|
Name |
Accession |
Description |
Interval |
E-value |
| Angiomotin_C |
pfam12240 |
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ... |
482-687 |
8.11e-94 |
|
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 and 211 amino acids in length. This family is the C terminal region of angiomotin. Angiomotin regulates the action of angiogenesis inhibitor angiostatin. The C terminal region of angiomotin appears to be involved in directing the protein chemotactically.
Pssm-ID: 463503 [Multi-domain] Cd Length: 200 Bit Score: 291.29 E-value: 8.11e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 482 YVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQAGAPGGSSGsggspELSALRLSEQLREKEEQILA 561
Cdd:pfam12240 1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPS-----EYSAPALMELLREKEERILA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 562 LEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHSPQPSPSSSFNEGLLTGGHRHQEMESRLKVLHAQILEKDA 641
Cdd:pfam12240 76 LEADMTKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSYDSSFNEELLLANRRCQEMENRIKNLHAQILEKDA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1394533522 642 VIKVLQQRSRRDPGKAIQGSLRPAKSVPSVFaAAAAGTQGWQGLSS 687
Cdd:pfam12240 156 MIKVLQQRSRKDPGKTDQQSLRPARSVPSIS-AAATGLHSRQTSLS 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
312-581 |
2.81e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 312 AQMEAVLRENARLQRDNERLQRELES-SAEKAGRIEKLESEIQRLSEAHESLTRASSKREALEKtmrnkmdsEMRRLQDF 390
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAElEAELEELRLELEELELELEEAQAEEYELLAELARLEQ--------DIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 391 NRDLRERLESANRRLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLEQALGNAQGRAA 470
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 471 RAEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQAGAPGGSSGSGGSPELSALRLSE 550
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270
....*....|....*....|....*....|.
gi 1394533522 551 QLREKEEQILALEADMTKWEQKYLEERAMRQ 581
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
309-704 |
7.08e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 7.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 309 AHLAQMEAVLRE-NARLqrdnERLQRElessAEKAGRIEKLESEIQ---------RLSEAHESLTRASSKREALEKTmRN 378
Cdd:COG1196 186 ENLERLEDILGElERQL----EPLERQ----AEKAERYRELKEELKeleaellllKLRELEAELEELEAELEELEAE-LE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 379 KMDSEMRRLQDFNRDLRERLESANRRLASKTQEAQAGSQDmVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELL 458
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE-LARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 459 EQALGNAQGRAARAEEELRKKQayvekvERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQAGAPGGSSGSG 538
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAE------AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 539 GSPELSALRLSEQLREKEEQILALEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHSPQPSPSSSFNEGLLtg 618
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA-- 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 619 ghRHQEMESRLKVLHAQILEKDAVIKVLQQRSRRDPGKAIQGSLRPAKSVPSVFAAAAAGTQGWQGLSSSERQTADAPAR 698
Cdd:COG1196 488 --EAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEY 565
|
....*.
gi 1394533522 699 LTTDRA 704
Cdd:COG1196 566 LKAAKA 571
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
312-578 |
1.01e-08 |
|
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: 58.93 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 312 AQMEAVLRENARLQRDNERLQRELESSAEK----AGRIEKLESEIQRLSEAHESLTRASSK-REALEKTMRN-------K 379
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDlsslEQEIENVKSELKELEARIEELEEDLHKlEEALNDLEARlshsripE 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 380 MDSEMRRLQDFNRDLRERLESANRRLASKTQEAQAgSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLE 459
Cdd:TIGR02169 796 IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY-LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 460 QALGNAQGRAARAEEELRKKQAyveKVERLQQALGQLQAACEKREQLELRLRTRLEqelkALRAQQRQAGAPGGSSGSGG 539
Cdd:TIGR02169 875 AALRDLESRLGDLKKERDELEA---QLRELERKIEELEAQIEKKRKRLSELKAKLE----ALEEELSEIEDPKGEDEEIP 947
|
250 260 270
....*....|....*....|....*....|....*....
