|
Name |
Accession |
Description |
Interval |
E-value |
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
444-640 |
7.88e-86 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 266.93 E-value: 7.88e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 444 YSQKDLDAVVNVMQQEN-------LELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIaedKIQKVLKER 516
Cdd:pfam05010 1 YSQKDMDAALEKARNEIeekeleiNELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHA---EIQKVLEEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 517 DQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSK 596
Cdd:pfam05010 78 DQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 755511422 597 AQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICDDLI 640
Cdd:pfam05010 158 AKAETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
426-631 |
1.44e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 426 VLEPRGLLPAEPIVDVLKYSQKDLDAVVNVMQQENLELKSKYEDLNTKYLEMGKSVDEFEKiaykSLEEAEKQRELKEIA 505
Cdd:COG3883 5 ALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA----EIDKLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 506 EDKIQKVLKER-----------DQLNADLNSmeKSFSDLFKRF-------EKRKEVIEGYQKNEESLKKYVGEcivkIEK 567
Cdd:COG3883 81 IEERREELGERaralyrsggsvSYLDVLLGS--ESFSDFLDRLsalskiaDADADLLEELKADKAELEAKKAE----LEA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755511422 568 EGQRYQALKIHAEEKLRLANEEIAQvhskAQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDE 631
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAE----QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
441-634 |
1.07e-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: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 441 VLKY------SQKDLDAVvnvmqQENL--------ELKSKYEDLNT------KYLEMGKSVDEFEKIAY-KSLEEAEKQR 499
Cdd:COG1196 167 ISKYkerkeeAERKLEAT-----EENLerledilgELERQLEPLERqaekaeRYRELKEELKELEAELLlLKLRELEAEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 500 ELkeiAEDKIQKVLKERDQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKiHA 579
Cdd:COG1196 242 EE---LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE-ER 317
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 755511422 580 EEKLRLANEEIAQVHSKAQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTR 634
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
442-634 |
1.10e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 442 LKYSQKDLDAVVNVMQQENLELKSKYEDLNTKYLEMG--KSVDEFEKI---------AYKSLEEAEKQREL-KEIAEDKI 509
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipEIQAELSKLeeevsrieaRLREIEQKLNRLTLeKEYLEKEI 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 510 QKVLKERDQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGEcivkIEKEGQRyqalkihAEEKLRLANEE 589
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD----LKKERDE-------LEAQLRELERK 904
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 755511422 590 IAQVhsKAQAEVLALQASLRKAQMQNhslemtLEQKTKEIDELTR 634
Cdd:TIGR02169 905 IEEL--EAQIEKKRKRLSELKAKLEA------LEEELSEIEDPKG 941
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
468-646 |
1.16e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 468 EDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKSFSDL---FKRFEKRKEVI 544
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELreeLEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 545 EGYQKNEEsLKKYVGECIVKIEKEGQRYQALKiHAEEKLRLANEEIAQVHSKAQAEV----LALQASLRKAQMQNHSLEM 620
Cdd:COG4717 129 PLYQELEA-LEAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEELEELLeqlsLATEEELQDLAEELEELQQ 206
|
170 180
....*....|....*....|....*.
gi 755511422 621 TLEQKTKEIDELTRICDDLISKMEKI 646
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQL 232
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
462-634 |
1.49e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 462 ELKSKYEDLNtKYLEMGKSVDEFEKIA--YKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKSFSD-LFKRFE 538
Cdd:PTZ00121 1402 EDKKKADELK-KAAAAKKKADEAKKKAeeKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADeAKKKAE 1480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 539 KRKEVIEGYQKNEESLKKyvGECIVKIEKEGQRYQALKiHAEEKLRLanEEIAQVHSKAQAEVLALQASLRKAQMQNHSL 618
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKK--ADEAKKAAEAKKKADEAK-KAEEAKKA--DEAKKAEEAKKADEAKKAEEKKKADELKKAE 1555
|
170
....*....|....*.
