|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
1465-1755 |
4.09e-123 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 389.73 E-value: 4.09e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1465 NRLMQDEIARLRLEKDTIKNQNLEK--KYLKDFEIVKRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLE 1542
Cdd:pfam14915 1 NCMLQDEIAMLRLEIDTIKNQNQEKekKYLEDIEILKEKNDDLQKTLKLNEETLTKTVFQYNGQLNVLKAENTMLNSKLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1543 KQRESRQRLETEMQSYHCRLNAARCDHDQSHSSKRDQELAFQGTVDKCRHLQENLNSHV-------LILSLQLSKAESKS 1615
Cdd:pfam14915 81 NEKQNKERLETEVESYRSRLAAAIQDHEQSQTSKRDLELAFQRERDEWLRLQDKMNFDVsnlrdenEILSQQLSKAESKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1616 RVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQ----ERFCQLKKQNMLLQQQLDDA 1691
Cdd:pfam14915 161 NSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKELEHMYQNEQDKVNKYIGKQesleERLAQLQSENMLLRQQLEDA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462496564 1692 RNKADNQEKAILNIQARCDARVQNLQAECRKHRLLLEEDNKMLVNELNHSKEKECQYEKEKAER 1755
Cdd:pfam14915 241 QNKADAKEKTVIDIQDQFQDIVKKLQAESEKQVLLLEERNKELINECNHLKERLYQYEKEKAER 304
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
36-197 |
6.18e-37 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 142.02 E-value: 6.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 115
Cdd:COG0666 58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 116 LLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDY 195
Cdd:COG0666 138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217
|
..
gi 2462496564 196 LG 197
Cdd:COG0666 218 DG 219
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
36-128 |
5.49e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 86.32 E-value: 5.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSrRCELNLCDrEDRTPLIKAVQLRQEACAT 115
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 2462496564 116 LLLQNGANPNITD 128
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
36-197 |
1.18e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 78.55 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLAC-----ATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQ--L 108
Cdd:PHA03100 39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISkkS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 109 RQEACATLLLQNGANPNITDFFGRTALHYAV-YNE-DTSMIEKLLSHGTNIEECSKCEY----------------QPLLF 170
Cdd:PHA03100 119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLeSNKiDLKILKLLIDKGVDINAKNRVNYllsygvpinikdvygfTPLHY 198
|
170 180
....*....|....*....|....*..
gi 2462496564 171 AVSRRKVKMVEFLLKKKANVNAIDYLG 197
Cdd:PHA03100 199 AVYNNNPEFVKYLLDLGANPNLVNKYG 225
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1228-1858 |
3.80e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 62.06 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1228 KNSVLNTATKMKDVQTSTPAEQDLEMASEGEQKRLEEyennqpQVKNQIH----SRDDLDDIIQSSQTVSEDGDSLCCNC 1303
Cdd:pfam15921 109 RQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRN------QLQNTVHeleaAKCLKEDMLEDSNTQIEQLRKMMLSH 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1304 KNVI-----LLIDQHEMKCK-----DCVHLLKIKNTFCLWKRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKS 1373
Cdd:pfam15921 183 EGVLqeirsILVDFEEASGKkiyehDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1374 QLKHEilELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQYRIEADVTKPIKPALKSAEVELKTGGNNSNQVS 1453
Cdd:pfam15921 263 QQHQD--RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMY 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1454 EtDEKEDLLHENRLMQDEIARLRLEKDTIKNQ--NLEKKYLKDFEIVKRKHEDLQKALKRNGETLAKTIAcysgqlAALT 1531
Cdd:pfam15921 341 E-DKIEELEKQLVLANSELTEARTERDQFSQEsgNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTG------NSIT 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1532 DENttLRSKLEKQRESRQRLETEMQSYHcrlnaarcdhDQSHSSKRDQELAFQG---TVDKCRHLQENLNSHVLILSLQL 1608
Cdd:pfam15921 414 IDH--LRRELDDRNMEVQRLEALLKAMK----------SECQGQMERQMAAIQGkneSLEKVSSLTAQLESTKEMLRKVV 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1609 SKAESKSRVLKTELHYTGE---ALKEKALVFEHVQSELKQKQS----QMKDIEKMYKSG---YNTMEKCIEKQERFCQLK 1678
Cdd:pfam15921 482 EELTAKKMTLESSERTVSDltaSLQEKERAIEATNAEITKLRSrvdlKLQELQHLKNEGdhlRNVQTECEALKLQMAEKD 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1679 KQNMLLQQQLDDARNKADNQEK---AILNIQARCDARVQNLQAECRKHRLLLEEDNKMlVNELnHSKEKECQYEKEK--- 1752
Cdd:pfam15921 562 KVIEILRQQIENMTQLVGQHGRtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDAK-IREL-EARVSDLELEKVKlvn 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1753 --AEREVAVRQLQQKRDDVLNKGSATKALLDASSRHCTYLENGMQDSRKKLD----QMRSQFQEIQDQLTATIRCTKEME 1826
Cdd:pfam15921 640 agSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMEtttnKLKMQLKSAQSELEQTRNTLKSME 719
|
650 660 670
....*....|....*....|....*....|...
gi 2462496564 1827 G-DTQKLEVEHVMMRKIIKKQdDQIERLEKILQ 1858
Cdd:pfam15921 720 GsDGHAMKVAMGMQKQITAKR-GQIDALQSKIQ 751
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1471-1826 |
3.24e-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: 58.91 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1471 EIARLRLEKdtiKNQNLEKkyLKD--FEIvKRKHEDLQ---------KALKRNGETLAKTIacYSGQLAALTDENTTLRS 1539
Cdd:TIGR02168 175 KETERKLER---TRENLDR--LEDilNEL-ERQLKSLErqaekaeryKELKAELRELELAL--LVLRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1540 KLEKQRESRQRLETEMQSYHCRLNAARCDHDQSHSSKRDQE---LAFQGTVDKC----RHLQE---NLNSHVLILSLQLS 1609
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQkelYALANEISRLeqqkQILRErlaNLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1610 KAESKSRVLKTELHytgeALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQER-FCQLKKQNMLLQQQL 1688
Cdd:TIGR02168 327 ELESKLDELAEELA----ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkVAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1689 DDARNKADNQEKAILNIQARCDARVQNLQ-AECRKHRLLLEEDNKMLVNELNHSKEKECQYEKEKAEREVAVRQLQQKRD 1767
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462496564 1768 DVLNKGSATKALLDASSRHCTYlengmQDSRKKLDQMRSQFQEIQDQLTATIRCTKEME 1826
Cdd:TIGR02168 483 ELAQLQARLDSLERLQENLEGF-----SEGVKALLKNQSGLSGILGVLSELISVDEGYE 536
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1351-1836 |
2.56e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1351 IRKLKNKASVLQKRISEKEEIKSQlkhEILELEKELcslrfaiqqeKKKRRNVEEVHQKVREKLRITEEQYRIEAdvtkp 1430
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLK---ELKELEEEL----------KEAEEKEEEYAELQEELEELEEELEELEA----- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1431 ikpALKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQNLEKKYLKDfEIvKRKHEDLQKALK 1510
Cdd:COG4717 110 ---ELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA-EL-AELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1511 RNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAArcdhdqshsskrdqelafqgtvDKC 1590
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA----------------------ALE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1591 RHLQENLNShVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMyksGYNTMEKCIEK 1670
Cdd:COG4717 243 ERLKEARLL-LLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL---QALPALEELEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1671 QERFCQLKKQNMLLQQQLDDARNKADNQEKAILNIQARCDARVQNLQAECRKHRL-LLEEDNKMLVNELNHSKEKECQYE 1749
Cdd:COG4717 319 EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAaLLAEAGVEDEEELRAALEQAEEYQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1750 KEKAEREVAVRQLQQKRDDVLnkgsatkALLDASSRhcTYLENGMQDSRKKLDQMRSQFQEIQDQLTATIRCTKEMEGDT 1829
Cdd:COG4717 399 ELKEELEELEEQLEELLGELE-------ELLEALDE--EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG 469
|
....*..
gi 2462496564 1830 QKLEVEH 1836
Cdd:COG4717 470 ELAELLQ 476
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
636-1107 |
9.07e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 9.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 636 SSQKQPALKATTDEEDSVSNIA-TEIKDGEKSGTVSSQKQPALKATTDEE----DSVSNIATEIKDGE---KSGTVSSQK 707
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAAkAEAEAAADEAEAAEEKAEAAEKKKEEAkkkaDAAKKKAEEKKKADeakKKAEEDKKK 1406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 708 QPALKATTDEK---DSVSNIATEIKDGEKSGTVSSQKPPALTATSDEEGS-----VLSIARENKDGEKSRTVSSRKKPAL 779
Cdd:PTZ00121 1407 ADELKKAAAAKkkaDEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkaeeAKKKAEEAKKADEAKKKAEEAKKAD 1486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 780 KATSDEKDSFSNITRGKKDGEISRKVSSQKPPTLKGTSDEedsvLGIARENKDGEKSRTVSSEKppglKASSAEKDSVLN 859
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE----AKKAEEAKKADEAKKAEEKK----KADELKKAEELK 1558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 860 IARGKKDGEKTKRVSSRKKPSLEATSDEKDSfsnitREKKDGEISRKVSSQKPPALKGTSDEEDSVLGIARENKDGEKSR 939
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKA-----EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK 1633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 940 TVSSEKPPGL----KATSDEKDSVLNIARGKKDGEKTRTVSSQKPPTLKATSDEEDSVLSIARENKDGEKSRTV----SS 1011
Cdd:PTZ00121 1634 KVEQLKKKEAeekkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELkkkeAE 1713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1012 EKPSGLKATSAEKDSVLNIARGKKYGEKTKRvssrKKPALKATSDEKDSVLYIAREKKdgEKSRTVSSPKQPALKAICDK 1091
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKKEAEEDKK----KAEEAKKDEEEKKKIAHLKKEEE--KKAEEIRKEKEAVIEEELDE 1787
|
490
....*....|....*.