gi 1394533522 540 SPELSALRLSEQLREKEEQILALEADMTKWEQKYLEERA 578
Cdd:TIGR02169 948 EEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLK 986
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
315-580 |
1.82e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 315 EAVLRENARLQRDNERLQRELESSAEKAGRIEKLESEIQRLSEAHESLTRASS---KREALEKTMRNKMDSEMRRLQDfN 391
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEakkKADEAKKAEEAKKADEAKKAEE-A 1533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 392 RDLRERLESANRRLASKTQEAQAgsqdmVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQ---RRRAELLEQALGNAQGR 468
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKKAEE-----LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeeARIEEVMKLYEEEKKMK 1608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 469 A--ARAEEELRKKQAYVEKVERLQQALGQLQA--ACEKREQLELR-----LRTRLEQELKALRAQQRQAGAPGGSSGSGG 539
Cdd:PTZ00121 1609 AeeAKKAEEAKIKAEELKKAEEEKKKVEQLKKkeAEEKKKAEELKkaeeeNKIKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1394533522 540 SPELSALRLSEQLREKEEQILALEADMTKWEQ--KYLEERAMR 580
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAEEKKKAEElkKAEEENKIK 1731
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
322-649 |
2.35e-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: 48.13 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 322 ARLQRDNERLQRELEssaekagrIEKLESEIQRLSEAHESLTRAsskrealektmRNKMDSEMRRLQDFNRDLRERLESA 401
Cdd:TIGR02168 664 GSAKTNSSILERRRE--------IEELEEKIEELEEKIAELEKA-----------LAELRKELEELEEELEQLRKELEEL 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 402 NRRLASKTQEAQAGSQdmvakllaqsyeqqqEQEKLEREMALLRGAIEDQRRRAELLEQALGNAQGRAARAEEELRKKQA 481
Cdd:TIGR02168 725 SRQISALRKDLARLEA---------------EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 482 yveKVERLQQALGQLqaacekREQLElrlrtRLEQELKALR-AQQRQAGAPGGSSGSGGSPELSALRLSEQLREKEEQIL 560
Cdd:TIGR02168 790 ---QIEQLKEELKAL------REALD-----ELRAELTLLNeEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 561 ALEADMTkwEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHspqpsPSSSFNEGLLTGGHRHQEMESRLKVLHAQILEKD 640
Cdd:TIGR02168 856 SLAAEIE--ELEELIEELESELEALLNERASLEEALALLRS-----ELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
....*....
gi 1394533522 641 AVIKVLQQR 649
Cdd:TIGR02168 929 LRLEGLEVR 937
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
312-527 |
5.66e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.76 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 312 AQMEAVLRENARLQRDNERLQR----ELESSAEKAGRIEKLESEIQRLSEAHESLTRASSKREALEKTMRNKMDSEMRR- 386
Cdd:pfam12128 312 AADAAVAKDRSELEALEDQHGAfldaDIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRd 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 387 LQDFNRDLRERLESANRRLASKTQEAQAGSQDMVAKLlaqsyeqqqeqekleremallRGAIEDQRRRAELLEQALGNAQ 466
Cdd:pfam12128 392 IAGIKDKLAKIREARDRQLAVAEDDLQALESELREQL---------------------EAGKLEFNEEEYRLKSRLGELK 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533522 467 GRAARA---EEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKAL-----RAQQRQ 527
Cdd:pfam12128 451 LRLNQAtatPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALrqasrRLEERQ 519
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
311-412 |
2.98e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.72 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 311 LAQMEAVLRENARLQRDNERLQRELESSAEKagrIEKLESEIQRlseahESLTRASSKREALEKTMRNKMDSEMRRLQDF 390
Cdd:smart00935 10 LQESPAGKAAQKQLEKEFKKRQAELEKLEKE---LQKLKEKLQK-----DAATLSEAAREKKEKELQKKVQEFQRKQQKL 81
|
90 100
....*....|....*....|..
gi 1394533522 391 NRDLRERLESANRRLASKTQEA 412
Cdd:smart00935 82 QQDLQKRQQEELQKILDKINKA 103
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Angiomotin_C |
pfam12240 |
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ... |
482-687 |
8.11e-94 |
|
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 and 211 amino acids in length. This family is the C terminal region of angiomotin. Angiomotin regulates the action of angiogenesis inhibitor angiostatin. The C terminal region of angiomotin appears to be involved in directing the protein chemotactically.