gi 755511422 619 EMTLEQKTKEIDELTR 634
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKK 1571
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
462-645 |
1.65e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 462 ELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIAEDKiqkvlKERDQLNADlnSMEKSFSDLFKRFEKRK 541
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK-----AEAAEKKKE--EAKKKADAAKKKAEEKK 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 542 EVIEGYQKNEESLKKyvGECIVKIEKEGQRYQALKIHAEEKlRLANEEIAQVHSKAQAEVLALQA-SLRKAQ-MQNHSLE 619
Cdd:PTZ00121 1392 KADEAKKKAEEDKKK--ADELKKAAAAKKKADEAKKKAEEK-KKADEAKKKAEEAKKADEAKKKAeEAKKAEeAKKKAEE 1468
|
170 180
....*....|....*....|....*.
gi 755511422 620 MTLEQKTKEIDELTRICDDLISKMEK 645
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKKKAEE 1494
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
445-625 |
2.83e-05 |
|
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: 47.36 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 445 SQKDLDA-VVNVMQQENLELKSKYEDLNtkylemgKSVDEFEKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADL 523
Cdd:TIGR02168 330 SKLDELAeELAELEEKLEELKEELESLE-------AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 524 NSMEKSFSDLFKRFEKRKEVIEGYQKN-EESLKKYVGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQvhskAQAEVL 602
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE----AEQALD 478
|
170 180
....*....|....*....|...
gi 755511422 603 ALQASLRKAQMQNHSLEMTLEQK 625
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQENL 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
448-632 |
3.48e-05 |
|
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: 47.36 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 448 DLDAVVNVMQQENLELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIAED-------KIQKVLKERDQLN 520
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAeltllneEAANLRERLESLE 830
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 521 ADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLkkyvGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSKAQA- 599
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEEL----EELIEELESELEALLNERASLEEALALLRSELEELSEELREl 906
|
170 180 190
....*....|....*....|....*....|....*
gi 755511422 600 --EVLALQASLRKAQMQNHSLEMTLEQKTKEIDEL 632
Cdd:TIGR02168 907 esKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
438-644 |
6.22e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 46.10 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 438 IVDVLKYSQKDLDAVVNVM---QQENLELKSKYEDLNTKYLEMGKSVDEFEKIAYKSL-EEAEKQRELKEIAEDKIQKVL 513
Cdd:COG5185 213 GNLGSESTLLEKAKEIINIeeaLKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLgENAESSKRLNENANNLIKQFE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 514 KERDQL--NADLNSMEKSFSDL---FKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALK-----IHAEEKL 583
Cdd:COG5185 293 NTKEKIaeYTKSIDIKKATESLeeqLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKeeienIVGEVEL 372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755511422 584 RLANEEI----AQVHSKAQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICDDLISKME 644
Cdd:COG5185 373 SKSSEELdsfkDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNE 437
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
457-634 |
8.13e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 8.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 457 QQENLELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKSFSDLFKR 536
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 537 FEKRKEVIEG-----YQKNEESLKKYV--GECIVKIEKEGQRYQALKIHAE---EKLRLANEEIAQVHSKAQAEVLALQA 606
Cdd:COG4942 99 LEAQKEELAEllralYRLGRQPPLALLlsPEDFLDAVRRLQYLKYLAPARReqaEELRADLAELAALRAELEAERAELEA 178
|
170 180
....*....|....*....|....*...
gi 755511422 607 SLRKAQMQNHSLEMTLEQKTKEIDELTR 634
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEK 206
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
462-612 |
8.61e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 8.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 462 ELKSKYEDLN------TKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEiaedKIQKVLKERDQLNADLNSMEKSFSDLFK 535
Cdd:PRK03918 277 ELEEKVKELKelkekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN----GIEERIKELEEKEERLEELKKKLKELEK 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 536 RFEKRKEVIEGYQK------NEESLKKYV-GECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSKAQAEVLALQAsL 608
Cdd:PRK03918 353 RLEELEERHELYEEakakkeELERLKKRLtGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE-L 431
|
....
