHPDLLPALAELLREASERTQVIVTTHSPALLDALEPEEVL--VLEREDDGETRIRRLSDLELPEWLEGYS 359
|
..
gi 948929654 540 AG 541
Cdd:COG4637 360 LG 361
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
2-54 |
6.70e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 45.38 E-value: 6.70e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 948929654 2 LQEISIKDFAIIDQLEVNFYSGMTVLSGETGAGKSIIIDAVGLLAGGRGSSHF 54
Cdd:COG3593 3 LEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKF 55
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
17-399 |
1.47e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 17 EVNFYSGMTVLSGETGAGKSIIIDAVgLLAGGRGSSHFIRkgANKS---ILQGMFAIPTDglTARVLDKFGID----HDD 89
Cdd:TIGR02169 18 VIPFSKGFTVISGPNGSGKSNIGDAI-LFALGLSSSKAMR--AERLsdlISNGKNGQSGN--EAYVTVTFKNDdgkfPDE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 90 DTVILQRELYRNGR-NVCRINGMLVntnTLKQVGETLVD--IYGQNeYQALMQPD--KHIG--------LLDEFAG---- 152
Cdd:TIGR02169 93 LEVVRRLKVTDDGKySYYYLNGQRV---RLSEIHDFLAAagIYPEG-YNVVLQGDvtDFISmspverrkIIDEIAGvaef 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 153 -SNLKPTLKKYRNKYEKYLKLKKELNSKNKN------EKEWAQRIDMLKYQVNEIEAADLTdGEEEDLIAERDRLnnfQA 225
Cdd:TIGR02169 169 dRKKEKALEELEEVEENIERLDLIIDEKRQQlerlrrEREKAERYQALLKEKREYEGYELL-KEKEALERQKEAI---ER 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 226 ISDSLGRSFNDINgdesiSPIDMIGDAMSALEDVerLDDEFKSISENVKNAYYTLQ----DASGEISNQIDTLEFDPDRL 301
Cdd:TIGR02169 245 QLASLEEELEKLT-----EEISELEKRLEEIEQL--LEELNKKIKDLGEEEQLRVKekigELEAEIASLERSIAEKEREL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 302 NEVEQRLNTIFELKRKYGDSIAQI-------LKYYDKISGELAEMESD-EKSGNNLEE---RYNAAVDELNHLGKELSKI 370
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELereieeeRKRRDKLTEEYAELKEElEDLRAELEEvdkEFAETRDELKDYREKLEKL 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 948929654 371 RH----------------QQAEKLTTEIHQQLADLYMDKTQFEVR 399
Cdd:TIGR02169 398 KReinelkreldrlqeelQRLSEELADLNAAIAGIEAKINELEEE 442
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
8-389 |
2.33e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 8 KDFAiiDQLEVNFYSGMTVLSGETGAGKSIIIDAVGLLAGGRGSSHfIRKGanksilqGMFAIPTDGLTAR--------- 78
Cdd:TIGR02168 11 KSFA--DPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGEQSAKA-LRGG-------KMEDVIFNGSETRkplslaeve 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 79 -VLDKfgIDH-----DDDTVILQRELYRNGRNVCRINGMLVntnTLKQVGETLVD---------IYGQNEYQALMQ--PD 141
Cdd:TIGR02168 81 lVFDN--SDGllpgaDYSEISITRRLYRDGESEYFINGQPC---RLKDIQDLFLDtglgkrsysIIEQGKISEIIEakPE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 142 KHIGLLDEFAG-SNLK----PTLKKYRNKYEKYLKLKKELNSKNKN------EKEWAQRIDMLKYQVNEIEAADLTDgee 210
Cdd:TIGR02168 156 ERRAIFEEAAGiSKYKerrkETERKLERTRENLDRLEDILNELERQlkslerQAEKAERYKELKAELRELELALLVL--- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 211 eDLIAERDRLNNFQAISDSLGRSFNDING--DESISPIDMIGDAMSALED-VERLDDEFKSISENVKNAYYTLQDASGEI 287
Cdd:TIGR02168 233 -RLEELREELEELQEELKEAEEELEELTAelQELEEKLEELRLEVSELEEeIEELQKELYALANEISRLEQQKQILRERL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 288 SNQIDTLEFDPDRLNEVEQRLNTIFELKRKYGDSIAQILKYYDKISGELAEMESDEKsgnNLEERYNAAVDELNHLGKEL 367
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE---ELESRLEELEEQLETLRSKV 388
|
410 420
....*....|....*....|..
gi 948929654 368 SKIRHQQAeKLTTEIHQQLADL 389
Cdd:TIGR02168 389 AQLELQIA-SLNNEIERLEARL 409
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
2-61 |
3.04e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.21 E-value: 3.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 2 LQEISIKDF-AIIDQLEVNFYSGMTVLSGETGAGKSIIIDAV-----GLLA----GGRGSSHFIRKGANK 61
Cdd:cd03240 1 IDKLSIRNIrSFHERSEIEFFSPLTLIVGQNGAGKTTIIEALkyaltGELPpnskGGAHDPKLIREGEVR 70
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
131-504 |
1.37e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.88 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 131 QNEYQALMQPDKHIGLLDEFAGSNLKPTLKKYRNKYEKYLKLKKELNSKNKNEKEWAQRIDMLKYQVNEIEAADLTDGEE 210
Cdd:pfam02463 734 INEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEE 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 211 EDLIAERDRLNNFQAISDSLGRSFNDINGDESISpidmigDAMSALEDVERLDDE-FKSISENVKNA---YYTLQDASGE 286
Cdd:pfam02463 814 AELLEEEQLLIEQEEKIKEEELEELALELKEEQK------LEKLAEEELERLEEEiTKEELLQELLLkeeELEEQKLKDE 887
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 287 ISNQIDTLEFDPDRLNEVEQRLNTIFELKRKYGDSIAQILKYYDKISGELAEMESDEKSGNN--------LEERYNAAVD 358
Cdd:pfam02463 888 LESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEkeennkeeEEERNKRLLL 967
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 359 ELNHLGKELSKIRHQQAEKLT--TEIHQQLADLYM-DKTQFEVRFSNLPK------DTFNRNGIEDVEFYIRTNPGED-- 427
Cdd:pfam02463 968 AKEELGKVNLMAIEEFEEKEEryNKDELEKERLEEeKKKLIRAIIEETCQrlkeflELFVSINKGWNKVFFYLELGGSae 1047
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 428 ------------------MAPLAKIA-----SGGELSRIMLALktIFS--RVQGVTSIVFDEVDTGVSGRVAQAIADKIS 482
Cdd:pfam02463 1048 lrledpddpfsggieisaRPPGKGVKnldllSGGEKTLVALAL--IFAiqKYKPAPFYLLDEIDAALDDQNVSRVANLLK 1125
|
410 420
....*....|....*....|..