Pssm-ID: 463503 [Multi-domain] Cd Length: 200 Bit Score: 291.29 E-value: 8.11e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 482 YVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQAGAPGGSSGsggspELSALRLSEQLREKEEQILA 561
Cdd:pfam12240 1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPS-----EYSAPALMELLREKEERILA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 562 LEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHSPQPSPSSSFNEGLLTGGHRHQEMESRLKVLHAQILEKDA 641
Cdd:pfam12240 76 LEADMTKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSYDSSFNEELLLANRRCQEMENRIKNLHAQILEKDA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1394533522 642 VIKVLQQRSRRDPGKAIQGSLRPAKSVPSVFaAAAAGTQGWQGLSS 687
Cdd:pfam12240 156 MIKVLQQRSRKDPGKTDQQSLRPARSVPSIS-AAATGLHSRQTSLS 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
312-581 |
2.81e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 312 AQMEAVLRENARLQRDNERLQRELES-SAEKAGRIEKLESEIQRLSEAHESLTRASSKREALEKtmrnkmdsEMRRLQDF 390
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAElEAELEELRLELEELELELEEAQAEEYELLAELARLEQ--------DIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 391 NRDLRERLESANRRLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLEQALGNAQGRAA 470
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 471 RAEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQAGAPGGSSGSGGSPELSALRLSE 550
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270
....*....|....*....|....*....|.
gi 1394533522 551 QLREKEEQILALEADMTKWEQKYLEERAMRQ 581
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
309-558 |
6.53e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 6.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 309 AHLAQMEAVLREN-ARLQRDNERLQRELESSAEKAGRIEKLESEIQRLSEAHESLTRASSKREALEKTMRNKMDSEMRRL 387
Cdd:COG1196 260 AELAELEAELEELrLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 388 QDfnrdLRERLESANRRLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELlEQALGNAQG 467
Cdd:COG1196 340 EE----LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL-EEAEEALLE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 468 RAARAEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQAGAPGGSSGSGGSPELSALR 547
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
250
....*....|.
gi 1394533522 548 LSEQLREKEEQ 558
Cdd:COG1196 495 LLLEAEADYEG 505
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
309-704 |
7.08e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 7.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 309 AHLAQMEAVLRE-NARLqrdnERLQRElessAEKAGRIEKLESEIQ---------RLSEAHESLTRASSKREALEKTmRN 378
Cdd:COG1196 186 ENLERLEDILGElERQL----EPLERQ----AEKAERYRELKEELKeleaellllKLRELEAELEELEAELEELEAE-LE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 379 KMDSEMRRLQDFNRDLRERLESANRRLASKTQEAQAGSQDmVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELL 458
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE-LARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 459 EQALGNAQGRAARAEEELRKKQayvekvERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQAGAPGGSSGSG 538
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAE------AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 539 GSPELSALRLSEQLREKEEQILALEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHSPQPSPSSSFNEGLLtg 618
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA-- 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 619 ghRHQEMESRLKVLHAQILEKDAVIKVLQQRSRRDPGKAIQGSLRPAKSVPSVFAAAAAGTQGWQGLSSSERQTADAPAR 698
Cdd:COG1196 488 --EAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEY 565
|
....*.
gi 1394533522 699 LTTDRA 704
Cdd:COG1196 566 LKAAKA 571
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
312-578 |
1.01e-08 |
|
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: 58.93 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 312 AQMEAVLRENARLQRDNERLQRELESSAEK----AGRIEKLESEIQRLSEAHESLTRASSK-REALEKTMRN-------K 379
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDlsslEQEIENVKSELKELEARIEELEEDLHKlEEALNDLEARlshsripE 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 380 MDSEMRRLQDFNRDLRERLESANRRLASKTQEAQAgSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLE 459
Cdd:TIGR02169 796 IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY-LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 460 QALGNAQGRAARAEEELRKKQAyveKVERLQQALGQLQAACEKREQLELRLRTRLEqelkALRAQQRQAGAPGGSSGSGG 539
Cdd:TIGR02169 875 AALRDLESRLGDLKKERDELEA---QLRELERKIEELEAQIEKKRKRLSELKAKLE----ALEEELSEIEDPKGEDEEIP 947
|
250 260 270
....*....|....*....|....*....|....*....