gi 755511422 609 RKAQ 612
Cdd:PRK03918 432 KKAK 435
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
462-645 |
1.35e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 462 ELKSKYEDLntKYLEMGKSVDEFEKIAykslEEAEKQRELKEIAE------DKIQKVLKERDQLNADLNSMEKSFSDLFK 535
Cdd:PTZ00121 1287 EEKKKADEA--KKAEEKKKADEAKKKA----EEAKKADEAKKKAEeakkkaDAAKKKAEEAKKAAEAAKAEAEAAADEAE 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 536 RFEKRKEVIEgyQKNEESLKKyvGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSKAQAEVLALQA-SLRKA-QM 613
Cdd:PTZ00121 1361 AAEEKAEAAE--KKKEEAKKK--ADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAeEKKKAdEA 1436
|
170 180 190
....*....|....*....|....*....|..
gi 755511422 614 QNHSLEMTLEQKTKEIDELTRICDDLISKMEK 645
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
481-632 |
1.57e-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: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 481 VDEFEKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKsfsdlFKRFEKRKEVIEGY------QKNEESL 554
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAER-----YQALLKEKREYEGYellkekEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 555 KKYVGEcIVKIEKEGQ----RYQALKIHAEEKLRLANEEIAQVHSKAQAEVLALQASLRKAQMQNHSLEMTLEQKTKEID 630
Cdd:TIGR02169 240 EAIERQ-LASLEEELEklteEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELE 318
|
..
gi 755511422 631 EL 632
Cdd:TIGR02169 319 DA 320
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
438-639 |
2.42e-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: 44.66 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 438 IVDVLKYSQKDLDAVVNVMQQENLEL---KSKYEDLNTKYLEMgKSVDEF-EKIAYKSLEEAEKQRELKEIAEDKIQKVL 513
Cdd:TIGR01612 756 ILEDFKNKEKELSNKINDYAKEKDELnkyKSKISEIKNHYNDQ-INIDNIkDEDAKQNYDKSKEYIKTISIKEDEIFKII 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 514 KERDQLNAD------------------LNSMEKSFSDLFKRF--EKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQ 573
Cdd:TIGR01612 835 NEMKFMKDDflnkvdkfinfennckekIDSEHEQFAELTNKIkaEISDDKLNDYEKKFNDSKSLINEINKSIEEEYQNIN 914
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755511422 574 ALKiHAEEKLRL---ANEEIAQVHSKAQAEVLALQASLRKAQMQNhSLEMTLEQK-----TKEIDELTRICDDL 639
Cdd:TIGR01612 915 TLK-KVDEYIKIcenTKESIEKFHNKQNILKEILNKNIDTIKESN-LIEKSYKDKfdntlIDKINELDKAFKDA 986
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
491-646 |
5.01e-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: 43.51 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 491 SLEEAEKQRelkEIAEDKIQKVLKERDQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQ 570
Cdd:TIGR02168 692 KIAELEKAL---AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 571 RY---QALKIHAEEKLRLANEEIAQV----------HSKAQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICD 637
Cdd:TIGR02168 769 RLeeaEEELAEAEAEIEELEAQIEQLkeelkalreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848
|
....*....
gi 755511422 638 DLISKMEKI 646
Cdd:TIGR02168 849 ELSEDIESL 857
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
446-646 |
5.35e-04 |
|
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: 43.09 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 446 QKDLDAVVNVMQQENLELKSKYEDLNTKYLEMGKSVDEFEK------IAYKSL---------EEAEKQRELKEIAEDKIQ 510
Cdd:TIGR04523 428 IERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETqlkvlsRSINKIkqnleqkqkELKSKEKELKKLNEEKKE 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 511 -----KVLKER--------DQLNADLNSMEKSFSDLFKRFEKRKEViegyqKNEESLKKYVGECIVKIEKegqryqaLKi 577
Cdd:TIGR04523 508 leekvKDLTKKisslkekiEKLESEKKEKESKISDLEDELNKDDFE-----LKKENLEKEIDEKNKEIEE-------LK- 574
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755511422 578 HAEEKLRLANEEIAQVHSKAQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICDDLISKMEKI 646
Cdd:TIGR04523 575 QTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
440-639 |