gi 2462496564 1092 EDSVPNMATEKKDEQI 1107
Cdd:PTZ00121 1788 EDEKRRMEVDKKIKDI 1803
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1345-1757 |
1.79e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1345 EQLRVKIRKLKNKASVLQKRISEKEEI-----KSQLKHEILELEKELCSLRFAIQQEKK--KRRNVEEVHQKVREKLRit 1417
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKAdeakkKAEEKKKADEAKKKAEEAKKADEAKKKaeEAKKAEEAKKKAEEAKK-- 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1418 EEQYRIEADVTKPIKPALKSAEvELKTGGNNSNQVSETDEKEDLLH--ENRLMQDEiarLRLEKDTIKNQNLEKKYLKDF 1495
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAE-EAKKKADEAKKAAEAKKKADEAKkaEEAKKADE---AKKAEEAKKADEAKKAEEKKK 1547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1496 EIVKRKHEDLQKALKRNGETLAKTiacysgqlaALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAARCDHDQSHSS 1575
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKK---------AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1576 K-RDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIE 1654
Cdd:PTZ00121 1619 KiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA 1698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1655 KMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARNKADNQEKAI--LNIQARCDARVQNLQAECRKHRLLLEEDNK 1732
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAeeAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
|
410 420
....*....|....*....|....*
gi 2462496564 1733 MLVNELNHSKEKECQYEKEKAEREV 1757
Cdd:PTZ00121 1779 AVIEEELDEEDEKRRMEVDKKIKDI 1803
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1350-1557 |
2.02e-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: 48.99 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1350 KIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQY-------- 1421
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIaelraele 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1422 RIEADVTKPIKPALKSAEVELKTGGNNSNQVSETDEKEDLLHE-NRLMQDEIARLRLEKDTIKNQNlekkylKDFEIVKR 1500
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALR------AELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462496564 1501 KHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQS 1557
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
67-154 |
7.20e-05 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 47.77 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 67 TALHLACATGQPEMVHLLVSR------RCELNLCDREDRTPLIKAVQLR--------QEACATLLLQNGANPNITDFFGR 132
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERgasvpaRACGDFFVKSQGVDSFYHGESPlnaaaclgSPSIVALLSEDPADILTADSLGN 209
|
90 100 110
....*....|....*....|....*....|.
gi 2462496564 133 TALHYAVYNED---------TSMIEKLLSHG 154
Cdd:TIGR00870 210 TLLHLLVMENEfkaeyeelsCQMYNFALSLL 240
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
131-159 |
1.93e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 40.26 E-value: 1.93e-04
10 20
....*....|....*....|....*....
gi 2462496564 131 GRTALHYAVYNEDTSMIEKLLSHGTNIEE 159
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
36-187 |
5.44e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 45.00 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 36 IHRAVLHGNLEKLKYLLltyyDANKRDRKE---------RTALHLACATGQPEMVHLLVSRRCELN------LCDREDRT 100
Cdd:cd22192 55 LHVAALYDNLEAAVVLM----EAAPELVNEpmtsdlyqgETALHIAVVNQNLNLVRELIARGADVVspratgTFFRPGPK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 101 --------PLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTS----MIEKLLSHGTNIEECS------K 162
Cdd:cd22192 131 nliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTfacqMYDLILSYDKEDDLQPldlvpnN 210
|
170 180
....*....|....*....|....*
gi 2462496564 163 CEYQPLLFAVSRRKVKMVEFLLKKK 187
Cdd:cd22192 211 QGLTPFKLAAKEGNIVMFQHLVQKR 235
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1345-1582 |
2.28e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1345 EQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKL-RITEEQYRI 1423
Cdd:PRK02224 352 DDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERdELREREAEL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1424 EADVtKPIKPALKSAEVELKTGG--------NNSNQVSETDEKEDLLHEnrlMQDEIARLRLEKDTIKNQNLEKKYLKDF 1495
Cdd:PRK02224 432 EATL-RTARERVEEAEALLEAGKcpecgqpvEGSPHVETIEEDRERVEE---LEAELEDLEEEVEEVEERLERAEDLVEA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1496 EIVKRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSyhCRLNAARCDHDQSHSS 1575
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE--AREEVAELNSKLAELK 585
|
....*..
gi 2462496564 1576 KRDQELA 1582
Cdd:PRK02224 586 ERIESLE 592
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1334-1563 |
3.82e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1334 KRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELcsLRFAIQQEKKKRRNVEEVHQKVREK 1413
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEAR 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1414 LRiteeqyrieadvtkpikpalksaEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRlekDTIKNQNLEKkylk 1493
Cdd:TIGR02169 814 LR-----------------------EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE---KEIENLNGKK---- 863
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1494 dfEIVKRKHEDLQKALKRngetlaktiacYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLN 1563
Cdd:TIGR02169 864 --EELEEELEELEAALRD-----------LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
1465-1755 |
4.09e-123 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 389.73 E-value: 4.09e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1465 NRLMQDEIARLRLEKDTIKNQNLEK--KYLKDFEIVKRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLE 1542
Cdd:pfam14915 1 NCMLQDEIAMLRLEIDTIKNQNQEKekKYLEDIEILKEKNDDLQKTLKLNEETLTKTVFQYNGQLNVLKAENTMLNSKLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1543 KQRESRQRLETEMQSYHCRLNAARCDHDQSHSSKRDQELAFQGTVDKCRHLQENLNSHV-------LILSLQLSKAESKS 1615
Cdd:pfam14915 81 NEKQNKERLETEVESYRSRLAAAIQDHEQSQTSKRDLELAFQRERDEWLRLQDKMNFDVsnlrdenEILSQQLSKAESKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1616 RVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQ----ERFCQLKKQNMLLQQQLDDA 1691
Cdd:pfam14915 161 NSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKELEHMYQNEQDKVNKYIGKQesleERLAQLQSENMLLRQQLEDA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462496564 1692 RNKADNQEKAILNIQARCDARVQNLQAECRKHRLLLEEDNKMLVNELNHSKEKECQYEKEKAER 1755
Cdd:pfam14915 241 QNKADAKEKTVIDIQDQFQDIVKKLQAESEKQVLLLEERNKELINECNHLKERLYQYEKEKAER 304
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
36-197 |
6.18e-37 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 142.02 E-value: 6.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 115
Cdd:COG0666 58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 116 LLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDY 195
Cdd:COG0666 138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217
|
..
gi 2462496564 196 LG 197
Cdd:COG0666 218 DG 219
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
36-212 |
1.01e-35 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 138.55 E-value: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 115
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 116 LLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDY 195
Cdd:COG0666 171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250
|
170
....*....|....*..
gi 2462496564 196 LGSIFDLIYEYERKRYE 212
Cdd:COG0666 251 DGLTALLLAAAAGAALI 267
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
36-197 |
2.12e-30 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 123.14 E-value: 2.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 115
Cdd:COG0666 124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 116 LLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDY 195
Cdd:COG0666 204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
|
..
gi 2462496564 196 LG 197
Cdd:COG0666 284 DL 285
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
28-197 |
3.13e-28 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 116.59 E-value: 3.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 28 IKPYHLKRIHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQ 107
Cdd:COG0666 17 LLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 108 LRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKK 187
Cdd:COG0666 97 NGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG 176
|
170
....*....|
gi 2462496564 188 ANVNAIDYLG 197
Cdd:COG0666 177 ADVNARDNDG 186
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
36-128 |
5.49e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 86.32 E-value: 5.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSrRCELNLCDrEDRTPLIKAVQLRQEACAT 115
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 2462496564 116 LLLQNGANPNITD 128
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
45-197 |
1.06e-16 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 82.69 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 45 LEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGANP 124
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462496564 125 NITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLG 197
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDG 153
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
102-194 |
7.63e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 74.38 E-value: 7.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 102 LIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGtNIEECSKcEYQPLLFAVSRRKVKMVE 181
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 2462496564 182 FLLKKKANVNAID 194
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
36-197 |
1.18e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 78.55 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLAC-----ATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQ--L 108
Cdd:PHA03100 39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISkkS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 109 RQEACATLLLQNGANPNITDFFGRTALHYAV-YNE-DTSMIEKLLSHGTNIEECSKCEY----------------QPLLF 170
Cdd:PHA03100 119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLeSNKiDLKILKLLIDKGVDINAKNRVNYllsygvpinikdvygfTPLHY 198
|
170 180
....*....|....*....|....*..
gi 2462496564 171 AVSRRKVKMVEFLLKKKANVNAIDYLG 197
Cdd:PHA03100 199 AVYNNNPEFVKYLLDLGANPNLVNKYG 225
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
51-195 |
3.40e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 77.23 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 51 LLLTY-YDANKRDR-KERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGANPNITD 128
Cdd:PHA02878 152 LLLSYgADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 129 FFGRTALHYAV-YNEDTSMIEKLLSHGTNIEECSKC-EYQPLLFAV-SRRKVKMvefLLKKKANVNAIDY 195
Cdd:PHA02878 232 KCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIkSERKLKL---LLEYGADINSLNS 298
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
44-198 |
2.58e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 68.07 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 44 NLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGAN 123
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462496564 124 PNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKvKMVEFLLkKKANVNAIDYLGS 198
Cdd:PHA02874 183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLI-NNASINDQDIDGS 255
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
36-198 |
5.76e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 67.21 E-value: 5.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACAT----GQPEMVHLLVSRRC-------------------ELN 92
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklGMKEMIRSINKCSVfytlvaikdafnnrnveifKII 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 93 LCDREDRTPLIKAVQLRQ-------EACAT-LLLQNGANPNITD-FFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKC 163
Cdd:PHA02878 121 LTNRYKNIQTIDLVYIDKkskddiiEAEITkLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200
|
170 180 190
....*....|....*....|....*....|....*
gi 2462496564 164 EYQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLGS 198
Cdd:PHA02878 201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGN 235
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
36-193 |
9.91e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 66.17 E-value: 9.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKE-RTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACA 114
Cdd:PHA02875 72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 115 TLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLL-FAVSRRKVKMVEFLLKKKANVNAI 193
Cdd:PHA02875 152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGADCNIM 231
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
39-210 |
1.35e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 65.78 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 39 AVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSR-----------RCELN-------------LC 94
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHgaipdvkypdiESELHdaveegdvkaveeLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 95 D----------REDRTPLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHG--TNIEECsk 162
Cdd:PHA02875 89 DlgkfaddvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKacLDIEDC-- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462496564 163 CEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLGSIFDLIYEYERKR 210
Cdd:PHA02875 167 CGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNK 214
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
30-194 |
1.73e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 65.46 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 30 PYHLKRIHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACAT--GQPEMVHLLVSRRCELNLCDREDRTPLIKAVq 107
Cdd:PHA03100 71 PLHYLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYL- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 108 lrqEACAT------LLLQNGANPN----------------ITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEY 165
Cdd:PHA03100 150 ---ESNKIdlkilkLLIDKGVDINaknrvnyllsygvpinIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226
|
170 180
....*....|....*....|....*....