gi 1394533522 540 SPELSALRLSEQLREKEEQILALEADMTKWEQKYLEERA 578
Cdd:TIGR02169 948 EEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLK 986
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
312-572 |
2.67e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 312 AQMEAVLRENARLQRDNERLQRELESSAEKAGRIEKLESEIQR-LSEAHESLTRASSKREALEKTMRNkMDSEMRRLQDF 390
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqISALRKDLARLEAEVEQLEERIAQ-LSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 391 NRDLRERLESANRRLASKTQEAQAGSQDmVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLEQALGNAQGRAA 470
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQ-IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 471 RAEEELRKKQayvEKVERLQQALGQLQAACEK-REQLE--LRLRTRLEQELKALRAQQRQagapggSSGSGGSPELSALR 547
Cdd:TIGR02168 842 DLEEQIEELS---EDIESLAAEIEELEELIEElESELEalLNERASLEEALALLRSELEE------LSEELRELESKRSE 912
|
250 260
....*....|....*....|....*
gi 1394533522 548 LSEQLREKEEQILALEADMTKWEQK 572
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVR 937
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
344-564 |
8.36e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 8.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 344 RIEKLESEIQRLSEAHESLTRASSKREALektmrnkmdsemrrlqdfnrdlrERLESANRRLASKTQEAQAgSQDMVAKL 423
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDAREQIELL-----------------------EPIRELAERYAAARERLAE-LEYLRAAL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 424 laqsyeqqqEQEKLEREMALLRGAIEDQRRRAELLEQALGNAQGRAARAEEELRK-KQAY----VEKVERLQQALGQLQA 498
Cdd:COG4913 282 ---------RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDElEAQIrgngGDRLEQLEREIERLER 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 499 ACEKREQLELRLRTRL----------EQELKALRAQQRQAGAPGGSSGSGGSPELSALR-----LSEQLREKEEQILALE 563
Cdd:COG4913 353 ELEERERRRARLEALLaalglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEaalrdLRRELRELEAEIASLE 432
|
.
gi 1394533522 564 A 564
Cdd:COG4913 433 R 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
320-575 |
1.39e-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: 55.46 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 320 ENARLQRDNERLQRELESSAEKAGRIEKLESEI-QRLSEAHESLTRASSKREALEKTmRNKMDSEMRRLQDFNRDLRERL 398
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELsQELSDASRKIGEIEKEIEQLEQE-EEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 399 ESANRRLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAEL----LEQALGNAQGRAARAEE 474
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEArlreIEQKLNRLTLEKEYLEK 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 475 ELRKKQAYVEKVERlqqalgQLQAACEKREQLELRLRtRLEQELKALRAQQRQagapggssgsggspelsalrLSEQLRE 554
Cdd:TIGR02169 834 EIQELQEQRIDLKE------QIKSIEKEIENLNGKKE-ELEEELEELEAALRD--------------------LESRLGD 886
|
250 260
....*....|....*....|.
gi 1394533522 555 KEEQILALEADMTKWEQKYLE 575
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEE 907
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
307-527 |
3.80e-07 |
|
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: 53.23 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 307 GSAHLAQMEAVLRENARLQRDNERLQRELESSAEKAGRIEKLESEIQRLSEAhesLTRASSKREALEKTMrNKMDSEMRR 386
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR---IAALARRIRALEQEL-AALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 387 LQDFNRDLRERLESANRRLASKTQEAQAGSQDMVAKLLAqsyeQQQEQEKLEREMALLRGAIEDQRRRAELLEQALGNAQ 466
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLL----SPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394533522 467 GRAARAEEELRKKQAYVEKVERLQQALGQLQAaceKREQLELRLRTRLEQELKALRAQQRQ 527
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKA---ERQKLLARLEKELAELAAELAELQQE 221
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
309-573 |
7.62e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 7.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 309 AHLAQMEAVLRENARLQRDNERLQRELESSAEKAGRIEKLESEI----------------QRLSEAHESLTRASSKREAL 372
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkikdlgeeeqlrvkEKIGELEAEIASLERSIAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 373 EKTMRN------KMDSEMRRLQDFNRDLRERLESANRRLASKTQEAQAGSQDM-------------VAKLLAQSYEQQQE 433
Cdd:TIGR02169 314 ERELEDaeerlaKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELedlraeleevdkeFAETRDELKDYREK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 434 QEKLEREMALLRGAIEDQRRRAELLEQALGNAQGRAARAEEELRKKQAYVE----KVERLQQALGQLQAACEKREQLELR 509
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEdkalEIKKQEWKLEQLAADLSKYEQELYD 473
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1394533522 510 LRTRLEQELKALRAQQRQAGAPGGSSGSGGSPELSALRLSEQLREKEEQILALEADMTKWEQKY 573
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERY 537
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
344-527 |
1.45e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 344 RIEKLESEIQRLSEAHESLTRASSKREALEKTMRNKmDSEMRRLQDFNRDLRErLESANRRLASKTQEAQA--GSQDMVA 421
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEID-VASAEREIAELEAELERldASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 422 KLlaqsyeqqqeqeklEREMALLRGAIEDQRRRAELLEQALGNAQGRAARAEEELRKKQAYVEKVERLQQAlgQLQAACE 501
Cdd:COG4913 689 AL--------------EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALLE 752
|
170 180 190
....*....|....*....|....*....|..