5.52e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 440 DVLKYSQKDLDAVVNVMQQENLELKSKYEDLNtkylEMGKSVDEFEKIayKSLEEAEKQRelkeiAEDKIQKVLKERDQL 519
Cdd:PRK01156 169 DKLKDVIDMLRAEISNIDYLEEKLKSSNLELE----NIKKQIADDEKS--HSITLKEIER-----LSIEYNNAMDDYNNL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 520 NADLNSMeKSFSDLFKRFEKRKEVIEG-----------YQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKlrlane 588
Cdd:PRK01156 238 KSALNEL-SSLEDMKNRYESEIKTAESdlsmeleknnyYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENK------ 310
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 755511422 589 eiAQVHSKAQAEVLALQASLRKAQMQnHSLEMTLEQKTKEIDELTRICDDL 639
Cdd:PRK01156 311 --KQILSNIDAEINKYHAIIKKLSVL-QKDYNDYIKKKSRYDDLNNQILEL 358
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
160-310 |
6.23e-04 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 43.10 E-value: 6.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 160 VTPPIEPVLEPSHQGLEPVLESELVTPPVEPVLEPSHQE----------LEPVLESELVTPPIEPVLEPSHQGLEPVLDS 229
Cdd:PRK10811 847 VVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSApvveavaevvEEPVVVAEPQPEEVVVVETTHPEVIAAPVTE 926
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 230 E--LVTPPIEPVLEPSHQGLEPVLESELVTPPIEPVLEPSHqglEPVLDSELVTPPIEPVLEPSHQglePVLDSELVTPP 307
Cdd:PRK10811 927 QpqVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAE---VVVAEPEVVAQPAAPVVAEVAA---EVETVTAVEPE 1000
|
...
gi 755511422 308 IEP 310
Cdd:PRK10811 1001 VAP 1003
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
457-645 |
6.29e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.92 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 457 QQENLELKSKYEDLNTKYLE----MGKSVDEFEKIayksLEEAEKQR----ELKE----IAEDKIQKVLKER-DQLNADL 523
Cdd:pfam06160 120 REEVEELKDKYRELRKTLLAnrfsYGPAIDELEKQ----LAEIEEEFsqfeELTEsgdyLEAREVLEKLEEEtDALEELM 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 524 NSMEKSFSDLFKRFEKR-KEVIEGYQKNEEslKKY------VGECIVKIEKEGQRYQA----LKI-HAEEKLRLANEEIA 591
Cdd:pfam06160 196 EDIPPLYEELKTELPDQlEELKEGYREMEE--EGYalehlnVDKEIQQLEEQLEENLAllenLELdEAEEALEEIEERID 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 592 QVHSKAQAEVLA----------LQASLRKAQMQNHSL--EMTLEQKT---------------KEIDELTRICDDLISKME 644
Cdd:pfam06160 274 QLYDLLEKEVDAkkyveknlpeIEDYLEHAEEQNKELkeELERVQQSytlnenelervrgleKQLEELEKRYDEIVERLE 353
|
.
gi 755511422 645 K 645
Cdd:pfam06160 354 E 354
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
458-646 |
6.70e-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: 6.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 458 QENLElksKYEDLNTkylEMGKSVDEFEKIAYKSLEEAEKQRELKEI------------------AEDKIQKVLKERDQL 519
Cdd:TIGR02168 185 RENLD---RLEDILN---ELERQLKSLERQAEKAERYKELKAELRELelallvlrleelreeleeLQEELKEAEEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 520 NADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKkyvgECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSK--- 596
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALA----NEISRLEQQKQILRERLANLERQLEELEAQLEELESKlde 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755511422 597 --------------AQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICDDLISKMEKI 646
Cdd:TIGR02168 335 laeelaeleekleeLKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
462-646 |
9.13e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 9.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 462 ELKSKYEDLNTKYLEMGKSVDEF----EKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSME--KSFSDLFK 535
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELkkaeEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEeaKKAEELKK 1709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 536 RFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKLRLAneeiaqvHSKAQAEVLALQASLRKAQMQN 615
Cdd:PTZ00121 1710 KEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIA-------HLKKEEEKKAEEIRKEKEAVIE 1782
|
170 180 190
....*....|....*....|....*....|.