gi 948929654 483 AIGQKSQVLCITHLPQVAAMAD 504
Cdd:pfam02463 1126 ELSKNAQFIVISLREEMLEKAD 1147
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-392 |
1.66e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 1 MLQEISIKDFAIIDQLEVNFYSGMTVLSGETGAGKSIIIDAVGLLAGG----RGSSHFIRKGANKSILQGMFAIPTDG-L 75
Cdd:PRK01156 2 IIKRIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTdkrtEKIEDMIKKGKNNLEVELEFRIGGHVyQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 76 TARVLDKFGIDHDDDTVILqrelyRNGRNVCR--------INGMLVNTNtlKQVGETLVdIYGQNEYQALMQ--PDKHIG 145
Cdd:PRK01156 82 IRRSIERRGKGSRREAYIK-----KDGSIIAEgfddttkyIEKNILGIS--KDVFLNSI-FVGQGEMDSLISgdPAQRKK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 146 LLDEFAGSN--------LKPTLKKYRNKYEKYLKLKKELNSKN----KNEKEWAQRIDMLKYQVNEIEAADLT-DGEEED 212
Cdd:PRK01156 154 ILDEILEINslernydkLKDVIDMLRAEISNIDYLEEKLKSSNleleNIKKQIADDEKSHSITLKEIERLSIEyNNAMDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 213 LIAERDRLNNFQAISDSLGRSFNDINGDES-ISPIDMIGDAMSALED-VERLDDEFKSISENVKNAYYTLQDASGEISNQ 290
Cdd:PRK01156 234 YNNLKSALNELSSLEDMKNRYESEIKTAESdLSMELEKNNYYKELEErHMKIINDPVYKNRNYINDYFKYKNDIENKKQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 291 IDTLEFDPDRLNEVEQRLNtifELKRKYGDSIaQILKYYDKISGELAEMESDeksgnnlEERYNAAVDELNHLGKELSKI 370
Cdd:PRK01156 314 LSNIDAEINKYHAIIKKLS---VLQKDYNDYI-KKKSRYDDLNNQILELEGY-------EMDYNSYLKSIESLKKKIEEY 382
|
410 420
....*....|....*....|..
gi 948929654 371 RHQQaEKLTTEIHQQLADLYMD 392
Cdd:PRK01156 383 SKNI-ERMSAFISEILKIQEID 403
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
8-42 |
1.83e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 39.76 E-value: 1.83e-03
10 20 30
....*....|....*....|....*....|....*
gi 948929654 8 KDFAiiDQLEVNFYSGMTVLSGETGAGKSIIIDAV 42
Cdd:cd03278 10 KSFA--DKTTIPFPPGLTAIVGPNGSGKSNIIDAI 42
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
1-46 |
2.64e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 40.30 E-value: 2.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 948929654 1 MLQEISIKDFAIIDQLEVNFySGMTVLSGETGAGKSIIIDAVGLLA 46
Cdd:COG4637 1 MITRIRIKNFKSLRDLELPL-GPLTVLIGANGSGKSNLLDALRFLS 45
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
22-42 |
8.71e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.88 E-value: 8.71e-03
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
259-505 |
9.98e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 38.90 E-value: 9.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 259 VERLDDEFKSIS---ENVKNAYYTLQDASGEISNQIDTLEfdpDRLNEVEQRLNTIFELKRKYGDSIAQILKY------Y 329
Cdd:TIGR02169 877 LRDLESRLGDLKkerDELEAQLRELERKIEELEAQIEKKR---KRLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsL 953
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 330 DKISGEL----AEMESDEKSGNNLEERYNAAVDELNHLGKELSKIRHQQAE--KLTTEIHQQLADLYMD-----KTQFEV 398
Cdd:TIGR02169 954 EDVQAELqrveEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAilERIEEYEKKKREVFMEafeaiNENFNE 1033
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948929654 399 RFSNL-----------PKDTFNrNGIEdvefyIRTNPGEDmaPLAKIA--SGGELSRIMLALKTIFSRVQGVTSIVFDEV 465
Cdd:TIGR02169 1034 IFAELsggtgelilenPDDPFA-GGLE-----LSAKPKGK--PVQRLEamSGGEKSLTALSFIFAIQRYKPSPFYAFDEV 1105
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 948929654 466 DTGVSGRVAQAIADKISAIGQKSQVLCITHLPQVAAMADN 505
Cdd:TIGR02169 1106 DMFLDGVNVERVAKLIREKAGEAQFIVVSLRSPMIEYADR 1145
|
|
| |