gi 1394533522 502 KR------EQLELRLRTRLEQELKALRAQQRQ 527
Cdd:COG4913 753 ERfaaalgDAVERELRENLEERIDALRARLNR 784
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
315-580 |
1.82e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 315 EAVLRENARLQRDNERLQRELESSAEKAGRIEKLESEIQRLSEAHESLTRASS---KREALEKTMRNKMDSEMRRLQDfN 391
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEakkKADEAKKAEEAKKADEAKKAEE-A 1533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 392 RDLRERLESANRRLASKTQEAQAgsqdmVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQ---RRRAELLEQALGNAQGR 468
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKKAEE-----LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeeARIEEVMKLYEEEKKMK 1608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 469 A--ARAEEELRKKQAYVEKVERLQQALGQLQA--ACEKREQLELR-----LRTRLEQELKALRAQQRQAGAPGGSSGSGG 539
Cdd:PTZ00121 1609 AeeAKKAEEAKIKAEELKKAEEEKKKVEQLKKkeAEEKKKAEELKkaeeeNKIKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1394533522 540 SPELSALRLSEQLREKEEQILALEADMTKWEQ--KYLEERAMR 580
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAEEKKKAEElkKAEEENKIK 1731
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
322-649 |
2.35e-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: 48.13 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 322 ARLQRDNERLQRELEssaekagrIEKLESEIQRLSEAHESLTRAsskrealektmRNKMDSEMRRLQDFNRDLRERLESA 401
Cdd:TIGR02168 664 GSAKTNSSILERRRE--------IEELEEKIEELEEKIAELEKA-----------LAELRKELEELEEELEQLRKELEEL 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 402 NRRLASKTQEAQAGSQdmvakllaqsyeqqqEQEKLEREMALLRGAIEDQRRRAELLEQALGNAQGRAARAEEELRKKQA 481
Cdd:TIGR02168 725 SRQISALRKDLARLEA---------------EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 482 yveKVERLQQALGQLqaacekREQLElrlrtRLEQELKALR-AQQRQAGAPGGSSGSGGSPELSALRLSEQLREKEEQIL 560
Cdd:TIGR02168 790 ---QIEQLKEELKAL------REALD-----ELRAELTLLNeEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 561 ALEADMTkwEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHspqpsPSSSFNEGLLTGGHRHQEMESRLKVLHAQILEKD 640
Cdd:TIGR02168 856 SLAAEIE--ELEELIEELESELEALLNERASLEEALALLRS-----ELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
....*....