gi 2462496564 166 QPLLFAVSRRKVKMVEFLLKKKANVNAID 194
Cdd:PHA03100 227 TPLHIAILNNNKEIFKLLLNNGPSIKTII 255
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
36-192 |
3.66e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 65.08 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 36 IHRAVLHGNLEKL-KYLLLTYYDANKRDRKERTALHLACATG-QPEMVHLLVSRRCELNLCDREDRTPLIKAVQL-RQEA 112
Cdd:PHA02876 277 LHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLdRNKD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 113 CATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKM-VEFLLKKKANVN 191
Cdd:PHA02876 357 IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVN 436
|
.
gi 2462496564 192 A 192
Cdd:PHA02876 437 S 437
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
100-216 |
8.93e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 63.15 E-value: 8.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 100 TPLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHY-----AVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSR 174
Cdd:PHA03100 37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISK 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2462496564 175 RK--VKMVEFLLKKKANVNAIDYLGsiFDLIYEYERKRYEDLPI 216
Cdd:PHA03100 117 KSnsYSIVEYLLDNGANVNIKNSDG--ENLLHLYLESNKIDLKI 158
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
99-151 |
1.30e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 55.36 E-value: 1.30e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2462496564 99 RTPLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLL 151
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
32-85 |
3.16e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.20 E-value: 3.16e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2462496564 32 HLKRIHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLV 85
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1228-1858 |
3.80e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 62.06 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1228 KNSVLNTATKMKDVQTSTPAEQDLEMASEGEQKRLEEyennqpQVKNQIH----SRDDLDDIIQSSQTVSEDGDSLCCNC 1303
Cdd:pfam15921 109 RQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRN------QLQNTVHeleaAKCLKEDMLEDSNTQIEQLRKMMLSH 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1304 KNVI-----LLIDQHEMKCK-----DCVHLLKIKNTFCLWKRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKS 1373
Cdd:pfam15921 183 EGVLqeirsILVDFEEASGKkiyehDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1374 QLKHEilELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQYRIEADVTKPIKPALKSAEVELKTGGNNSNQVS 1453
Cdd:pfam15921 263 QQHQD--RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMY 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1454 EtDEKEDLLHENRLMQDEIARLRLEKDTIKNQ--NLEKKYLKDFEIVKRKHEDLQKALKRNGETLAKTIAcysgqlAALT 1531
Cdd:pfam15921 341 E-DKIEELEKQLVLANSELTEARTERDQFSQEsgNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTG------NSIT 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1532 DENttLRSKLEKQRESRQRLETEMQSYHcrlnaarcdhDQSHSSKRDQELAFQG---TVDKCRHLQENLNSHVLILSLQL 1608
Cdd:pfam15921 414 IDH--LRRELDDRNMEVQRLEALLKAMK----------SECQGQMERQMAAIQGkneSLEKVSSLTAQLESTKEMLRKVV 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1609 SKAESKSRVLKTELHYTGE---ALKEKALVFEHVQSELKQKQS----QMKDIEKMYKSG---YNTMEKCIEKQERFCQLK 1678
Cdd:pfam15921 482 EELTAKKMTLESSERTVSDltaSLQEKERAIEATNAEITKLRSrvdlKLQELQHLKNEGdhlRNVQTECEALKLQMAEKD 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1679 KQNMLLQQQLDDARNKADNQEK---AILNIQARCDARVQNLQAECRKHRLLLEEDNKMlVNELnHSKEKECQYEKEK--- 1752
Cdd:pfam15921 562 KVIEILRQQIENMTQLVGQHGRtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDAK-IREL-EARVSDLELEKVKlvn 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1753 --AEREVAVRQLQQKRDDVLNKGSATKALLDASSRHCTYLENGMQDSRKKLD----QMRSQFQEIQDQLTATIRCTKEME 1826
Cdd:pfam15921 640 agSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMEtttnKLKMQLKSAQSELEQTRNTLKSME 719
|
650 660 670
....*....|....*....|....*....|...
gi 2462496564 1827 G-DTQKLEVEHVMMRKIIKKQdDQIERLEKILQ 1858
Cdd:pfam15921 720 GsDGHAMKVAMGMQKQITAKR-GQIDALQSKIQ 751
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
44-194 |
8.39e-09 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 60.04 E-value: 8.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 44 NLEKLKYLLLTYYDANKRDRKERTALHLACATGQP--EMVHLLVSRRCELNLCDREDRTPLIKAVQlrQEACATLLLQN- 120
Cdd:PHA03095 166 NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMAT--GSSCKRSLVLPl 243
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462496564 121 ---GANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAID 194
Cdd:PHA03095 244 liaGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA 320
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
32-197 |
8.39e-09 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 60.04 E-value: 8.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 32 HLKRIHRAVLHGNL--------EKLKYLLLTYYDANKRDRKERTALHLacatgqpemvhlLVSRRCElnlcdredrtPLI 103
Cdd:PHA03095 6 SVDIIMEAALYDYLlnasnvtvEEVRRLLAAGADVNFRGEYGKTPLHL------------YLHYSSE----------KVK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 104 KAVQLrqeacatlLLQNGANPNITDFFGRTALHYAVYNEDT-SMIEKLLSHGTNIEECSKCEYQPL--LFAVSRRKVKMV 180
Cdd:PHA03095 64 DIVRL--------LLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVI 135
|
170
....*....|....*..
gi 2462496564 181 EFLLKKKANVNAIDYLG 197
Cdd:PHA03095 136 RLLLRKGADVNALDLYG 152
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1471-1826 |
3.24e-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: 58.91 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1471 EIARLRLEKdtiKNQNLEKkyLKD--FEIvKRKHEDLQ---------KALKRNGETLAKTIacYSGQLAALTDENTTLRS 1539
Cdd:TIGR02168 175 KETERKLER---TRENLDR--LEDilNEL-ERQLKSLErqaekaeryKELKAELRELELAL--LVLRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1540 KLEKQRESRQRLETEMQSYHCRLNAARCDHDQSHSSKRDQE---LAFQGTVDKC----RHLQE---NLNSHVLILSLQLS 1609
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQkelYALANEISRLeqqkQILRErlaNLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1610 KAESKSRVLKTELHytgeALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQER-FCQLKKQNMLLQQQL 1688
Cdd:TIGR02168 327 ELESKLDELAEELA----ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkVAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1689 DDARNKADNQEKAILNIQARCDARVQNLQ-AECRKHRLLLEEDNKMLVNELNHSKEKECQYEKEKAEREVAVRQLQQKRD 1767
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462496564 1768 DVLNKGSATKALLDASSRHCTYlengmQDSRKKLDQMRSQFQEIQDQLTATIRCTKEME 1826
Cdd:TIGR02168 483 ELAQLQARLDSLERLQENLEGF-----SEGVKALLKNQSGLSGILGVLSELISVDEGYE 536
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
131-184 |
4.86e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.12 E-value: 4.86e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2462496564 131 GRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLL 184
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1348-1712 |
7.41e-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: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1348 RVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKL-RITEEQYRIEAD 1426
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVeQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1427 VTKPIKpalKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQ-NLEKKYLKDFEIVKRKHEDL 1505
Cdd:TIGR02168 756 LTELEA---EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAElTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1506 QKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAARCDHDQSHSSKRDQELAFQG 1585
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1586 TVDKCRHLQENLNSHVlilsLQLSKAESKSRVLKTEL--HY--TGEALKEKALVFEHVQSELKQKQSQMK-DIEKMYKSG 1660
Cdd:TIGR02168 913 LRRELEELREKLAQLE----LRLEGLEVRIDNLQERLseEYslTLEEAEALENKIEDDEEEARRRLKRLEnKIKELGPVN 988
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2462496564 1661 YNTMEKCIEKQERFCQLKKQnmllQQQLDDARNKAdnqEKAILNIQARCDAR 1712
Cdd:TIGR02168 989 LAAIEEYEELKERYDFLTAQ----KEDLTEAKETL---EEAIEEIDREARER 1033
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1348-1859 |
7.70e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 57.67 E-value: 7.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1348 RVKIRKLKNKASVLQKRISEKE---EIKSQLKHEILE-LEKELCSLRFAIQQEKkkrrnveEVHQKVREKLRITEEQYRI 1423
Cdd:TIGR00618 186 FAKKKSLHGKAELLTLRSQLLTlctPCMPDTYHERKQvLEKELKHLREALQQTQ-------QSHAYLTQKREAQEEQLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1424 EAdvtkpikpALKSAEVELKTGGNNSNQVSETDEKED--------LLHENRLMQDEIARLRLEKDTIKNQNLEKKYLKDF 1495
Cdd:TIGR00618 259 QQ--------LLKQLRARIEELRAQEAVLEETQERINrarkaaplAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1496 EIVKRKHEDLQKALKRNGETLAKTIacysgQLAALTDENTTLRSKLEKQRESRQRLETEMQSyhcrlNAARCDHDQSHSS 1575