gi 755511422 616 HSLEMTLEQKTKEIDELTRicdDLISKMEKI 646
Cdd:PTZ00121 1783 EELDEEDEKRRMEVDKKIK---DIFDNFANI 1810
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
462-646 |
1.10e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 462 ELKSKYEDLNtKYLEMGKSVDEFEKIAYKSLEeaEKQRELKEIaEDKIQKVLKERDQLNADLnsmeksfsdlfKRFEKRK 541
Cdd:PRK03918 173 EIKRRIERLE-KFIKRTENIEELIKEKEKELE--EVLREINEI-SSELPELREELEKLEKEV-----------KELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 542 EVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEkLRLANEEIAQVHSKAQaEVLALQASLRKAQMQNHSLEMT 621
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE-LEEKVKELKELKEKAE-EYIKLSEFYEEYLDELREIEKR 315
|
170 180
....*....|....*....|....*
gi 755511422 622 LEQKTKEIDELTRICDDLISKMEKI 646
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERL 340
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
462-646 |
1.69e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 462 ELKSKYEDLNTKYLEmgKSVDEFEKIAYKSLEEAEKQRELKEIAEdKIQKVLKERDQLNADLNSMEKSFSDLFKR----- 536
Cdd:PRK03918 507 ELEEKLKKYNLEELE--KKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKEleelg 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 537 FEKRKEVIEGYQKNEESLKKYVGecIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSKAQAEVLALQASLRKAQMQNH 616
Cdd:PRK03918 584 FESVEELEERLKELEPFYNEYLE--LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEY 661
|
170 180 190
....*....|....*....|....*....|....*...
gi 755511422 617 --------SLEMTLEQKTKEIDELTRICDDLISKMEKI 646
Cdd:PRK03918 662 eelreeylELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
|
| DUF4407 |
pfam14362 |
Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins ... |
431-609 |
2.06e-03 |
|
Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins in this family are typically between 366 and 597 amino acids in length. There is a single completely conserved residue R that may be functionally important.
Pssm-ID: 464151 [Multi-domain] Cd Length: 295 Bit Score: 40.70 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 431 GLLPAEPIVdvLKYSQKDLDAVVNVMQQEnlelkskyedlntkylemgksvdefekiaykslEEAEKQRELKEIAEDKIQ 510
Cdd:pfam14362 92 GVVISEPLE--LKIFEKEIDRELLEIQQE---------------------------------EADAAKAQLAAAYRARLA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 511 KVLKERDQLNADLNSMEKSFSDLFKrfEKRKEvIEGYQKNEESLKKYVGECIVK---IEKEGQRYQALKIHAEEKLRLAN 587
Cdd:pfam14362 137 ELEAQIAALDAEIDAAEARLDALQA--EARCE-LDGTPGTGTGVPGDGPVAKTKqaqLDAAQAELAALQAQNDARLAALR 213
|
170 180
....*....|....*....|..
gi 755511422 588 EEIAQVHSKAQAEVLALQASLR 609
Cdd:pfam14362 214 AELARLTAERAAARARSQAAID 235
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
479-592 |
2.16e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 479 KSVDEFEKIAYKSLEEAEKqrELKEIAEDKI----QKVLKERDQLNADLNSMEKSFSDLFKR--------------FEKR 540
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKK--EAEAIKKEALleakEEIHKLRNEFEKELRERRNELQKLEKRllqkeenldrklelLEKR 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 755511422 541 KEVIEGYQKNEESLKKYVGECIVKIEkegqryqalKIHAEEKLRLanEEIAQ 592
Cdd:PRK12704 109 EEELEKKEKELEQKQQELEKKEEELE---------ELIEEQLQEL--ERISG 149
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
23-274 |
2.35e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 41.22 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 23 PKLCGVAAPICNPSTgkaDWR-IPGAPWPD-CLAELKENVPPQSQAKATNVTFQTPPRDPqtHRILSPNMTNKREAPFGL 100
Cdd:PRK10263 344 PPVASVDVPPAQPTV---AWQpVPGPQTGEpVIAPAPEGYPQQSQYAQPAVQYNEPLQQP--VQPQQPYYAPAAEQPAQQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 101 QNDHCVFLQKENQRPLAPVDDAPVVQMAAEILRAEGELQEgiltssslsastslldselvtppiEPVLEPSHQGLEPVLE 180
Cdd:PRK10263 419 PYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAP------------------------QSTYQTEQTYQQPAAQ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 181 SELVTPPvEPVLEPSHQELEPVLESelvTPPIEPVLEPSHQGLEP-VLDSELVTPPIEPVlePshqglEPVLESELVTPP 259
Cdd:PRK10263 475 EPLYQQP-QPVEQQPVVEPEPVVEE---TKPARPPLYYFEEVEEKrAREREQLAAWYQPI--P-----EPVKEPEPIKSS 543