gi 1394533522 641 AVIKVLQQR 649
Cdd:TIGR02168 929 LRLEGLEVR 937
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
312-527 |
5.66e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.76 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 312 AQMEAVLRENARLQRDNERLQR----ELESSAEKAGRIEKLESEIQRLSEAHESLTRASSKREALEKTMRNKMDSEMRR- 386
Cdd:pfam12128 312 AADAAVAKDRSELEALEDQHGAfldaDIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRd 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 387 LQDFNRDLRERLESANRRLASKTQEAQAGSQDMVAKLlaqsyeqqqeqekleremallRGAIEDQRRRAELLEQALGNAQ 466
Cdd:pfam12128 392 IAGIKDKLAKIREARDRQLAVAEDDLQALESELREQL---------------------EAGKLEFNEEEYRLKSRLGELK 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533522 467 GRAARA---EEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKAL-----RAQQRQ 527
Cdd:pfam12128 451 LRLNQAtatPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALrqasrRLEERQ 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
309-652 |
5.73e-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: 46.97 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 309 AHLAQMEAVLREnarLQRDNERLQRELESsAEKAGRIEKLESEIQ------RLSEAHESLTRASSKREALEkTMRNKMDS 382
Cdd:TIGR02168 186 ENLDRLEDILNE---LERQLKSLERQAEK-AERYKELKAELRELElallvlRLEELREELEELQEELKEAE-EELEELTA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 383 EMRRLQDfnrdLRERLESANRRLASKTQEAQAGSQDMVAKLlaqsyeqqqeqekleremALLRGAIEDQRRRAELLEQal 462
Cdd:TIGR02168 261 ELQELEE----KLEELRLEVSELEEEIEELQKELYALANEI------------------SRLEQQKQILRERLANLER-- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 463 gNAQGRAARAEEELRKKQAYVEKVERLQQALGQLQAACEkREQLELRLRTRLEQELKALRAQQRQAGAPGGSSGSGGSPE 542
Cdd:TIGR02168 317 -QLEELEAQLEELESKLDELAEELAELEEKLEELKEELE-SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 543 LSALRlsEQLREKEEQILALEADMTKWEQKYLEERamRQFAMDAAATAAAQRDTTLIRHSPQPSPSSSFNEGLLTGGHRH 622
Cdd:TIGR02168 395 IASLN--NEIERLEARLERLEDRRERLQQEIEELL--KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
330 340 350
....*....|....*....|....*....|
gi 1394533522 623 QEMESRLKVLHAQILEKDAVIKVLQQRSRR 652
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSLERLQEN 500
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
309-576 |
1.30e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 309 AHLAQMEAVLRENARLQRDNERLQRELESSAEKAGRIEKL-ESEIQRLSEahesltrASSKREALEKTMRNKMDSEMRRL 387
Cdd:PTZ00121 1064 AHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAkKTETGKAEE-------ARKAEEAKKKAEDARKAEEARKA 1136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 388 QDFNRDLRERLESANRRLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAieDQRRRAELLEQALGNAQG 467
Cdd:PTZ00121 1137 EDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKA--EDARKAEAARKAEEERKA 1214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 468 RAARAEEELRKKQAyVEKVERLQQALGQLQAACEKREQLELRlrtRLEQELKALRAQQRQAGAPGGSSGSGGSPELSALR 547
Cdd:PTZ00121 1215 EEARKAEDAKKAEA-VKKAEEAKKDAEEAKKAEEERNNEEIR---KFEEARMAHFARRQAAIKAEEARKADELKKAEEKK 1290
|
250 260
....*....|....*....|....*....
gi 1394533522 548 LSEQLREKEEQILALEADMTKWEQKYLEE 576
Cdd:PTZ00121 1291 KADEAKKAEEKKKADEAKKKAEEAKKADE 1319
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
441-572 |
1.64e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 441 MALLRGAIEDQRRRAELLEQALGNAQG---RAARAEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQE 517
Cdd:COG1196 634 AALRRAVTLAGRLREVTLEGEGGSAGGsltGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAE 713
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1394533522 518 LKALRAQQRQAGAPGGSSGSGGSPELSALRLSEQLREKEEQILALEADMTKWEQK 572
Cdd:COG1196 714 EERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE 768
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
320-527 |
1.79e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 320 ENARLQRDNERLQRELessAEKAGRIEKLESEIQRLSEAHESLTRASSKREALEKTMR---NKMDSEMRRLQDFNRDLRE 396
Cdd:COG4942 21 AAAEAEAELEQLQQEI---AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEqelAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 397 RLESANRRLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKlereMALLRGAIEDQRRRAELLEQALGNAQGRAARAEEEL 476
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRR----LQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394533522 477 RKKQAYVEKVERLQQALGQLQAACEK------------REQLE--LRLRTRLEQELKALRAQQRQ 527
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKllarlekelaelAAELAelQQEAEELEALIARLEAEAAA 238
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
311-483 |
2.52e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 311 LAQMEAVLRENARLQRDNERLQRELESSAEKAGRIEKLESEIQRLSEAHESLTRASSKREALE--KTMRNKMDSEMRRLQ 388
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQelEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 389 DFN------RDLRERLESANRRLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLEQAL 462
Cdd:COG4717 150 ELEerleelRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180
....*....|....*....|.