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQTLHSQEI-----HIRDAHEVATSIREISCQQHTLTQHIHTLQQQ-----KTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1576 KRDQELAFQGTVDKCRHLQENLNSHVLIL--SLQLSKAESKSRVLKTELHYTGEALKEKALVfEHVQS--ELKQKQSQMK 1651
Cdd:TIGR00618 401 ELDILQREQATIDTRTSAFRDLQGQLAHAkkQQELQQRYAELCAAAITCTAQCEKLEKIHLQ-ESAQSlkEREQQLQTKE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1652 DIEKMYKSGYNTMEKCIEK-QERFCQLKKQNMLLQQQLDDARNKADNQEK--AILNIQARCDARVQNLQAEC---RKHRL 1725
Cdd:TIGR00618 480 QIHLQETRKKAVVLARLLElQEEPCPLCGSCIHPNPARQDIDNPGPLTRRmqRGEQTYAQLETSEEDVYHQLtseRKQRA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1726 LLEEDnkmlVNELNHSKEKECQYEKEKAEREVAVRQLQQKRDDVLNKGS-ATKALLDASSRHCTYLENGMQDSRKKLDQm 1804
Cdd:TIGR00618 560 SLKEQ----MQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSeAEDMLACEQHALLRKLQPEQDLQDVRLHL- 634
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462496564 1805 rSQFQEIQDQLTATIrcTKEMEGDTQKLEVEHVMMRKIIKKQDDQI-ERLEKILQH 1859
Cdd:TIGR00618 635 -QQCSQELALKLTAL--HALQLTLTQERVREHALSIRVLPKELLASrQLALQKMQS 687
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1332-1653 |
2.09e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1332 LWKRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELcslrfaiqQEKKKRRN--VEEVHQK 1409
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI--------EELQKELYalANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1410 VREKLRITEEQYRIEADvtkpikpaLKSAEVELKTGGnnsnqvSETDEKEDLLHEnrlMQDEIARLRLEKDTIKNQNLEK 1489
Cdd:TIGR02168 301 EQQKQILRERLANLERQ--------LEELEAQLEELE------SKLDELAEELAE---LEEKLEELKEELESLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1490 KylKDFEIVKRKHEDLQKALkrngETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAARCDH 1569
Cdd:TIGR02168 364 E--AELEELESRLEELEEQL----ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1570 DQSHSSKRDQELAfqgtvdKCRHLQENLNSHVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFEHVQS------EL 1643
Cdd:TIGR02168 438 LQAELEELEEELE------ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsegvkAL 511
|
330
....*....|
gi 2462496564 1644 KQKQSQMKDI 1653
Cdd:TIGR02168 512 LKNQSGLSGI 521
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1351-1836 |
2.56e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1351 IRKLKNKASVLQKRISEKEEIKSQlkhEILELEKELcslrfaiqqeKKKRRNVEEVHQKVREKLRITEEQYRIEAdvtkp 1430
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLK---ELKELEEEL----------KEAEEKEEEYAELQEELEELEEELEELEA----- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1431 ikpALKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQNLEKKYLKDfEIvKRKHEDLQKALK 1510
Cdd:COG4717 110 ---ELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA-EL-AELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1511 RNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAArcdhdqshsskrdqelafqgtvDKC 1590
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA----------------------ALE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1591 RHLQENLNShVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMyksGYNTMEKCIEK 1670
Cdd:COG4717 243 ERLKEARLL-LLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL---QALPALEELEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1671 QERFCQLKKQNMLLQQQLDDARNKADNQEKAILNIQARCDARVQNLQAECRKHRL-LLEEDNKMLVNELNHSKEKECQYE 1749
Cdd:COG4717 319 EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAaLLAEAGVEDEEELRAALEQAEEYQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1750 KEKAEREVAVRQLQQKRDDVLnkgsatkALLDASSRhcTYLENGMQDSRKKLDQMRSQFQEIQDQLTATIRCTKEMEGDT 1829
Cdd:COG4717 399 ELKEELEELEEQLEELLGELE-------ELLEALDE--EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG 469
|
....*..
gi 2462496564 1830 QKLEVEH 1836
Cdd:COG4717 470 ELAELLQ 476
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
36-209 |
4.48e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 54.58 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 115
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 116 LLLQNGANPNITDFFGRTALHYAV-YNEdtSMIEKLLSHGTnIEECSKCEYQPLLFAVSRR-KVKMVEFLLKKKANVNAI 193
Cdd:PHA02874 208 LLIDHGNHIMNKCKNGFTPLHNAIiHNR--SAIELLINNAS-INDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIK 284
|
170
....*....|....*..
gi 2462496564 194 DYLG-SIFDLIYEYERK 209
Cdd:PHA02874 285 DNKGeNPIDTAFKYINK 301
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
37-135 |
6.70e-07 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 53.03 E-value: 6.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 37 HRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATL 116
Cdd:COG0666 191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
|
90
....*....|....*....
gi 2462496564 117 LLQNGANPNITDFFGRTAL 135
Cdd:COG0666 271 LLLALLLLAAALLDLLTLL 289
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
43-192 |
2.61e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 52.56 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 43 GNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQ--N 120
Cdd:PLN03192 536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfaS 615
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462496564 121 GANPNItdffGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNA 192
Cdd:PLN03192 616 ISDPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
57-105 |
3.78e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.80 E-value: 3.78e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2462496564 57 DANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKA 105
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
32-197 |
4.05e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 51.99 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 32 HLKRIHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQE 111
Cdd:PHA02876 145 YMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNI 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 112 ACATLLLQNGANPNITDFfgrtALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKV-KMVEFLLKKKANV 190
Cdd:PHA02876 225 DTIKAIIDNRSNINKNDL----SLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADV 300
|
....*..
gi 2462496564 191 NAIDYLG 197
Cdd:PHA02876 301 NAKNIKG 307
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
41-234 |
4.65e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 51.18 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 41 LHGNLEKLK---YLLLTY-YDANKRDRKERTALHL-ACATGQPEMVHLLVSRRCELNLCDREDRTPLikavqlrqEACAT 115
Cdd:PHA03095 55 LHYSSEKVKdivRLLLEAgADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPL--------HVYLS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 116 ----------LLLQNGANPNITDFFGRTALHyaVYnedtsmiekLLSHGTNIEecskceyqpllfavsrrkvkMVEFLLK 185
Cdd:PHA03095 127 gfninpkvirLLLRKGADVNALDLYGMTPLA--VL---------LKSRNANVE--------------------LLRLLID 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462496564 186 KKANVNAID-YLGSIFDLIYEYERKRYEdlpINSNPVSSQKQPALKATSG 234
Cdd:PHA03095 176 AGADVYAVDdRFRSLLHHHLQSFKPRAR---IVRELIRAGCDPAATDMLG 222
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
65-118 |
5.07e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.34 E-value: 5.07e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2462496564 65 ERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLL 118
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
636-1107 |
9.07e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 9.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 636 SSQKQPALKATTDEEDSVSNIA-TEIKDGEKSGTVSSQKQPALKATTDEE----DSVSNIATEIKDGE---KSGTVSSQK 707
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAAkAEAEAAADEAEAAEEKAEAAEKKKEEAkkkaDAAKKKAEEKKKADeakKKAEEDKKK 1406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 708 QPALKATTDEK---DSVSNIATEIKDGEKSGTVSSQKPPALTATSDEEGS-----VLSIARENKDGEKSRTVSSRKKPAL 779
Cdd:PTZ00121 1407 ADELKKAAAAKkkaDEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkaeeAKKKAEEAKKADEAKKKAEEAKKAD 1486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 780 KATSDEKDSFSNITRGKKDGEISRKVSSQKPPTLKGTSDEedsvLGIARENKDGEKSRTVSSEKppglKASSAEKDSVLN 859
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE----AKKAEEAKKADEAKKAEEKK----KADELKKAEELK 1558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 860 IARGKKDGEKTKRVSSRKKPSLEATSDEKDSfsnitREKKDGEISRKVSSQKPPALKGTSDEEDSVLGIARENKDGEKSR 939
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKA-----EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK 1633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 940 TVSSEKPPGL----KATSDEKDSVLNIARGKKDGEKTRTVSSQKPPTLKATSDEEDSVLSIARENKDGEKSRTV----SS 1011
Cdd:PTZ00121 1634 KVEQLKKKEAeekkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELkkkeAE 1713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1012 EKPSGLKATSAEKDSVLNIARGKKYGEKTKRvssrKKPALKATSDEKDSVLYIAREKKdgEKSRTVSSPKQPALKAICDK 1091
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKKEAEEDKK----KAEEAKKDEEEKKKIAHLKKEEE--KKAEEIRKEKEAVIEEELDE 1787
|
490
....*....|....*.