|
250
....*....|....*
gi 755511422 260 IEPVLEPSHQGLEPV 274
Cdd:PRK10263 544 LKAPSVAAVPPVEAA 558
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
115-292 |
2.82e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 40.79 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 115 PLAPVDDAPVV-QMAAEILRAEGELQEgiltssslSASTSLLDSELVTPPIEPVLEPSHqglEPVLESELVTPPVEPVlE 193
Cdd:PRK10811 846 PVVRPQDVQVEeQREAEEVQVQPVVAE--------VPVAAAVEPVVSAPVVEAVAEVVE---EPVVVAEPQPEEVVVV-E 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 194 PSHQEL--EPVLES-ELVTPPIEPVLEPSHQGLEPVLDSELVTPPIEPVLEPSHqglEPVLESELVTPPIEPVLEPSHQG 270
Cdd:PRK10811 914 TTHPEViaAPVTEQpQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAE---VVVAEPEVVAQPAAPVVAEVAAE 990
|
170 180
....*....|....*....|....*
gi 755511422 271 L--EPVLDSELVTPPI-EPVLEPSH 292
Cdd:PRK10811 991 VetVTAVEPEVAPAQVpEATVEHNH 1015
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
486-601 |
3.20e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 39.05 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 486 KIAYKSLEEAEKQRELKEIAEDKIQKvlkERDQLNADLNSMEKSFSDLFKRFEKRKEVIegyqkNEESLKKYVGEcIVKI 565
Cdd:COG2825 25 KIGVVDVQRILQESPEGKAAQKKLEK---EFKKRQAELQKLEKELQALQEKLQKEAATL-----SEEERQKKERE-LQKK 95
|
90 100 110
....*....|....*....|....*....|....*..
gi 755511422 566 EKEGQRYQALkihAEEKLRLA-NEEIAQVHSKAQAEV 601
Cdd:COG2825 96 QQELQRKQQE---AQQDLQKRqQELLQPILEKIQKAI 129
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
538-646 |
4.30e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 538 EKRKEVIEGYQKNEESLKKyvgECIVKIEKEgqrYQALKIHAEEKLRLANEEIAQVHSKAQAEVLAL---QASLRKAQMQ 614
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKK---EALLEAKEE---IHKLRNEFEKELRERRNELQKLEKRLLQKEENLdrkLELLEKREEE 111
|
90 100 110
....*....|....*....|....*....|..
gi 755511422 615 NHSLEMTLEQKTKEIDELTRICDDLISKMEKI 646
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
442-645 |
4.43e-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: 40.39 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 442 LKYSQKDLDAVVNVMQQENLELKSKYEDLNTKYLEmgksvdefekiayKSLEEAEKQRELKEIAEDKIQKVL-KERDQLN 520
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE-------------KESKISDLEDELNKDDFELKKENLeKEIDEKN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 521 ADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKegqryqalkihAEEKLRLANEEiaqvHSKAQAE 600
Cdd:TIGR04523 568 KEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISS-----------LEKELEKAKKE----NEKLSSI 632
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 755511422 601 VLALQASLRKAQMQNHSLEMTLEQ---KTKEID----ELTRICDDLISKMEK 645
Cdd:TIGR04523 633 IKNIKSKKNKLKQEVKQIKETIKEirnKWPEIIkkikESKTKIDDIIELMKD 684
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
442-639 |
5.60e-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: 39.95 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 442 LKYSQKDLDAVVNVMQQENLELKSKYEDLNTKYLEMGKSV------DEFEKIAYKSLEEAEKQRELKEIAEDKIQKVLKE 515
Cdd:pfam02463 267 LAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLErrkvddEEKLKESEKEKKKAEKELKKEKEEIEELEKELKE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 516 RDQLNADLNSMEKSFSDLFKRFEKRKEVIE----GYQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKLRLANEEIA 591
Cdd:pfam02463 347 LEIKREAEEEEEEELEKLQEKLEQLEEELLakkkLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKK 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 755511422 592 QVHSKAQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICDDL 639
Cdd:pfam02463 427 EELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLL 474
|
|
| DUF3829 |
pfam12889 |
Protein of unknown function (DUF3829); This is a small family of proteins from several ... |
459-645 |
6.30e-03 |
|
Protein of unknown function (DUF3829); This is a small family of proteins from several bacterial species, whose function is not known. It may, however, be related to the GvpL_GvpF family of proteins, pfam06386.