gi 1394533522 463 GNAQGRAARAEEELRKKQAYV 483
Cdd:COG4717 230 EQLENELEAAALEERLKEARL 250
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
311-481 |
3.59e-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: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 311 LAQMEAVLRENARLQRDNERLQRELESSAEKAGRIEK----------LESEIQRLSEAHESLTRASSKREALEKTmRNKM 380
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeidvasAEREIAELEAELERLDASSDDLAALEEQ-LEEL 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 381 DSEMRRLQDFNRDLRERLESANRRLASKTQEAQAgsqdmvAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRR--AELL 458
Cdd:COG4913 698 EAELEELEEELDELKGEIGRLEKELEQAEEELDE------LQDRLEAAEDLARLELRALLEERFAAALGDAVERelRENL 771
|
170 180
....*....|....*....|...
gi 1394533522 459 EQALGNAQGRAARAEEELRKKQA 481
Cdd:COG4913 772 EERIDALRARLNRAEEELERAMR 794
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
309-499 |
4.01e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 309 AHLAQMEAVLRENARLQRDNERLQRELESSAEKAGRIEKLESEIQRLSEAHESLTRASSKREALEKTmRNKMDSEMRRLQ 388
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL-EAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 389 DFNRDLRErLESANRRLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLEQALGNAQGR 468
Cdd:COG4717 150 ELEERLEE-LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180 190
....*....|....*....|....*....|.
gi 1394533522 469 AARAEEELRKKQAYvekvERLQQALGQLQAA 499
Cdd:COG4717 229 LEQLENELEAAALE----ERLKEARLLLLIA 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
450-577 |
4.87e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 450 DQRRRAELLEQALGNAQGRAARAEEELRKKQAYVEKVERLQQALGQLQ----------AACEKREQLELRLR-------- 511
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAeyswdeidvaSAEREIAELEAELErldassdd 686
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533522 512 -TRLEQELKALRAQQRQAGAPGGSSGSGGSPELSAL-RLSEQLREKEEQILALEADMTKWEQKYLEER 577
Cdd:COG4913 687 lAALEEQLEELEAELEELEEELDELKGEIGRLEKELeQAEEELDELQDRLEAAEDLARLELRALLEER 754
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
444-652 |
1.12e-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: 42.74 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 444 LRGAIEDQRRRAELLEQALGNAQGRAARAEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALrA 523
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL-E 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 524 QQRQAGAPGGSSGSGGSPELSALR--LSEQLREKEEQILALEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRH 601
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIeeLEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1394533522 602 SPQPSPSSSFNEGLLTGGHRHQEMESRLKVLHAQILEKDAVIKVLQQRSRR 652
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
311-412 |
1.93e-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: 39.82 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 311 LAQMEAVLRENARLQRDNERLQRELESsaeKAGRIEKLESEIQRlseahESLTRASSKREALEKTMRNKMDSEMRRLQDF 390
Cdd:COG2825 35 LQESPEGKAAQKKLEKEFKKRQAELQK---LEKELQALQEKLQK-----EAATLSEEERQKKERELQKKQQELQRKQQEA 106
|
90 100
....*....|....*....|..
gi 1394533522 391 NRDLRERLESANRRLASKTQEA 412
Cdd:COG2825 107 QQDLQKRQQELLQPILEKIQKA 128
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
320-557 |
2.29e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 320 ENARLQRDNERLqrELESSAEKAGRIE--KLESEIQRLSEAH--ESLTRASSKREALE--KTMRNKMDSEMRRLQDFNRD 393
Cdd:PTZ00121 1143 EEARKAEDAKRV--EIARKAEDARKAEeaRKAEDAKKAEAARkaEEVRKAEELRKAEDarKAEAARKAEEERKAEEARKA 1220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 394 LRERLESANRRLASKTQEAQAGSQdmvAKLLAQSYEQQQEQEKLEREMALLRGAIE-DQRRRAELLEQALGNAQGRAARA 472
Cdd:PTZ00121 1221 EDAKKAEAVKKAEEAKKDAEEAKK---AEEERNNEEIRKFEEARMAHFARRQAAIKaEEARKADELKKAEEKKKADEAKK 1297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 473 EEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQAGAPGGSSGSGGSPELSALRLSEQL 552
Cdd:PTZ00121 1298 AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
....*
gi 1394533522 553 REKEE 557
Cdd:PTZ00121 1378 KKADA 1382
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
318-513 |
2.66e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.26 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 318 LRENARL----QRDNERLQRELESsaekAGRIEKLESEIQRlseaheSLTRASSKREALEKTMRNKMDSEMRRLQDFN-R 392
Cdd:pfam17380 377 MRELERLqmerQQKNERVRQELEA----ARKVKILEEERQR------KIQQQKVEMEQIRAEQEEARQREVRRLEEERaR 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 393 DL-RERLESANR-----RLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLEQALGNAQ 466
Cdd:pfam17380 447 EMeRVRLEEQERqqqveRLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQ 526
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1394533522 467 GRAA-----RAEEELRKKQAYVEKVERLQQalgQLQAACEKREQLELRLRTR 513
Cdd:pfam17380 527 KAIYeeerrREAEEERRKQQEMEERRRIQE---QMRKATEERSRLEAMERER 575
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
311-412 |
2.98e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.72 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 311 LAQMEAVLRENARLQRDNERLQRELESSAEKagrIEKLESEIQRlseahESLTRASSKREALEKTMRNKMDSEMRRLQDF 390
Cdd:smart00935 10 LQESPAGKAAQKQLEKEFKKRQAELEKLEKE---LQKLKEKLQK-----DAATLSEAAREKKEKELQKKVQEFQRKQQKL 81
|
90 100
....*....|....*....|..