gi 2462496564 1092 EDSVPNMATEKKDEQI 1107
Cdd:PTZ00121 1788 EDEKRRMEVDKKIKDI 1803
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
36-197 |
1.10e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 50.02 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 36 IHRAVLHGNLEKLKYLLLTY-YDANKRDRKERTALHlACATGQ---PEMVHLLVSRRCELNLCDREDRTPLikAVQLRQE 111
Cdd:PHA03095 87 LHLYLYNATTLDVIKLLIKAgADVNAKDKVGRTPLH-VYLSGFninPKVIRLLLRKGADVNALDLYGMTPL--AVLLKSR 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 112 ACAT----LLLQNGANPNITDFFGRTALHY---------AVYNEDT----------------------------SMIEKL 150
Cdd:PHA03095 164 NANVellrLLIDAGADVYAVDDRFRSLLHHhlqsfkpraRIVRELIragcdpaatdmlgntplhsmatgssckrSLVLPL 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462496564 151 LSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLG 197
Cdd:PHA03095 244 LIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDG 290
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1345-1757 |
1.79e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1345 EQLRVKIRKLKNKASVLQKRISEKEEI-----KSQLKHEILELEKELCSLRFAIQQEKK--KRRNVEEVHQKVREKLRit 1417
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKAdeakkKAEEKKKADEAKKKAEEAKKADEAKKKaeEAKKAEEAKKKAEEAKK-- 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1418 EEQYRIEADVTKPIKPALKSAEvELKTGGNNSNQVSETDEKEDLLH--ENRLMQDEiarLRLEKDTIKNQNLEKKYLKDF 1495
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAE-EAKKKADEAKKAAEAKKKADEAKkaEEAKKADE---AKKAEEAKKADEAKKAEEKKK 1547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1496 EIVKRKHEDLQKALKRNGETLAKTiacysgqlaALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAARCDHDQSHSS 1575
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKK---------AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1576 K-RDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIE 1654
Cdd:PTZ00121 1619 KiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA 1698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1655 KMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARNKADNQEKAI--LNIQARCDARVQNLQAECRKHRLLLEEDNK 1732
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAeeAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
|
410 420
....*....|....*....|....*
gi 2462496564 1733 MLVNELNHSKEKECQYEKEKAEREV 1757
Cdd:PTZ00121 1779 AVIEEELDEEDEKRRMEVDKKIKDI 1803
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1350-1557 |
2.02e-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: 48.99 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1350 KIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQY-------- 1421
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIaelraele 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1422 RIEADVTKPIKPALKSAEVELKTGGNNSNQVSETDEKEDLLHE-NRLMQDEIARLRLEKDTIKNQNlekkylKDFEIVKR 1500
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALR------AELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462496564 1501 KHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQS 1557
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1334-1655 |
2.06e-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: 49.68 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1334 KRLIKLKDNHCEQLRVKI---RKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKK----KRRNVEEV 1406
Cdd:TIGR02169 198 QQLERLRREREKAERYQAllkEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKrleeIEQLLEEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1407 HQKVREKlrITEEQYRIEADVtkpikpalksAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQn 1486
Cdd:TIGR02169 278 NKKIKDL--GEEEQLRVKEKI----------GELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE- 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1487 lekkyLKDFEIVKRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEK---QRESRQRLETEMQSYHCRLN 1563
Cdd:TIGR02169 345 -----IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKlkrEINELKRELDRLQEELQRLS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1564 AARCDHDQSHSSKRDQELAFQGTVD----KCRHLQENLNShvliLSLQLSKAESKSRVLKTELhytgealkekalvfEHV 1639
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEdkalEIKKQEWKLEQ----LAADLSKYEQELYDLKEEY--------------DRV 481
|
330
....*....|....*.
gi 2462496564 1640 QSELKQKQSQMKDIEK 1655
Cdd:TIGR02169 482 EKELSKLQRELAEAEA 497
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1366-1869 |
2.49e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.40 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1366 SEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQYRIEADVTKPIKPALKSAEVELKTG 1445
Cdd:pfam01576 57 AEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1446 GNNSNQVSETDEKedLLHENRLMQDEIARL--RLEKDTIKNQNLEKkylkdfeiVKRKHE----DLQKALKRNGET---L 1516
Cdd:pfam01576 137 EEDILLLEDQNSK--LSKERKLLEERISEFtsNLAEEEEKAKSLSK--------LKNKHEamisDLEERLKKEEKGrqeL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1517 AKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAARCDHDQSHSSKRDQElafqgtvDKCRHLQEN 1596
Cdd:pfam01576 207 EKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELE-------AQISELQED 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1597 LNSHvlilSLQLSKAESKSRVLKTELhytgEALK---EKALVFEHVQSELKQKQSQMkdiekmyksgYNTMEKCIEKQER 1673
Cdd:pfam01576 280 LESE----RAARNKAEKQRRDLGEEL----EALKtelEDTLDTTAAQQELRSKREQE----------VTELKKALEEETR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1674 FCQLKKQNML---------LQQQLDDARNKADNQEKAilniqarcdarvqnlqaecrkhRLLLEEDNKMLVNELNHSKEK 1744
Cdd:pfam01576 342 SHEAQLQEMRqkhtqaleeLTEQLEQAKRNKANLEKA----------------------KQALESENAELQAELRTLQQA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1745 ECQYEKEKAEREVAVRQLQQK-------RDDVLNKGSATKALLDASSRHCTYLENGMQDSRKKLDQMRSQFQEIQDQLTA 1817
Cdd:pfam01576 400 KQDSEHKRKKLEGQLQELQARlseserqRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2462496564 1818 TIRCTKEMEGDTQKLEVEHVMMRKIIKKQDDQIERLEKilQHSSLMLQVFES 1869
Cdd:pfam01576 480 ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVER--QLSTLQAQLSDM 529
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
67-197 |
3.42e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 48.42 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 67 TALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGANP---------------------- 124
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTsilpipciekdmiktildcgid 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462496564 125 -NITDFFGRTALHYAVYNEDTSMIEKLLSHG--TNIEECSKCeyQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLG 197
Cdd:PHA02874 117 vNIKDAELKTFLHYAIKKGDLESIKMLFEYGadVNIEDDNGC--YPIHIAIKHNFFDIIKLLLEKGAYANVKDNNG 190
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1345-1772 |
4.94e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1345 EQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQYRIE 1424
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1425 ADVTKpIKPALKSAEVELKTGGNNSNQVSETDEKEDLLhenrlmQDEIARLrlekdtiknqnleKKYLKDFEIVKRKHED 1504
Cdd:PRK03918 314 KRLSR-LEEEINGIEERIKELEEKEERLEELKKKLKEL------EKRLEEL-------------EERHELYEEAKAKKEE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1505 LQKALKR-NGETLAKTIAcysgQLAALTDENTTLRSKLEKQRESRQRLETEMQSyhcrlnaarcdhdqshsskrdqelaf 1583
Cdd:PRK03918 374 LERLKKRlTGLTPEKLEK----ELEELEKAKEEIEEEISKITARIGELKKEIKE-------------------------- 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1584 qgtvdkcrhLQENLNshvlilslQLSKAESKSRVLKTEL--HYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMYKSgy 1661
Cdd:PRK03918 424 ---------LKKAIE--------ELKKAKGKCPVCGRELteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE-- 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1662 ntMEKCIEKQERFCQLKKqnmlLQQQLDDARNKAD--NQEKailniqarcdarvqnLQAECRKHRLLLEEDNKML--VNE 1737
Cdd:PRK03918 485 --LEKVLKKESELIKLKE----LAEQLKELEEKLKkyNLEE---------------LEKKAEEYEKLKEKLIKLKgeIKS 543
|
410 420 430
....*....|....*....|....*....|....*
gi 2462496564 1738 LNHSKEKECQYEKEKAEREVAVRQLQQKRDDVLNK 1772
Cdd:PRK03918 544 LKKELEKLEELKKKLAELEKKLDELEEELAELLKE 578
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
67-154 |
7.20e-05 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 47.77 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 67 TALHLACATGQPEMVHLLVSR------RCELNLCDREDRTPLIKAVQLR--------QEACATLLLQNGANPNITDFFGR 132
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERgasvpaRACGDFFVKSQGVDSFYHGESPlnaaaclgSPSIVALLSEDPADILTADSLGN 209
|
90 100 110
....*....|....*....|....*....|.
gi 2462496564 133 TALHYAVYNED---------TSMIEKLLSHG 154
Cdd:TIGR00870 210 TLLHLLVMENEfkaeyeelsCQMYNFALSLL 240
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1345-1557 |
8.19e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 8.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1345 EQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQYRIE 1424
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1425 ADVTKpikpALKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQNLEKKYLKDFEIVKRKHED 1504
Cdd:COG1196 364 EEALL----EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462496564 1505 LQKALKRNGETLAKTIAcysgQLAALTDENTTLRSKLEKQRESRQRLETEMQS 1557
Cdd:COG1196 440 EEEALEEAAEEEAELEE----EEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1336-1859 |
8.46e-05 |
|
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: 47.71 E-value: 8.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1336 LIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVRE-KL 1414
Cdd:TIGR04523 153 ELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQlKD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1415 RITEEQYRIEA------DVTKPIKPALKSAEVELKTGGNNSNQVSETDEKEDLLhENRLMQDEIARLRLEKDtiKNQNLE 1488
Cdd:TIGR04523 233 NIEKKQQEINEktteisNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL-EKQLNQLKSEISDLNNQ--KEQDWN 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1489 KKYLKDFEIVKRKHEDLQKALKRNGET---LAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNaa 1565
Cdd:TIGR04523 310 KELKSELKNQEKKLEEIQNQISQNNKIisqLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK-- 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1566 rcdhdQSHSSKRDQELAFQGTVDKCRHLQENLNShVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFEHVQSELKQ 1645
Cdd:TIGR04523 388 -----NLESQINDLESKIQNQEKLNQQKDEQIKK-LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDN 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1646 KQSQMKDIEKMYKSGYNTMEKCIEKQerfcqlkkqnmllQQQLDDarnkaDNQEKAILNIQARcdarvqnlqaecrkhrl 1725
Cdd:TIGR04523 462 TRESLETQLKVLSRSINKIKQNLEQK-------------QKELKS-----KEKELKKLNEEKK----------------- 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1726 LLEEDNKMLVNELNHSKEKECQYEKEKAEREVAVRQLQQ---KRDDVLNKGSATKAL------LDASSRHCTYLENGMQD 1796
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDelnKDDFELKKENLEKEIdeknkeIEELKQTQKSLKKKQEE 586
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462496564 1797 SRKKLDQMRSQFQEIQDQLTATIRCTKEMEGDTQKLEVEHVMMRKIIKKQDDQIERLEKILQH 1859
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1237-1765 |
1.10e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.41 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1237 KMKDVqtSTPAEQDLEMASEGEQKRLEEYENNQPQVKNQIHSRDDLDDI-------IQSSQTVSEDgdsLCCNCKNVILL 1309
Cdd:pfam05483 255 KMKDL--TFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIkmslqrsMSTQKALEED---LQIATKTICQL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1310 IDQHEMKCKD-----CVHLL---KIKNTFCLWKRLIKLK----DNHCEQLRVKIRKLKNKASVLQkrisEKEEIKSQLKH 1377
Cdd:pfam05483 330 TEEKEAQMEElnkakAAHSFvvtEFEATTCSLEELLRTEqqrlEKNEDQLKIITMELQKKSSELE----EMTKFKNNKEV 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1378 EILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQYR------IEADVTKPIKPALKSAEVELKTGGNNS-- 1449
Cdd:pfam05483 406 ELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKeihdleIQLTAIKTSEEHYLKEVEDLKTELEKEkl 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1450 NQVSETDEKEDLLHENRLMQDEIARLRLEkdtiknqnlekkylkdfeiVKRKHEDLQKALKRNGETLAktiacysgQLAA 1529
Cdd:pfam05483 486 KNIELTAHCDKLLLENKELTQEASDMTLE-------------------LKKHQEDIINCKKQEERMLK--------QIEN 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1530 LTDENTTLRSKLEKQRESRQRLETEMQsyhCRLNAARCDHDQSHSSKRDQELAFQGTVDKCRHLQENLnshvlilslqls 1609
Cdd:pfam05483 539 LEEKEMNLRDELESVREEFIQKGDEVK---CKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI------------ 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1610 kaESKSRVLKtELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQERFCQLKKQNMLlqQQLD 1689
Cdd:pfam05483 604 --ENKNKNIE-ELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLL--EEVE 678
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462496564 1690 DARNKADNQEKAILNIQARCDARVQNLQAECRKHRLLLEEDNKMLVNELNHSKEKECQYEKEKAEREVAVRQLQQK 1765
Cdd:pfam05483 679 KAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAE 754
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
83-138 |
1.46e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.18 E-value: 1.46e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462496564 83 LLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYA 138
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1332-1613 |
1.49e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1332 LWKRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVR 1411
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1412 EKLR-ITEEQYRIEADVTkpikpALKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQNLEKK 1490
Cdd:COG1196 309 ERRReLEERLEELEEELA-----ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1491 YLKDFEIVKRKHEDLQKALKRNGETLAKTIAcysgQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAARCDHD 1570
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLE----RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2462496564 1571 QSHSSKRDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAES 1613
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
131-159 |
1.93e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 40.26 E-value: 1.93e-04
10 20
....*....|....*....|....*....