Pssm-ID: 432856 [Multi-domain] Cd Length: 283 Bit Score: 38.95 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 459 ENLELKSKYEDLNTKYLEMGKSVDEFEKIayksLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKSFSDLFKRFE 538
Cdd:pfam12889 64 AAAALKPAMPELDEAAKKYIAALEELAPT----LNEMDAYYDQKDYLDDDFAKGKELHPKLLAAYKAYAEAAKAFSAAID 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 539 K-----RKEVIEGYQKNEESLKKYVgecivkiekegqryQALKIHAEEKLRLANEeiaqvhskaqaevlalqaslrkaQM 613
Cdd:pfam12889 140 KvsderRKEELEAIKKDERMIKYYT--------------LNFMIEAKQLIDELNR-----------------------DK 182
|
170 180 190
....*....|....*....|....*....|..
gi 755511422 614 QNHSLEMTLEQKTKEIDELTRICDDLISKMEK 645
Cdd:pfam12889 183 ITAKNELDLAAFKAKLDDLEADLEAFEEASKN 214
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
478-646 |
6.41e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 478 GKSVDEFEKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNeeslkky 557
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 558 vgecIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHS---KAQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTR 634
Cdd:COG4372 82 ----LEELNEQLQAAQAELAQAQEELESLQEEAEELQEeleELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
|
170
....*....|..
gi 755511422 635 ICDDLISKMEKI 646
Cdd:COG4372 158 QLESLQEELAAL 169
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
491-616 |
7.04e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 38.51 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 491 SLEEAEK--QRELKEiAEDKIQKVLKERDQLNADLNSMEKSFSDLFKRFEKRKE-VIEGYQKNEESLKKYVGECIVKIEK 567
Cdd:pfam04012 19 KAEDPEKmlEQAIRD-MQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEkAQAALTKGNEELAREALAEKKSLEK 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 755511422 568 EGQRYQALKIHAE---EKLRLANEEIAQVHSKAQAEVLALQASLRKAQMQNH 616
Cdd:pfam04012 98 QAEALETQLAQQRsavEQLRKQLAALETKIQQLKAKKNLLKARLKAAKAQEA 149
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
456-632 |
7.16e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.64 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 456 MQQENLELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAE----KQRELKEIAEDKIQKVLKERDQLNADLNSMEKSFS 531
Cdd:TIGR00606 886 FEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEelisSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQ 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 532 DLFKRFEKRKEviegyqKNEESLKKYVGECivkiEKEGQRYqalkihaEEKLRLANEEIAQvhSKAQAEVLALQASLRKA 611
Cdd:TIGR00606 966 DGKDDYLKQKE------TELNTVNAQLEEC----EKHQEKI-------NEDMRLMRQDIDT--QKIQERWLQDNLTLRKR 1026
|
170 180
....*....|....*....|.
gi 755511422 612 QMQNHSLEMTLEQKTKEIDEL 632
Cdd:TIGR00606 1027 ENELKEVEEELKQHLKEMGQM 1047
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
462-645 |
7.79e-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: 39.65 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 462 ELKSKYEDLNTKYLEMGKSVDEFE---KIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKSFSDLFKRFE 538
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTaelQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511422 539 KRKEVIEGYQKNEESLKKYVGECIVKIEKEGQ----RYQALKIHAEEK------LRLANEEIAQVHSKAQAEVLALQASL 608
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEelkeELESLEAELEELeaeleeLESRLEELEEQLETLRSKVAQLELQI 395
|
170 180 190
....*....|....*....|....*....|....*..
gi 755511422 609 RKAQMQNHSLEMTLEQKTKEIDELTRICDDLISKMEK 645
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
|
|
| |