gi 1394533522 391 NRDLRERLESANRRLASKTQEA 412
Cdd:smart00935 82 QQDLQKRQQEELQKILDKINKA 103
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
299-521 |
5.09e-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: 40.43 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 299 AQASSATSGSAHLAQMEAVLRENARLQRDNERLQRELESSAEKAGRIEKLESEIQRLSEAHESLTRASSKREALektmRN 378
Cdd:TIGR02168 794 LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL----IE 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 379 KMDSEMRRLQDFNRDLRERLESANRRLASKTQEAQAGSQDMVAkllaqsyeqqqeqekleremalLRGAIEDQRRRAELL 458
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE----------------------LRRELEELREKLAQL 927
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1394533522 459 EQALGNAQGRAARAEEELRkkqayvEKVERLQQALGQLQAACE-KREQLELRLRtRLEQELKAL 521
Cdd:TIGR02168 928 ELRLEGLEVRIDNLQERLS------EEYSLTLEEAEALENKIEdDEEEARRRLK-RLENKIKEL 984
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
312-568 |
5.92e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 40.06 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 312 AQMEAVLRENARL--QRDNER-LQRELESSAEKAGRIEKLESEIQRLSEAHESLTRASSKREALEKTMRnkmdsemrrLQ 388
Cdd:pfam05622 218 EKLEALQKEKERLiiERDTLReTNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIR---------LQ 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 389 DFNRDLRERLESANRRLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAE---LLEQALGNA 465
Cdd:pfam05622 289 HENKMLRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEdssLLKQKLEEH 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 466 QGRAARAEEELRKKQAYVEKVE-----RLQQALGQLQAACEKREQ----LELRLRTRLEQE---LKALRAQQRQagapgg 533
Cdd:pfam05622 369 LEKLHEAQSELQKKKEQIEELEpkqdsNLAQKIDELQEALRKKDEdmkaMEERYKKYVEKAksvIKTLDPKQNP------ 442
|
250 260 270
....*....|....*....|....*....|....*
gi 1394533522 534 ssgsGGSPELSALRlsEQLREKEEQILALEADMTK 568
Cdd:pfam05622 443 ----ASPPEIQALK--NQLLEKDKKIEHLERDFEK 471
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
311-527 |
7.68e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 311 LAQMEAVLRENARLQRDNERLQRE---------------LESSAEKAGRIEKLESEIQRLSEAHESLTRASSKREALEKT 375
Cdd:PRK02224 428 EAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533522 376 MRNKMDSEMRR--LQDFNRDLRERLESANRRLASKTQEAQAGSQDMVAKllaqsyeqqqeqeklEREMALLRGAIEDQRR 453
Cdd:PRK02224 508 EDRIERLEERRedLEELIAERRETIEEKRERAEELRERAAELEAEAEEK---------------REAAAEAEEEAEEARE 572
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1394533522 454 RAELLEQALGNAQGRAaraeEELRKKQAYVEKVERLQQALGQLQaacEKREQLELRLRTRLEQeLKALRAQQRQ 527
Cdd:PRK02224 573 EVAELNSKLAELKERI----ESLERIRTLLAAIADAEDEIERLR---EKREALAELNDERRER-LAEKRERKRE 638
|
|
|