gi 2462496564 131 GRTALHYAVYNEDTSMIEKLLSHGTNIEE 159
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
51-107 |
2.19e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.04 E-value: 2.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462496564 51 LLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQ 107
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
682-900 |
2.21e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 46.58 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 682 DEEDSVSNIATEIKDGEKSGTVSS---QKQPALKATTDEKDSV-----SNIATEIKDGEKSGTVSSQKPPALTATSDEEG 753
Cdd:PTZ00108 1144 QEEVEEKEIAKEQRLKSKTKGKASklrKPKLKKKEKKKKKSSAdkskkASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGS 1223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 754 SVLSIARENKDGEKS------RTVSSRKKPALKATSDEKDSFSNITRGKKDGEISRKVSSQKPPTLKGTSDEEDSVLGIA 827
Cdd:PTZ00108 1224 DQEDDEEQKTKPKKSsvkrlkSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPS 1303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 828 RENKDGEKSRTVSSEKppGLKASSAEKDSVLNIARGKKD-----GEKTKRVSSRKKPSLEATS--DEKDSFSNITREKKD 900
Cdd:PTZ00108 1304 SPTKKKVKKRLEGSLA--ALKKKKKSEKKTARKKKSKTRvkqasASQSSRLLRRPRKKKSDSSseDDDDSEVDDSEDEDD 1381
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
117-171 |
2.41e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.79 E-value: 2.41e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462496564 117 LLQNG-ANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFA 171
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1374-1704 |
2.44e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1374 QLKHEILELEKELCSLRFAIQQEKKKRRNvEEVHQKVREKLRITEEQYRIEAdvtkpikpALKSAEVELKTggnnsnqvs 1453
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELE-AELEELEAELEELEAELAELEA--------ELEELRLELEE--------- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1454 ETDEKEDLLHENRLMQDEIArlRLEKDTIKNQNLEKKYLKDFEIVKRKHEDLQKALKRNGETLAKTIAcysgQLAALTDE 1533
Cdd:COG1196 279 LELELEEAQAEEYELLAELA--RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE----ELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1534 NTTLRSKLEKQRESRQRLETEMQsyhcrlnaarcDHDQSHSSKRDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAES 1613
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELA-----------EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1614 KSRVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDIEKMYKsgyntmekciEKQERFCQLKKQNMLLQQQLDDARN 1693
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA----------ELLEEAALLEAALAELLEELAEAAA 491
|
330
....*....|.
gi 2462496564 1694 KADNQEKAILN 1704
Cdd:COG1196 492 RLLLLLEAEAD 502
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1338-1729 |
4.93e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1338 KLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKvREKLRIT 1417
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRK-ELLEEYT 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1418 EEQYRIEADVtKPIKPALKSAEVELKtggnnsnQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQNLEKKYlKDFEI 1497
Cdd:PRK03918 459 AELKRIEKEL-KEIEEKERKLRKELR-------ELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKA-EEYEK 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1498 VKRKHEDLQKALKRNGETLAKtiacysgqLAALTDENTTLRSKLEKQRESRQRLETEMQSY--------HCRLNAARCDH 1569
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKELEK--------LEELKKKLAELEKKLDELEEELAELLKELEELgfesveelEERLKELEPFY 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1570 DQSHSSKrDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAES-KSRVLKTELHYTGEALKEKALVFEHVQSELKQKQS 1648
Cdd:PRK03918 602 NEYLELK-DAEKELEREEKELKKLEEELDKAFEELAETEKRLEElRKELEELEKKYSEEEYEELREEYLELSRELAGLRA 680
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1649 QMKDIEKMYKsgynTMEKCIEKQERfcQLKKqnmllqqqLDDARNKADNQEKAIlniqarcdARVQNLQAECRKHRLLLE 1728
Cdd:PRK03918 681 ELEELEKRRE----EIKKTLEKLKE--ELEE--------REKAKKELEKLEKAL--------ERVEELREKVKKYKALLK 738
|
.
gi 2462496564 1729 E 1729
Cdd:PRK03918 739 E 739
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
36-187 |
5.44e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 45.00 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 36 IHRAVLHGNLEKLKYLLltyyDANKRDRKE---------RTALHLACATGQPEMVHLLVSRRCELN------LCDREDRT 100
Cdd:cd22192 55 LHVAALYDNLEAAVVLM----EAAPELVNEpmtsdlyqgETALHIAVVNQNLNLVRELIARGADVVspratgTFFRPGPK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 101 --------PLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTS----MIEKLLSHGTNIEECS------K 162
Cdd:cd22192 131 nliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTfacqMYDLILSYDKEDDLQPldlvpnN 210
|
170 180
....*....|....*....|....*
gi 2462496564 163 CEYQPLLFAVSRRKVKMVEFLLKKK 187
Cdd:cd22192 211 QGLTPFKLAAKEGNIVMFQHLVQKR 235
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1340-1826 |
6.72e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.71 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1340 KDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKL-RITE 1418
Cdd:pfam05483 252 KENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTIcQLTE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1419 EqyrieadvtkpikpalKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQNLEkkylkdfeiV 1498
Cdd:pfam05483 332 E----------------KEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITME---------L 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1499 KRKHEDLQK--ALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRL-------ETEMQSYHCRLNAARCdh 1569
Cdd:pfam05483 387 QKKSSELEEmtKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELifllqarEKEIHDLEIQLTAIKT-- 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1570 DQSHSSKRDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAESKSRVLKTELHYtgealkekalvfEHVQSELKQKQSQ 1649
Cdd:pfam05483 465 SEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQ------------EDIINCKKQEERM 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1650 MKDIEkmyksgyNTMEKCIEKQERFCQLKKQnmlLQQQLDDARNKADNQEKAILNIQARCdarvqnlqaecrkhrLLLEE 1729
Cdd:pfam05483 533 LKQIE-------NLEEKEMNLRDELESVREE---FIQKGDEVKCKLDKSEENARSIEYEV---------------LKKEK 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1730 DNKMLVNELNHSKekecqyeKEKAEREVAVRQLQQKRDDVLNKGSATKALLDASSRHCTYLENGMQDSRKKLDQMRSQFQ 1809
Cdd:pfam05483 588 QMKILENKCNNLK-------KQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQ 660
|
490
....*....|....*...
gi 2462496564 1810 -EIQDQLTATIRCTKEME 1826
Cdd:pfam05483 661 kEIEDKKISEEKLLEEVE 678
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
114-209 |
6.78e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 44.62 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 114 ATLLLQNGA-----NPNITDFF-GRTALHYAVYNEDTSMIEKLLSHGTNI------------EECSKCEY--QPLLFAVS 173
Cdd:cd22192 66 AAVVLMEAApelvnEPMTSDLYqGETALHIAVVNQNLNLVRELIARGADVvspratgtffrpGPKNLIYYgeHPLSFAAC 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2462496564 174 RRKVKMVEFLLKKKANVNAIDYLGS-----------------IFDLIYEYERK 209
Cdd:cd22192 146 VGNEEIVRLLIEHGADIRAQDSLGNtvlhilvlqpnktfacqMYDLILSYDKE 198
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1345-1855 |
7.07e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 7.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1345 EQLRVKIRKLKNKASVLQKRISEK----EEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQ 1420
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAkkaaEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1421 YRIEADVTKpiKPALKSAEVELKTGGNNSNQVSETDEKEDLLH--ENRLMQDEIARLRLEKDTIKNQNLEKKYLKDFEIV 1498
Cdd:PTZ00121 1398 KKAEEDKKK--ADELKKAAAAKKKADEAKKKAEEKKKADEAKKkaEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEA 1475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1499 KRKHEDLQKA--LKRNGETLAKTiacysgqlaalTDEnttLRSKLEKQRESRQRLETEmqsyhcrlNAARCDHDQSHSSK 1576
Cdd:PTZ00121 1476 KKKAEEAKKAdeAKKKAEEAKKK-----------ADE---AKKAAEAKKKADEAKKAE--------EAKKADEAKKAEEA 1533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1577 RdqelafqgTVDKCRHLQENLNSHVLILSLQLSKAESKSrvlKTELHYTGEALKEKAL--VFEHVQSELKQKQSQMKDIE 1654
Cdd:PTZ00121 1534 K--------KADEAKKAEEKKKADELKKAEELKKAEEKK---KAEEAKKAEEDKNMALrkAEEAKKAEEARIEEVMKLYE 1602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1655 KMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARNKADNQEKAilnIQARCDARVQNLQAECRKHRlllEEDNKML 1734
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA---EELKKAEEENKIKAAEEAKK---AEEDKKK 1676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1735 VNELNHSKEKECQYE---KEKAEREVAVRQLQQKRDDVLNKGSATKALLDASSRHCTYLENGMQDSRKKLDQMRSqfQEI 1811
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAealKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK--DEE 1754
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2462496564 1812 QDQLTATIRCTKEMEGDTQKLEVEHVMMRKIIKKQDDQIERLEK 1855
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1352-1867 |
8.85e-04 |
|
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: 44.44 E-value: 8.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1352 RKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQE--------KKKRRNVEEVHQKVREKLRITEEQYRI 1423
Cdd:pfam12128 265 FGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGElsaadaavAKDRSELEALEDQHGAFLDADIETAAA 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1424 EADVTKPIKPALKSAEVELKTGGNNSNQVSETDEKEDLLHENRLmQDEIARLRLEKDTIKN-------------QNLEKK 1490
Cdd:pfam12128 345 DQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQN-NRDIAGIKDKLAKIREardrqlavaeddlQALESE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1491 YLKDFEIVKRKHEDLQKALKRNGETLAKTI--ACYSG----QLAALTDENTTLRSKLEKQRESRQRLETEmqsyhcrLNA 1564
Cdd:pfam12128 424 LREQLEAGKLEFNEEEYRLKSRLGELKLRLnqATATPelllQLENFDERIERAREEQEAANAEVERLQSE-------LRQ 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1565 ARCDHDQSHSSKRDQELAFQGTVDKCRHLQENLN--SHVLILSLQLSKA---ESKSRVLKTELhytgeaLKEKALVFEHV 1639
Cdd:pfam12128 497 ARKRRDQASEALRQASRRLEERQSALDELELQLFpqAGTLLHFLRKEAPdweQSIGKVISPEL------LHRTDLDPEVW 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1640 QSELKQKQSQMK---DIEKMYKSGYNTMEKciekqerfcQLKKQNMLLQQQLDDARNKADNQEKAILNIqarcDARVQNL 1716
Cdd:pfam12128 571 DGSVGGELNLYGvklDLKRIDVPEWAASEE---------ELRERLDKAEEALQSAREKQAAAEEQLVQA----NGELEKA 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1717 QAECRKHRLLLE---EDNKMLVNELNHSKEK-ECQYEKEKAEREVAVRQLQQKRDDVLNKGSATKA-----LLDASSRHC 1787
Cdd:pfam12128 638 SREETFARTALKnarLDLRRLFDEKQSEKDKkNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEeqkeqKREARTEKQ 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1788 TYLENGMQDSRKKLDQMRSQFQEIQDQLTATIR-CTKEMEGDTQKLEVEHVMMRKIIKKQDDQIERLEKILQHSSLMLQV 1866
Cdd:pfam12128 718 AYWQVVEGALDAQLALLKAAIAARRSGAKAELKaLETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRY 797
|
.
gi 2462496564 1867 F 1867
Cdd:pfam12128 798 F 798
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
31-196 |
1.10e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 43.90 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 31 YHLKRIHRAVLHGNlEKLKYLLLTY-YDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDredrTPLIKAVQLR 109
Cdd:PHA02876 177 YCITPIHYAAERGN-AKMVNLLLSYgADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND----LSLLKAIRNE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 110 QEACATLLLQNGANPNITDFFGRTALHYAVYNEDTS-MIEKLLSHGTNIEECSKCEYQPL-LFAVSRRKVKMVEFLLKKK 187
Cdd:PHA02876 252 DLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLyLMAKNGYDTENIRTLIMLG 331
|
....*....
gi 2462496564 188 ANVNAIDYL 196
Cdd:PHA02876 332 ADVNAADRL 340
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
64-187 |
1.63e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 43.33 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 64 KERTALHLACATGQPEMVHLLVSRRCELNL--CDREDRT-----------PLIKAVQLRQEACATLLLQNGANP---NIT 127
Cdd:cd21882 72 QGQTALHIAIENRNLNLVRLLVENGADVSAraTGRFFRKspgnlfyfgelPLSLAACTNQEEIVRLLLENGAQPaalEAQ 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462496564 128 DFFGRTALHYAVYNED---------TSMIEKLLSHGTNIEECSKCE-------YQPLLFAVSRRKVKMVEFLLKKK 187
Cdd:cd21882 152 DSLGNTVLHALVLQADntpensafvCQMYNLLLSYGAHLDPTQQLEeipnhqgLTPLKLAAVEGKIVMFQHILQRE 227
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
66-96 |
1.70e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 37.65 E-value: 1.70e-03
10 20 30
....*....|....*....|....*....|..
gi 2462496564 66 RTALHLACA-TGQPEMVHLLVSRRCELNLCDR 96
Cdd:pfam00023 3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
66-93 |
2.23e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.18 E-value: 2.23e-03
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1345-1582 |
2.28e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1345 EQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKL-RITEEQYRI 1423
Cdd:PRK02224 352 DDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERdELREREAEL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1424 EADVtKPIKPALKSAEVELKTGG--------NNSNQVSETDEKEDLLHEnrlMQDEIARLRLEKDTIKNQNLEKKYLKDF 1495
Cdd:PRK02224 432 EATL-RTARERVEEAEALLEAGKcpecgqpvEGSPHVETIEEDRERVEE---LEAELEDLEEEVEEVEERLERAEDLVEA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1496 EIVKRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSyhCRLNAARCDHDQSHSS 1575
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE--AREEVAELNSKLAELK 585
|
....*..
gi 2462496564 1576 KRDQELA 1582
Cdd:PRK02224 586 ERIESLE 592
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1637-1855 |
2.84e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1637 EHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARnKADNQEKAILNiqarcdARVQNL 1716
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI-ENVKSELKELE------ARIEEL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1717 QAECRKHRLLLEEdnkmLVNELNHSKEKECQYEKEKAEREVA-----VRQLQQKrddvLNKGSATKALLDASSRHctyLE 1791
Cdd:TIGR02169 771 EEDLHKLEEALND----LEARLSHSRIPEIQAELSKLEEEVSriearLREIEQK----LNRLTLEKEYLEKEIQE---LQ 839
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462496564 1792 NGMQDSRKKLDQMRSQFQEIQDQLTATIRCTKEMEGDTQKLEVEHVMMRKiikkqddQIERLEK 1855
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKK-------ERDELEA 896
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
98-195 |
2.90e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 42.29 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 98 DRTPLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKV 177
Cdd:PHA02875 2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV 81
|
90
....*....|....*...
gi 2462496564 178 KMVEFLLKKKANVNAIDY 195
Cdd:PHA02875 82 KAVEELLDLGKFADDVFY 99
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
131-162 |
3.67e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 36.50 E-value: 3.67e-03
10 20 30
....*....|....*....|....*....|...
gi 2462496564 131 GRTALHYAVYNE-DTSMIEKLLSHGTNIEECSK 162
Cdd:pfam00023 2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1334-1563 |
3.82e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1334 KRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKELcsLRFAIQQEKKKRRNVEEVHQKVREK 1413
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEAR 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1414 LRiteeqyrieadvtkpikpalksaEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARLRlekDTIKNQNLEKkylk 1493
Cdd:TIGR02169 814 LR-----------------------EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE---KEIENLNGKK---- 863
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1494 dfEIVKRKHEDLQKALKRngetlaktiacYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLN 1563
Cdd:TIGR02169 864 --EELEEELEELEAALRD-----------LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1345-1817 |
3.97e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1345 EQLRVKIRKLKNKASVLQKRISEKEEIK--SQLKHEILELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKlriTEEQYR 1422
Cdd:COG4717 105 EELEAELEELREELEKLEKLLQLLPLYQelEALEAELAELPERLEELEERLEELRELEEELEELEAELAEL---QEELEE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1423 IEADVTKPIKPALKSAevelktggnnsnqvseTDEKEDLLHENRLMQDEIARLRLEKDTIKNQnleKKYLKDFEIVKRKH 1502
Cdd:COG4717 182 LLEQLSLATEEELQDL----------------AEELEELQQRLAELEEELEEAQEELEELEEE---LEQLENELEAAALE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1503 EDLQK------------ALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRlnaarcdhd 1570
Cdd:COG4717 243 ERLKEarlllliaaallALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAL--------- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1571 qshssKRDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAESKSRVLktelhytgEALKEKALVfEHVQSELKQ--KQS 1648
Cdd:COG4717 314 -----EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA--------EELEEELQL-EELEQEIAAllAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1649 QMKDIEKMYksgyntmeKCIEKQERFCQLKKQNMLLQQQLDDARNkaDNQEKAILNIQARCDARVQNLQAEcrkhrllLE 1728
Cdd:COG4717 380 GVEDEEELR--------AALEQAEEYQELKEELEELEEQLEELLG--ELEELLEALDEEELEEELEELEEE-------LE 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1729 EDNKMLvNELnHSKEKECQYEKEKAEREVAVRQLQQKRDDVLNK-------GSATKALLDASSRHCTYLEngmqdsRKKL 1801
Cdd:COG4717 443 ELEEEL-EEL-REELAELEAELEQLEEDGELAELLQELEELKAElrelaeeWAALKLALELLEEAREEYR------EERL 514
|
490
....*....|....*.
gi 2462496564 1802 DQMRSQFQEIQDQLTA 1817
Cdd:COG4717 515 PPVLERASEYFSRLTD 530
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1333-1862 |
4.83e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1333 WKRLIKLKDNHCEQLRVKIRKLKN-------KASVLQKRISEKEEIKSQLKHEILELEKELCSLRFAIQQEKKKRRNVEE 1405
Cdd:TIGR04523 24 YKNIANKQDTEEKQLEKKLKTIKNelknkekELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1406 VHQKVREKLRITEEQYRIEADVTKPIKPALKSAEVELKTggNNSNQVSETDEKEDLLHENRLMQDEIARLRLEKDTIKNQ 1485
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDK--FLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1486 NLEKKYlkdfEIVKRKHEDLQKALK-RNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNA 1564
Cdd:TIGR04523 182 KLNIQK----NIDKIKNKLLKLELLlSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1565 ARCDHDQSHSSKRDQELAFQGTVDKCRHLQENLN---SHVLILSLQ------------LSKAESKSRVLKTELHYTGEAL 1629
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNqlkSEISDLNNQkeqdwnkelkseLKNQEKKLEEIQNQISQNNKII 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1630 KEKALVFEHVQSELKQKQSQMKDIEKMYKSGYNTMEKCIEKQErfcQLKKQNMLLQQQLDDARNKADNQEKailnIQARC 1709
Cdd:TIGR04523 338 SQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ---SYKQEIKNLESQINDLESKIQNQEK----LNQQK 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1710 DARVQNLQAEcrkhRLLLEEDNKMLVNELNHSKEKECQYEKEKAEREVAVRQLQQKRDDVLNKGSATKALLDASSRHCTY 1789
Cdd:TIGR04523 411 DEQIKKLQQE----KELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQ 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462496564 1790 LENGMQDSRKKLDQMRSQFQEIQDQLTATIRCTKEMEGDTQKLEVEHVMMRKIIKKQDDQIERLEKILQHSSL 1862
Cdd:TIGR04523 487 KQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENL 559
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1577-1851 |
6.40e-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: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1577 RDQELAFQgtVDKCRHLQEnlnshvlilsLQLSKAESKSRVlKTELhytgEALKEKALVFEHVQSELKQKQSQMKDIEKM 1656
Cdd:pfam17380 366 RQEEIAME--ISRMRELER----------LQMERQQKNERV-RQEL----EAARKVKILEEERQRKIQQQKVEMEQIRAE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1657 YKSGYN-TMEKCIEKQER-FCQLKKQNMLLQQQLDDARNKADNQEKAILNiqarcdarvqnLQAECRKHRLLLEEDNKML 1734
Cdd:pfam17380 429 QEEARQrEVRRLEEERAReMERVRLEEQERQQQVERLRQQEEERKRKKLE-----------LEKEKRDRKRAEEQRRKIL 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1735 VNELNHSKEKECQ-------YEKEKAEREVAVRQLQQKRDdvlnkgsatkalldassrhctylengMQDSRKKLDQMRSQ 1807
Cdd:pfam17380 498 EKELEERKQAMIEeerkrklLEKEMEERQKAIYEEERRRE--------------------------AEEERRKQQEMEER 551
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2462496564 1808 fQEIQDQltatIRCTKEMEGDTQKLEVEHVMMRKIIKKQDDQIE 1851
Cdd:pfam17380 552 -RRIQEQ----MRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1345-1859 |
6.41e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.49 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1345 EQLRVKIRKLKNKASVLQKRISEKEEIKSQLK--HEILELEKELCSLRFAIQQEKKKRRNVEevHQKvreklRITEEQYR 1422
Cdd:TIGR00618 236 QQTQQSHAYLTQKREAQEEQLKKQQLLKQLRAriEELRAQEAVLEETQERINRARKAAPLAA--HIK-----AVTQIEQQ 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1423 IEADVTKpIKPALKSAEVELKTGGNNSNQVSETDEKEDLLHENRLMQDEIARL----RLEKDTIKNQNLEKKYLKDFEIV 1498
Cdd:TIGR00618 309 AQRIHTE-LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAhevaTSIREISCQQHTLTQHIHTLQQQ 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1499 KRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAARCDH-DQSHSSKR 1577
Cdd:TIGR00618 388 KTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKiHLQESAQS 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1578 DQELAFQGTVDKCRHLQENlNSHVLILSLQLSKAESKSRVLKTELHYTGEAlkEKALVFEHVQSELKQKQSQMKDIEKmy 1657
Cdd:TIGR00618 468 LKEREQQLQTKEQIHLQET-RKKAVVLARLLELQEEPCPLCGSCIHPNPAR--QDIDNPGPLTRRMQRGEQTYAQLET-- 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1658 kSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDdARNKADNQEKAILNIQARCDARVQNLQAECRKHRLLLEEDNKMLVNE 1737
Cdd:TIGR00618 543 -SEEDVYHQLTSERKQRASLKEQMQEIQQSFS-ILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRK 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1738 LNHSKEK------ECQYEKEKAEREVAVRQLQQK--RDDVLNKGSATKALLDASSRHCTYLENGMQDSRKKLDQMRSQFQ 1809
Cdd:TIGR00618 621 LQPEQDLqdvrlhLQQCSQELALKLTALHALQLTltQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLA 700
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2462496564 1810 EIQDQLtatiRC--TKEMEGDTQKLEVEHVMMRKI--IKKQDDQIERLEKILQH 1859
Cdd:TIGR00618 701 QCQTLL----REleTHIEEYDREFNEIENASSSLGsdLAAREDALNQSLKELMH 750
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1352-1831 |
8.18e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 8.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1352 RKLKNKASVLQKRISEKEEIKSQLKHEIL-ELEKELCSLRFAIQQEKKKRRNVEEVHQKVREKLRITEEQyRIEADVtkp 1430
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEEKEEKDLHERLnGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER-REELET--- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1431 ikpaLKSAEVELKTggnnsnQVSET-DEKEDLLHENRLMQDEIARLRLEKDTIknqnLEKKYLKDFEI--VKRKHEDLQK 1507
Cdd:PRK02224 256 ----LEAEIEDLRE------TIAETeREREELAEEVRDLRERLEELEEERDDL----LAEAGLDDADAeaVEARREELED 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1508 ---ALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETEMQSYHCRLNAARCDHDQSHSSKRDQELAFQ 1584
Cdd:PRK02224 322 rdeELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1585 GTVDKcrhlQENLNSHVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFE---------------HVQS-------- 1641
Cdd:PRK02224 402 DAPVD----LGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpecgqpvegspHVETieedrerv 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1642 -ELKQKQSQMKDIEKMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARNKADNQEKAIlniqARCDARVQNLQAEC 1720
Cdd:PRK02224 478 eELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERA----EELRERAAELEAEA 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1721 RKHRLLLE------EDNKMLVNELNhSKEKECQYEKEKAER-----------EVAVRQLQQKRDDVLNKGSATKALLDAS 1783
Cdd:PRK02224 554 EEKREAAAeaeeeaEEAREEVAELN-SKLAELKERIESLERirtllaaiadaEDEIERLREKREALAELNDERRERLAEK 632
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2462496564 1784 SRHCTYLENGMQDSR-KKLDQMRSQFQEIQDQLTATIRCTKEMEGDTQK 1831
Cdd:PRK02224 633 RERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELREERDDLQA 681
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1334-1781 |
8.53e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.11 E-value: 8.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1334 KRLIKLKDNHCEQLRVKIRKLKNKASVLQKRISEKEEIKSQLKHEILELEKElcslrfaiQQEKKKRRNVEEVHQKVREK 1413
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEE--------YLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1414 LRiTEEQYRIEADVTKPIKPALKSAEVELKTggNNSNQVSETDEKEDLLHENRLMQDEIARLRLEkdtiKNQNLEKKYLK 1493
Cdd:pfam02463 245 LL-RDEQEEIESSKQEIEKEEEKLAQVLKEN--KEEEKEKKLQEEELKLLAKEEEELKSELLKLE----RRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1494 DFEIVKRKHEDLQKALKRNGETLAKTIACYSGQLAALTDENTTLRSKLEKQRESRQRLETemqsyhcrlnaarcdhdqsh 1573
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLA-------------------- 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1574 ssKRDQELAFQGTVDKCRHLQENLNSHVLILSLQLSKAESKSRVLKTELHYTGEALKEKALVFEHVQSELKQKQSQMKDI 1653
Cdd:pfam02463 378 --KKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 1654 EKMYKSGYNTMEKCIEKQERFCQLKKQNMLLQQQLDDARNKADNQ-EKAILNIQARCDARVQNLQAECRKHRLLLEEDNK 1732
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQkESKARSGLKVLLALIKDGVGGRIISAHGRLGDLG 535
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2462496564 1733 MLVNELNHSKEKECQYEKEKAEREVAVRQLQQKRDDVLNKGSATKALLD 1781
Cdd:pfam02463 536 VAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLI 584
|
|
| PRK08581 |
PRK08581 |
amidase domain-containing protein; |
838-1127 |
9.95e-03 |
|
amidase domain-containing protein;
Pssm-ID: 236304 [Multi-domain] Cd Length: 619 Bit Score: 40.93 E-value: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 838 TVSSEKPPGLKASSAEKDSVlniarGKKDGEKTKRVSSRKKPSLEATSDEKDSFSNITREKKD-----GEISRKVSSQKP 912
Cdd:PRK08581 30 PQKDSTAKTTSHDSKKSNDD-----ETSKDTSSKDTDKADNNNTSNQDNNDKKFSTIDSSTSDsnniiDFIYKNLPQTNI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 913 PALKGTSDEEDSV-LGIARENKDGEKSRTVSSEKPpgLKATSDEKDSVLNIARGKKDGEKTRTVSSQKPPTLKATSDEED 991
Cdd:PRK08581 105 NQLLTKNKYDDNYsLTTLIQNLFNLNSDISDYEQP--RNSEKSTNDSNKNSDSSIKNDTDTQSSKQDKADNQKAPSSNNT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462496564 992 SVLSIARENKDGEKSRTVSSEKPSGLKATSAEKDSvlniargkkygekTKRVSSRKKPALKATSDE------KDSVLYIA 1065
Cdd:PRK08581 183 KPSTSNKQPNSPKPTQPNQSNSQPASDDTANQKSS-------------SKDNQSMSDSALDSILDQysedakKTQKDYAS 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462496564 1066 REKKDGEKSRTVSSPKQPALKAICDKEDSVPNMATEKKDEQISGTVSCQKQPALKATSDKKD 1127
Cdd:PRK08581 250 QSKKDKTETSNTKNPQLPTQDELKHKSKPAQSFENDVNQSNTRSTSLFETGPSLSNNDDSGS 311
|
|
| |
